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Conserved domains on  [gi|2914526]
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Chain B, Protocatechuate 3,4-dioxygenase

Protein Classification

protocatechuate 3,4-dioxygenase subunit alpha( domain architecture ID 10020751)

protocatechuate 3,4-dioxygenase subunit alpha is part of an oligomeric enzyme, composed of 12 copies of the alpha and beta subunits, that catalyzes the intradiol addition of both oxygen atoms from molecular oxygen to 3,4-dihydroxybenzoate, resulting in ortho-cleavage of the aromatic ring to form 3-carboxy-cis,cis-muconate, during the beta-ketoadipate pathway of aromatic compound metabolism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
8-200 9.72e-108

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: 306.61  E-value: 9.72e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526      8 TPSQTAGPYVHIGLALEAAGnpTRDQEIWNRLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYNL-- 85
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPEQAG--TFTQEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLra 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526     86 ---ENAFNSFGRTATtFDAGEWTLHTVKPGVVNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNLIE 162
Cdd:TIGR02423  79 patDPGFRGWGRTGT-DESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEAAANASDPVLALVP 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2914526    163 qPQRRETLIAKRcEVDGKTAYRFDIRIQGEGETVFFDF 200
Cdd:TIGR02423 158 -AERRATLIAKR-ERDGKVAYRFDIRLQGEGETVFFDV 193
 
Name Accession Description Interval E-value
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
8-200 9.72e-108

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: 306.61  E-value: 9.72e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526      8 TPSQTAGPYVHIGLALEAAGnpTRDQEIWNRLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYNL-- 85
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPEQAG--TFTQEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLra 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526     86 ---ENAFNSFGRTATtFDAGEWTLHTVKPGVVNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNLIE 162
Cdd:TIGR02423  79 patDPGFRGWGRTGT-DESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEAAANASDPVLALVP 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2914526    163 qPQRRETLIAKRcEVDGKTAYRFDIRIQGEGETVFFDF 200
Cdd:TIGR02423 158 -AERRATLIAKR-ERDGKVAYRFDIRLQGEGETVFFDV 193
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
5-199 2.15e-94

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: 272.60  E-value: 2.15e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    5 LPETPSQTAGPYVHIGLALEAAGnptrdqeiWNRLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYN 84
Cdd:cd03463   1 LGETPSQTVGPYVHIGLPPTREG--------GNDLVPPDTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPAD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526   85 ----LENAFNSFGRTATTFDaGEWTLHTVKPGVVNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEAqANAKCPVLNL 160
Cdd:cd03463  73 srrrLDPGFRGFGRVATDAD-GRFSFTTVKPGAVPGRDGAGQAPHINVWVFARGLLKHLFTRIYFPDEE-ANAADPVLAL 150
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 2914526  161 iEQPQRRETLIAKRcevDGKTAYRFDIRIQGEGETVFFD 199
Cdd:cd03463 151 -VPEERRATLIAKR---EGDGAYRFDIRLQGEGETVFFD 185
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
3-200 2.93e-68

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


Pssm-ID: 226016 [Multi-domain]  Cd Length: 226  Bit Score: 208.03  E-value: 2.93e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    3 ELLPETPSQTAGPYVHIGLALEAAGN-PTRDQEIWN-RLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQ 80
Cdd:COG3485  25 SSLKETPSQTLGPYVHIGLETEGTVFgPYYLNDAPNdLLTNDKARGERILLEGRVLDGNGRPVPDALVEIWQADADGRYS 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526   81 DAYNLENA----FNSFGRTATTfDAGEWTLHTVKPGVVNNAAGVPM--APHINISLFARGINIHLHTRLYFDDEAqANAK 154
Cdd:COG3485 105 HPKDSRLAplpnFNGRGRTITD-EDGEYRFRTIKPGPYPWRNGGPMwrPAHIHFSVFARGINTRLVTQLYFPDDP-ANAR 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 2914526  155 CPVLNLIEQPQRRETLIAKRCevDGKTAYRFDIRIQGEGETVFFDF 200
Cdd:COG3485 183 DPILALVPDEDRIQTLIAQLD--DDALAYRFDIVLQGRNETVFFDI 226
Dioxygenase_C pfam00775
Dioxygenase;
38-191 1.66e-09

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 54.79  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526     38 RLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEY-QDAYNLENAFNSFGRTATTFDaGEWTLHTVKP----- 111
Cdd:pfam00775  18 RMDDGDPIGEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYsHFDPTEAPEPNFRGRILTDSQ-GSYRFRTIQPapypi 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    112 ------GVVNNAAGV-PMAP-HINISLFARGINiHLHTRLYF-------DDEAQANakcpvlnlieqpqrRETLIAKRCE 176
Cdd:pfam00775  97 pndgptGKLLDALGRhAWRPaHIHFFISAPGHR-RLTTQLYFegdpylpDDIAYAV--------------RQGLVANYDE 161
                         170       180
                  ....*....|....*....|
gi 2914526    177 VDGKT-----AYRFDIRIQG 191
Cdd:pfam00775 162 REDGTpekflEYHFDFVLDG 181
 
