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Conserved domains on  [gi|3212784|pdb|3PCD|O]
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Chain O, Protocatechuate 3,4-dioxygenase

Protein Classification

protocatechuate 3,4-dioxygenase subunit beta( domain architecture ID 11494257)

protocatechuate 3,4-dioxygenase subunit beta, together with subunit alpha, forms an oligomeric enzyme that participates in the degradation of aromatic compounds, catalyzing the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
16-237 6.81e-152

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: 420.98  E-value: 6.81e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         16 HPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNfnNGGLPIGERIIVAGRVVDQYGKPVPNT 95
Cdd:TIGR02422   1 HPPALTPDYKTSVLRSPKNALISIPQSLSELTGPVFGHDDLGPIDNDLTLA--HGGEPIGERIIVHGRVLDEDGRPVPNT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         96 LVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNDWRPAHIHFGISGPSIATKLI 175
Cdd:TIGR02422  79 LVEVWQANAAGRYRHKNDQYLAPLDPNFGGVGRTLTDSDGYYRFRTIKPGPYPWGNHHNAWRPAHIHFSLFGTSFAQRLI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
3PCD_O        176 TQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFEN 237
Cdd:TIGR02422 159 TQMYFEGDPLIAYDPIVNSIPDEAARERLIATLDLDNTIPMDALGYRFDIVLRGRRATPFEN 220
 
Name Accession Description Interval E-value
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
16-237 6.81e-152

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: 420.98  E-value: 6.81e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         16 HPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNfnNGGLPIGERIIVAGRVVDQYGKPVPNT 95
Cdd:TIGR02422   1 HPPALTPDYKTSVLRSPKNALISIPQSLSELTGPVFGHDDLGPIDNDLTLA--HGGEPIGERIIVHGRVLDEDGRPVPNT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         96 LVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNDWRPAHIHFGISGPSIATKLI 175
Cdd:TIGR02422  79 LVEVWQANAAGRYRHKNDQYLAPLDPNFGGVGRTLTDSDGYYRFRTIKPGPYPWGNHHNAWRPAHIHFSLFGTSFAQRLI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
3PCD_O        176 TQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFEN 237
Cdd:TIGR02422 159 TQMYFEGDPLIAYDPIVNSIPDEAARERLIATLDLDNTIPMDALGYRFDIVLRGRRATPFEN 220
3,4-PCD_beta cd03464
Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring ...
11-232 8.50e-145

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: 403.23  E-value: 8.50e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       11 RDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNFNngGLPIGERIIVAGRVVDQYGK 90
Cdd:cd03464   1 RDTEAHPPALTPDYKSSVLRSPKQPLISIPHTLSELTGPVFGHDDLGPLDNDLTRNHN--GEPIGERIIVHGRVLDEDGR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       91 PVPNTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNDWRPAHIHFGISGPSI 170
Cdd:cd03464  79 PVPNTLVEIWQANAAGRYRHKRDQHDAPLDPNFGGAGRTLTDDDGYYRFRTIKPGAYPWGNHPNAWRPAHIHFSLFGPSF 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3PCD_O      171 ATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRK 232
Cdd:cd03464 159 ATRLVTQMYFPGDPLIPHDPIYNSIPDEAARQRLIARFDLSATQPEWALGYRFDIVLRGRRA 220
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
8-237 1.58e-93

