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Conserved domains on  [gi|1004926768|gb|AMP81963|]
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beta-xylosidase, partial [Enterobacter ludwigii]

Protein Classification

glycoside hydrolase family 43 protein( domain architecture ID 14406677)

glycoside hydrolase family 43 protein is an inverting enzyme that has an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orientation of the catalytic acid

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
6-306 0e+00

Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


:

Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 539.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   6 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSGGIWAPCLSYADGQF 85
Cdd:cd09000     1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  86 WLLYTDVKIVDSPWKNGRNFLVTAPSIEGPWSEPIPMGNGGFGPSLFHDDDGRKYYLYRPWGPRHHSNPHNTIVMQEFDP 165
Cdd:cd09000    81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 166 QTGTFSPERKTLFTGTPLCYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVMTSWHLPENPLQ 245
Cdd:cd09000   161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004926768 246 KSGHGSLLQTHTGEWYMAYLTSRPLRlpgipllasgGRGYCPLGRETGIARIEWR-DGWPYV 306
Cdd:cd09000   241 KAGHGSLVETPDGEWYLAHLCGRPLP----------GRGRCPLGRETAIQKVEWTdDGWPRL 292
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
333-535 8.94e-84

Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.


:

Pssm-ID: 436093  Cd Length: 203  Bit Score: 258.74  E-value: 8.94e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 333 REDFDGSTLDPELQTLRIPFDDSLGSLSVRPGYLRLYGNDSLNSTFTQSTVARRWQHFAFRAETRMQSSPVHFQQSAGLT 412
Cdd:pfam17851   1 RDDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 413 CYYNSKNWSYCFVDYEEGQGRTIKVIQLDHNVPSWPLHEQPIPVPDSAESIWLRVDVDTLVYRYSYSFDGDTWHTVPVTY 492
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1004926768 493 EAWKLSDDYiGGRGFFTGAFVGLHCEDI-SGDGCHADFDYFTYE 535
Cdd:pfam17851 161 DASILSDEY-AAGGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
 
Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
6-306 0e+00

Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 539.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   6 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSGGIWAPCLSYADGQF 85
Cdd:cd09000     1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  86 WLLYTDVKIVDSPWKNGRNFLVTAPSIEGPWSEPIPMGNGGFGPSLFHDDDGRKYYLYRPWGPRHHSNPHNTIVMQEFDP 165
Cdd:cd09000    81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 166 QTGTFSPERKTLFTGTPLCYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVMTSWHLPENPLQ 245
Cdd:cd09000   161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004926768 246 KSGHGSLLQTHTGEWYMAYLTSRPLRlpgipllasgGRGYCPLGRETGIARIEWR-DGWPYV 306
Cdd:cd09000   241 KAGHGSLVETPDGEWYLAHLCGRPLP----------GRGRCPLGRETAIQKVEWTdDGWPRL 292
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
4-304 3.62e-114

Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 398349 [Multi-domain]  Cd Length: 281  Bit Score: 339.68  E-value: 3.62e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   4 ITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSggiWAPCLSYADG 83
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNAS---WAPDISYHDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  84 QFWLLYTDVKivdspwknGRNFLVTAPSIEGPWSEPIPMGNGGFG--PSLFHDDDGRKYYLYRPWGPRHhsnPHNTIVMQ 161
Cdd:pfam04616  78 KYYLYYTAVA--------HGIFVATADSPDGPWSDPGKLKSGGGGidPSLFHDDDGKKYLVWGGWDPRH---GHGGIYLQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 162 EFDPQTGTFSPERKTLFTG----TPLCYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVMTSW 237
Cdd:pfam04616 147 ELDNDGLKLVGPVTKLIYPgtrwVGGKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSR 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004926768 238 HlPENPLQKSGHGSLLQTHTGEWYMAYLTSRPlrlpgipllasgGRGYCPLGRETGIARIEWR-DGWP 304
Cdd:pfam04616 227 S-PENPIYGPGHASLVETPDGEWWIVYHAGRP------------GDGGYGLGRETRIQPVEWRaDGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
3-416 4.11e-104

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 316.50  E-value: 4.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   3 TITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLdmkGNPDSGGIWAPCLSYAD 82
Cdd:COG3507    21 TYTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQW---ADPYSGGIWAPDIRYHN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  83 GQFWLLYTDvkiVDSPWKNGRNFLVTAPSIEGPWSEPIPMGNGGFG---PSLFHDDDGRKYYLYrpwgprhhSNPHNTIV 159
Cdd:COG3507    98 GKYYLYYTA---VDGGKNRSGIGVATADDPEGPWSDPGPLVCPGGNgidPSVFVDDDGKAYLVY--------GSGGGGIY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 160 MQEFDPQTGTFSPERKTLFTGTPLCYTEGAHLYRKEGWYYLMVAEGGT-SYEHAVVVLRSKTLDGPYELHPDVTVMTSWH 238
Cdd:COG3507   167 VAELDPDTGKLLGEPKTLAPGGEGGWIEGPHIYKRNGYYYLFYSEGGTcNSGYAVRVARSKSPTGPYEDAPGNPILTQRS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 239 lpENPLQKSGHGSLLQTHTGEWYMAYLTSRPLRlpgipllasggrgycPLGRETGIARIEWR-DGWPYVDggkhaqltvP 317
Cdd:COG3507   247 --DGGIQGPGHGSLVETPDGEWYLVYHAYRPPG---------------GLGRETFLDPVTWNeDGWPVVG---------P 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 318 GPQIAEQPASSrdSWREDFDGStldpelqtlrIPFDDSLgslsvrpGYLRLYGndslnstftqstvarrwqhfAFRAETR 397
Cdd:COG3507   301 GTGEPPQPLPA--PESDDFDGP----------LGLQWSL-------GYLRLTR--------------------QFTATTK 341
                         410
                  ....*....|....*....
gi 1004926768 398 MQsspvhfqqsAGLTCYYN 416
Cdd:COG3507   342 LR---------AGLVLYGN 351
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
333-535 8.94e-84

Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.


Pssm-ID: 436093  Cd Length: 203  Bit Score: 258.74  E-value: 8.94e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 333 REDFDGSTLDPELQTLRIPFDDSLGSLSVRPGYLRLYGNDSLNSTFTQSTVARRWQHFAFRAETRMQSSPVHFQQSAGLT 412
Cdd:pfam17851   1 RDDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 413 CYYNSKNWSYCFVDYEEGQGRTIKVIQLDHNVPSWPLHEQPIPVPDSAESIWLRVDVDTLVYRYSYSFDGDTWHTVPVTY 492
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1004926768 493 EAWKLSDDYiGGRGFFTGAFVGLHCEDI-SGDGCHADFDYFTYE 535
Cdd:pfam17851 161 DASILSDEY-AAGGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
Ree1 COG3506
Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function ...
392-536 4.94e-09

Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function unknown];


Pssm-ID: 442729  Cd Length: 195  Bit Score: 56.06  E-value: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 392 FRAETRMQSSPVH-FQQsAGLTCYYNSKNWSYCFVDYE-EGQGRTIKVIQLDHNvpSWPLHeqpiPVPDSAESIWLRVDV 469
Cdd:COG3506    58 FTFEVKVTGDFKElYDQ-AGLMVRVDEENWIKAGIEYVpDGVPRLGSVVTNGYS--DWSTG----PVPGDPKSVWLRLSR 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004926768 470 DTLVYRYSYSFDGDTWHTVPVTYeawkLSDDyiggrgffTGAFVGLHCEDISGDGCHADFDYFTYEP 536
Cdd:COG3506   131 RGDALRIQYSLDGKTWTLLRLAP----LPPA--------APVKVGLMACSPTGEGFTVRFSDFSLTP 185
 
Name Accession Description Interval E-value
GH43_SXA-like cd09000
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ...
6-306 0e+00

Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350114 [Multi-domain]  Cd Length: 292  Bit Score: 539.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   6 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSGGIWAPCLSYADGQF 85
Cdd:cd09000     1 NPILPGFNPDPSICRVGDDYYIATSTFEWFPGVQIHHSKDLVNWELVARPLTRVSQLDMRGNPDSGGIWAPCLSYADGKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  86 WLLYTDVKIVDSPWKNGRNFLVTAPSIEGPWSEPIPMGNGGFGPSLFHDDDGRKYYLYRPWGPRHHSNPHNTIVMQEFDP 165
Cdd:cd09000    81 WLVYTDVKSVDGPFKDVHNYLVTAESIEGPWSEPIYLNSSGFDPSLFHDDDGRKYLVNMLWDHRPGHNRFAGIVLQEFDP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 166 QTGTFSPERKTLFTGTPLCYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVMTSWHLPENPLQ 245
Cdd:cd09000   161 ETKKLVGERKVIFKGTELGLTEGPHLYKRDGYYYLLTAEGGTGYEHAVTVARSRNIFGPYEVDPDNPLLTSWDDPENPLQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004926768 246 KSGHGSLLQTHTGEWYMAYLTSRPLRlpgipllasgGRGYCPLGRETGIARIEWR-DGWPYV 306
Cdd:cd09000   241 KAGHGSLVETPDGEWYLAHLCGRPLP----------GRGRCPLGRETAIQKVEWTdDGWPRL 292
GH43_XynB-like cd18617
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ...
6-306 2.47e-117

Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB); This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350129 [Multi-domain]  Cd Length: 285  Bit Score: 347.96  E-value: 2.47e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   6 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSGGIWAPCLSYADGQF 85
Cdd:cd18617     1 NPILPGFYPDPSICRVGDDYYLVTSSFEYFPGLPIYHSKDLVNWELIGHALDRPSQLDLRGVPSSGGIFAPTIRYHDGRF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  86 WLLYTDVKIVdspwkNGRNFLVTAPSIEGPWSEPIPMGNGGFGPSLFHDDDGRKYYLYRPWGPRHHsNPHNTIVMQEFDP 165
Cdd:cd18617    81 YIITTNVSTD-----GRGNFIVTADDPAGPWSDPVWLDGPGIDPSLFFDDDGKVYLTGTGPPPDPY-EGHGGIWQQEIDL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 166 QTGTFSPERKTLFT-GTPLCYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVMTSWHLPENPL 244
Cdd:cd18617   155 ETGKLLGEPKVLWNgGTGGRWPEGPHLYKIDGWYYLLIAEGGTEEGHSETIARSRSPWGPYEPCPNNPILTHRHLGSNPV 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004926768 245 QKSGHGSLLQTHTGEWYMAYLTSRPlrlpgipllasGGRGYCPLGRETGIARIEWRDGWPYV 306
Cdd:cd18617   235 QNTGHADLVEDPDGSWWAVFLGVRP-----------YGGGFHNLGRETFLAPVEWEDGWPVV 285
GH43_XYL-like cd08989
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ...
6-299 2.90e-116

Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350103 [Multi-domain]  Cd Length: 272  Bit Score: 344.73  E-value: 2.90e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   6 NPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSGGIWAPCLSYADGQF 85
Cdd:cd08989     1 NPVLPGFHPDPSVVRVGDDYYMVNSTFQYFPGIPISHSKDLVHWTPIGHALTRPEQLDLTGGPDGGGIWAPDISYHDGKF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  86 WLLYTDVKIVDSpWKNGRNFLVTAPSIEGPWSEPIPMGNGGFGPSLFHDDDGRKYYLYRPwgprhhsnphNTIVMQEFDP 165
Cdd:cd08989    81 YIYYTVVLNVGS-WKGRRNYLVTSEDPEGPWSEPVWLDEGGIDPSLFVDDDGKHYMLLNP----------GGIRLAELNP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 166 QTGTFSPERKTLFTGTPLCYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVMTsWHLPENPLQ 245
Cdd:cd08989   150 DCTKQIGEPKRIWEGTGGRAPEGPHLYKKDGYYYLLTAEGGTGYGHAITIARSKTIYGPYEPCPYNPILR-QQDPQAPLQ 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1004926768 246 KSGHGSLLQTHTGEWYMAYLTSRPLrlpgipllasgGRGYCPLGRETGIARIEW 299
Cdd:cd08989   229 RCGHGKLVETPDGEWWMVYLCGRPL-----------PGGYCPLGRETALAPVEW 271
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
4-304 3.62e-114

Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 398349 [Multi-domain]  Cd Length: 281  Bit Score: 339.68  E-value: 3.62e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   4 ITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSggiWAPCLSYADG 83
Cdd:pfam04616   1 YRNPVLPGFYPDPSILRVGDDYYLTTSSFEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNAS---WAPDISYHDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  84 QFWLLYTDVKivdspwknGRNFLVTAPSIEGPWSEPIPMGNGGFG--PSLFHDDDGRKYYLYRPWGPRHhsnPHNTIVMQ 161
Cdd:pfam04616  78 KYYLYYTAVA--------HGIFVATADSPDGPWSDPGKLKSGGGGidPSLFHDDDGKKYLVWGGWDPRH---GHGGIYLQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 162 EFDPQTGTFSPERKTLFTG----TPLCYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVMTSW 237
Cdd:pfam04616 147 ELDNDGLKLVGPVTKLIYPgtrwVGGKVTEGPHLYKRNGYYYLTYAAGGTGGPYAVGVARSRSPLGPYEWHPGNPILTSR 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004926768 238 HlPENPLQKSGHGSLLQTHTGEWYMAYLTSRPlrlpgipllasgGRGYCPLGRETGIARIEWR-DGWP 304
Cdd:pfam04616 227 S-PENPIYGPGHASLVETPDGEWWIVYHAGRP------------GDGGYGLGRETRIQPVEWRaDGWP 281
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
3-416 4.11e-104

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 316.50  E-value: 4.11e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   3 TITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLdmkGNPDSGGIWAPCLSYAD 82
Cdd:COG3507    21 TYTNPVLPGDYPDPSIIRVGDTYYLYGTSFEYFPGLPIFHSKDLVNWELVGHALDRLPQW---ADPYSGGIWAPDIRYHN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  83 GQFWLLYTDvkiVDSPWKNGRNFLVTAPSIEGPWSEPIPMGNGGFG---PSLFHDDDGRKYYLYrpwgprhhSNPHNTIV 159
Cdd:COG3507    98 GKYYLYYTA---VDGGKNRSGIGVATADDPEGPWSDPGPLVCPGGNgidPSVFVDDDGKAYLVY--------GSGGGGIY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 160 MQEFDPQTGTFSPERKTLFTGTPLCYTEGAHLYRKEGWYYLMVAEGGT-SYEHAVVVLRSKTLDGPYELHPDVTVMTSWH 238
Cdd:COG3507   167 VAELDPDTGKLLGEPKTLAPGGEGGWIEGPHIYKRNGYYYLFYSEGGTcNSGYAVRVARSKSPTGPYEDAPGNPILTQRS 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 239 lpENPLQKSGHGSLLQTHTGEWYMAYLTSRPLRlpgipllasggrgycPLGRETGIARIEWR-DGWPYVDggkhaqltvP 317
Cdd:COG3507   247 --DGGIQGPGHGSLVETPDGEWYLVYHAYRPPG---------------GLGRETFLDPVTWNeDGWPVVG---------P 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 318 GPQIAEQPASSrdSWREDFDGStldpelqtlrIPFDDSLgslsvrpGYLRLYGndslnstftqstvarrwqhfAFRAETR 397
Cdd:COG3507   301 GTGEPPQPLPA--PESDDFDGP----------LGLQWSL-------GYLRLTR--------------------QFTATTK 341
                         410
                  ....*....|....*....
gi 1004926768 398 MQsspvhfqqsAGLTCYYN 416
Cdd:COG3507   342 LR---------AGLVLYGN 351
GH43_C2 pfam17851
Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus ...
333-535 8.94e-84

Beta xylosidase C-terminal Concanavalin A-like domain; This domain is found to the C-terminus of the pfam04616 domain. This domain adopts a concanavalin A-like fold.


