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Conserved domains on  [gi|3219706|gb|AAC23508|]
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dichloro-catechol 1,2-dioxygenase, partial [Burkholderia cepacia]

Protein Classification

peptidase associated/transthyretin-like domain-containing protein( domain architecture ID 229422)

peptidase associated/transthyretin-like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_M14NE-CP-C_like super family cl21470
Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, ...
1-78 2.27e-38

Peptidase associated domain: C-terminal domain of M14 N/E carboxypeptidase; putative folding, regulation, or interaction domain; This domain is found C-terminal to the M14 carboxypeptidase (CP) N/E subfamily containing zinc-binding enzymes that hydrolyze single C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes enzymatically active members (carboxypeptidase N, E, M, D, and Z), as well as non-active members (carboxypeptidase-like protein 1, -2, aortic CP-like protein, and adipocyte enhancer binding protein-1) which lack the critical active site and substrate-binding residues considered necessary for activity. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation. For M14 CPs, it has been suggested that this domain may assist in folding of the CP domain, regulate enzyme activity, or be involved in interactions with other proteins or with membranes; for carboxypeptidase M, it may interact with the bradykinin 1 receptor at the cell surface. This domain may also be found in other peptidase families.


The actual alignment was detected with superfamily member cd03462:

Pssm-ID: 473874 [Multi-domain]  Cd Length: 247  Bit Score: 127.45  E-value: 2.27e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219706    1 DGRYSGFggyHGDMPVEYYRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVHSKTRKDGSEPL 78
Cdd:cd03462 127 DGKYSGF---HPNIPEDYYRGKIRTDEDGRYEVRTTVPVPYQIPNDGPTGALLEAMGGHSWRPAHVHFKVRADGYETL 201
 
Name Accession Description Interval E-value
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
1-78 2.27e-38

chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol dioxygenases that degrade chlorocatechols via the addition of molecular oxygen and the subsequent cleavage between two adjacent hydroxyl groups. This reaction is part of the modified ortho-cleavage pathway which is a central oxidative bacterial pathway that channels chlorocatechols, derived from the degradation of chlorinated benzoic acids, phenoxyacetic acids, phenols, benzenes, and other aromatics into the energy-generating tricarboxylic acid pathway.


Pssm-ID: 239545 [Multi-domain]  Cd Length: 247  Bit Score: 127.45  E-value: 2.27e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219706    1 DGRYSGFggyHGDMPVEYYRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVHSKTRKDGSEPL 78
Cdd:cd03462 127 DGKYSGF---HPNIPEDYYRGKIRTDEDGRYEVRTTVPVPYQIPNDGPTGALLEAMGGHSWRPAHVHFKVRADGYETL 201
catachol_actin TIGR02438
catechol 1,2-dioxygenase, Actinobacterial; Members of this family are catechol 1, ...
1-78 2.34e-13

catechol 1,2-dioxygenase, Actinobacterial; Members of this family are catechol 1,2-dioxygenases of the Actinobacteria. They are more closely related to actinobacterial chlorocatechol 1,2-dioxygenases than to proteobacterial catechol 1,2-dioxygenases, and so are built in this separate model. The member from Rhodococcus rhodochrous NCIMB 13259 (GB|AAC33003.1) is described as a homodimer with bound Fe, similarly active on catechol, 3-methylcatechol and 4-methylcatechol.


Pssm-ID: 274133 [Multi-domain]  Cd Length: 281  Bit Score: 62.49  E-value: 2.34e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219706      1 DGRYSGFGGyhgDMPVEYYRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVHSKTRKDGSEPL 78
Cdd:TIGR02438 160 DGFYSQFAP---GIPEWNLRGTIIADDEGRFEITTMQPAPYQIPTDGPTGKFIAAAGGHPWRPAHLHLKVSAPGHELI 234
Dioxygenase_C pfam00775
Dioxygenase;
2-67 3.27e-13

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 60.95  E-value: 3.27e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219706      2 GRYSGFGgyHGDMPVEYYRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVH 67
Cdd:pfam00775  57 GRYSHFD--PTEAPEPNFRGRILTDSQGSYRFRTIQPAPYPIPNDGPTGKLLDALGRHAWRPAHIH 120
 
Name Accession Description Interval E-value
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
1-78 2.27e-38

chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol dioxygenases that degrade chlorocatechols via the addition of molecular oxygen and the subsequent cleavage between two adjacent hydroxyl groups. This reaction is part of the modified ortho-cleavage pathway which is a central oxidative bacterial pathway that channels chlorocatechols, derived from the degradation of chlorinated benzoic acids, phenoxyacetic acids, phenols, benzenes, and other aromatics into the energy-generating tricarboxylic acid pathway.


