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Conserved domains on  [gi|495853378|ref|WP_008577957|]
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MULTISPECIES: protocatechuate 3,4-dioxygenase subunit alpha [Xanthomonas]

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 ...
6-187 6.67e-97

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: 278.88  E-value: 6.67e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378    6 TPSQTVGPYYRLGLEP--------LYRQQIAPAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRCEA 77
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPeqagtftqEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLRAPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   78 HDPSFDGWGRVPTDANGRFTFSTIKPGRVAGPDGKQQAAHLTVLVFMRGLLRGVSTRLYFADD-PHLGSDPILALVPAER 156
Cdd:TIGR02423  81 TDPGFRGWGRTGTDESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEaAANASDPVLALVPAER 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 495853378  157 RATLLAQPHPGG--AYTWDIHMQGDAETVFFRY 187
Cdd:TIGR02423 161 RATLIAKRERDGkvAYRFDIRLQGEGETVFFDV 193
 
Name Accession Description Interval E-value
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
6-187 6.67e-97

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: 278.88  E-value: 6.67e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378    6 TPSQTVGPYYRLGLEP--------LYRQQIAPAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRCEA 77
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPeqagtftqEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLRAPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   78 HDPSFDGWGRVPTDANGRFTFSTIKPGRVAGPDGKQQAAHLTVLVFMRGLLRGVSTRLYFADD-PHLGSDPILALVPAER 156
Cdd:TIGR02423  81 TDPGFRGWGRTGTDESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEaAANASDPVLALVPAER 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 495853378  157 RATLLAQPHPGG--AYTWDIHMQGDAETVFFRY 187
Cdd:TIGR02423 161 RATLIAKRERDGkvAYRFDIRLQGEGETVFFDV 193
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
3-186 2.48e-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: 272.21  E-value: 2.48e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   3 LHATPSQTVGPYYRLGLEP--LYRQQIAPAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRCEaHDP 80
Cdd:cd03463    1 LGETPSQTVGPYVHIGLPPtrEGGNDLVPPDTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPADSRRR-LDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  81 SFDGWGRVPTDANGRFTFSTIKPGRVAGPDGKQQAAHLTVLVFMRGLLRGVSTRLYFADDPHLGSDPILALVPAERRATL 160
Cdd:cd03463   80 GFRGFGRVATDADGRFSFTTVKPGAVPGRDGAGQAPHINVWVFARGLLKHLFTRIYFPDEEANAADPVLALVPEERRATL 159
                        170       180
                 ....*....|....*....|....*.
gi 495853378 161 LAQPHPGGAYTWDIHMQGDAETVFFR 186
Cdd:cd03463  160 IAKREGDGAYRFDIRLQGEGETVFFD 185
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
5-182 1.66e-63

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


Pssm-ID: 442708  Cd Length: 171  Bit Score: 193.50  E-value: 1.66e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   5 ATPSQTVGPYYRLGLEPLYRQQIApAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRceaHDPSFDG 84
Cdd:COG3485    1 ETPSQTEGPFYVDGLPLPLGADLA-RDAPGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDDGP---LDPNFNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  85 WGRVPTDANGRFTFSTIKPGRVAGPDGKQQAAHLTVLVFMRGlLRGVSTRLYFADDPHLGSDPILAlvpaeRRATLLAQP 164
Cdd:COG3485   77 RGRFTTDADGRYRFRTIKPGPYPIPNHPGRPAHIHFSVFAPG-FERLTTQLYFPGDPYNASDPVFG-----VRDTLIARF 150
                        170       180
                 ....*....|....*....|.
gi 495853378 165 HPGG---AYTWDIHMQGDAET 182
Cdd:COG3485  151 EPEDgalVYRFDIVLQGPGET 171
Dioxygenase_C pfam00775
Dioxygenase;
34-178 2.91e-20

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 83.29  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   34 GTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGrcEAHDPSFDgwGRVPTDANGRFTFSTIKPG----RVAGP 109
Cdd:pfam00775  26 GEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDPT--EAPEPNFR--GRILTDSQGSYRFRTIQPApypiPNDGP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  110 DGK---------QQAAHLTVLVFMRGlLRGVSTRLYFADDPHLGSDPILALVP---AERRATLLAQPHPGGAYTWDIHMQ 177
Cdd:pfam00775 102 TGKlldalgrhaWRPAHIHFFISAPG-HRRLTTQLYFEGDPYLPDDIAYAVRQglvANYDEREDGTPEKFLEYHFDFVLD 180