Name Accession Description Interval E-value
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
8-200 9.72e-108

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: 306.61  E-value: 9.72e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526      8 TPSQTAGPYVHIGLALEAAGnpTRDQEIWNRLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYNL-- 85
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPEQAG--TFTQEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLra 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526     86 ---ENAFNSFGRTATtFDAGEWTLHTVKPGVVNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNLIE 162
Cdd:TIGR02423  79 patDPGFRGWGRTGT-DESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEAAANASDPVLALVP 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2914526    163 qPQRRETLIAKRcEVDGKTAYRFDIRIQGEGETVFFDF 200
Cdd:TIGR02423 158 -AERRATLIAKR-ERDGKVAYRFDIRLQGEGETVFFDV 193
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
5-199 2.15e-94

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: 272.60  E-value: 2.15e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    5 LPETPSQTAGPYVHIGLALEAAGnptrdqeiWNRLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYN 84
Cdd:cd03463   1 LGETPSQTVGPYVHIGLPPTREG--------GNDLVPPDTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPAD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526   85 ----LENAFNSFGRTATTFDaGEWTLHTVKPGVVNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEAqANAKCPVLNL 160
Cdd:cd03463  73 srrrLDPGFRGFGRVATDAD-GRFSFTTVKPGAVPGRDGAGQAPHINVWVFARGLLKHLFTRIYFPDEE-ANAADPVLAL 150
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 2914526  161 iEQPQRRETLIAKRcevDGKTAYRFDIRIQGEGETVFFD 199
Cdd:cd03463 151 -VPEERRATLIAKR---EGDGAYRFDIRLQGEGETVFFD 185
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
3-200 2.93e-68

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


Pssm-ID: 226016 [Multi-domain]  Cd Length: 226  Bit Score: 208.03  E-value: 2.93e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    3 ELLPETPSQTAGPYVHIGLALEAAGN-PTRDQEIWN-RLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQ 80
Cdd:COG3485  25 SSLKETPSQTLGPYVHIGLETEGTVFgPYYLNDAPNdLLTNDKARGERILLEGRVLDGNGRPVPDALVEIWQADADGRYS 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526   81 DAYNLENA----FNSFGRTATTfDAGEWTLHTVKPGVVNNAAGVPM--APHINISLFARGINIHLHTRLYFDDEAqANAK 154
Cdd:COG3485 105 HPKDSRLAplpnFNGRGRTITD-EDGEYRFRTIKPGPYPWRNGGPMwrPAHIHFSVFARGINTRLVTQLYFPDDP-ANAR 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 2914526  155 CPVLNLIEQPQRRETLIAKRCevDGKTAYRFDIRIQGEGETVFFDF 200
Cdd:COG3485 183 DPILALVPDEDRIQTLIAQLD--DDALAYRFDIVLQGRNETVFFDI 226
3,4-PCD cd03459
Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3, ...
37-189 7.10e-63

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: 191.71  E-value: 7.10e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526   37 NRLAKPD---APGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYN-----LENAFNSFGRTATTFDaGEWTLHT 108
Cdd:cd03459   1 NDLTRKGggeAIGERIILEGRVLDGDGRPVPDALVEIWQADAAGRYRHPRDshrapLDPNFTGFGRVLTDAD-GRYRFRT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526  109 VKPGVVNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEAqANAKCPVLNLIeQPQRRETLIAKRCEVDGKTAYRFDIR 188
Cdd:cd03459  80 IKPGAYPWRNGAWRAPHIHVSVFARGLLERLVTRLYFPGDP-ANAADPVLASV-PEERRETLIARRDGSDGALAYRFDIV 157

                .
gi 2914526  189 I 189
Cdd:cd03459 158 L 158
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
42-189 6.54e-42

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: 138.15  E-value: 6.54e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526   42 PDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEY--QDAYNLENAFNSFGRTATTFDaGEWTLHTVKPGvvnnAAG 119
Cdd:cd00421   5 EDAPGEPLTLTGTVLDGDGCPVPDALVEIWQADADGRYsgQDDSGLDPEFFLRGRQITDAD-GRYRFRTIKPG----PYP 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526  120 VPMAPHINISLFARGINIHLHTRLYFDDEAqANAKCPVLNLIeQPQRRETLIAKRCEVDGKTaYRFDIRI 189
Cdd:cd00421  80 IGRPPHIHFKVFAPGYNRRLTTQLYFPGDP-LNDSDPVFAPY-SENVRPTLIADFDGIEFLE-YRFDIVL 146
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
1-197 1.02e-21

