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Conserved domains on  [gi|1085814099|emb|SDS17487|]
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protocatechuate 3,4-dioxygenase, beta subunit [Pseudomonas chlororaphis]

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 ...
17-238 2.10e-146

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: 407.50  E-value: 2.10e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  17 HPKALTPDYKTSVARSPRQALVSIPQSLSETSGPDFSHLKTGRFDNDLLLNfnNGGLPVGERIIVAGRVCDQYGQPIPHT 96
Cdd:TIGR02422   1 HPPALTPDYKTSVLRSPKNALISIPQSLSELTGPVFGHDDLGPIDNDLTLA--HGGEPIGERIIVHGRVLDEDGRPVPNT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  97 LVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRALTDRDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFSISGPSIATRLI 176
Cdd:TIGR02422  79 LVEVWQANAAGRYRHKNDQYLAPLDPNFGGVGRTLTDSDGYYRFRTIKPGPYPWGNHHNAWRPAHIHFSLFGTSFAQRLI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085814099 177 TQLYFEGDPLIPLCPIVKSIANPEAVQSLIARLDMSSANPMDCLAYRFDIVLRGQRKTHFEN 238
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 ...
17-238 2.10e-146

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: 407.50  E-value: 2.10e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  17 HPKALTPDYKTSVARSPRQALVSIPQSLSETSGPDFSHLKTGRFDNDLLLNfnNGGLPVGERIIVAGRVCDQYGQPIPHT 96
Cdd:TIGR02422   1 HPPALTPDYKTSVLRSPKNALISIPQSLSELTGPVFGHDDLGPIDNDLTLA--HGGEPIGERIIVHGRVLDEDGRPVPNT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  97 LVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRALTDRDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFSISGPSIATRLI 176
Cdd:TIGR02422  79 LVEVWQANAAGRYRHKNDQYLAPLDPNFGGVGRTLTDSDGYYRFRTIKPGPYPWGNHHNAWRPAHIHFSLFGTSFAQRLI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085814099 177 TQLYFEGDPLIPLCPIVKSIANPEAVQSLIARLDMSSANPMDCLAYRFDIVLRGQRKTHFEN 238
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 ...
12-233 2.62e-143

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: 399.38  E-value: 2.62e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  12 RDRNWHPKALTPDYKTSVARSPRQALVSIPQSLSETSGPDFSHLKTGRFDNDLLLNFNngGLPVGERIIVAGRVCDQYGQ 91
Cdd:cd03464     1 RDTEAHPPALTPDYKSSVLRSPKQPLISIPHTLSELTGPVFGHDDLGPLDNDLTRNHN--GEPIGERIIVHGRVLDEDGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  92 PIPHTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRALTDRDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFSISGPSI 171
Cdd:cd03464    79 PVPNTLVEIWQANAAGRYRHKRDQHDAPLDPNFGGAGRTLTDDDGYYRFRTIKPGAYPWGNHPNAWRPAHIHFSLFGPSF 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085814099 172 ATRLITQLYFEGDPLIPLCPIVKSIANPEAVQSLIARLDMSSANPMDCLAYRFDIVLRGQRK 233
Cdd:cd03464   159 ATRLVTQMYFPGDPLIPHDPIYNSIPDEAARQRLIARFDLSATQPEWALGYRFDIVLRGRRA 220
Dioxygenase_C pfam00775
Dioxygenase;
49-230 1.30e-70

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 213.88  E-value: 1.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  49 GPDFSHLktGRFDNDLLLNFNngGLPVGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRyLAPlDPNFGgvG 128
Cdd:pfam00775   3 GPLYVEG--APSDEDLARMDD--GDPIGEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDPT-EAP-EPNFR--G 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099 129 RALTDRDGYYSFRTIKPGPYPWRN-----------GPNDWRPAHIHFSISGPSIaTRLITQLYFEGDPLIPlCPIVKSia 197
Cdd:pfam00775  75 RILTDSQGSYRFRTIQPAPYPIPNdgptgklldalGRHAWRPAHIHFFISAPGH-RRLTTQLYFEGDPYLP-DDIAYA-- 150
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1085814099 198 npeAVQSLIARLDMSSAN-PMDCLAYRFDIVLRG 230
Cdd:pfam00775 151 ---VRQGLVANYDEREDGtPEKFLEYHFDFVLDG 181
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
42-234 2.17e-70