                  .
gi 495853378  178 G 178
Cdd:pfam00775 181 G 181
 
Name Accession Description Interval E-value
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
6-187 6.67e-97

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: 278.88  E-value: 6.67e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378    6 TPSQTVGPYYRLGLEP--------LYRQQIAPAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRCEA 77
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPeqagtftqEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLRAPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   78 HDPSFDGWGRVPTDANGRFTFSTIKPGRVAGPDGKQQAAHLTVLVFMRGLLRGVSTRLYFADD-PHLGSDPILALVPAER 156
Cdd:TIGR02423  81 TDPGFRGWGRTGTDESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEaAANASDPVLALVPAER 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 495853378  157 RATLLAQPHPGG--AYTWDIHMQGDAETVFFRY 187
Cdd:TIGR02423 161 RATLIAKRERDGkvAYRFDIRLQGEGETVFFDV 193
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
3-186 2.48e-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: 272.21  E-value: 2.48e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   3 LHATPSQTVGPYYRLGLEP--LYRQQIAPAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRCEaHDP 80
Cdd:cd03463    1 LGETPSQTVGPYVHIGLPPtrEGGNDLVPPDTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPADSRRR-LDP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  81 SFDGWGRVPTDANGRFTFSTIKPGRVAGPDGKQQAAHLTVLVFMRGLLRGVSTRLYFADDPHLGSDPILALVPAERRATL 160
Cdd:cd03463   80 GFRGFGRVATDADGRFSFTTVKPGAVPGRDGAGQAPHINVWVFARGLLKHLFTRIYFPDEEANAADPVLALVPEERRATL 159
                        170       180
                 ....*....|....*....|....*.
gi 495853378 161 LAQPHPGGAYTWDIHMQGDAETVFFR 186
Cdd:cd03463  160 IAKREGDGAYRFDIRLQGEGETVFFD 185
3,4-PCD cd03459
Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3, ...
27-176 1.24e-65

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: 198.26  E-value: 1.24e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  27 IAPAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRCEAHDPSFDGWGRVPTDANGRFTFSTIKPGRV 106
Cdd:cd03459    6 KGGGEAIGERIILEGRVLDGDGRPVPDALVEIWQADAAGRYRHPRDSHRAPLDPNFTGFGRVLTDADGRYRFRTIKPGAY 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495853378 107 AGPDGKQQAAHLTVLVFMRGLLRGVSTRLYFADDPHLGSDPILALVPAERRATLLAQPHP---GGAYTWDIHM 176
Cdd:cd03459   86 PWRNGAWRAPHIHVSVFARGLLERLVTRLYFPGDPANAADPVLASVPEERRETLIARRDGsdgALAYRFDIVL 158
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
5-182 1.66e-63

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


Pssm-ID: 442708  Cd Length: 171  Bit Score: 193.50  E-value: 1.66e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   5 ATPSQTVGPYYRLGLEPLYRQQIApAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRceaHDPSFDG 84
Cdd:COG3485    1 ETPSQTEGPFYVDGLPLPLGADLA-RDAPGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDDGP---LDPNFNG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  85 WGRVPTDANGRFTFSTIKPGRVAGPDGKQQAAHLTVLVFMRGlLRGVSTRLYFADDPHLGSDPILAlvpaeRRATLLAQP 164
Cdd:COG3485   77 RGRFTTDADGRYRFRTIKPGPYPIPNHPGRPAHIHFSVFAPG-FERLTTQLYFPGDPYNASDPVFG-----VRDTLIARF 150
                        170       180
                 ....*....|....*....|.
gi 495853378 165 HPGG---AYTWDIHMQGDAET 182
Cdd:COG3485  151 EPEDgalVYRFDIVLQGPGET 171
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
31-176 5.69e-46

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: 148.16  E-value: 5.69e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  31 QAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRceaHDPSFDGWGRVPTDANGRFTFSTIKPGRVAGpd 110
Cdd:cd00421    6 DAPGEPLTLTGTVLDGDGCPVPDALVEIWQADADGRYSGQDDSG---LDPEFFLRGRQITDADGRYRFRTIKPGPYPI-- 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495853378 111 gkQQAAHLTVLVFMRGLLRGVSTRLYFADDPHLGSDPILALVPAERRATLLAQ--PHPGGAYTWDIHM 176
Cdd:cd00421   81 --GRPPHIHFKVFAPGYNRRLTTQLYFPGDPLNDSDPVFAPYSENVRPTLIADfdGIEFLEYRFDIVL 146
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
2-184 3.66e-30