Pssm-ID: 436093  Cd Length: 203  Bit Score: 258.74  E-value: 8.94e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 333 REDFDGSTLDPELQTLRIPFDDSLGSLSVRPGYLRLYGNDSLNSTFTQSTVARRWQHFAFRAETRMQSSPVHFQQSAGLT 412
Cdd:pfam17851   1 RDDFDSPKLGLQWQWLRNPRDESWYSLTERPGYLRLYGRESLSSLFAPSLLARRQQHFSFTATTKLEFEPQKEGEEAGLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 413 CYYNSKNWSYCFVDYEEGQGRTIKVIQLDHNVPSWPLHEQPIPVPDSAESIWLRVDVDTLVYRYSYSFDGDTWHTVPVTY 492
Cdd:pfam17851  81 VYYNEYNHYYLGVTKDEDGGRVLRLVRCDNGELTEELAEEEVPLGGEVKTVYLRVEVDGDTYQFSYSYDGKDWKTIGPEL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1004926768 493 EAWKLSDDYiGGRGFFTGAFVGLHCEDI-SGDGCHADFDYFTYE 535
Cdd:pfam17851 161 DASILSDEY-AAGGGFTGAFVGLYATDNgKGSSGYADFDWFEYE 203
GH43_PcXyl-like cd18833
Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium ...
6-304 1.72e-65

Glycosyl hydrolase family 43 protein such as the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl); This glycosyl hydrolase family 43 (GH43) subgroup includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a characterized bifunctional enzyme with beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) activities. This subgroup belongs to the GH43_XybB subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_XybB subgroup includes enzymes having beta-1,4-xylosidase and alpha-L-arabinofuranosidase activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43_XybB subgroup includes Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350154  Cd Length: 292  Bit Score: 214.42  E-value: 1.72e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   6 NPILTGFNPDPSLCRQGED---YYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMK---GNPDSGGIWAPCLS 79
Cdd:cd18833     1 NPIIPGFHPDPSCIFVPEWdgtFFCVTSSFLAFPGIPIYASKDLINWKLISNVLSRPSQLPELattGTGQQGGIWAPTLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  80 YADGQFWLLYTDVKIVDSPWKNGRNFLVTA--PSIEGPWSEPIPMGNGGFGPSLFHDDDGRKYYLYRpwgprHHSNPHNT 157
Cdd:cd18833    81 YHDGTFYVITTLVFPDKTDASRWDNLLFTTtdPYSDSAWSDPIRFDFPGYDPDLFWDDDGTAYVQGA-----HYWRVRPE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 158 IVMQEFDPQTG-TFSPERKTLFTGTPlcYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVMTS 236
Cdd:cd18833   156 IQQQEIDLKTGeSLSPSPIWNGTGGS--APEGPHMYKKDGWYYLLIAEGGTGLGHSVTIARSRSIWGPYESYPSNPVLTN 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004926768 237 WHLPENpLQKSGHGSLLQTHTGEWYMAYLTSRplrlpgipllasGGRGYC--PLGRETGIARIEW-RDGWP 304
Cdd:cd18833   234 ANTSEY-FQTVGHADLFQDANGNWWGVALATR------------SGPEYEiyPMGRETVLYPVTWeEGEWP 291
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
3-306 5.40e-54

Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase; This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350115 [Multi-domain]  Cd Length: 270  Bit Score: 183.48  E-value: 5.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   3 TITNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPD-----SGGIWAPC 77
Cdd:cd09001     1 TYTNPVLWADYPDPDVIRVGDTYYMVSSTMHFSPGAPILHSKDLVNWEIVGYVVDRLDDGDAYYLEDgknayGKGIWAPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  78 LSYADGQFWLLYTDVkivdspwkNGRNFLVTAPSIEGPWSEPIPMGNGGFGPSLFHDDDGRKYYLYrpwgprhhsnPHNT 157
Cdd:cd09001    81 LRYHNGKFYVYFCTN--------TGGTYVYTADDPAGPWSRPALIGKGYHDPSLLFDDDGKAYLVY----------GNGE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 158 IVMQEFDPQTGTFSPERKTLFTGTPLCYT-EGAHLYRKEGWYYLMVAEGGtSYEHAVVVLRSKTLDGPYELHpdvTVMts 236
Cdd:cd09001   143 IRLTELSPDGTGVGGEGRVIIDGTEEGLGaEGSHLYKINGYYYIFNIEWG-GGGRTQVVLRSKSLYGPYEGR---VVL-- 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004926768 237 wHLPENPLQKSGH-GSLLQTHTGEWY-MAYLtsrplrlpgipllasgGRGycPLGRETGIARIEWRDGWPYV 306
Cdd:cd09001   217 -DDGSGTGDNGPHqGGLVDTPDGEWWfMLFQ----------------DRG--AVGRIPVLVPVTWKDGWPVI 269
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
14-266 2.06e-52

Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350092 [Multi-domain]  Cd Length: 251  Bit Score: 178.78  E-value: 2.06e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  14 PDPSLCRQGEDYYIATSTFEW--FPGVRIYHSRDMKNWSLVSTPLNRvsmlDMKGNPDSGGIWAPCLSY-ADGQFWLLYT 90
Cdd:cd08978     1 ADPSILKDNGRYYIYATTDDTgtGTGIVVWKSKDLVNWKEEGTVLSR----GKSKSWGTGNLWAPEVYYfNSGKWYLYYS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  91 DVkivdSPWKNGRNFLVTAPSIEGPWSEPIPM-----GNGGFGPSLFHDDDGRKYYLYRPWgprhhsNPHNTIVMQEFDP 165
Cdd:cd08978    77 AV----PNGGGGRIYVATSDSPEGPFTPIVSGklgdrGSGSIDPTVFVDDDGKLYLYYGDE------DDSGDIYVAELDP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 166 QTGTFSPERKTLF-----TGTPLCYTEGAHLYRKEGWYYLMVAEGGTSYEHAVVVLRSKTLDGPYELHPDVTVmtSWHLP 240
Cdd:cd08978   147 DLLTIKGDVTLLIgevvgSGFRGNYFEGPAVFKRNGYYYLIYSAGGTDGGYAIGYATSDSPLGPWEKASHNPG--LQTSG 224
                         250       260
                  ....*....|....*....|....*.
gi 1004926768 241 ENPLQKSGHGSLLQTHTGEWYMAYLT 266
Cdd:cd08978   225 ATGIYGPGHGSIFQDEGDRWYIVYHA 250
GH43_XYL-like cd09002
Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase ...
5-306 7.42e-49

Glycosyl hydrolase family 43, beta-D-xylosidase (uncharacterized); This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350116 [Multi-domain]  Cd Length: 271  Bit Score: 170.10  E-value: 7.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   5 TNPILTGFNPDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWSLVSTPLNRVsmldmkgnpdSGGIWAPCLSYADGQ 84
Cdd:cd09002     2 LNPILAGDYPDPSILRDGDDYYMTHSSFDYYPGLLIWHSRDLVNWEPIGAALTEY----------IGTVWAPDLIKHDGR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  85 FWLLYtdvkivdsPWKNGRNFLVTAPSIEGPWSEPIPMG-NGGFGPSLFHDDDGRKyYLYRpwgprhhsnphNTIVMQEF 163
Cdd:cd09002    72 YYIYF--------PAKGGTNYVITADDIAGPWSEPIDLKvGSGIDPGHVVDEDGKR-YLFL-----------SGGRRVRL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 164 DPQTGTFSPERKTLFTGTPL-------C-YTEGAHLYRKEGWYYLMVAEGGT---SYEHAVVVLRSKTLDGPYELHPDVT 232
Cdd:cd09002   132 TDDGLSVAGPPEKVYDGWRYpdewdveCfCLEGPKLFRRGGYYYLTTAQGGTagpPTSHMVVSARSKSPHGPWENSPYNP 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1004926768 233 VMTSWHlPENPLQKSGHGSLLQTHTGEWYMAYLTSRplrlpgipllasggRGYCPLGRETGIARIEW-RDGWPYV 306
Cdd:cd09002   212 LVRTQS-REEKWWSKGHGTLVEGPDGKWWMVYHGYE--------------NGYRTLGRQTLLEPVEWtADGWFRI 271
GH43_ABN-like cd08999
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ...
6-305 1.82e-22

Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350113 [Multi-domain]  Cd Length: 284  Bit Score: 97.21  E-value: 1.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   6 NPILTGFNPDPSLCRQGEDYYiATSTFEWFPGVRIYHSRDMKNWSLVST-PLNRVSmldmKGNPDSGGIWAPCLSY-ADG 83
Cdd:cd08999     1 NPVIDGDFPDPSVIRVGGTYY-AFATNSGGKNVQVATSTDLVTWTLLGGdALPDLP----AWAAAGGNTWAPDVVRrPDG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  84 QFWLLYTdvkivdSPWKNGRNFLV---TAPSIEGPW---SEPIPMGNGGFG---PSLFHDDDGRKYYLYRPWGPrhhSNP 154
Cdd:cd08999    76 KYVMYYS------ARLKSSGKHCIgvaTSDSPLGPFtpvGEPPLCPLDQGGaidPSGFVDPDGKRYLVYKVDGN---SIG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 155 HNT-IVMQEFDPQTGTFSPERKTLFTGT-----PLcyTEGAHLYRKEGWYYLMVAEG---GTSYehAVVVLRSKTLDGPY 225
Cdd:cd08999   147 VPTpIMLQELSADGLTLVGEPVELLLNDgpwdgPL--VEAPSLVKRDGTYYLFYSSNcycSPSY--AVGYATSKSITGPY 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 226 ElhpdvtvmtswHLPENPLQKS-------GHGSLLQThTGEWYMAYLTSRPLRLPGipllasGGRG-YcplgretgIARI 297
Cdd:cd08999   223 T-----------KAGEPLLLTGdggltgpGGADVVED-DGGDWMVFHAWDGGDDVG------GGRAmY--------TAEL 276

                  ....*...
gi 1004926768 298 EWRDGWPY 305
Cdd:cd08999   277 TWEGGWPV 284
GH43_bXyl-like cd09004
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
15-302 7.42e-22

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350118 [Multi-domain]  Cd Length: 266  Bit Score: 95.37  E-value: 7.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYI--ATSTFEWFPGVR--IYHSRDMKNWslvsTPLNRVSMLDMKGNPDSGGIWAPCLSYADGQFWLLYT 90
Cdd:cd09004     2 DPDIVVFGGRYYIypTTDGPPGWSSTSfhVFSSTDLVNW----TDHGIILDLANDVWWANKGAWAPAVAERNGKYYFYFS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  91 -DVKIvdspwknGrnfLVTAPSIEGPW---SEP-IPMGNGGFG---PSLFHDDDGRkYYLYrpWGprhhsnpHNTIVMQE 162
Cdd:cd09004    78 aGSQI-------G---VAVSDSPTGPFtdlGRPlVTGGDYGGQaidPMVFVDDDGQ-AYLY--WG-------NGTAYVAR 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 163 FDPQTGTFSPERKTLFTgtPLCYTEGAHLYRKEGWYYLMVAEGGT-SYEHAVVVLRSKTLDGPYELHPDVTVMTswhlPE 241
Cdd:cd09004   138 LNDDMVSFDGEVVVSIT--PPNFREGPFVHKRNGIYYLSWSENDTrDPDYRVRYATSDSPLGPWTYRGVGLLLD----SA 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004926768 242 NPLQKSGHGSLLQT-HTGEWYMAYltSRpLRLPgipllasGGRGYcplGRETGIARIEWRDG 302
Cdd:cd09004   212 GGIKGTGHHSIVQVpGTDEWYIAY--HR-FAVP-------GGDGY---HREVAIDRLEFDAD 260
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
15-262 1.86e-20

Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350100 [Multi-domain]  Cd Length: 257  Bit Score: 91.14  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYIATST----FEWFP--GVRIYHSRDMKNWSLVSTP----------LNRVSMLDMKGNPdsGGIWAPCL 78
Cdd:cd08986     4 DPYITLGPDGYYYLTGTtggpDWWGVndGIRLWRSKDLKDWEYLGLVwdlekdgwwqWEPQWWTPDSKNK--RALWAPEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  79 SYADGQFWLLYtdvkivdSPWKNGRNFLV-TAPSIEGPWSEPI--PMGNGgFGPSLFHDDDGRKYYLYrpwgprhhsnpH 155
Cdd:cd08986    82 HYINGTWYITH-------SMNGGGTGLLKsTTGKPEGPYVDPMggPLGKG-IDPSLFEDDDGTVYLVW-----------G 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 156 NTIVMQEFDPQTGTFSPERKTLFTGTPLCYTEGAHLYRKEGWYYLMVA------EGGTSYEHAVVVlrSKTLDGPYelHP 229
Cdd:cd08986   143 NGQIARLKKDMSGFAEEPRKIDPSGNREIGHEGAFIFKIGGKYVLFGAawstdkMRKGTYDLYYAT--SDSIYGPY--SE 218
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1004926768 230 DVTVMTswHLpenplqksGHGSLLQTHTGEWYM 262
Cdd:cd08986   219 RRFAGP--HG--------GHGTPFKDKDGQWWC 241
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
6-264 5.90e-19

Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350128 [Multi-domain]  Cd Length: 291  Bit Score: 87.25  E-value: 5.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   6 NPILTGFNPDPSLCRQGEDYYIATSTFE-WFPG-----VRIYHSRDMKNWSLVSTPLNRVsmlDMKGNPDSGGIWAPCLS 79
Cdd:cd18616     1 NPVFEPTFADPTVIRGDDGYFYAYATEDpWGDGggfrlVPILRSKDLVNWEYVGDAFTSK---PRWKWDPGGGLWAPDIR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  80 YADGQFWLLYTdvkivDSPWKNGRNF---LVTAPSIEGPW--------SEPIPMGNgGFGPSLFHDDDgrKYYLYrpWGP 148
Cdd:cd18616    78 YIDGKYVLYYS-----LSDWGADPNPgigVATADSPAGPFtdqgklfdSNEIGVRN-SIDPFVFEDDG--KKYLF--WGS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 149 RHhsnphnTIVMQEFDPQTGTFSPERKTLFTGTPLcytEGAHLYRKEGWYYLMVAEGG------TSYEhaVVVLRSKTLD 222
Cdd:cd18616   148 FY------GIYAVELTADGLALKPGEKVQIAGDRY---EGPYIVKRDGYYYLFGSAGSccegpnSTYR--VVVGRSESLL 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1004926768 223 GPYeLHPDVTVMT---SWHLPENpLQKS------GHGSLLQTHTGEWYMAY 264
Cdd:cd18616   217 GPY-VDRDGRSLLdsgGGGTPVV-LQNGnrfvgpGHNAVITDDAGQDWMLY 265
GH43_ABN cd08988
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ...
14-225 2.48e-18

Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350102 [Multi-domain]  Cd Length: 277  Bit Score: 85.26  E-value: 2.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  14 PDPSLCRQGEDYYI-ATSTFEWfpGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSGG-IWAPCLSYADGQFWLLYTd 91
Cdd:cd08988     1 HDPSIIKEGGTYYAfGTGTDGF--GIPIAKSKDLGNWTIVGEAFATLPSWKGGSPPSADGnLWAPDISQHKGKYYLYYS- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  92 vkIVDSPWKNGRNFLVTAPSIEGP-WSEPIPMGN-------GGFGPSLFHDDDGRKYYLYRPWgprhhsnpHNTIVMQEF 163
Cdd:cd08988    78 --VSDNGSNTSAIGLATANNPQGPfKDEGPAKPVvtsdnagNAIDPDLFQDEDGQNWLLYGSF--------WGGIWLQKL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1004926768 164 DPQTG-TFSPERKTLFTGTPLCYTEGAHLYRKEGWYYLMV-----AEGGTSYEHaVVVLRSKTLDGPY 225
Cdd:cd08988   148 DKNGLvVNPPGNGKSIAVLYYVSIEAPYITYAGGYYYLFVsagscCDGGNSTYH-TRVGRSKKVTGPY 214
GH43_F5-8_typeC-like cd18608
Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 ...
15-265 2.64e-18

Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 domain; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), xylanase (EC 3.2.1.8), and beta-galactosidase (EC 3.2.1.145) activities, and some as F5/8 type C domain (also known as the discoidin (DS) domain)-containing proteins. Most contain a F5/8 type C domain C-terminal to the GH43 domain. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350120 [Multi-domain]  Cd Length: 276  Bit Score: 85.03  E-value: 2.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYIATSTFEWF------PGVriYHSRDMKNWSL--VSTPLNRVSMLDMkgnpdsggIWAPCLSYA-DGQF 85
Cdd:cd18608     3 DPSIVKFGGTYYLYATTDGWGgfnsgePVV--WKSKDFVNWKFegLNWPTKAASGDSK--------VWAPSVVKGkDGKY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  86 WLLYT-DVKIvdspwkngrnFLVTAPSIEGPW------SEPIPMGN-----GGFGPSLFHDDDGrKYYLYrpWGPRHHSN 153
Cdd:cd18608    73 YMYVSvGSEI----------YVGVADSPLGPWknangdGPPIIPGDgkpnyHMIDAEPFIDDDG-KAYLY--WGSGLHVN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 154 PHNTIVmqEFDPQTGTFSPERKTLftGTPLCYTEGAHLYRKEGWYYLMVAEGGTSYE-HAVVVLRSKTLDGPYELHPDVT 232
Cdd:cd18608   140 GHCFAA--KLNPDMVTFDGSEPTI--VTPRDYFEAPFMFKRNGIYYLMYSGGGCWDEtYNVRYAVSDNPLGPFEEGENSP 215
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1004926768 233 VMTSwhLPENPLQKSGHGSLLQtHTGEWYMAYL 265
Cdd:cd18608   216 ILQT--DEAKGIFGPGHHSVFE-EGGQYYILYH 245
GH43_Arb43a-like cd08998
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
15-225 4.57e-18

Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350112 [Multi-domain]  Cd Length: 278  Bit Score: 84.52  E-value: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYIATSTFewfPGVRIYHSRDMKNWSLVSTPLNRV-SMLDMKGNPDSGGIWAPCLSYADGQFWLLYtdvk 93
Cdd:cd08998     3 DPSIIKDDGGTYYVFSTG---AGIQIRTSKDLVNWEFVGTVFPEGpAWAAAEVPGGAGGLWAPDVVYVNGRYYLYY---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  94 ivdSPWKNGRN----FLVTAPSIE-GPWSE--PIPMGNGGFG-----PSLFHDDDGRKYYLYRPWgprhhsnpHNTIVMQ 161
Cdd:cd08998    76 ---SASTFGSNrsaiGLATSTTLDdGPWTDqgLVVSSSPGDDynaidPNVFVDADGRLWLAYGSF--------WGGIKLV 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004926768 162 EFDPQTGTFSPERktlfTGTPLCYT-------EGAHLYRKEGWYYLMVAEG------GTSYEhaVVVLRSKTLDGPY 225
Cdd:cd08998   145 ELDPATGKLRPGS----TGTSIASRpggpgaiEAPYIIYRGGYYYLFVSYGsccrgaNSTYN--IRVGRSTSITGPY 215
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
14-308 4.85e-17

Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580); This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350105 [Multi-domain]  Cd Length: 283  Bit Score: 81.45  E-value: 4.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  14 PDPSLCRQGEDYYIATSTFEWFPGVRIYHSRDMKNWslvsTPLNRVsmLDMKGNPDSGGIWAPCLSYADGQFWLLYTdvk 93
Cdd:cd08991     1 ADPFVLKHNGTYYLYGTGGDDGRGFKVYVSDDLVNW----EYPGGA--LEEPGLWGTKGFWAPEVFYYNGKFYMYYS--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  94 iVDSPWKNGRNFLVTAPSIEGP--WSEPIPMGNGGFG--PSLFHDDDGrKYYLY---RPWGprhhSNPHNTIVMQEF-DP 165
Cdd:cd08991    72 -ANGGDHGEHIAVAVSDSPLGPfrDKGKLLIPAGGFSidAHVFIDDDG-KWYLYyvrDDLG----GEPGNRIYVAELeDD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 166 QTGTFSPERKTLFTGTPLCY---------TEGAHLYRKEGWYYLMVAEGGTSYEH-AVVVLRSKTLDGPYELHPDVTVMT 235
Cdd:cd08991   146 LSLIGEPTLVLCPTADERWEygegrdwhtTEGPTVLKHNGTYYLTYSANHFRSPDyAVGYATADSPLGPWTKYEGNPILS 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004926768 236 SwhlPENPLQKSGHGSLLQTHTGEWYMAYLTSRPLRLPGipllasggrgycplGRETGIARIEWRDGWPYVDG 308
Cdd:cd08991   226 R---NDGGVNGPGHNSVFKDPDGDLYIVYHTHDSDETVE--------------PRKMRIDRLRFDGDKLSVLG 281
GH43_AXH_like cd08990
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ...
36-301 3.89e-14

Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase; This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350104 [Multi-domain]  Cd Length: 269  Bit Score: 72.63  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  36 PGVRIYHSRDMKNWSLVSTPLNrvsmLDMKGNPDSGGIWAPCLSYADGQFWLlYTDVKIVDSPWKNGrnfLVTAPSIEGP 115
Cdd:cd08990    30 DDWHVFSSTDLVNWTDHGEILP----PDDVFWWASGNAWAPDAVYKNGKYYF-YFPVGQASDGFGIG---VAVSDSPAGP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 116 W-----SEPIPMGNGG---FGPSLFHDDDGRkYYLYrpWGPRHH-------SNphntivMQEFDPQTgtfsperKTLFTG 180
Cdd:cd08990   102 FkdalgKPLIPEGLNGiegIDPAVFVDDDGR-AYLY--FGGGGGyyvaklkDD------MISLAGEP-------QKIKNG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 181 TPLCYTEGAHLYRKEGWYYLMVAeGGTSYEHAVVVLRSKTLDGPYElhPDVTVMtswhlpENPLQKSGHGSLLQTHtGEW 260
Cdd:cd08990   166 GLKGFFEAPWVFKRNGTYYLSYA-GGWAYPAEIAYSTADSPLGPYT--YRGVIL------DPVGSGTNHGSIVEFK-GQW 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1004926768 261 YMAYLTSrplrlpgiplLASGGRGYcplGRETGIARIEWRD 301
Cdd:cd08990   236 YLFYHTA----------DLSGGGDF---RRSVCIDYLHYNA 263
GH43_BT3675-like cd18828
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
15-303 1.83e-12