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


Pssm-ID: 442708  Cd Length: 171  Bit Score: 213.14  E-value: 2.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  42 QSLSETSGPDFSHLKTGRFDNDLLLNfnngglPVGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRylaPLD 121
Cdd:COG3485     1 ETPSQTEGPFYVDGLPLPLGADLARD------APGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDDG---PLD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099 122 PNFGGVGRALTDRDGYYSFRTIKPGPYPWRNGPndWRPAHIHFSISGPSIaTRLITQLYFEGDPLIPLCPIVKsianpeA 201
Cdd:COG3485    72 PNFNGRGRFTTDADGRYRFRTIKPGPYPIPNHP--GRPAHIHFSVFAPGF-ERLTTQLYFPGDPYNASDPVFG------V 142
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1085814099 202 VQSLIARLDMSSanpmDCLAYRFDIVLRGQRKT 234
Cdd:COG3485   143 RDTLIARFEPED----GALVYRFDIVLQGPGET 171
 
Name Accession Description Interval E-value
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
17-238 2.10e-146

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: 407.50  E-value: 2.10e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  17 HPKALTPDYKTSVARSPRQALVSIPQSLSETSGPDFSHLKTGRFDNDLLLNfnNGGLPVGERIIVAGRVCDQYGQPIPHT 96
Cdd:TIGR02422   1 HPPALTPDYKTSVLRSPKNALISIPQSLSELTGPVFGHDDLGPIDNDLTLA--HGGEPIGERIIVHGRVLDEDGRPVPNT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  97 LVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRALTDRDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFSISGPSIATRLI 176
Cdd:TIGR02422  79 LVEVWQANAAGRYRHKNDQYLAPLDPNFGGVGRTLTDSDGYYRFRTIKPGPYPWGNHHNAWRPAHIHFSLFGTSFAQRLI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085814099 177 TQLYFEGDPLIPLCPIVKSIANPEAVQSLIARLDMSSANPMDCLAYRFDIVLRGQRKTHFEN 238
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 ...
12-233 2.62e-143

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: 399.38  E-value: 2.62e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  12 RDRNWHPKALTPDYKTSVARSPRQALVSIPQSLSETSGPDFSHLKTGRFDNDLLLNFNngGLPVGERIIVAGRVCDQYGQ 91
Cdd:cd03464     1 RDTEAHPPALTPDYKSSVLRSPKQPLISIPHTLSELTGPVFGHDDLGPLDNDLTRNHN--GEPIGERIIVHGRVLDEDGR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  92 PIPHTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRALTDRDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFSISGPSI 171
Cdd:cd03464    79 PVPNTLVEIWQANAAGRYRHKRDQHDAPLDPNFGGAGRTLTDDDGYYRFRTIKPGAYPWGNHPNAWRPAHIHFSLFGPSF 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085814099 172 ATRLITQLYFEGDPLIPLCPIVKSIANPEAVQSLIARLDMSSANPMDCLAYRFDIVLRGQRK 233
Cdd:cd03464   159 ATRLVTQMYFPGDPLIPHDPIYNSIPDEAARQRLIARFDLSATQPEWALGYRFDIVLRGRRA 220
3,4-PCD cd03459
Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3, ...
62-228 1.80e-75

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: 225.61  E-value: 1.80e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  62 NDLLLNfnNGGLPVGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRALTDRDGYYSFR 141
Cdd:cd03459     1 NDLTRK--GGGEAIGERIILEGRVLDGDGRPVPDALVEIWQADAAGRYRHPRDSHRAPLDPNFTGFGRVLTDADGRYRFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099 142 TIKPGPYPWRNgpNDWRPAHIHFSISGPSIATRLITQLYFEGDPLIPLCPIVKSIaNPEAVQSLIARLDMSSanpmDCLA 221
Cdd:cd03459    79 TIKPGAYPWRN--GAWRAPHIHVSVFARGLLERLVTRLYFPGDPANAADPVLASV-PEERRETLIARRDGSD----GALA 151

                  ....*..
gi 1085814099 222 YRFDIVL 228
Cdd:cd03459   152 YRFDIVL 158
Dioxygenase_C pfam00775
Dioxygenase;
49-230 1.30e-70

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 213.88  E-value: 1.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  49 GPDFSHLktGRFDNDLLLNFNngGLPVGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRyLAPlDPNFGgvG 128
Cdd:pfam00775   3 GPLYVEG--APSDEDLARMDD--GDPIGEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDPT-EAP-EPNFR--G 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099 129 RALTDRDGYYSFRTIKPGPYPWRN-----------GPNDWRPAHIHFSISGPSIaTRLITQLYFEGDPLIPlCPIVKSia 197
Cdd:pfam00775  75 RILTDSQGSYRFRTIQPAPYPIPNdgptgklldalGRHAWRPAHIHFFISAPGH-RRLTTQLYFEGDPYLP-DDIAYA-- 150
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1085814099 198 npeAVQSLIARLDMSSAN-PMDCLAYRFDIVLRG 230
Cdd:pfam00775 151 ---VRQGLVANYDEREDGtPEKFLEYHFDFVLDG 181
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
42-234 2.17e-70