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


Pssm-ID: 226016 [Multi-domain]  Cd Length: 226  Bit Score: 273.52  E-value: 1.58e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O        8 FVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNFNNGGlpigERIIVAGRVVDQ 87
Cdd:COG3485   7 FLTRDGAIPAPGVQPAYLSSLKETPSQTLGPYVHIGLETEGTVFGPYYLNDAPNDLLTNDKARG----ERILLEGRVLDG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       88 YGKPVPNTLVEMWQANAGGRYRHKNDRYLAPlDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNDWRPAHIHFGISG 167
Cdd:COG3485  83 NGRPVPDALVEIWQADADGRYSHPKDSRLAP-LPNFNGRGRTITDEDGEYRFRTIKPGPYPWRNGGPMWRPAHIHFSVFA 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O      168 PSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDmnnanpMDCLAYRFDIVLRGQRKTHFEN 237
Cdd:COG3485 162 RGINTRLVTQLYFPDDPANARDPILALVPDEDRIQTLIAQLD------DDALAYRFDIVLQGRNETVFFD 225
Dioxygenase_C pfam00775
Dioxygenase;
47-229 2.33e-74

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 223.51  E-value: 2.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         47 TGPNFSHLGfgAHDHDLLLNFNngGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRyLAPlDPNFGgv 126
Cdd:pfam00775   2 EGPLYVEGA--PSDEDLARMDD--GDPIGEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDPT-EAP-EPNFR-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O        127 GRCLTDSDGYYSFRTIKPGPHPWRN-----------GPNDWRPAHIHFGISGPSIaTKLITQLYFEGDPLIPmCPIVKSi 195
Cdd:pfam00775  74 GRILTDSQGSYRFRTIQPAPYPIPNdgptgklldalGRHAWRPAHIHFFISAPGH-RRLTTQLYFEGDPYLP-DDIAYA- 150
                         170       180       190
                  ....*....|....*....|....*....|....*
3PCD_O        196 anpeAVQQLIAKLDMNNAN-PMDCLAYRFDIVLRG 229
Cdd:pfam00775 151 ----VRQGLVANYDEREDGtPEKFLEYHFDFVLDG 181
 
Name Accession Description Interval E-value
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
16-237 6.81e-152

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: 420.98  E-value: 6.81e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         16 HPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNfnNGGLPIGERIIVAGRVVDQYGKPVPNT 95
Cdd:TIGR02422   1 HPPALTPDYKTSVLRSPKNALISIPQSLSELTGPVFGHDDLGPIDNDLTLA--HGGEPIGERIIVHGRVLDEDGRPVPNT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         96 LVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNDWRPAHIHFGISGPSIATKLI 175
Cdd:TIGR02422  79 LVEVWQANAAGRYRHKNDQYLAPLDPNFGGVGRTLTDSDGYYRFRTIKPGPYPWGNHHNAWRPAHIHFSLFGTSFAQRLI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
3PCD_O        176 TQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFEN 237
Cdd:TIGR02422 159 TQMYFEGDPLIAYDPIVNSIPDEAARERLIATLDLDNTIPMDALGYRFDIVLRGRRATPFEN 220
3,4-PCD_beta cd03464
Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring ...
11-232 8.50e-145

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: 403.23  E-value: 8.50e-145
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       11 RDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNFNngGLPIGERIIVAGRVVDQYGK 90
Cdd:cd03464   1 RDTEAHPPALTPDYKSSVLRSPKQPLISIPHTLSELTGPVFGHDDLGPLDNDLTRNHN--GEPIGERIIVHGRVLDEDGR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       91 PVPNTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNDWRPAHIHFGISGPSI 170
Cdd:cd03464  79 PVPNTLVEIWQANAAGRYRHKRDQHDAPLDPNFGGAGRTLTDDDGYYRFRTIKPGAYPWGNHPNAWRPAHIHFSLFGPSF 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3PCD_O      171 ATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRK 232
Cdd:cd03464 159 ATRLVTQMYFPGDPLIPHDPIYNSIPDEAARQRLIARFDLSATQPEWALGYRFDIVLRGRRA 220
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
8-237 1.58e-93

