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Conserved domains on  [gi|1568632074|ref|WP_129286796|]
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protocatechuate 3,4-dioxygenase subunit alpha [Streptomyces sp. GZWMJZ-114]

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, ...
5-185 6.62e-62

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 cd03463:

Pssm-ID: 473874  Cd Length: 185  Bit Score: 189.78  E-value: 6.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   5 HPTPSQTVGPFYGYALPF--PGGDDLAPGD--PRALTLHGTVRDGSGAPVPDALLEFWQAAPDNSRTGATGSMRRDPVDg 80
Cdd:cd03463     2 GETPSQTVGPYVHIGLPPtrEGGNDLVPPDtaGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPADSRRRLDPG- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  81 rvigrdgtrFTGFGRVPTDADGHYALRTLPP--------PPEAPYLGVLVLARGLLHHLHTRAYLPGHP---HDTLLAGL 149
Cdd:cd03463    81 ---------FRGFGRVATDADGRFSFTTVKPgavpgrdgAGQAPHINVWVFARGLLKHLFTRIYFPDEEanaADPVLALV 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1568632074 150 APQRRATLLAHEERAKLYRFDIRLQGDDteETVFLD 185
Cdd:cd03463   152 PEERRATLIAKREGDGAYRFDIRLQGEG--ETVFFD 185
 
Name Accession Description Interval E-value
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
5-185 6.62e-62

Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-subunit-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+.


Pssm-ID: 239546  Cd Length: 185  Bit Score: 189.78  E-value: 6.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   5 HPTPSQTVGPFYGYALPF--PGGDDLAPGD--PRALTLHGTVRDGSGAPVPDALLEFWQAAPDNSRTGATGSMRRDPVDg 80
Cdd:cd03463     2 GETPSQTVGPYVHIGLPPtrEGGNDLVPPDtaGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPADSRRRLDPG- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  81 rvigrdgtrFTGFGRVPTDADGHYALRTLPP--------PPEAPYLGVLVLARGLLHHLHTRAYLPGHP---HDTLLAGL 149
Cdd:cd03463    81 ---------FRGFGRVATDADGRFSFTTVKPgavpgrdgAGQAPHINVWVFARGLLKHLFTRIYFPDEEanaADPVLALV 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1568632074 150 APQRRATLLAHEERAKLYRFDIRLQGDDteETVFLD 185
Cdd:cd03463   152 PEERRATLIAKREGDGAYRFDIRLQGEG--ETVFFD 185
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
7-186 2.46e-48

protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of protocatechuate 3,4-dioxygenase. The most closely related family outside this family is that of the beta chain (TIGR02422), typically encoded in an adjacent locus. This enzyme acts in the degradation of aromatic compounds by way of p-hydroxybenzoate to succinate and acetyl-CoA. [Energy metabolism, Other]


Pssm-ID: 274126  Cd Length: 193  Bit Score: 155.61  E-value: 2.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   7 TPSQTVGPFYGYALPFPG--------GDDLAP--GDPRALTLHGTVRDGSGAPVPDALLEFWQAAPDNSRTGATGSMrrd 76
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPEQagtftqefGNNLVTpdADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLR--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  77 pvdgrvIGRDGTRFTGFGRVPTDADGHYALRTLPP--------PPEAPYLGVLVLARGLLHHLHTRAYLPG----HPHDT 144
Cdd:TIGR02423  78 ------APATDPGFRGWGRTGTDESGEFTFETVKPgavpdrdgVLQAPHINVSVFARGINRRLYTRLYFDDeaaaNASDP 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1568632074 145 LLAGLAPQRRATLLAHEERA--KLYRFDIRLQGDDteETVFLDF 186
Cdd:TIGR02423 152 VLALVPAERRATLIAKRERDgkVAYRFDIRLQGEG--ETVFFDV 193
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
6-177 4.65e-41

Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442708  Cd Length: 171  Bit Score: 136.49  E-value: 4.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   6 PTPSQTVGPFYGYALPFPGGDDLAPGDP-RALTLHGTVRDGSGAPVPDALLEFWQAAPdnsrtgatgsmrrdpvDGRVIG 84
Cdd:COG3485     1 ETPSQTEGPFYVDGLPLPLGADLARDAPgEPIRVTGRVLDGDGRPVAGALVEIWQADA----------------DGRYSH 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  85 RDGTR----FTGFGRVPTDADGHYALRTLPP--------PPEAPYLGVLVLARGlLHHLHTRAYLPGHPH---DTLLAgl 149
Cdd:COG3485    65 QDDGPldpnFNGRGRFTTDADGRYRFRTIKPgpypipnhPGRPAHIHFSVFAPG-FERLTTQLYFPGDPYnasDPVFG-- 141
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1568632074 150 apqRRATLLA---HEERAKLYRFDIRLQGDD 177
Cdd:COG3485   142 ---VRDTLIArfePEDGALVYRFDIVLQGPG 169
Dioxygenase_C pfam00775
Dioxygenase;
13-175 1.79e-09

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 54.40  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  13 GPFYGYALPFPGG-----DDLAPGDPraLTLHGTVRDGSGAPVPDALLEFWQAapdnsRTGATGSMRRDpvdgrvigRDG 87
Cdd:pfam00775   3 GPLYVEGAPSDEDlarmdDGDPIGEP--LILSGRVFDAAGKPLAGALVEIWHA-----NDEGRYSHFDP--------TEA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  88 TRFTGFGRVPTDADGHYALRTLPP-----PPEAPyLGVLVLARGL-------LH---------HLHTRAYLPGHPH--DT 144
Cdd:pfam00775  68 PEPNFRGRILTDSQGSYRFRTIQPapypiPNDGP-TGKLLDALGRhawrpahIHffisapghrRLTTQLYFEGDPYlpDD 146
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1568632074 145 LLAGLAPQRRATLLAHE----ERAKLYRFDIRLQG 175
Cdd:pfam00775 147 IAYAVRQGLVANYDEREdgtpEKFLEYHFDFVLDG 181
 
Name Accession Description Interval E-value
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
5-185 6.62e-62

Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-subunit-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+.


Pssm-ID: 239546  Cd Length: 185  Bit Score: 189.78  E-value: 6.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   5 HPTPSQTVGPFYGYALPF--PGGDDLAPGD--PRALTLHGTVRDGSGAPVPDALLEFWQAAPDNSRTGATGSMRRDPVDg 80
Cdd:cd03463     2 GETPSQTVGPYVHIGLPPtrEGGNDLVPPDtaGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPADSRRRLDPG- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  81 rvigrdgtrFTGFGRVPTDADGHYALRTLPP--------PPEAPYLGVLVLARGLLHHLHTRAYLPGHP---HDTLLAGL 149
Cdd:cd03463    81 ---------FRGFGRVATDADGRFSFTTVKPgavpgrdgAGQAPHINVWVFARGLLKHLFTRIYFPDEEanaADPVLALV 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1568632074 150 APQRRATLLAHEERAKLYRFDIRLQGDDteETVFLD 185
Cdd:cd03463   152 PEERRATLIAKREGDGAYRFDIRLQGEG--ETVFFD 185
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
7-186 2.46e-48

protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of protocatechuate 3,4-dioxygenase. The most closely related family outside this family is that of the beta chain (TIGR02422), typically encoded in an adjacent locus. This enzyme acts in the degradation of aromatic compounds by way of p-hydroxybenzoate to succinate and acetyl-CoA. [Energy metabolism, Other]


Pssm-ID: 274126  Cd Length: 193  Bit Score: 155.61  E-value: 2.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   7 TPSQTVGPFYGYALPFPG--------GDDLAP--GDPRALTLHGTVRDGSGAPVPDALLEFWQAAPDNSRTGATGSMrrd 76
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPEQagtftqefGNNLVTpdADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLR--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  77 pvdgrvIGRDGTRFTGFGRVPTDADGHYALRTLPP--------PPEAPYLGVLVLARGLLHHLHTRAYLPG----HPHDT 144
Cdd:TIGR02423  78 ------APATDPGFRGWGRTGTDESGEFTFETVKPgavpdrdgVLQAPHINVSVFARGINRRLYTRLYFDDeaaaNASDP 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1568632074 145 LLAGLAPQRRATLLAHEERA--KLYRFDIRLQGDDteETVFLDF 186
Cdd:TIGR02423 152 VLALVPAERRATLIAKRERDgkVAYRFDIRLQGEG--ETVFFDV 193
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
6-177 4.65e-41

Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442708  Cd Length: 171  Bit Score: 136.49  E-value: 4.65e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   6 PTPSQTVGPFYGYALPFPGGDDLAPGDP-RALTLHGTVRDGSGAPVPDALLEFWQAAPdnsrtgatgsmrrdpvDGRVIG 84
Cdd:COG3485     1 ETPSQTEGPFYVDGLPLPLGADLARDAPgEPIRVTGRVLDGDGRPVAGALVEIWQADA----------------DGRYSH 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  85 RDGTR----FTGFGRVPTDADGHYALRTLPP--------PPEAPYLGVLVLARGlLHHLHTRAYLPGHPH---DTLLAgl 149
Cdd:COG3485    65 QDDGPldpnFNGRGRFTTDADGRYRFRTIKPgpypipnhPGRPAHIHFSVFAPG-FERLTTQLYFPGDPYnasDPVFG-- 141
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1568632074 150 apqRRATLLA---HEERAKLYRFDIRLQGDD 177
Cdd:COG3485   142 ---VRDTLIArfePEDGALVYRFDIVLQGPG 169
3,4-PCD cd03459
Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3, ...
26-173 1.47e-37

Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+.


Pssm-ID: 239542 [Multi-domain]  Cd Length: 158  Bit Score: 127.00  E-value: 1.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  26 DDLAPGDPRALTLHGTVRDGSGAPVPDALLEFWQAAPDNSRTGATGSMRrdpvdgrviGRDGTRFTGFGRVPTDADGHYA 105
Cdd:cd03459     6 KGGGEAIGERIILEGRVLDGDGRPVPDALVEIWQADAAGRYRHPRDSHR---------APLDPNFTGFGRVLTDADGRYR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074 106 LRTLPPPP--------EAPYLGVLVLARGLLHHLHTRAYLPGHP---HDTLLAGLAPQRRATLLA---HEERAKLYRFDI 171
Cdd:cd03459    77 FRTIKPGAypwrngawRAPHIHVSVFARGLLERLVTRLYFPGDPanaADPVLASVPEERRETLIArrdGSDGALAYRFDI 156

                  ..
gi 1568632074 172 RL 173
Cdd:cd03459   157 VL 158
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
29-173 2.48e-28

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: 103.09  E-value: 2.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  29 APGDPraLTLHGTVRDGSGAPVPDALLEFWQAAPDNSRTGATGSMRRDpvdgrvigrdgtRFTGFGRVPTDADGHYALRT 108
Cdd:cd00421     7 APGEP--LTLTGTVLDGDGCPVPDALVEIWQADADGRYSGQDDSGLDP------------EFFLRGRQITDADGRYRFRT 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1568632074 109 LPPPP----EAPYLGVLVLARGLLHHLHTRAYLPGHP---HDTLLAGLAPQRRATLLAHEER--AKLYRFDIRL 173
Cdd:cd00421    73 IKPGPypigRPPHIHFKVFAPGYNRRLTTQLYFPGDPlndSDPVFAPYSENVRPTLIADFDGieFLEYRFDIVL 146
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
1-177 1.39e-15

protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of protocatechuate 3,4-dioxygenase. The most closely related family outside this family is that of the alpha chain (TIGR02423), typically encoded in an adjacent locus. This enzyme acts in the degradation of aromatic compounds by way of p-hydroxybenzoate to succinate and acetyl-CoA. [Energy metabolism, Other]