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


Pssm-ID: 442708  Cd Length: 171  Bit Score: 213.14  E-value: 2.17e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  42 QSLSETSGPDFSHLKTGRFDNDLLLNfnngglPVGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRylaPLD 121
Cdd:COG3485     1 ETPSQTEGPFYVDGLPLPLGADLARD------APGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDDG---PLD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099 122 PNFGGVGRALTDRDGYYSFRTIKPGPYPWRNGPndWRPAHIHFSISGPSIaTRLITQLYFEGDPLIPLCPIVKsianpeA 201
Cdd:COG3485    72 PNFNGRGRFTTDADGRYRFRTIKPGPYPIPNHP--GRPAHIHFSVFAPGF-ERLTTQLYFPGDPYNASDPVFG------V 142
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1085814099 202 VQSLIARLDMSSanpmDCLAYRFDIVLRGQRKT 234
Cdd:COG3485   143 RDTLIARFEPED----GALVYRFDIVLQGPGET 171
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
76-228 5.39e-53

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: 167.81  E-value: 5.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  76 GERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRYLaplDPNFGGVGRALTDRDGYYSFRTIKPGPYPWrngpn 155
Cdd:cd00421     9 GEPLTLTGTVLDGDGCPVPDALVEIWQADADGRYSGQDDSGL---DPEFFLRGRQITDADGRYRFRTIKPGPYPI----- 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085814099 156 dWRPAHIHFSISGPSIATRLITQLYFEGDPLIPLCPIVKSIaNPEAVQSLIARLDMssanpMDCLAYRFDIVL 228
Cdd:cd00421    81 -GRPPHIHFKVFAPGYNRRLTTQLYFPGDPLNDSDPVFAPY-SENVRPTLIADFDG-----IEFLEYRFDIVL 146
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
45-236 6.93e-36

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: 125.57  E-value: 6.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  45 SETSGPDFSHLKTGRFDNDLLLNFNNGGLP---VGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRYLAPLD 121
Cdd:TIGR02423   3 SQTVGPYVHIGLTPEQAGTFTQEFGNNLVTpdaDGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLRAPATD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099 122 PNFGGVGRALTDRDGYYSFRTIKPGPYPWRNGPNdwRPAHIHFSISGPSIATRLITQLYFEGD-PLIPLCPIVKSIAnPE 200
Cdd:TIGR02423  83 PGFRGWGRTGTDESGEFTFETVKPGAVPDRDGVL--QAPHINVSVFARGINRRLYTRLYFDDEaAANASDPVLALVP-AE 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1085814099 201 AVQSLIARldmssANPMDCLAYRFDIVLRGQRKTHF 236
Cdd:TIGR02423 160 RRATLIAK-----RERDGKVAYRFDIRLQGEGETVF 190
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
45-236 8.00e-35

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: 122.76  E-value: 8.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  45 SETSGPDFSHLKTGRFDNDLLLnFNNGglPVGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRyLAPLDPNF 124
Cdd:cd03463     6 SQTVGPYVHIGLPPTREGGNDL-VPPD--TAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPADS-RRRLDPGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099 125 GGVGRALTDRDGYYSFRTIKPGPYPWRNGPNdwRPAHIHFSISGPSIATRLITQLYFEGDPLIPLCPIVKSIAnPEAVQS 204
Cdd:cd03463    82 RGFGRVATDADGRFSFTTVKPGAVPGRDGAG--QAPHINVWVFARGLLKHLFTRIYFPDEEANAADPVLALVP-EERRAT 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1085814099 205 LIARldmssanPMDCLAYRFDIVLRGQRKTHF 236
Cdd:cd03463   159 LIAK-------REGDGAYRFDIRLQGEGETVF 183
Catechol_intradiol_dioxygenases cd03458
Catechol intradiol dioxygenases can be divided into several subgroups according to their ...
72-187 2.88e-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: 110.34  E-value: 2.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  72 GLPVGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNdrylaPLDPNFGGVGRALTDRDGYYSFRTIKPGPYPWr 151
Cdd:cd03458    98 DTADGEPLFVHGTVTDTDGKPLAGATVDVWHADPDGFYSQQD-----PDQPEFNLRGKFRTDEDGRYRFRTIRPVPYPI- 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1085814099 152 ngPND--------------WRPAHIHFSISGPSIATrLITQLYFEGDPLI 187
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, ...
74-187 9.87e-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: 101.54  E-value: 9.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  74 PVGERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNdrylaPLDPNFGGVGRALTDRDGYYSFRTIKPGPYPWrng 153
Cdd:cd03461   116 ADGEPCFVHGRVTDTDGKPLPGATVDVWQADPNGLYDVQD-----PDQPEFNLRGKFRTDEDGRYAFRTLRPTPYPI--- 187
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1085814099 154 PND--------------WRPAHIHFSISGPSIATrLITQLYFEGDPLI 187
Cdd:cd03461   188 PTDgpvgkllkamgrhpMRPAHIHFMVTAPGYRT-LVTQIFDSGDPYL 234
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
76-187 2.14e-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: 92.02  E-value: 2.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  76 GERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHKNDRylapLDPNFGGvGRALTDRDGYYSFRTIKPGPY--PwRNG 153
Cdd:cd03462    97 HKPLLFRGTVKDLAGAPVAGAVIDVWHSTPDGKYSGFHPN----IPEDYYR-GKIRTDEDGRYEVRTTVPVPYqiP-NDG 170
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085814099 154 P----------NDWRPAHIHFSISGPSIATrLITQLYFEGDPLI 187
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 ...
76-205 4.23e-20

