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Conserved domains on  [gi|148535224|gb|ABQ85552|]
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metallo-beta-lactamase 7, partial [Pseudomonas aeruginosa]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 1-160 1.50e-96

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


The actual alignment was detected with superfamily member cd16301:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 215  Bit Score: 277.63  E-value: 1.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGASYWL 80
Cdd:cd16301   42 LIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTGGIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  81 VKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKP---YGLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSEVGD 157
Cdd:cd16301  122 LKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSlesKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGD 201


                 ...
gi 148535224 158 ASL 160
Cdd:cd16301  202 VSL 204
 
Name Accession Description Interval E-value
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 1-160 1.50e-96

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 277.63  E-value: 1.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGASYWL 80
Cdd:cd16301   42 LIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTGGIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  81 VKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKP---YGLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSEVGD 157
Cdd:cd16301  122 LKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSlesKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGD 201


                 ...
gi 148535224 158 ASL 160
Cdd:cd16301  202 VSL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 1-152 3.10e-22

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 87.22  E-value: 3.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224     1 LIDTPFtaKDTEKLVTWFVERGY-KIKGSISSHFHSDSTGGIEWLNSQS-IPTYASELTNELLKKDGKVQAKNSFSGASY 78
Cdd:smart00849  13 LIDTGP--GEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPgAPVYAPEGTAELLKDLLALLGELGAEAEPA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224    79 WLVK------------KKIEIFYPgPGHTPDNVVVWLPEHRVLFGGCFVKPYGLGNL----GDANLEAWPKSAKLLVSKy 142
Cdd:smart00849  91 PPDRtlkdgdeldlggGELEVIHT-PGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTlvdgGDAAASDALESLLKLLKL- 168

                          170
                   ....*....|
gi 148535224   143 gKAKLVVPSH 152
Cdd:smart00849 169 -LPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 1-158 1.50e-21

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 86.28  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSQS-IPTYASELTNELLKKDGK--------VQAKN 71
Cdd:COG0491   28 LIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgAPVYAHAAEAEALEAPAAgalfgrepVPPDR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  72 SFS-GASYWLVKKKIEIFYpGPGHTPDNVVVWLPEHRVLFGGCFVKPYGLGN--LGDANLEAWPKSAKLLVSKygKAKLV 148
Cdd:COG0491  108 TLEdGDTLELGGPGLEVIH-TPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRpdLPDGDLAQWLASLERLLAL--PPDLV 184

                        170
                 ....*....|
gi 148535224 149 VPSHSEVGDA 158
Cdd:COG0491  185 IPGHGPPTTA 194
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
1-152 2.32e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 56.61  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224    1 LIDT-PFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWL-NSQSIPTYASELTNELLKKDGKVQAKNSFSGASY 78
Cdd:pfam00753  19 LIDTgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaEATDVPVIVVAEEARELLDEELGLAASRLGLPGP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   79 WLVKKKIEI----------------FYPGPGHTPDNVVVWLPEHRVLFGGCFVKPYGLGNLGDANLEAWP------KSAK 136
Cdd:pfam00753  99 PVVPLPPDVvleegdgilggglgllVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGGLLVlhpssaESSL 178

                         170
                  ....*....|....*...
gi 148535224  137 LLVSKYG--KAKLVVPSH 152
Cdd:pfam00753 179 ESLLKLAklKAAVIVPGH 196
 
Name Accession Description Interval E-value
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 1-160 1.50e-96

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 277.63  E-value: 1.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGASYWL 80
Cdd:cd16301   42 LIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTGGIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWL 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  81 VKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKP---YGLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSEVGD 157
Cdd:cd16301  122 LKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSlesKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGD 201


                 ...
gi 148535224 158 ASL 160
Cdd:cd16301  202 VSL 204
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 1-160 3.08e-81

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 238.72  E-value: 3.08e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVER-GYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGAsYW 79
Cdd:cd16285   39 LIDTPWTEAQTATLLDWIEKKlGKPVTAAISTHSHDDRTGGIKALNARGIPTYATALTNELAKKEGKPVPTHSLKGA-LT 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  80 LVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKP---YGLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSEVG 156
Cdd:cd16285  118 LGFGPLEVFYPGPGHTPDNIVVWLPKSKILFGGCLVKSasaTSLGNVGDADVEAWPKSIENLKAKYPEARMVVPGHGAPG 197