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: 109.74  E-value: 3.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378    2 SLHATPSQTVGPYY-RLGLEPLYRQQIA--PAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRCEAH 78
Cdd:TIGR02422  23 SIPQSLSELTGPVFgHDDLGPIDNDLTLahGGEPIGERIIVHGRVLDEDGRPVPNTLVEVWQANAAGRYRHKNDQYLAPL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   79 DPSFDGWGRVPTDANGRFTFSTIKPGRVAGPDGKQ--QAAHLTVLVFMRGLLRGVSTRLYFADDPHLGSDPILALVPAER 156
Cdd:TIGR02422 103 DPNFGGVGRTLTDSDGYYRFRTIKPGPYPWGNHHNawRPAHIHFSLFGTSFAQRLITQMYFEGDPLIAYDPIVNSIPDEA 182
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 495853378  157 -RATLLA-------QPHPGGAYTWDIHMQGDAETVF 184
Cdd:TIGR02422 183 aRERLIAtldldntIPMDALGYRFDIVLRGRRATPF 218
3,4-PCD_beta cd03464
Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring ...
2-178 1.95e-25

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: 97.77  E-value: 1.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   2 SLHATPSQTVGPYY-----RLGLEPLYRQQIAPAQaaGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRCE 76
Cdd:cd03464   28 SIPHTLSELTGPVFghddlGPLDNDLTRNHNGEPI--GERIIVHGRVLDEDGRPVPNTLVEIWQANAAGRYRHKRDQHDA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  77 AHDPSFDGWGRVPTDANGRFTFSTIKPGrvAGPDGKQ----QAAHLTVLVFMRGLLRGVSTRLYFADDPHLGSDPILALV 152
Cdd:cd03464  106 PLDPNFGGAGRTLTDDDGYYRFRTIKPG--AYPWGNHpnawRPAHIHFSLFGPSFATRLVTQMYFPGDPLIPHDPIYNSI 183
                        170       180       190
                 ....*....|....*....|....*....|....
gi 495853378 153 PAER-RATLLA-------QPHPGGAYTWDIHMQG 178
Cdd:cd03464  184 PDEAaRQRLIArfdlsatQPEWALGYRFDIVLRG 217
Dioxygenase_C pfam00775
Dioxygenase;
34-178 2.91e-20

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 83.29  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   34 GTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGrcEAHDPSFDgwGRVPTDANGRFTFSTIKPG----RVAGP 109
Cdd:pfam00775  26 GEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDPT--EAPEPNFR--GRILTDSQGSYRFRTIQPApypiPNDGP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  110 DGK---------QQAAHLTVLVFMRGlLRGVSTRLYFADDPHLGSDPILALVP---AERRATLLAQPHPGGAYTWDIHMQ 177
Cdd:pfam00775 102 TGKlldalgrhaWRPAHIHFFISAPG-HRRLTTQLYFEGDPYLPDDIAYAVRQglvANYDEREDGTPEKFLEYHFDFVLD 180

                  .
gi 495853378  178 G 178
Cdd:pfam00775 181 G 181
1,2-HQD cd03461
Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2, ...
5-184 8.60e-20

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: 83.82  E-value: 8.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   5 ATPSQTVGPYYRLGlEPLYRQ--QIApAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYahvadgrcEAHDPS- 81
Cdd:cd03461   89 ATESTVLGPFYRED-APEYENgaSIV-QGADGEPCFVHGRVTDTDGKPLPGATVDVWQADPNGLY--------DVQDPDq 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  82 --FDGWGRVPTDANGRFTFSTIKPgrVA------GPDGK---------QQAAHLTVLVFMRGlLRGVSTRLYFADDPHLG 144
Cdd:cd03461  159 peFNLRGKFRTDEDGRYAFRTLRP--TPypiptdGPVGKllkamgrhpMRPAHIHFMVTAPG-YRTLVTQIFDSGDPYLD 235
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495853378 145 SDPILALvpaerRATLLA--QPHPGGAYTWDIHMQGDAETVF 184
Cdd:cd03461  236 SDAVFGV-----KDSLVVdfVPVEDDDAPGRLVPGADLELEY 272
Catechol_intradiol_dioxygenases cd03458
Catechol intradiol dioxygenases can be divided into several subgroups according to their ...
4-176 1.27e-19