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


Pssm-ID: 226016 [Multi-domain]  Cd Length: 226  Bit Score: 273.52  E-value: 1.58e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O        8 FVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNFNNGGlpigERIIVAGRVVDQ 87
Cdd:COG3485   7 FLTRDGAIPAPGVQPAYLSSLKETPSQTLGPYVHIGLETEGTVFGPYYLNDAPNDLLTNDKARG----ERILLEGRVLDG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       88 YGKPVPNTLVEMWQANAGGRYRHKNDRYLAPlDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNDWRPAHIHFGISG 167
Cdd:COG3485  83 NGRPVPDALVEIWQADADGRYSHPKDSRLAP-LPNFNGRGRTITDEDGEYRFRTIKPGPYPWRNGGPMWRPAHIHFSVFA 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O      168 PSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDmnnanpMDCLAYRFDIVLRGQRKTHFEN 237
Cdd:COG3485 162 RGINTRLVTQLYFPDDPANARDPILALVPDEDRIQTLIAQLD------DDALAYRFDIVLQGRNETVFFD 225
3,4-PCD cd03459
Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3, ...
61-227 1.61e-76

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: 227.92  E-value: 1.61e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       61 HDLLLNfnNGGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFR 140
Cdd:cd03459   1 NDLTRK--GGGEAIGERIILEGRVLDGDGRPVPDALVEIWQADAAGRYRHPRDSHRAPLDPNFTGFGRVLTDADGRYRFR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O      141 TIKPGPHPWRNgpNDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIaNPEAVQQLIAKLDMNNanpmDCLA 220
Cdd:cd03459  79 TIKPGAYPWRN--GAWRAPHIHVSVFARGLLERLVTRLYFPGDPANAADPVLASV-PEERRETLIARRDGSD----GALA 151

                ....*..
3PCD_O      221 YRFDIVL 227
Cdd:cd03459 152 YRFDIVL 158
Dioxygenase_C pfam00775
Dioxygenase;
47-229 2.33e-74

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 223.51  E-value: 2.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         47 TGPNFSHLGfgAHDHDLLLNFNngGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRyLAPlDPNFGgv 126
Cdd:pfam00775   2 EGPLYVEGA--PSDEDLARMDD--GDPIGEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDPT-EAP-EPNFR-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O        127 GRCLTDSDGYYSFRTIKPGPHPWRN-----------GPNDWRPAHIHFGISGPSIaTKLITQLYFEGDPLIPmCPIVKSi 195
Cdd:pfam00775  74 GRILTDSQGSYRFRTIQPAPYPIPNdgptgklldalGRHAWRPAHIHFFISAPGH-RRLTTQLYFEGDPYLP-DDIAYA- 150
                         170       180       190
                  ....*....|....*....|....*....|....*
3PCD_O        196 anpeAVQQLIAKLDMNNAN-PMDCLAYRFDIVLRG 229
Cdd:pfam00775 151 ----VRQGLVANYDEREDGtPEKFLEYHFDFVLDG 181
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
73-227 4.76e-54

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: 170.50  E-value: 4.76e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       73 PIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRYlapLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWrng 152
Cdd:cd00421   7 APGEPLTLTGTVLDGDGCPVPDALVEIWQADADGRYSGQDDSG---LDPEFFLRGRQITDADGRYRFRTIKPGPYPI--- 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3PCD_O      153 pndWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIaNPEAVQQLIAKLDMNNAnpmdcLAYRFDIVL 227
Cdd:cd00421  81 ---GRPPHIHFKVFAPGYNRRLTTQLYFPGDPLNDSDPVFAPY-SENVRPTLIADFDGIEF-----LEYRFDIVL 146
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
44-235 9.02e-37

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: 127.88  E-value: 9.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         44 SETTGPnFSHLG-FGAHDHDLLLNFNNGGLP---IGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRYLAPL 119
Cdd:TIGR02423   3 SQTVGP-YVHIGlTPEQAGTFTQEFGNNLVTpdaDGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLRAPAT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O        120 DPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNdwRPAHIHFGISGPSIATKLITQLYFEGD-PLIPMCPIVKSIAnP 198
Cdd:TIGR02423  82 DPGFRGWGRTGTDESGEFTFETVKPGAVPDRDGVL--QAPHINVSVFARGINRRLYTRLYFDDEaAANASDPVLALVP-A 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
3PCD_O        199 EAVQQLIAKldmnnANPMDCLAYRFDIVLRGQRKTHF 235
Cdd:TIGR02423 159 ERRATLIAK-----RERDGKVAYRFDIRLQGEGETVF 190
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
44-235 1.36e-36