                 ....
gi 148535224 157 DASL 160
Cdd:cd16285  198 GTEL 201
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 1-160 1.08e-53

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 168.96  E-value: 1.08e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWfVER--GYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGASY 78
Cdd:cd16302   40 VFDTPTNDSQSEELIDW-IENslKAKVKAVVPTHFHDDCLGGLKAFHRRGIPSYANQKTIALAKEKGLPVPQHGFSDSLT 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  79 WLV-KKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPY--GLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSEV 155
Cdd:cd16302  119 LKLgGKKIVCRYFGEGHTKDNIVVYFPSEKVLFGGCMVKSLgaGKGNLEDANVEAWPKTVEKVKAKYPDVKIVIPGHGKI 198


                 ....*
gi 148535224 156 GDASL 160
Cdd:cd16302  199 GGSEL 203
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 1-160 9.97e-52

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 163.99  E-value: 9.97e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYK-IKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGASYW 79
Cdd:cd16304   39 LIDTPWDDEQTEELLDWIKKKLKKpVTLAIVTHAHDDRIGGIKALQKRGIPVYSTKLTAQLAKKQGYPSPDGILKDDTTL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  80 LV-KKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPY---GLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSEV 155
Cdd:cd16304  119 KFgNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLeakDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEW 198


                 ....*
gi 148535224 156 GDASL 160
Cdd:cd16304  199 GDKQL 203
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 1-160 2.42e-47

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 153.08  E-value: 2.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWfVER--GYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKD-------------- 64
Cdd:cd07707   34 LVDSTWTPKTTKELIKE-IEKvsQKPVTEVINTHFHTDRAGGNAYLKERGAKTVSTALTRDLAKSEwaeivaftrkglpe 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  65 ----GKVQAKNSFSGAsYWLVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPYGLGNLGDANLEAWPKSAKLLVS 140
Cdd:cd07707  113 ypdlGYELPDGVLDGD-FNLQFGKVEAFYPGPAHTPDNIVVYFPQENVLYGGCIIKETDLGNVADADVKEWPTSIERLKK 191

                        170       180
                 ....*....|....*....|
gi 148535224 141 KYGKAKLVVPSHSEVGDASL 160
Cdd:cd07707  192 RYRNIKAVIPGHGEVGGPEL 211
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 1-154 7.68e-44

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 143.74  E-value: 7.68e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVER-GYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSF-SGASY 78
Cdd:cd16299   39 LFDTPWDKDQYQPLLDSIRKKhNLPVIAVIATHSHEDRAGGLGYFNKIGIPTYATAMTNSILKKENKPQATYLIeTDKTY 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148535224  79 WLVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVK---PYGLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSE 154
Cdd:cd16299  119 KIGGEKFVVYFFGEGHTADNVVVWFPKEKVLDGGCLIKsaeATDLGYIGEANVKEWPKTIHKLKQKFKKAKVVIPGHDE 197
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 1-154 5.29e-43

Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Myroides odoratimimus MUS-1 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293876  Cd Length: 214  Bit Score: 141.72  E-value: 5.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWF-VERGYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSF-SGASY 78
Cdd:cd16318   39 LIDTPWDKDQYEPLLEYIrSNHNKEVKWVITTHFHEDRSGGLGYFNSIGAQTYTYALTNEILKERNEPQAQFSFnKEKQF 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148535224  79 WLVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKP---YGLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSE 154
Cdd:cd16318  119 TFGNEKLAVYFLGEGHSLDNTVVWFPKEEVLYGGCLIKSaeaTTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDE 197
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 1-153 2.20e-40

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 134.95  E-value: 2.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYK-IKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNS--FSGAS 77
Cdd:cd16300   40 LVDTAWTDDQTAQILNWAKQELNLpVRLAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGLVPAQHSltFAAEP 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148535224  78 YWLVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPYG---LGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHS 153
Cdd:cd16300  120 STAPNFPLKVFYPGPGHTRDNIVVGIDGTGIAFGGCLIRPSKatsLGNLADADTEHWAASARAFGAAFPDASMIVPSHG 198
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 1-156 1.99e-39