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: 82.99  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   4 HATPSQTVGPYYRLGlEPLYRQ--QIAPAQAAGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADGRceahdPS 81
Cdd:cd03458   71 GGTESTILGPFYVAG-APEVDNgaTIDDDTADGEPLFVHGTVTDTDGKPLAGATVDVWHADPDGFYSQQDPDQ-----PE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  82 FDGWGRVPTDANGRFTFSTIKPgrVA------GPDGK---------QQAAHLTVLVFMRGlLRGVSTRLYFADDPHLGSD 146
Cdd:cd03458  145 FNLRGKFRTDEDGRYRFRTIRP--VPypippdGPTGEllealgrhpWRPAHIHFMVSAPG-YRTLTTQIYFEGDPYLDDD 221
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495853378 147 PILA-----LVPAERRATLLAQPHPGGAYTWDIHM 176
Cdd:cd03458  222 AVFAvkdslIVDFVPVEDGTGVPGPFAELDFDFVL 256
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
12-146 4.16e-13

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: 65.44  E-value: 4.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  12 GPYYRLGleplyrqqiAPAQA---------AGTHVQISGCIFDGAGAPVADAVLEVWQADAAGIYAHVADgrceaHDPSF 82
Cdd:cd03462   75 GPYFIEN---------APFVDgklktydddDHKPLLFRGTVKDLAGAPVAGAVIDVWHSTPDGKYSGFHP-----NIPED 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495853378  83 DGWGRVPTDANGRFTFSTIKPGRV----AGPDGKQQA---------AHLTVLVFMRGlLRGVSTRLYFADDPHLGSD 146
Cdd:cd03462  141 YYRGKIRTDEDGRYEVRTTVPVPYqipnDGPTGALLEamgghswrpAHVHFKVRADG-YETLTTQLYFEGGEWVDDD 216
1,2-CTD cd03460
Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to ...
5-168 1.46e-10

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: 58.53  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   5 ATPSQTVGPYYRLGlEPLY----RQQIAPAQAAGTHVqISGCIFDGAGAPVADAVLEVWQADAAGIYAHVadgrceahDP 80
Cdd:cd03460   91 GTPRTIEGPLYVAG-APESdgfaRLDDGSDDDGETLV-MHGTVTDTDGKPVPGAKVEVWHANSKGFYSHF--------DP 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378  81 S---FDGWGRVPTDANGRFTFSTIKP-GRVAGPDGKQQA------------AHLTVLVFMRGlLRGVSTRLYFADDPHLG 144
Cdd:cd03460  161 TqspFNLRRSIITDADGRYRFRSIMPsGYGVPPGGPTQQllnalgrhgnrpAHIHFFVSAPG-HRKLTTQINIEGDPYIW 239
                        170       180
                 ....*....|....*....|....*...
gi 495853378 145 SDPILA----LVPAERRATLLAQPHPGG 168
Cdd:cd03460  240 DDFAFAtregLIPEVVEVEDAAALKQYG 267
intradiol_dioxygenase_like cd03457
Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage ...
9-140 4.64e-09

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: 53.43  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495853378   9 QTVGPYYRLGlEPLyRQQIAPAQAaGTHVQISGCIFD-GAGAPVADAVLEVWQADAAGIYAHVADGRCEAHDPSFDGW-- 85
Cdd:cd03457    2 VTEGPYYVDG-ELV-RSDITEGQP-GVPLTLDLQVVDvATCCPPPNAAVDIWHCDATGVYSGYSAGGGGGEDTDDETFlr 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495853378  86 GRVPTDANGRFTFSTIKPGRVAGpdgkqQAAHLTVLVF--MRGLLRGVSTR----LYFADD 140
Cdd:cd03457   79 GVQPTDADGVVTFTTIFPGWYPG-----RATHIHFKVHpdATSATSGGNVAhtgqLFFDED 134
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
38-105 2.49e-03

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 35.33  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495853378   38 QISGCIFDGAGAPVADAVLEVwQADAAGIYAHVAdgrceahdpsfdgwgrvpTDANGRFTFSTIKPGR 105
Cdd:pfam13620   1 TISGTVTDPSGAPVPGATVTV-TNTDTGTVRTTT------------------TDADGRYRFPGLPPGT 49
 
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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