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: 126.99  E-value: 1.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       44 SETTGPnFSHLGfgahdhdLLLNFNNGGL-----PIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRyLAP 118
Cdd:cd03463   6 SQTVGP-YVHIG-------LPPTREGGNDlvppdTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPADS-RRR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O      119 LDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWRNGPNdwRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIAnP 198
Cdd:cd03463  77 LDPGFRGFGRVATDADGRFSFTTVKPGAVPGRDGAG--QAPHINVWVFARGLLKHLFTRIYFPDEEANAADPVLALVP-E 153
                       170       180       190
                ....*....|....*....|....*....|....*..
3PCD_O      199 EAVQQLIAKLDMNNanpmdclAYRFDIVLRGQRKTHF 235
Cdd:cd03463 154 ERRATLIAKREGDG-------AYRFDIRLQGEGETVF 183
Catechol_intradiol_dioxygenases cd03458
Catechol intradiol dioxygenases can be divided into several subgroups according to their ...
71-186 4.14e-29

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: 109.57  E-value: 4.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       71 GLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNdrylaPLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWr 150
Cdd:cd03458  98 DTADGEPLFVHGTVTDTDGKPLAGATVDVWHADPDGFYSQQD-----PDQPEFNLRGKFRTDEDGRYRFRTIRPVPYPI- 171
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
3PCD_O      151 ngPND--------------WRPAHIHFGISGPSIATkLITQLYFEGDPLI 186
Cdd:cd03458 172 --PPDgptgellealgrhpWRPAHIHFMVSAPGYRT-LTTQIYFEGDPYL 218
1,2-HQD cd03461
Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2, ...
73-186 2.55e-26

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: 102.70  E-value: 2.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       73 PIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNdrylaPLDPNFGGVGRCLTDSDGYYSFRTIKPGPHPWrng 152
Cdd:cd03461 116 ADGEPCFVHGRVTDTDGKPLPGATVDVWQADPNGLYDVQD-----PDQPEFNLRGKFRTDEDGRYAFRTLRPTPYPI--- 187
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
3PCD_O      153 PND--------------WRPAHIHFGISGPSIATkLITQLYFEGDPLI 186
Cdd:cd03461 188 PTDgpvgkllkamgrhpMRPAHIHFMVTAPGYRT-LVTQIFDSGDPYL 234
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
75-186 6.74e-22

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: 90.47  E-value: 6.74e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       75 GERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRylapLDPNFGGvGRCLTDSDGYYSFRTIKPGPH--PwRNG 152
Cdd:cd03462  97 HKPLLFRGTVKDLAGAPVAGAVIDVWHSTPDGKYSGFHPN----IPEDYYR-GKIRTDEDGRYEVRTTVPVPYqiP-NDG 170
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3PCD_O      153 P----------NDWRPAHIHFGISGPSIATkLITQLYFEGDPLI 186
Cdd:cd03462 171 PtgalleamggHSWRPAHVHFKVRADGYET-LTTQLYFEGGEWV 213
1,2-CTD cd03460
Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to ...
57-186 8.46e-21