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: 88.17  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526      1 PIELLPETPSQTAGP-YVHIGLAleaagnptrdqEIWNRL--AKPDAP-GEHILLLGQVYDGNGHLVRDSFLEVWQADAN 76
Cdd:TIGR02422  20 ALISIPQSLSELTGPvFGHDDLG-----------PIDNDLtlAHGGEPiGERIIVHGRVLDEDGRPVPNTLVEVWQANAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526     77 GEY---QDAYN--LENAFNSFGRTATTFDaGEWTLHTVKPGV--VNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEA 149
Cdd:TIGR02422  89 GRYrhkNDQYLapLDPNFGGVGRTLTDSD-GYYRFRTIKPGPypWGNHHNAWRPAHIHFSLFGTSFAQRLITQMYFEGDP 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2914526    150 QAnAKCPVLNLIEQPQRRETLIAK-----RCEVDGkTAYRFDIRIQGEGETVF 197
Cdd:TIGR02422 168 LI-AYDPIVNSIPDEAARERLIATldldnTIPMDA-LGYRFDIVLRGRRATPF 218
3,4-PCD_beta cd03464
Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring ...
1-191 1.46e-18

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: 80.05  E-value: 1.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    1 PIELLPETPSQTAGP-YVH--IG-----LALEAAGNPTrdqeiwnrlakpdapGEHILLLGQVYDGNGHLVRDSFLEVWQ 72
Cdd:cd03464  25 PLISIPHTLSELTGPvFGHddLGpldndLTRNHNGEPI---------------GERIIVHGRVLDEDGRPVPNTLVEIWQ 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526   73 ADANGEY---QDAYN--LENAFNSFGRTATTfDAGEWTLHTVKPGV--VNNAAGVPMAPHINISLFARGINIHLHTRLYF 145
Cdd:cd03464  90 ANAAGRYrhkRDQHDapLDPNFGGAGRTLTD-DDGYYRFRTIKPGAypWGNHPNAWRPAHIHFSLFGPSFATRLVTQMYF 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 2914526  146 DDEAQAnAKCPVLNLIEQPQRRETLIAKrceVDGKT-------AYRFDIRIQG 191
Cdd:cd03464 169 PGDPLI-PHDPIYNSIPDEAARQRLIAR---FDLSAtqpewalGYRFDIVLRG 217
Dioxygenase_C pfam00775
Dioxygenase;
38-191 1.66e-09

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 54.79  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526     38 RLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEY-QDAYNLENAFNSFGRTATTFDaGEWTLHTVKP----- 111
Cdd:pfam00775  18 RMDDGDPIGEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYsHFDPTEAPEPNFRGRILTDSQ-GSYRFRTIQPapypi 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    112 ------GVVNNAAGV-PMAP-HINISLFARGINiHLHTRLYF-------DDEAQANakcpvlnlieqpqrRETLIAKRCE 176
Cdd:pfam00775  97 pndgptGKLLDALGRhAWRPaHIHFFISAPGHR-RLTTQLYFegdpylpDDIAYAV--------------RQGLVANYDE 161
                         170       180
                  ....*....|....*....|
gi 2914526    177 VDGKT-----AYRFDIRIQG 191
Cdd:pfam00775 162 REDGTpekflEYHFDFVLDG 181
Catechol_intradiol_dioxygenases cd03458
Catechol intradiol dioxygenases can be divided into several subgroups according to their ...
8-147 9.80e-07

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: 47.55  E-value: 9.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    8 TPSQTAGPYvHIGLALEAAGNPTRDQEiwnrlakpDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEY------QD 81
Cdd:cd03458  73 TESTILGPF-YVAGAPEVDNGATIDDD--------TADGEPLFVHGTVTDTDGKPLAGATVDVWHADPDGFYsqqdpdQP 143
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2914526   82 AYNLENAFnsfgrtaTTFDAGEWTLHTVKP-----------GVVNNAAGV-PMAP-HINISLFARGINiHLHTRLYFDD 147
Cdd:cd03458 144 EFNLRGKF-------RTDEDGRYRFRTIRPvpypippdgptGELLEALGRhPWRPaHIHFMVSAPGYR-TLTTQIYFEG 214
1,2-CTD cd03460
Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to ...
8-85 3.29e-05

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: 43.13  E-value: 3.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526    8 TPSQTAGP-YVhiglaleaAGNPTRDQEiwNRL-AKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEY------ 79
Cdd:cd03460  92 TPRTIEGPlYV--------AGAPESDGF--ARLdDGSDDDGETLVMHGTVTDTDGKPVPGAKVEVWHANSKGFYshfdpt 161

                ....*.
gi 2914526   80 QDAYNL 85
Cdd:cd03460 162 QSPFNL 167
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
42-111 4.00e-05

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: 42.71  E-value: 4.00e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2914526   42 PDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYNLENAFNSFGRTaTTFDAGEWTLHTVKP 111
Cdd:cd03462  93 DDDDHKPLLFRGTVKDLAGAPVAGAVIDVWHSTPDGKYSGFHPNIPEDYYRGKI-RTDEDGRYEVRTTVP 161
1,2-HQD cd03461
Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2, ...
43-111 7.61e-05

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: 42.22  E-value: 7.61e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2914526   43 DAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEY------QDAYNLENAFnsfgrtaTTFDAGEWTLHTVKP 111
Cdd:cd03461 115 GADGEPCFVHGRVTDTDGKPLPGATVDVWQADPNGLYdvqdpdQPEFNLRGKF-------RTDEDGRYAFRTLRP 182
 
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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