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 132.68  E-value: 1.99e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWF-VERGYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGASYW 79
Cdd:cd16303   41 LIDTAWGAKNTAALLAEIeKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEAEGNEIPTHSLEGLSSS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  80 LVKKK---IEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPY---GLGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHS 153
Cdd:cd16303  121 GDAVRfgpVELFYPGAAHSTDNLVVYVPSARVLYGGCAVRELsstSAGNVADADLAEWPTSIERIQKHYPEAEFVIPGHG 200


                 ...
gi 148535224 154 EVG 156
Cdd:cd16303  201 LPG 203
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 1-157 3.80e-39

Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBL Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293874  Cd Length: 214  Bit Score: 131.82  E-value: 3.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLV-TWFVERGYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGASYW 79
Cdd:cd16316   39 VIDAPWDETQFQPFLdSIQKKHHKKVIMNIATHSHDDRAGGLEYFGKKGAKTYTTKLTDSILKKNNKPRAEYTFDNDTTF 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  80 LV-KKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPYG---LGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSEV 155
Cdd:cd16316  119 KVgKYEFQVYYPGKGHTADNIVVWFPKEKVLYGGCLIKSADakdLGYLGEAYVNDWTQSIHNIQQKFPNPQYVIAGHDDW 198


                 ..
gi 148535224 156 GD 157
Cdd:cd16316  199 KD 200
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 1-160 2.38e-38

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 130.34  E-value: 2.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWfVERGYKIKG--SISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGK------------ 66
Cdd:cd16286   41 IVDSPYTNLATQTVLDW-IAKTMGPRKvvAINTHFHLDGTGGNEALKKRGIPTWGSDLTKQLLLERGKadrikaaeflkn 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  67 ------------VQAKNSF---SGASYWLVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPY-GLGNLGDANLEA 130
Cdd:cd16286  120 edlkrriessppVPPDNVFdlkEGKVFSFGNELVEVSFPGPAHAPDNVVVYFPERKILFGGCMIKPGkELGNLGDANMKA 199

                        170       180       190
                 ....*....|....*....|....*....|
gi 148535224 131 WPKSAKLLvsKYGKAKLVVPSHSEVGDASL 160
Cdd:cd16286  200 WPDSVRRL--KKFDAKIVIPGHGERGDPGM 227
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 1-154 1.05e-33

Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Chryseobacterium indologenes IND-1, IND-2, and IND-7 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293875  Cd Length: 215  Bit Score: 117.81  E-value: 1.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGY-KIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSF-SGASY 78
Cdd:cd16317   41 LFDVPWQKVQYQSLMDTIQKRHHlPVIAVFATHSHDDRAGDLSFYNNKGIKTYATAKTNEFLKKDGKATSTEIIkTGKPY 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148535224  79 WLVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPYG---LGNLGDANLEAWPKSAKLLVSKYGKAKLVVPSHSE 154
Cdd:cd16317  121 RIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSNSatdLGYTGEANVEQWPKTMNKLKAKYAQATLIIPGHDE 199
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 1-152 3.10e-22

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 87.22  E-value: 3.10e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224     1 LIDTPFtaKDTEKLVTWFVERGY-KIKGSISSHFHSDSTGGIEWLNSQS-IPTYASELTNELLKKDGKVQAKNSFSGASY 78
Cdd:smart00849  13 LIDTGP--GEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPgAPVYAPEGTAELLKDLLALLGELGAEAEPA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224    79 WLVK------------KKIEIFYPgPGHTPDNVVVWLPEHRVLFGGCFVKPYGLGNL----GDANLEAWPKSAKLLVSKy 142
Cdd:smart00849  91 PPDRtlkdgdeldlggGELEVIHT-PGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTlvdgGDAAASDALESLLKLLKL- 168

                          170
                   ....*....|
gi 148535224   143 gKAKLVVPSH 152
Cdd:smart00849 169 -LPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 1-158 1.50e-21