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: 86.27  E-value: 4.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  76 GERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYRHkndrylapLDPN---FGGVGRALTDRDGYYSFRTIKPGPY---P 149
Cdd:cd03460   122 GETLVMHGTVTDTDGKPVPGAKVEVWHANSKGFYSH--------FDPTqspFNLRRSIITDADGRYRFRSIMPSGYgvpP 193
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085814099 150 wrNGPNDW----------RPAHIHFSISGPSiATRLITQLYFEGDPLI----------PLCPIVKSIANPEAVQSL 205
Cdd:cd03460   194 --GGPTQQllnalgrhgnRPAHIHFFVSAPG-HRKLTTQINIEGDPYIwddfafatreGLIPEVVEVEDAAALKQY 266
chlorocat_1_2 TIGR02465
chlorocatechol 1,2-dioxygenase; Members of this protein family are chlorocatechol 1, ...
76-187 1.70e-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: 78.66  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  76 GERIIVAGRVCDQYGQPIPHTLVEMWQANAGGRYR--HKN--DRYLApldpnfggvGRALTDRDGYYSFRTIKPGPYPWR 151
Cdd:TIGR02465  96 HKPLLIRGTVRDLSGTPVAGAVIDVWHSTPDGKYSgfHDNipDDYYR---------GKLVTAADGSYEVRTTMPVPYQIP 166
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1085814099 152 N-GP----------NDWRPAHIHFSISGPSIATrLITQLYFEGDPLI 187
Cdd:TIGR02465 167 DaGPtgalletmgrHSWRPAHVHYKVRADGYRP-LTTQAYFEGGPYI 212
PCDO_beta_N pfam12391
Protocatechuate 3,4-dioxygenase beta subunit N terminal; This domain family is found in ...
12-42 2.54e-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: 2.54e-11
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1085814099  12 RDRNWHPKALTPDYKTSVARSPRQALVSIPQ 42
Cdd:pfam12391   2 RDRGSHPPALYPPYRSSVLRAPKQPLISLPQ 32
intradiol_dioxygenase_like cd03457
Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage ...
90-181 7.29e-10

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: 56.51  E-value: 7.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085814099  90 GQPIPHTLVEMWQANAGGRY---RHKNDRYLAPLDPNFG-GVGraLTDRDGYYSFRTIKPGPYPwrnGpndwRPAHIHFS 165
Cdd:cd03457    39 CCPPPNAAVDIWHCDATGVYsgySAGGGGGEDTDDETFLrGVQ--PTDADGVVTFTTIFPGWYP---G----RATHIHFK 109
                          90       100
                  ....*....|....*....|..
gi 1085814099 166 I-SGPSIATR-----LITQLYF 181
Cdd:cd03457   110 VhPDATSATSggnvaHTGQLFF 131
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
81-148 2.82e-04

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 38.41  E-value: 2.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085814099  81 VAGRVCDQYGQPIPHTLVEMwqanaggryrhkndrylapLDPNFGGVGRALTDRDGYYSFRTIKPGPY 148
Cdd:pfam13620   2 ISGTVTDPSGAPVPGATVTV-------------------TNTDTGTVRTTTTDADGRYRFPGLPPGTY 50
 
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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