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: 88.19  E-value: 8.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       57 GAHDHDLLLNFNNGGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHkndrylapLDPN---FGGVGRCLTDS 133
Cdd:cd03460 104 GAPESDGFARLDDGSDDDGETLVMHGTVTDTDGKPVPGAKVEVWHANSKGFYSH--------FDPTqspFNLRRSIITDA 175
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3PCD_O      134 DGYYSFRTIKP---GPHPwrNGPNDW----------RPAHIHFGISGPSiATKLITQLYFEGDPLI 186
Cdd:cd03460 176 DGRYRFRSIMPsgyGVPP--GGPTQQllnalgrhgnRPAHIHFFVSAPG-HRKLTTQINIEGDPYI 238
chlorocat_1_2 TIGR02465
chlorocatechol 1,2-dioxygenase; Members of this protein family are chlorocatechol 1, ...
75-186 5.30e-17

chlorocatechol 1,2-dioxygenase; Members of this protein family are chlorocatechol 1,2-dioxygenase. This protein is closely related to catechol 1,2-dioxygenase, TIGR02439, EC 1.13.11.1. Note that annotated database entries have appeared for the present protein family with the EC number that refers to that of family TIGR02439. This protein acts in pathways of the biodegradation of chlorinated aromatic compounds.


Pssm-ID: 131518 [Multi-domain]  Cd Length: 246  Bit Score: 77.12  E-value: 5.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O         75 GERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYR--HKN--DRYLApldpnfggvGRCLTDSDGYYSFRTIKPGPHPWR 150
Cdd:TIGR02465  96 HKPLLIRGTVRDLSGTPVAGAVIDVWHSTPDGKYSgfHDNipDDYYR---------GKLVTAADGSYEVRTTMPVPYQIP 166
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
3PCD_O        151 N-GP----------NDWRPAHIHFGISGPSIATkLITQLYFEGDPLI 186
Cdd:TIGR02465 167 DaGPtgalletmgrHSWRPAHVHYKVRADGYRP-LTTQAYFEGGPYI 212
PCDO_beta_N pfam12391
Protocatechuate 3,4-dioxygenase beta subunit N terminal; This domain family is found in ...
11-41 2.21e-11

Protocatechuate 3,4-dioxygenase beta subunit N terminal; This domain family is found in bacteria, and is approximately 40 amino acids in length. The family is found in association with pfam00775. There are two completely conserved residues (Y and R) that may be functionally important. This family is the N terminal region of the beta subunit of protocatechuate 3,4-dioxidase. This enzyme utilizes a mononuclear, non-heme Fe3+ centre to catalyze metabolic cellular reactions.


Pssm-ID: 432520 [Multi-domain]  Cd Length: 32  Bit Score: 56.70  E-value: 2.21e-11
                          10        20        30
                  ....*....|....*....|....*....|.
3PCD_O         11 RDRNWHPKALTPDYKTSIARSPRQALVSIPQ 41
Cdd:pfam12391   2 RDRGSHPPALYPPYRSSVLRAPKQPLISLPQ 32
intradiol_dioxygenase_like cd03457
Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage ...
83-180 7.37e-11

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: 59.20  E-value: 7.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3PCD_O       83 RVVD-QYGKPVPNTLVEMWQANAGGRY---RHKNDRYLAPLDPNFG-GVGrcLTDSDGYYSFRTIKPGphpWRNGpndwR 157
Cdd:cd03457  32 QVVDvATCCPPPNAAVDIWHCDATGVYsgySAGGGGGEDTDDETFLrGVQ--PTDADGVVTFTTIFPG---WYPG----R 102
                        90       100
                ....*....|....*....|....*....
3PCD_O      158 PAHIHFGI-SGPSIATK-----LITQLYF 180
Cdd:cd03457 103 ATHIHFKVhPDATSATSggnvaHTGQLFF 131
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
80-147 9.72e-05

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 39.96  E-value: 9.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3PCD_O         80 VAGRVVDQYGKPVPNTLVEMwqanaggryrhkndrylapLDPNFGGVGRCLTDSDGYYSFRTIKPGPH 147
Cdd:pfam13620   2 ISGTVTDPSGAPVPGATVTV-------------------TNTDTGTVRTTTTDADGRYRFPGLPPGTY 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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