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675); This glycosyl hydrolase family 43 (GH43) subgroup includes the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the GH43_bXyl subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl subgroup also includes enzymes annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350149 [Multi-domain]  Cd Length: 283  Bit Score: 68.07  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYIATSTfEWFPG-----VRIYHSRDMKNWSlvstplNRVSMLDMKGNPDS----GGIWAPCLSYADGQF 85
Cdd:cd18828     2 DPDIAYFDGKYYIYPTT-DGFPGwsgtqFHVFSSDDLVTWK------DEGVILDLKNDQVVpwatGNAWAPTIEERDGKY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  86 WLLYTDvkivDSPWKNGRNFLVTAPSIEGPW---SEP-IPMGNGGFG------PSLFHDDDGRKYYLYrpWGprhhsnpH 155
Cdd:cd18828    75 YFYFCG----KNPDGRSQIGVAVADSPTGPFtaqGSPlITHEMARVTmgqaidPSVFTDPVDGKYYLY--WG-------N 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 156 NTIVMQEFDPQTGTFSPErkTLFTGTPLC-YTEGAHLYRKEGWYYLMVAEGGTSYE-HAVVVLRSKTLDGPYELHPDVTV 233
Cdd:cd18828   142 GYAAIAELNDDMISIKPG--TLVNLDGLTdFREAVTVLYRDGLYHFTWSCDDTGSEnYHVNYGTSDSPYGPITYRGVILQ 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004926768 234 MTswhlPENPLQKSGHGSLLQ-THTGEWYMAYltsrpLRLpGIPLLA-SGGRGYcplGRETGIARIEW-RDGW 303
Cdd:cd18828   220 KD----PSKGILGTGHHSILQvPGTDEWYIAY-----HRF-ATPLGIyGSGLGY---HRETCIDRLTFdADGL 279
GH43_XlnD-like cd18827
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ...
41-270 9.47e-11

Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have mostly been annotated as xylanases (endo-alpha-L-arabinanase, EC 3.2.1.8). It belongs to the GH43_bXyl-like subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl-like subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidases (EC 3.2.1.37) and xylanases, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350148 [Multi-domain]  Cd Length: 277  Bit Score: 62.68  E-value: 9.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  41 YHSRDMKNWSLVSTPLnrvsmlDMKGNP-DSGGIWAPCLSYADGQFWLLYT--DVKIVDSPwknGRNFLVTAPSIEGPWS 117
Cdd:cd18827    31 FSSPDLVHWTKHERIL------DMADVPwANRAVWAPSVIEKNGKYYLYFAanDIQSDDEG---GGIGVAVADRPEGPFK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 118 ----EPIpMGNGGFG-----PSLFHDDDGRkYYLYrpWGPRHHSNphntivMQEFDPQTGTFSP-ERKTLFTG-TPLCYT 186
Cdd:cd18827   102 dalgKPL-IGEFHNGaqpidQHVFKDDDGQ-AYLY--YGGWGHCN------VAKLNDDMTSLVPfDDGETFKEiTPEGYV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 187 EGAHLYRKEGWYYLMVAEGG---TSYEHAVVVLRSKTldGPYE-----LHPDVTVMTSwhlpenplqkSGHGSLLQT-HT 257
Cdd:cd18827   172 EGPFMFKRNGKYYFMWSEGGwtgPDYSVAYAVADSPL--GPFKrigkiLQQDPAIATG----------AGHHSVVNVpGT 239
                         250
                  ....*....|...
gi 1004926768 258 GEWYMAYlTSRPL 270
Cdd:cd18827   240 DDWYIVY-HRRPL 251
GH43-like cd08982
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
41-264 2.62e-10

Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350096 [Multi-domain]  Cd Length: 308  Bit Score: 61.81  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  41 YHSRDMKNWSLVSTPlnrvsmldmkGNPDSGgiWAPCLSYADGQFWLLYTDvkivdspwkNGRNFLVTAPSIEGPWSE-P 119
Cdd:cd08982    28 WHSDDLVNWKFIPTN----------GLPIED--YAPTVVEINGTLYFTASG---------GPGPIYRTDDPLGGKWELvA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 120 IPMGNGGFGPSLFHDDDGRkYYLYrpWGprhhSNPHNTIVMQEFDPQTG-TFSPERKTLFTGTPLC-------------- 184
Cdd:cd08982    87 ESGPFGFWDPALFVDDDGR-LYLY--WG----CSNKDPIYGVELDPNTGfRPIGEPVPLISFDPDKhgwerfgednedpg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 185 ---YTEGAHLYRKEGWYYLMVAEGGT---SYEHAVVVlrSKTLDGPYELHPDvtvmtswhlpeNPL--------QKSGHG 250
Cdd:cd08982   160 lapWIEGAWMTKHNGKYYLQYAAPGTefkTYADGVYV--SDSPLGPFTYAPN-----------NPFsykpggfiTGAGHG 226
                         250
                  ....*....|....
gi 1004926768 251 SLLQTHTGEWYMAY 264
Cdd:cd08982   227 STFQDKYGNYWHFG 240
GH43_GsAbnA-like cd18832
Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1, ...
15-225 4.52e-09

Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350153 [Multi-domain]  Cd Length: 332  Bit Score: 58.03  E-value: 4.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYIATStfewfpgvriyH-----SRDMKNWSLVSTPLNR---------VSMLDMKGNPD----SGGIWAP 76
Cdd:cd18832     3 DPSIVKDDGTYYVFGS-----------HlaaakSTDLMNWTQFTNGVTTdnpllfnlfDSTAWELAEDFnwagGGNLWAP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  77 CLSY--ADGQFWLLYTdvkiVDSPWKNGRNFLVTAPSIEGPW----------------SEPIPMGNGG----------FG 128
Cdd:cd18832    72 DVIYnkAMGKYCMYYS----VSGDDSPSAIGLATADNIEGPYtykgtvlksgftgstsADADVYLTGGkynnnyhpnaID 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 129 PSLFHDDDGRKYYLYRPW--GprhhsnphntIVMQEFDPQTG--TFSPERKTL----FTGTPL---CYT--EGAH-LYRK 194
Cdd:cd18832   148 PCVFYDKDGKLWMVYGSWsgG----------IFLLELDPKTGlrDYSVETDGNlpdqYYGKKIaggYHAsgEGPYiLYDK 217
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1004926768 195 E-GWYYLMVAEGGTSYE--HAVVVLRSKTLDGPY 225
Cdd:cd18832   218 DtGYYYLFVSYGGLDANggYNIRVFRSKNPDGPY 251
Ree1 COG3506
Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function ...
392-536 4.94e-09

Regulation of enolase protein 1 (function unknown), concanavalin A-like superfamily [Function unknown];


Pssm-ID: 442729  Cd Length: 195  Bit Score: 56.06  E-value: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 392 FRAETRMQSSPVH-FQQsAGLTCYYNSKNWSYCFVDYE-EGQGRTIKVIQLDHNvpSWPLHeqpiPVPDSAESIWLRVDV 469
Cdd:COG3506    58 FTFEVKVTGDFKElYDQ-AGLMVRVDEENWIKAGIEYVpDGVPRLGSVVTNGYS--DWSTG----PVPGDPKSVWLRLSR 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004926768 470 DTLVYRYSYSFDGDTWHTVPVTYeawkLSDDyiggrgffTGAFVGLHCEDISGDGCHADFDYFTYEP 536
Cdd:COG3506   131 RGDALRIQYSLDGKTWTLLRLAP----LPPA--------APVKVGLMACSPTGEGFTVRFSDFSLTP 185
GH43_AnAbnA-like cd18831
Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); ...
15-225 5.63e-08

Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities such as Aspergillus niger AbnA, Aspergillus niveus AbnA, and Chrysosporium lucknowense Abn1. It belongs to the GH43_Arb43a subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_Arb43a subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. The GH43_Arb43a subgroup includes many enzymes such as Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, and are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350152 [Multi-domain]  Cd Length: 286  Bit Score: 54.52  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYIATSTFewfPGVRIYHSRDMKN-WSLVSTPLNRVSMLDMKGNPDsggIWAPCLSYADGQFWLLYTdVK 93
Cdd:cd18831     3 DPSIIRREDGTYFRFSTG---GGIRIATAPSLTGpWTYVGSVLPGGSSIDLAGNDD---LWAPDVHYVNGTYYCYYS-VS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  94 IVDSpwKNGRNFLVTAPSIE-GPWS---EPIPMGNG----GFGPSLFHDDDGRKYYLYRPWGprhhsnphNTIVMQEF-- 163
Cdd:cd18831    76 TFGS--QDSAIGVATSPTMEpGSWTdhgAVIRSSSGdpynAIDPNLIVDDDGTPYLTFGSYW--------QGIFQVPLtd 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004926768 164 DPQTGTFSPERKTL-FTGTPLCYTEGAHLYRKEGWYYLMVAEGGTSY----------EHAVVVLRSKTLDGPY 225
Cdd:cd18831   146 PLLSPAAGPPPTHLaYNPSGNHPEEGSFMYKHGGYYYLFFSSGICCGydpslpapgeEYKIRVCRSTSPTGPF 218
GH43_CjArb43A-like cd18830
Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1, ...
15-225 6.27e-08

Glycosyl hydrolase family 43 protein such as Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A); This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes annotated with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes the bifunctional Cellvibrio japonicus Ueda107 endo-alpha-1,5-L-arabinanase / exo-alpha-1,5-L-arabinanase 43A (ArbA;CJA_0805) (Arb43A). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350151 [Multi-domain]  Cd Length: 291  Bit Score: 54.20  E-value: 6.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYIatstFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPD-SGGIWAPCLSYADGQFWLLYT--- 90
Cdd:cd18830     3 DPVMAREGGTYYL----FSTGPGISVMSSKDLKNWTQERPVFDEPPQWAKEAVPGfNGHIWAPDISFHNGRYYLYYScsa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  91 ----------------DVKIVDSPWKN---------GR--------NFLVTApsiEG-PWsepipMGNGGF--GPSLFHD 134
Cdd:cd18830    79 fgkntsaigvatnktlDPDSPDYKWEDhgmvvqsvpGRdlwnaidpNVIVDE---KGtPW-----LSFGSFwgGIKLVKL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 135 DDGRKyYLYRPWGPRHHSNPHNTIVMQEFDPQTGTFsperktlftgtplcytEGAHLYRKEGWYYLMVA-----EGGTSY 209
Cdd:cd18830   151 DPDLK-SLAEPQEWHTIARRERTFKLTDSEAGPGAI----------------EAPFIFKKGGYYYLFVSwdyccRGVNST 213
                         250
                  ....*....|....*.
gi 1004926768 210 EHaVVVLRSKTLDGPY 225
Cdd:cd18830   214 YK-VVVGRSKNVTGPY 228
GH43_Xsa43E-like cd18618
Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase ...
32-226 1.79e-07

Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350130 [Multi-domain]  Cd Length: 275  Bit Score: 52.61  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  32 FEWfpgvRIYHSRDMKNWSLVSTPLnrvSMLDMKGNpdSGGIWAPCLSYADGQFWLLYTdvkiVDSPWKNGRNFLV-TAP 110
Cdd:cd18618    33 NDW----RVFSTTDMVNWTDHGAVL---SLKDFSWA--KGDAWAGQVIERNGKFYWYVP----VHHKTNGGFAIGVaVSD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 111 SIEGPWSEPI-------------PMGNGGFGPSLFHDDDGRKYyLYrpWGprhhsNPHNTIV-----MQEFDPQTGTFSP 172
Cdd:cd18618   100 SPTGPFKDALgkplitndmtgttNHSWDDIDPTVFIDDDGQAY-LY--WG-----NPELYYVklkedMISLDGEIGTIDI 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1004926768 173 ERKTLFTgtplcytEGAHLYRKEGWYYLMVAEGG---TSYEhavvvlRSKTLDGPYE 226
Cdd:cd18618   172 SGLPDFT-------EAPWVHKRNGLYYLSYAAGFpekIAYA------TSDSPTGPWT 215
DUF1349 pfam07081
Protein of unknown function (DUF1349); This family consists of several hypothetical bacterial ...
392-536 1.41e-06

Protein of unknown function (DUF1349); This family consists of several hypothetical bacterial proteins but contains one sequence from Saccharomyces cerevisiae. Members of this family are typically around 200 residues in length. The function of this family is unknown.


Pssm-ID: 462084  Cd Length: 168  Bit Score: 48.33  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 392 FRAETRMQSSPVHFQQSAGLTCYYNSKNWSYCFVDYEEGQGRTIKVIQLDHnvPSWPLheQPIPVPDSAESIWLRVDVDT 471
Cdd:pfam07081  40 FTAEVKVSGDFKELYDQAGLMVRVDEENWIKAGIEYNDGVQRLGSVVTNGY--SDWST--SPLPSEWDPKEVWLRVSRRG 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1004926768 472 LVYRYSYSFDGDTWHTVPVTYeawkLSDDyiggrgffTGAFVGLHCEDISGDGCHADFDYFTYEP 536
Cdd:pfam07081 116 DAFTIEYSTDGEKWTLLRLAH----LPAA--------EEVQVGLYACSPTGEGFTVTFDEFRLTP 168
GH43_BsArb43A-like cd18829
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ...
15-226 1.63e-06

Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes annotated as having endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities, and includes Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase (AbnA;BSU28810) (Arb43A). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the arabinofuranosidase (ABF; EC 3.2.1.55) enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350150 [Multi-domain]  Cd Length: 273  Bit Score: 49.67  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  15 DPSLCRQGEDYYiatsTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMLDMKGNPDSGG--IWAPCLSYADGQFWLLYtdv 92
Cdd:cd18829     3 DPSIIKEGSTWW----TFSTGDGIPVKYSSDGLNWTQGPPIFGSPLSWWKTYVPANTTndVWAPDVHYYNGKYWLYY--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  93 kivdSPWKNGRNF----LVTAPSIE-GPWSEP---IPMGNG----GFGPSLFHDDDGRKYYLYRPWgprhhsnpHNTIVM 160
Cdd:cd18829    76 ----AISTFGSNTsaigLASASSIAaGNWTDEglvLRSTSAdnynAIDPNLVIDASGNPWLVFGSF--------WSGIKI 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1004926768 161 QEFDPQT--GTFSPERKTLFTGTPLcytEGAHLYRKEGWYYLMVAEG----GTSYEHAVVVLRSKTLDGPYE 226
Cdd:cd18829   144 TRLDKATmkPTGSIYSIASRPSGGI---EGPFIVYRDGYYYLFVSIDkccrGVNSTYKIAYGRSTSITGPYL 212
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
5-143 2.11e-05

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655; This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350097  Cd Length: 262  Bit Score: 46.07  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768   5 TNPILTGFNP-----DPSLCRQGED---YYIAT-------STFEWFPGVRIYHSRDMKNWSlvstplnRVSMLDMKGNPD 69
Cdd:cd08983     5 GNPVLTSTVGtkgvrDPFIIRGPEDgkfYLVATdlwiaggAQWNGSRGIGVWESTDLVNWS-------EQRLVKMVSPPN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  70 SGGIWAPCLSY--ADGQ---FW--------------LLYT----------------------DVKIVDSP------WKNG 102
Cdd:cd08983    78 AGNAWAPEAIYdpETGQyvvYWssslygdggggnhrIYYAttkdfktfsepkvlfdpgfnviDTTIVKDGgtyyrfYKDE 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1004926768 103 RN----FLVTAPSIEGPWSEP----IPMGNGGF-GPSLFHDDDGRKYYLY 143
Cdd:cd08983   158 TTgkgiRLATSDSLTGPWTTVttggGAGTGGGVeGPTVFKLNDGGKWYLY 207
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
35-224 6.51e-05

Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350142 [Multi-domain]  Cd Length: 262  Bit Score: 44.92  E-value: 6.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  35 FPGVRIYHSRDMKNWSLVSTPLNRVSMLDMkgNPDSGGiWAPCLSYAD--GQFWLLytdVKIVDSPWKNGRNFLVTAPSI 112
Cdd:cd18821    29 FQGVSCYSSTDLVNWTFEGLALPPQESGDL--GPNRVV-ERPKVIYNPstGKYVMW---MHIDSSNYGDARVGVATSDTV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 113 EGPWS---EPIPMGNGGFGPSLFHDDDGRKYYLYrpwgprhHSNPHNTIVMQEFDPQTGtfSPERKTLFTGTPLcytEGA 189
Cdd:cd18821   103 TGPYTyvgSFRPLGYESRDIGVFQDDDGTAYLLF-------EDRDNGLRIYRLSDDYLS--VVELVYTFIAAGL---EAP 170
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1004926768 190 HLYRKEGWYYLMVAeGGTSYEH-AVVVLRSKTLDGP 224
Cdd:cd18821   171 AMFKVDGTYYLLGS-HLTGWRPnDNVYFTATSLSGP 205
GH43_XynD-like cd09003
Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan ...
11-143 1.61e-04

Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized Bacillus subtilis arabinoxylan arabinofuranohydrolase (AXH), Caldicellulosiruptor sp. Tok7B.1 beta-1,4-xylanase (EC 3.2.1.8) / alpha-L-arabinosidase (EC 3.2.1.55) XynA, Caldicellulosiruptor sp. Rt69B.1 xylanase C (EC 3.2.1.8) XynC, and Caldicellulosiruptor saccharolyticus beta-xylosidase (EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) XynF. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. It belongs to the GH43_AXH-like subgroup which includes enzymes that have been annotated as having beta-xylosidase, alpha-L-arabinofuranosidase and arabinoxylan alpha-L-1,3-arabinofuranohydrolase, xylanase (endo-alpha-L-arabinanase) as well as AXH activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis AXH (BsAXH-m2,3) has been shown to cleave arabinose units from O-2- or O-3-mono-substituted xylose residues and superposition of its structure with known structures of the GH43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350117 [Multi-domain]  Cd Length: 315  Bit Score: 43.79  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  11 GFNPDPSLCRQGEDYYIATStfewfpgVRIYHSRDMKNWS-----LVSTPlNRVSmldmkgnPDSGGIWAPCLSY----A 81
Cdd:cd09003    29 DQQYNANGKKKDNSYYNINS-------LTVISSDDMVNWTdhgeiPVAGP-NGIA-------KWAGNSWAPSVAYkninG 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1004926768  82 DGQFWLLYTDvkivdspwkNGRNF-LVTAPSIEGPWSEPI--PM------GNGG----FGPSLFHDDDGRKyYLY 143
Cdd:cd09003    94 KDKFYLYFAN---------GGGGIgVLTADSPTGPWTDPLgkPLitrstpGCAGvvwlFDPAVFIDDDGQG-YLY 158
GH43_62_32_68_117_130 cd08772
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
43-145 1.77e-03

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


Pssm-ID: 350091 [Multi-domain]  Cd Length: 257  Bit Score: 40.27  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  43 SRDMKNWSLVSTPLNRVSmldmKGNPDSGGIWAPCLSYADGQFWLLYTDVKIVDSPWKNGRNFLVTAPSIEGPW--SEPI 120
Cdd:cd08772    32 SKDLIHWEEEPPAIVARG----GGSYDTSYAFDPEVVYIEGTYYLTYCSDDLGDILRHGQHIGVAYSKDPKGPWtrKDAP 107
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1004926768 121 PMGNGGF------GPSLFHDDDGRKYYLYRP 145
Cdd:cd08772   108 LIEPPNAyspknrDPVLFPRKIGKYYLLNVP 138
GH43_CtGH43-like cd18824
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
35-243 4.33e-03

Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350145 [Multi-domain]  Cd Length: 282  Bit Score: 39.32  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  35 FPGVRIYHSRDMKNWSLvstplNRVSMLDMKGNPDSGGIWAP--CLSYADGQFWLLYtdvkivDSPWKNGRNFLVTAPSI 112
Cdd:cd18824    34 FCGFVVYSSVDLVNWTY-----RGVLFDPNTCAGSPGVCFRPhvVYNARTGRYVLWY------NAYDGSSGYAVATSSTP 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 113 EGPW---SEPIPMGnGGFGP---SLFHDDDGRKYYLYRPWGPRHhsnphnTIVMQEFDPQ----TGTFSPErktlftGTP 182
Cdd:cd18824   103 TGPFvtvPDPVLAP-AGLQAgdfSLFVDDDGTGYLAYTTIDFPQ------SIVVEQLTDDylntTGEYVRD------LID 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1004926768 183 LcYTEGAHLYRKEGWYYLMVAE------GGTSyehaVVVLRSKTLDGPYELHPDVTVMTSWHLPENP 243
Cdd:cd18824   170 Q-EAEAPSIFKRNGIYYILASNtccgccQGTG----ARVYRATSPLGPWTRQIDINSCAGALFPPSD 231
GH43_XylA-like cd18620
Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium ...
45-264 4.64e-03

Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium alpha-L-arabinofuranosidase XylA; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. The GH43_XylA-like subgroup includes Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase (EC 3.2.1.-) as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan.


Pssm-ID: 350132 [Multi-domain]  Cd Length: 274  Bit Score: 39.11  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  45 DMKNWSLVSTPLNrvSMLDMKGNPDSGGI-WAPCLSYADGQFWLLYTDVKivdspwknGRNFLV-TAPSIEGPWS----- 117
Cdd:cd18620    40 DLSNWRYHGVIFR--SDQDPDEVPPGKGLlYAPDVVKGPGRYYLYYCLSK--------GSVEGVaVSDSPAGPFEylgpv 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 118 -EPIPMGNGGFGPSLFHDDDGRkYYLYrpWGprhhsnphntivmqEFDPQTGTFSPERKTLFTGT----PLCYTEGAHLY 192
Cdd:cd18620   110 kYPRKGDIFQIDPAVLVDDDGR-VYLY--WG--------------QGGSKGAELDPDMLTIKPETivdvPAGITFEGHGF 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768 193 ------RK-EGWYYL----MVAEGGTSYEHAVvvlrSKTLDGPYE----LHpDVTVMT--SWhlpenplqkSGHGSLLQT 255
Cdd:cd18620   173 fegssiRKiNGIYYLvyssISRGRPTELCYAT----SKSPLGPFTyggvII-DNGGCDppSG---------NNHGSIVEI 238

                  ....*....
gi 1004926768 256 HtGEWYMAY 264
Cdd:cd18620   239 N-GQWYIFY 246
GH43_CtGH43-like cd18822
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
22-201 5.58e-03

Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350143  Cd Length: 266  Bit Score: 38.75  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  22 GEDYYiatsTFEWFPGVRIYHSRDMKNWSLVSTPLNRVSMldmkGNPDSGG--IWAPCLSY--ADGQF--WLlytdvkiv 95
Cdd:cd18822    19 GENRD----NNNGFNGVSLYSSTDLVNWEFRNTVLTRDTC----SASELASckIERPKVIYnpKTGKFvmWA-------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004926768  96 dsPWKNGRNF------LVTAPSIEGPWS---EPIPMGNGGFGPSLFHDDDGRKYYLyrpwgprhHSNPHNT-IVMQEFDP 165
Cdd:cd18822    83 --HWENGKDYglaraaVATSDTPDGDYTfhgSFRPLGYDSRDMTLFVDDDGTAYLI--------SAANDNAdLNIYRLTP 152
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1004926768 166 QTGTFSPERKTLFTGTplcYTEGAHLYRKEGWYYLM 201
Cdd:cd18822   153 DYLSVDSLVATLFKGQ---HREAPALVKRNGYYYLF 185
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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