NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490245615|ref|WP_004143799|]
View 

MULTISPECIES: protocatechuate 3,4-dioxygenase subunit alpha [Klebsiella]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
8-206 1.07e-103

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: 296.98  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615    8 TASQTAGPYVHIGLAPDAAGFhiFEKNFGPVLTTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRQQ 87
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPEQAGT--FTQEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   88 qKAVDPAFRGWGRTCSDfTSGIWRFETIKPGPVVGRDGRLMAPHVNLWVVARGINIGLNTRMYFADEHAANASDPVLNLI 167
Cdd:TIGR02423  79 -PATDPGFRGWGRTGTD-ESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEAAANASDPVLALV 156
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 490245615  168 EwEVRRKTLIAEREVRGtEVVYRFDIHLQGENETVFFDI 206
Cdd:TIGR02423 157 P-AERRATLIAKRERDG-KVAYRFDIRLQGEGETVFFDV 193
 
Name Accession Description Interval E-value
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
8-206 1.07e-103

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: 296.98  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615    8 TASQTAGPYVHIGLAPDAAGFhiFEKNFGPVLTTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRQQ 87
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPEQAGT--FTQEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   88 qKAVDPAFRGWGRTCSDfTSGIWRFETIKPGPVVGRDGRLMAPHVNLWVVARGINIGLNTRMYFADEHAANASDPVLNLI 167
Cdd:TIGR02423  79 -PATDPGFRGWGRTGTD-ESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEAAANASDPVLALV 156
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 490245615  168 EwEVRRKTLIAEREVRGtEVVYRFDIHLQGENETVFFDI 206
Cdd:TIGR02423 157 P-AERRATLIAKRERDG-KVAYRFDIRLQGEGETVFFDV 193
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
5-205 9.43e-99

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: 284.16  E-value: 9.43e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   5 LPETASQTAGPYVHIGLAPdaagfhifEKNFGPVLTTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDD 84
Cdd:cd03463    1 LGETPSQTVGPYVHIGLPP--------TREGGNDLVPPDTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPAD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  85 RqqQKAVDPAFRGWGRTCSDFtSGIWRFETIKPGPVVGRDGRLMAPHVNLWVVARGINIGLNTRMYFADEhAANASDPVL 164
Cdd:cd03463   73 S--RRRLDPGFRGFGRVATDA-DGRFSFTTVKPGAVPGRDGAGQAPHINVWVFARGLLKHLFTRIYFPDE-EANAADPVL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 490245615 165 NLiEWEVRRKTLIAEREVRGTevvYRFDIHLQGENETVFFD 205
Cdd:cd03463  149 AL-VPEERRATLIAKREGDGA---YRFDIRLQGEGETVFFD 185
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
7-201 6.07e-69

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


Pssm-ID: 442708  Cd Length: 171  Bit Score: 208.14  E-value: 6.07e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   7 ETASQTAGPYVHIGLaPDAAGFHIfeknfgpvltTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRq 86
Cdd:COG3485    1 ETPSQTEGPFYVDGL-PLPLGADL----------ARDAPGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDDG- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  87 qqkAVDPAFRGWGRTCSDfTSGIWRFETIKPGPVVGRDGRLMAPHVNLWVVARGInIGLNTRMYFADEhAANASDPVLNl 166
Cdd:COG3485   69 ---PLDPNFNGRGRFTTD-ADGRYRFRTIKPGPYPIPNHPGRPAHIHFSVFAPGF-ERLTTQLYFPGD-PYNASDPVFG- 141
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490245615 167 iewevRRKTLIAEREVRGTEVVYRFDIHLQGENET 201
Cdd:COG3485  142 -----VRDTLIARFEPEDGALVYRFDIVLQGPGET 171
Dioxygenase_C pfam00775
Dioxygenase;
46-197 5.17e-19

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 80.60  E-value: 5.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   46 GERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRQQQkavDPAFRgwGRTCSDfTSGIWRFETIKPGPV----V 121
Cdd:pfam00775  26 GEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDPTEAP---EPNFR--GRILTD-SQGSYRFRTIQPAPYpipnD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  122 GRDGRLMAP---------HVNLWVVARGINIgLNTRMYFA-DEHAAnasDPVLNLIewevrRKTLIAEREVR-----GTE 186
Cdd:pfam00775 100 GPTGKLLDAlgrhawrpaHIHFFISAPGHRR-LTTQLYFEgDPYLP---DDIAYAV-----RQGLVANYDERedgtpEKF 170
                         170
                  ....*....|.
gi 490245615  187 VVYRFDIHLQG 197
Cdd:pfam00775 171 LEYHFDFVLDG 181
 