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 86.28  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSQS-IPTYASELTNELLKKDGK--------VQAKN 71
Cdd:COG0491   28 LIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgAPVYAHAAEAEALEAPAAgalfgrepVPPDR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  72 SFS-GASYWLVKKKIEIFYpGPGHTPDNVVVWLPEHRVLFGGCFVKPYGLGN--LGDANLEAWPKSAKLLVSKygKAKLV 148
Cdd:COG0491  108 TLEdGDTLELGGPGLEVIH-TPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRpdLPDGDLAQWLASLERLLAL--PPDLV 184

                        170
                 ....*....|
gi 148535224 149 VPSHSEVGDA 158
Cdd:COG0491  185 IPGHGPPTTA 194
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 1-158 3.18e-19

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 80.30  E-value: 3.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKL------VT----WFVergykikgsISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAK 70
Cdd:cd16282   28 VIDTGASPRLARALlaairkVTdkpvRYV---------VNTHYHGDHTLGNAAFADAGAPIIAHENTREELAARGEAYLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  71 NSFSGASYWLV--------------------KKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPYGLGNLGDANLEA 130
Cdd:cd16282   99 LMRRLGGDAMAgtelvlpdrtfddgltldlgGRTVELIHLGPAHTPGDLVVWLPEEGVLFAGDLVFNGRIPFLPDGSLAG 178

                        170       180
                 ....*....|....*....|....*...
gi 148535224 131 WPKSAKLLVSKygKAKLVVPSHSEVGDA 158
Cdd:cd16282  179 WIAALDRLLAL--DATVVVPGHGPVGDK 204
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 4-152 1.55e-16

Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293864  Cd Length: 222  Bit Score: 73.44  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   4 TPFTAKDTEKLVTWFVERgyKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGK----------------- 66
Cdd:cd16306   40 TPDTARELHKLIKRVSRK--PVLEVINTNYHTDRAGGNAYWKSIGAKVVSTRQTRDLMKSDWAeivaftrkglpeypdlp 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  67 -VQAKNSFSGaSYWLVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPyGLGNLGDANLEAWPKSAKLLVSKYGKA 145
Cdd:cd16306  118 lVLPNVVHDG-DFTLQEGKVRAFYLGPAHTPDGIFVYFPDEQVLYGNCILKE-KLGNLSFADVKAYPQTLERLKAMKLPI 195


                 ....*..
gi 148535224 146 KLVVPSH 152
Cdd:cd16306  196 KTVIGGH 202
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 4-156 4.69e-16

metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293845  Cd Length: 226  Bit Score: 72.08  E-value: 4.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   4 TPFTAKDTEKLVTWFVERgyKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKD-GKVQA------------- 69
Cdd:cd16287   40 TPETAETLYKEIRKVSPL--PINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQKSQwGSIVNftrqgnnkypnle 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  70 ---KNSFSGASYWLVKKKIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPyGLGNLGDANLEAWPKSAKLLvsKYGKAK 146
Cdd:cd16287  118 kslPDTVFPGDFNLQNGSIRAMYLGEAHTKDGIFVYFPAERVLYGNCILKE-NLGNMSFANRTEYPKTLEKL--KGLIEQ 194

                        170
                 ....*....|
gi 148535224 147 LVVPSHSEVG 156
Cdd:cd16287  195 GELKVDSIIA 204
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 1-152 9.43e-14

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 65.38  E-value: 9.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKdtEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSQS-IPTYASELTNELLKKDgkvqAKNSFSGASYW 79
Cdd:cd06262   24 LIDPGAGAL--EKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPgAPVYIHEADAELLEDP----ELNLAFFGGGP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  80 LVKKKIEIFYPG----------------PGHTPDNVVVWLPEHRVLFGGCFVKPYGLGN--LGDANLEAWPKSAKLLVSK 141
Cdd:cd06262   98 LPPPEPDILLEDgdtielgglelevihtPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRtdLPGGDPEQLIESIKKLLLL 177

                        170
                 ....*....|.
gi 148535224 142 YGKAKLVVPSH 152
Cdd:cd06262  178 LPDDTVVYPGH 188
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 4-151 6.41e-12

Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293863  Cd Length: 226  Bit Score: 61.17  E-value: 6.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   4 TPFTAKDTEKLVTWFveRGYKIKGSISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGKVQAKNSFSGASYWLVKK 83
Cdd:cd16305   40 TPETAETLEKEIRKV--SPLPIKEVINTNYHTDRAGGNAYWKTLGASIVSTQMTYDLEKSQWGSIVDFTRQGNNKYPNLE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  84 K-----------------IEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVKPyGLGNLGDANLEAWPKSAKLLVSKYGKAK 146
Cdd:cd16305  118 KslpdtvypgdfnlqngsVRALYLGEAHTEDGIFVYFPAERVLYGNCILKE-KLGNMSFANRTEYPKTLKKLKGLIEQGE 196


                 ....*
gi 148535224 147 LVVPS 151
Cdd:cd16305  197 LKVES 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
1-152 2.32e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 56.61  E-value: 2.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224    1 LIDT-PFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWL-NSQSIPTYASELTNELLKKDGKVQAKNSFSGASY 78
Cdd:pfam00753  19 LIDTgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaEATDVPVIVVAEEARELLDEELGLAASRLGLPGP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   79 WLVKKKIEI----------------FYPGPGHTPDNVVVWLPEHRVLFGGCFVKPYGLGNLGDANLEAWP------KSAK 136
Cdd:pfam00753  99 PVVPLPPDVvleegdgilggglgllVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGGLLVlhpssaESSL 178

                         170
                  ....*....|....*...
gi 148535224  137 LLVSKYG--KAKLVVPSH 152
Cdd:pfam00753 179 ESLLKLAklKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-110 2.91e-10

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 56.05  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  29 ISSHFHSDSTGGIEWLNSQSIPTYASELTNELLKKDGK---VQAKNSFSGA-SYWLVKKKIEIFYPGPGHTPDNVVVWLP 104
Cdd:cd16276   50 VYSHNHADHIGGASIFKDEGATIIAHEATAELLKRNPDpkrPVPTVTFDDEyTLEVGGQTLELSYFGPNHGPGNIVIYLP 129


                 ....*.
gi 148535224 105 EHRVLF 110
Cdd:cd16276  130 KQKVLM 135
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 1-152 3.95e-07

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 47.50  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSQ--SIPTYASELTNELLKK--DGKVQAKNSFSGA 76
Cdd:cd07739   29 LVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAfpDAKVVATPAVVAHIKAqlEPKLAFWGPLLGG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  77 SywLVKK-----------------KIEIFYPGPGHTPDNVVVWLPEHRVLFGGCFVkpYG------LGNLGDANLEAWPK 133
Cdd:cd07739  109 N--APARlvvpepldgdtltleghPLEIVGVGGGDTDDTTYLWIPSLKTVVAGDVV--YNgvhvwlADATTPELRAAWLA 184

                        170       180
                 ....*....|....*....|...
gi 148535224 134 S----AKLlvskygKAKLVVPSH 152
Cdd:cd07739  185 AldkiEAL------NPETVVPGH 201
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 1-152 2.05e-06

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 45.68  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDT--PFTAKDTEKLVTwfvERGYK---IKGSISSHFHSDSTGGIEWLNSQS-IPTYASELTNELL--KKDGKVQAKNS 72
Cdd:cd07721   24 LIDTglPGSAKRILKALR---ELGLSpkdIRRILLTHGHIDHIGSLAALKEAPgAPVYAHEREAPYLegEKPYPPPVRLG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  73 FSGASYWLVKKKI-----------EIFYPG-------PGHTPDNVVVWLPEHRVLFGGCFVKPYGLGNLG-----DANLE 129
Cdd:cd07721  101 LLGLLSPLLPVKPvpvdrtledgdTLDLAGglrvihtPGHTPGHISLYLEEDGVLIAGDALVTVGGELVPppppfTWDME 180

                        170       180
                 ....*....|....*....|...
gi 148535224 130 AWPKSAKLLVSKygKAKLVVPSH 152
Cdd:cd07721  181 EALESLRKLAEL--DPEVLAPGH 201
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 1-153 5.58e-06