Pssm-ID: 239545 [Multi-domain]  Cd Length: 247  Bit Score: 127.45  E-value: 2.27e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219706    1 DGRYSGFggyHGDMPVEYYRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVHSKTRKDGSEPL 78
Cdd:cd03462 127 DGKYSGF---HPNIPEDYYRGKIRTDEDGRYEVRTTVPVPYQIPNDGPTGALLEAMGGHSWRPAHVHFKVRADGYETL 201
Catechol_intradiol_dioxygenases cd03458
Catechol intradiol dioxygenases can be divided into several subgroups according to their ...
1-78 4.50e-27

Catechol intradiol dioxygenases can be divided into several subgroups according to their substrate specificity for catechol, chlorocatechols and hydroxyquinols. Almost all members of this family are homodimers containing one ferric ion (Fe3+) per monomer. They belong to the intradiol dioxygenase family, a family of mononuclear non-heme iron intradiol-cleaving enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings.


Pssm-ID: 239541 [Multi-domain]  Cd Length: 256  Bit Score: 98.40  E-value: 4.50e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219706    1 DGRYSGFggyHGDMPVEYYRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVHSKTRKDGSEPL 78
Cdd:cd03458 132 DGFYSQQ---DPDQPEFNLRGKFRTDEDGRYRFRTIRPVPYPIPPDGPTGELLEALGRHPWRPAHIHFMVSAPGYRTL 206
1,2-HQD cd03461
Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2, ...
19-78 1.25e-13

Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2,4-trihydroxybenzene), a intermediate in the degradation of a large variety of aromatic compounds including some polychloro- and nitroaromatic pollutants, to form 3-hydroxy-cis,cis-muconates. 1,2-HQD blongs to the aromatic dioxygenase family, a family of mononuclear non-heme intradiol-cleaving enzymes.


Pssm-ID: 239544 [Multi-domain]  Cd Length: 277  Bit Score: 63.02  E-value: 1.25e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3219706   19 YRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVHSKTRKDGSEPL 78
Cdd:cd03461 163 LRGKFRTDEDGRYAFRTLRPTPYPIPTDGPVGKLLKAMGRHPMRPAHIHFMVTAPGYRTL 222
catachol_actin TIGR02438
catechol 1,2-dioxygenase, Actinobacterial; Members of this family are catechol 1, ...
1-78 2.34e-13

catechol 1,2-dioxygenase, Actinobacterial; Members of this family are catechol 1,2-dioxygenases of the Actinobacteria. They are more closely related to actinobacterial chlorocatechol 1,2-dioxygenases than to proteobacterial catechol 1,2-dioxygenases, and so are built in this separate model. The member from Rhodococcus rhodochrous NCIMB 13259 (GB|AAC33003.1) is described as a homodimer with bound Fe, similarly active on catechol, 3-methylcatechol and 4-methylcatechol.


Pssm-ID: 274133 [Multi-domain]  Cd Length: 281  Bit Score: 62.49  E-value: 2.34e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3219706      1 DGRYSGFGGyhgDMPVEYYRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVHSKTRKDGSEPL 78
Cdd:TIGR02438 160 DGFYSQFAP---GIPEWNLRGTIIADDEGRFEITTMQPAPYQIPTDGPTGKFIAAAGGHPWRPAHLHLKVSAPGHELI 234
Dioxygenase_C pfam00775
Dioxygenase;
2-67 3.27e-13

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 60.95  E-value: 3.27e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3219706      2 GRYSGFGgyHGDMPVEYYRGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVH 67
Cdd:pfam00775  57 GRYSHFD--PTEAPEPNFRGRILTDSQGSYRFRTIQPAPYPIPNDGPTGKLLDALGRHAWRPAHIH 120
1,2-CTD cd03460
Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to ...
20-67 1.86e-09

Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to form cis,cis-muconate. 1,2-CTDs is homodimers with one catalytic non-heme ferric ion per monomer. They belong to the aromatic dioxygenase family, a family of mononuclear non-heme iron intradiol-cleaving enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings.


Pssm-ID: 239543 [Multi-domain]  Cd Length: 282  Bit Score: 51.60  E-value: 1.86e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 3219706   20 RGKVRTGAQGRWRVQTALPAPYQTPNKGPTGALPTMMGSHSWRPARVH 67
Cdd:cd03460 168 RRSIITDADGRYRFRSIMPSGYGVPPGGPTQQLLNALGRHGNRPAHIH 215
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
1-74 2.48e-08

Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. This family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases which are mononuclear non-heme iron enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings. The members are intradiol-cleaving enzymes which break the catechol C1-C2 bond and utilize Fe3+, as opposed to the extradiol-cleaving enzymes which break the C2-C3 or C1-C6 bond and utilize Fe2+ and Mn+. Catechol 1,2-dioxygenases are mostly homodimers with one catalytic ferric ion per monomer. Protocatechuate 3,4-dioxygenases form more diverse oligomers.


Pssm-ID: 238241  Cd Length: 146  Bit Score: 47.24  E-value: 2.48e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3219706    1 DGRYSGFGGYHGDmPVEYYRGKVRTGAQGRWRVQTALPAPYQTpnkgptgalptmmgshsWRPARVHSKTRKDG 74
Cdd:cd00421  39 DGRYSGQDDSGLD-PEFFLRGRQITDADGRYRFRTIKPGPYPI-----------------GRPPHIHFKVFAPG 94
 
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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