Name Accession Description Interval E-value
protocat_alph TIGR02423
protocatechuate 3,4-dioxygenase, alpha subunit; This model represents the alpha chain of ...
8-206 1.07e-103

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: 296.98  E-value: 1.07e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615    8 TASQTAGPYVHIGLAPDAAGFhiFEKNFGPVLTTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRQQ 87
Cdd:TIGR02423   1 TPSQTVGPYVHIGLTPEQAGT--FTQEFGNNLVTPDADGERIRLEGRVLDGDGHPVPDALIEIWQADAAGRYNSPADLRA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   88 qKAVDPAFRGWGRTCSDfTSGIWRFETIKPGPVVGRDGRLMAPHVNLWVVARGINIGLNTRMYFADEHAANASDPVLNLI 167
Cdd:TIGR02423  79 -PATDPGFRGWGRTGTD-ESGEFTFETVKPGAVPDRDGVLQAPHINVSVFARGINRRLYTRLYFDDEAAANASDPVLALV 156
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 490245615  168 EwEVRRKTLIAEREVRGtEVVYRFDIHLQGENETVFFDI 206
Cdd:TIGR02423 157 P-AERRATLIAKRERDG-KVAYRFDIRLQGEGETVFFDV 193
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
5-205 9.43e-99

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: 284.16  E-value: 9.43e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   5 LPETASQTAGPYVHIGLAPdaagfhifEKNFGPVLTTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDD 84
Cdd:cd03463    1 LGETPSQTVGPYVHIGLPP--------TREGGNDLVPPDTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYAHPAD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  85 RqqQKAVDPAFRGWGRTCSDFtSGIWRFETIKPGPVVGRDGRLMAPHVNLWVVARGINIGLNTRMYFADEhAANASDPVL 164
Cdd:cd03463   73 S--RRRLDPGFRGFGRVATDA-DGRFSFTTVKPGAVPGRDGAGQAPHINVWVFARGLLKHLFTRIYFPDE-EANAADPVL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 490245615 165 NLiEWEVRRKTLIAEREVRGTevvYRFDIHLQGENETVFFD 205
Cdd:cd03463  149 AL-VPEERRATLIAKREGDGA---YRFDIRLQGEGETVFFD 185
3,4-PCD cd03459
Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3, ...
44-195 9.20e-70

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: 209.81  E-value: 9.20e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  44 TAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDrQQQKAVDPAFRGWGRTCSDFtSGIWRFETIKPGPVVGR 123
Cdd:cd03459   11 AIGERIILEGRVLDGDGRPVPDALVEIWQADAAGRYRHPRD-SHRAPLDPNFTGFGRVLTDA-DGRYRFRTIKPGAYPWR 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490245615 124 DGRLMAPHVNLWVVARGINIGLNTRMYFADEhAANASDPVLNLIeWEVRRKTLIAEREVRGTEVVYRFDIHL 195
Cdd:cd03459   89 NGAWRAPHIHVSVFARGLLERLVTRLYFPGD-PANAADPVLASV-PEERRETLIARRDGSDGALAYRFDIVL 158
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
7-201 6.07e-69

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


Pssm-ID: 442708  Cd Length: 171  Bit Score: 208.14  E-value: 6.07e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   7 ETASQTAGPYVHIGLaPDAAGFHIfeknfgpvltTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRq 86
Cdd:COG3485    1 ETPSQTEGPFYVDGL-PLPLGADL----------ARDAPGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDDG- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  87 qqkAVDPAFRGWGRTCSDfTSGIWRFETIKPGPVVGRDGRLMAPHVNLWVVARGInIGLNTRMYFADEhAANASDPVLNl 166
Cdd:COG3485   69 ---PLDPNFNGRGRFTTD-ADGRYRFRTIKPGPYPIPNHPGRPAHIHFSVFAPGF-ERLTTQLYFPGD-PYNASDPVFG- 141
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 490245615 167 iewevRRKTLIAEREVRGTEVVYRFDIHLQGENET 201
Cdd:COG3485  142 -----VRDTLIARFEPEDGALVYRFDIVLQGPGET 171
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
41-195 3.78e-47