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 44.41  E-value: 5.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVE-RGYK-IKGSISSHFHSDSTGGIEWL----NSQSIPTYASELTNE--------------- 59
Cdd:cd07710   31 IIDTLESAEAAKAALELFRKhTGDKpVKAIIYTHSHPDHFGGAGGFveeeDSGKVPIIAPEGFMEeavsenvlagnamsr 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  60 --------LLKKDGKVQ-----AKNSFSGASYWL--------VKKKIEI------FYPGPGHTPDNVVVWLPEHRVLFGG 112
Cdd:cd07710  111 raayqfgaLLPKGEKGQvgaglGPGLSTGTVGFIpptititeTGETLTIdgveleFQHAPGEAPDEMMVWLPDYKVLFCA 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148535224 113 -----CFvkPyglgNL----G----DANleAWPKSAKLLVSKygKAKLVVPSHS 153
Cdd:cd07710  191 dnvyhTF--P----NLytlrGakyrDAL--AWAKSLDEAISL--KAEVLFPSHT 234
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 16-63 2.10e-04

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 40.08  E-value: 2.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 148535224  16 TWFVERGYKIKGSISSHFHSDSTGGIEWLNSQ-SIPTYASELTNELLKK 63
Cdd:cd07714   47 SYLEENKDKIKGIFITHGHEDHIGALPYLLPElNVPIYATPLTLALIKK 95
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 1-112 3.36e-04

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 39.20  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDT-PFTAKDTEKLVTWFVERGYKIkGSIS----SHFHSDSTGGIEWLNSQSIPTYASELTNELlkKDGkvqakNSFSG 75
Cdd:cd07725   28 LIDTgLATEEDAEALWEGLKELGLKP-SDIDrvllTHHHPDHIGLAGKLQEKSGATVYILDVTPV--KDG-----DKIDL 99

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 148535224  76 ASYWLvkKKIEifypGPGHTPDNVVVWLPEHRVLFGG 112
Cdd:cd07725  100 GGLRL--KVIE----TPGHTPGHIVLYDEDRRELFVG 130
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 1-152 5.66e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 38.38  E-value: 5.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224   1 LIDTPFTAKDTEKLVTWFVERGYKIkgsISSHFHSDSTGGIE-----WLNSQSIPTYASELTNELLKKDGKvQAKNSFSG 75
Cdd:cd07712   22 LIDTGLGIGDLKEYVRTLTDLPLLV---VATHGHFDHIGGLHefeevYVHPADAEILAAPDNFETLTWDAA-TYSVPPAG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  76 ASYWLV--------KKKIEIFYPgPGHTPDNVVVWLPEHRVLFGGCFVkpyGLGNL----GDANLEAWPKSAKLLVSKYG 143
Cdd:cd07712   98 PTLPLRdgdvidlgDRQLEVIHT-PGHTPGSIALLDRANRLLFSGDVV---YDGPLimdlPHSDLDDYLASLEKLSKLPD 173


                 ....*....
gi 148535224 144 KAKLVVPSH 152
Cdd:cd07712  174 EFDKVLPGH 182
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 10-113 5.81e-04

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 38.21  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  10 DTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWL--NSQSIPTYASeltnellkKDGKVQAKNSF--SGASYWLVKKKI 85
Cdd:cd07723   29 EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELkaLFPDAPVYGP--------AEDRIPGLDHPvkDGDEIKLGGLEV 100

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 148535224  86 EIFYPgPGHTPDNVVVWLPEHRVLF-------GGC 113
Cdd:cd07723  101 KVLHT-PGHTLGHICYYVPDEPALFtgdtlfsGGC 134
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 24-152 2.72e-03

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 36.70  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  24 KIKGSISSHFHSDSTGGI-EWL--NSQsIPTYASELTNELLKKDGKVQAKNsfsgasYWLVKKKIEI--------FYPGP 92
Cdd:cd07709   68 KIDYIVVNHQEPDHSGSLpELLelAPN-AKIVCSKKAARFLKHFYPGIDER------FVVVKDGDTLdlgkhtlkFIPAP 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148535224  93 G-HTPDNVVVWLPEHRVLF----GGCFvkpYGLGNLGDANLEAWPKSAKL----LVSKYGKA-------------KLVVP 150
Cdd:cd07709  141 MlHWPDTMVTYDPEDKILFsgdaFGAH---GASGELFDDEVEDYLEEARRyyanIMGPFSKQvrkaleklealdiKMIAP 217


                 ..
gi 148535224 151 SH 152
Cdd:cd07709  218 SH 219
 
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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