Pssm-ID: 131475 [Multi-domain]  Cd Length: 220  Bit Score: 71.61  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   1 MTPPHPTPSQTVGPFYGYALPFPGGDDL---APGDP--RALTLHGTVRDGSGAPVPDALLEFWQAapdNSrtgatGSMRR 75
Cdd:TIGR02422  21 LISIPQSLSELTGPVFGHDDLGPIDNDLtlaHGGEPigERIIVHGRVLDEDGRPVPNTLVEVWQA---NA-----AGRYR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  76 DPVDGRVIGRDgTRFTGFGRVPTDADGHYALRTLPPPP----------EAPYLGVLVLARGLLHHLHTRAYLPGHP---H 142
Cdd:TIGR02422  93 HKNDQYLAPLD-PNFGGVGRTLTDSDGYYRFRTIKPGPypwgnhhnawRPAHIHFSLFGTSFAQRLITQMYFEGDPliaY 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1568632074 143 DTLLAGLA-PQRRATLLAH-------EERAKLYRFDIRLQGDD 177
Cdd:TIGR02422 172 DPIVNSIPdEAARERLIATldldntiPMDALGYRFDIVLRGRR 214
3,4-PCD_beta cd03464
Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring ...
7-177 1.26e-14

Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-subunit-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+.


Pssm-ID: 239547  Cd Length: 220  Bit Score: 68.88  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   7 TPSQTVGPFYGYALPFPGGDDL---APGDPRA--LTLHGTVRDGSGAPVPDALLEFWQAapdnsrtGATGSMR--RD--- 76
Cdd:cd03464    32 TLSELTGPVFGHDDLGPLDNDLtrnHNGEPIGerIIVHGRVLDEDGRPVPNTLVEIWQA-------NAAGRYRhkRDqhd 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  77 -PVDgrvigrdgTRFTGFGRVPTDADGHYALRTLPPPP----------EAPYLGVLVLARGLLHHLHTRAYLPGHP---H 142
Cdd:cd03464   105 aPLD--------PNFGGAGRTLTDDDGYYRFRTIKPGAypwgnhpnawRPAHIHFSLFGPSFATRLVTQMYFPGDPlipH 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1568632074 143 DTLLAGLAP--QRRATL------LAHEERAKLYRFDIRLQGDD 177
Cdd:cd03464   177 DPIYNSIPDeaARQRLIarfdlsATQPEWALGYRFDIVLRGRR 219
Catechol_intradiol_dioxygenases cd03458
Catechol intradiol dioxygenases can be divided into several subgroups according to their ...
2-142 1.24e-11

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: 61.42  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   2 TPPHPTPSQTVGPFYGYALPF-PGGDDLAPGDPRALTL--HGTVRDGSGAPVPDALLEFWQAAPdnsrtgatgsmrrdpv 78
Cdd:cd03458    68 KDTGGTESTILGPFYVAGAPEvDNGATIDDDTADGEPLfvHGTVTDTDGKPLAGATVDVWHADP---------------- 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1568632074  79 DGR--VIGRDGTRFTGFGRVPTDADGHYALRTLPP-----PPEAPylgvlvlARGLLHHLHTRAYLPGHPH 142
Cdd:cd03458   132 DGFysQQDPDQPEFNLRGKFRTDEDGRYRFRTIRPvpypiPPDGP-------TGELLEALGRHPWRPAHIH 195
1,2-HQD cd03461
Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2, ...
2-142 5.40e-11