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: 151.63  E-value: 3.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  41 TADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDrqqqKAVDPAFRGWGRTCSDFtSGIWRFETIKPGPV 120
Cdd:cd00421    4 TEDAPGEPLTLTGTVLDGDGCPVPDALVEIWQADADGRYSGQDD----SGLDPEFFLRGRQITDA-DGRYRFRTIKPGPY 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490245615 121 -VGRdgrlmAPHVNLWVVARGINIGLNTRMYFaDEHAANASDPVLNLIeWEVRRKTLIAEREvRGTEVVYRFDIHL 195
Cdd:cd00421   79 pIGR-----PPHIHFKVFAPGYNRRLTTQLYF-PGDPLNDSDPVFAPY-SENVRPTLIADFD-GIEFLEYRFDIVL 146
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
4-203 3.43e-37

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: 128.62  E-value: 3.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615    4 YLPETASQTAGP-YVHIGLAPDAAGfhifeknfgpvLTTADTA---GERITIEGRVIDGSGTPVRDVLLEIWQANAAGRY 79
Cdd:TIGR02422  23 SIPQSLSELTGPvFGHDDLGPIDND-----------LTLAHGGepiGERIIVHGRVLDEDGRPVPNTLVEVWQANAAGRY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   80 NHPDDrQQQKAVDPAFRGWGRTCSDfTSGIWRFETIKPGPVVGRDgrlmapHVNLW--------VVARGINIGLNTRMYF 151
Cdd:TIGR02422  92 RHKND-QYLAPLDPNFGGVGRTLTD-SDGYYRFRTIKPGPYPWGN------HHNAWrpahihfsLFGTSFAQRLITQMYF 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490245615  152 ADEHAAnASDPVLNLIEWEVRRKTLIAEREVRGTE----VVYRFDIHLQGENETVF 203
Cdd:TIGR02422 164 EGDPLI-AYDPIVNSIPDEAARERLIATLDLDNTIpmdaLGYRFDIVLRGRRATPF 218
3,4-PCD_beta cd03464
Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring ...
5-200 1.33e-34

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: 122.04  E-value: 1.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   5 LPETASQTAGP-YVHIGLAPdaaGFHIFEKNFGpvlttADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPD 83
Cdd:cd03464   29 IPHTLSELTGPvFGHDDLGP---LDNDLTRNHN-----GEPIGERIIVHGRVLDEDGRPVPNTLVEIWQANAAGRYRHKR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  84 DrQQQKAVDPAFRGWGRTCSDfTSGIWRFETIKPG--PVVGRDGRLMAPHVNLWVVARGINIGLNTRMYFADEHAAnASD 161
Cdd:cd03464  101 D-QHDAPLDPNFGGAGRTLTD-DDGYYRFRTIKPGayPWGNHPNAWRPAHIHFSLFGPSFATRLVTQMYFPGDPLI-PHD 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490245615 162 PVLNLIEWEVRRKTLIAEREVRGTE----VVYRFDIHLQGENE 200
Cdd:cd03464  178 PIYNSIPDEAARQRLIARFDLSATQpewaLGYRFDIVLRGRRA 220
Dioxygenase_C pfam00775
Dioxygenase;
46-197 5.17e-19

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 80.60  E-value: 5.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   46 GERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRQQQkavDPAFRgwGRTCSDfTSGIWRFETIKPGPV----V 121
Cdd:pfam00775  26 GEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDPTEAP---EPNFR--GRILTD-SQGSYRFRTIQPAPYpipnD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  122 GRDGRLMAP---------HVNLWVVARGINIgLNTRMYFA-DEHAAnasDPVLNLIewevrRKTLIAEREVR-----GTE 186
Cdd:pfam00775 100 GPTGKLLDAlgrhawrpaHIHFFISAPGHRR-LTTQLYFEgDPYLP---DDIAYAV-----RQGLVANYDERedgtpEKF 170
                         170
                  ....*....|.
gi 490245615  187 VVYRFDIHLQG 197
Cdd:pfam00775 171 LEYHFDFVLDG 181
Catechol_intradiol_dioxygenases cd03458
Catechol intradiol dioxygenases can be divided into several subgroups according to their ...
6-195 3.41e-12