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: 59.94  E-value: 5.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   2 TPPHPTPSQTVGPFYGYALPF-PGGDDLAPGDPRALTL-HGTVRDGSGAPVPDALLEFWQAAPDNSRTGatgsmrRDPvd 79
Cdd:cd03461    85 KPSGATESTVLGPFYREDAPEyENGASIVQGADGEPCFvHGRVTDTDGKPLPGATVDVWQADPNGLYDV------QDP-- 156
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1568632074  80 grvigrDGTRFTGFGRVPTDADGHYALRTLPPPPEA-PYLGVlvlARGLLHHLHTRAYLPGHPH 142
Cdd:cd03461   157 ------DQPEFNLRGKFRTDEDGRYAFRTLRPTPYPiPTDGP---VGKLLKAMGRHPMRPAHIH 211
1,2-CTD cd03460
Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to ...
6-144 1.14e-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: 56.22  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074   6 PTPSQTVGPFYGYALPFPGG----DDLAPGDPRALTLHGTVRDGSGAPVPDALLEFWQAapdNSRTGATgsmRRDPvdgr 81
Cdd:cd03460    91 GTPRTIEGPLYVAGAPESDGfarlDDGSDDDGETLVMHGTVTDTDGKPVPGAKVEVWHA---NSKGFYS---HFDP---- 160
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1568632074  82 vigrDGTRFTGFGRVPTDADGHYALRTLPP-----PPEAPYLGVL-VLARgllH-----HLHTRAYLPGHPHDT 144
Cdd:cd03460   161 ----TQSPFNLRRSIITDADGRYRFRSIMPsgygvPPGGPTQQLLnALGR---HgnrpaHIHFFVSAPGHRKLT 227
Dioxygenase_C pfam00775
Dioxygenase;
13-175 1.79e-09

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 54.40  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  13 GPFYGYALPFPGG-----DDLAPGDPraLTLHGTVRDGSGAPVPDALLEFWQAapdnsRTGATGSMRRDpvdgrvigRDG 87
Cdd:pfam00775   3 GPLYVEGAPSDEDlarmdDGDPIGEP--LILSGRVFDAAGKPLAGALVEIWHA-----NDEGRYSHFDP--------TEA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  88 TRFTGFGRVPTDADGHYALRTLPP-----PPEAPyLGVLVLARGL-------LH---------HLHTRAYLPGHPH--DT 144
Cdd:pfam00775  68 PEPNFRGRILTDSQGSYRFRTIQPapypiPNDGP-TGKLLDALGRhawrpahIHffisapghrRLTTQLYFEGDPYlpDD 146
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1568632074 145 LLAGLAPQRRATLLAHE----ERAKLYRFDIRLQG 175
Cdd:pfam00775 147 IAYAVRQGLVANYDEREdgtpEKFLEYHFDFVLDG 181
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
13-142 1.90e-09

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: 55.04  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  13 GPFYGYALPFPGG-----DDlAPGDPraLTLHGTVRDGSGAPVPDALLEFWQAAPDNSRTGATGSMRRDPVDGRVIgrdg 87
Cdd:cd03462    75 GPYFIENAPFVDGklktyDD-DDHKP--LLFRGTVKDLAGAPVAGAVIDVWHSTPDGKYSGFHPNIPEDYYRGKIR---- 147
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1568632074  88 trftgfgrvpTDADGHYALRT-LPPPPEAPYLGvlvlARG-LLHHLHTRAYLPGHPH 142
Cdd:cd03462   148 ----------TDEDGRYEVRTtVPVPYQIPNDG----PTGaLLEAMGGHSWRPAHVH 190
intradiol_dioxygenase_like cd03457
Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage ...
10-108 6.87e-05

Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. They 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+. The family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases. The specific function of this subgroup is unknown.


Pssm-ID: 239540  Cd Length: 188  Bit Score: 41.48  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1568632074  10 QTVGPFY-GYALPFPGGDDLAPGDPraLTLHGTVRD-GSGAPVPDALLEFWQAapdnsrtGATG--SMRRDPVDGRVIGR 85
Cdd:cd03457     2 VTEGPYYvDGELVRSDITEGQPGVP--LTLDLQVVDvATCCPPPNAAVDIWHC-------DATGvySGYSAGGGGGEDTD 72
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1568632074  86 DGT--RftgfGRVPTDADG----------HYALRT 108
Cdd:cd03457    73 DETflR----GVQPTDADGvvtfttifpgWYPGRA 103
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
37-111 2.47e-04

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 38.41  E-value: 2.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1568632074  37 TLHGTVRDGSGAPVPDALLEFwqaapdnsRTGATGSMRrdpvdgrvigrdgtrftgfgRVPTDADGHYALRTLPP 111
Cdd:pfam13620   1 TISGTVTDPSGAPVPGATVTV--------TNTDTGTVR--------------------TTTTDADGRYRFPGLPP 47
 
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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