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: 63.35  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615   6 PETASQTA--GPYvHIGLAPdaagfhifEKNFGPVLTTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPD 83
Cdd:cd03458   69 DTGGTESTilGPF-YVAGAP--------EVDNGATIDDDTADGEPLFVHGTVTDTDGKPLAGATVDVWHADPDGFYSQQD 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  84 DRQQqkavDPAFRGWGRTCSDftsGIWRFETIKP--------GPVvgrdGRLMA--------P-HVNLWVVARGINiGLN 146
Cdd:cd03458  140 PDQP----EFNLRGKFRTDED---GRYRFRTIRPvpypippdGPT----GELLEalgrhpwrPaHIHFMVSAPGYR-TLT 207
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490245615 147 TRMYFA-----DEHAANASDPVLnLIEWEVRRktliAEREVRGTEVVYRFDIHL 195
Cdd:cd03458  208 TQIYFEgdpylDDDAVFAVKDSL-IVDFVPVE----DGTGVPGPFAELDFDFVL 256
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
36-164 1.08e-10

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: 59.27  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  36 GPVLTTADTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRY-----NHPDDRqqqkavdpaFRGWGRTCSDftsGIW 110
Cdd:cd03462   87 GKLKTYDDDDHKPLLFRGTVKDLAGAPVAGAVIDVWHSTPDGKYsgfhpNIPEDY---------YRGKIRTDED---GRY 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490245615 111 RFETIKPGPV----VGRDGRLMA---------PHVNLWVVARGINIgLNTRMYF-----ADEHAANASDPVL 164
Cdd:cd03462  155 EVRTTVPVPYqipnDGPTGALLEamgghswrpAHVHFKVRADGYET-LTTQLYFeggewVDDDCCNGVKPEL 225
1,2-HQD cd03461
Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2, ...
43-195 5.47e-09

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: 54.55  E-value: 5.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  43 DTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYnhpdDRQQQKAVDPAFRGWGRTCSDftsGIWRFETIKP----- 117
Cdd:cd03461  115 GADGEPCFVHGRVTDTDGKPLPGATVDVWQADPNGLY----DVQDPDQPEFNLRGKFRTDED---GRYAFRTLRPtpypi 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615 118 ---GPVvgrdGRL--------MAP-HVNLWVVARGINiGLNTRMYFADEHAANaSDPVL----NLI-EWEVRRKTLIAER 180
Cdd:cd03461  188 ptdGPV----GKLlkamgrhpMRPaHIHFMVTAPGYR-TLVTQIFDSGDPYLD-SDAVFgvkdSLVvDFVPVEDDDAPGR 261
                        170
                 ....*....|....*
gi 490245615 181 EVRGTEVVYRFDIHL 195
Cdd:cd03461  262 LVPGADLELEYDFVL 276
1,2-CTD cd03460
Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to ...
43-196 8.10e-09

Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to form cis,cis-muconate. 1,2-CTDs is homodimers with one catalytic non-heme ferric ion per monomer. They belong to the aromatic dioxygenase family, a family of mononuclear non-heme iron intradiol-cleaving enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings.


Pssm-ID: 239543 [Multi-domain]  Cd Length: 282  Bit Score: 53.91  E-value: 8.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  43 DTAGERITIEGRVIDGSGTPVRDVLLEIWQANAAGRYNHPDDRQQqkavdpAFRGWGRTCSDfTSGIWRFETIKP----- 117
Cdd:cd03460  119 DDDGETLVMHGTVTDTDGKPVPGAKVEVWHANSKGFYSHFDPTQS------PFNLRRSIITD-ADGRYRFRSIMPsgygv 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615 118 ---GP------VVGRDGRLMApHVNLWVVARG-------INIGLNTrmYFADEHAANASDpvlNLIEwEVRRKTLIAERE 181
Cdd:cd03460  192 ppgGPtqqllnALGRHGNRPA-HIHFFVSAPGhrklttqINIEGDP--YIWDDFAFATRE---GLIP-EVVEVEDAAALK 264
                        170
                 ....*....|....*...
gi 490245615 182 VRGTEVVY---RFDIHLQ 196
Cdd:cd03460  265 QYGLDGPFaeiAFDFQLQ 282
intradiol_dioxygenase_like cd03457
Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage ...
50-154 2.65e-08

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: 51.50  E-value: 2.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245615  50 TIEGRVID-GSGTPVRDVLLEIWQANAAGRY--------NHPDDRQQQkavdpAFRGWGRTCSDftsGIWRFETIKPGPV 120
Cdd:cd03457   28 TLDLQVVDvATCCPPPNAAVDIWHCDATGVYsgysagggGGEDTDDET-----FLRGVQPTDAD---GVVTFTTIFPGWY 99
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490245615 121 VGRdgrlmAPHV------NLWVVARGINIGLNTRMYFADE 154
Cdd:cd03457  100 PGR-----ATHIhfkvhpDATSATSGGNVAHTGQLFFDED 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH