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Conserved domains on  [gi|1088342800|gb|OHB91225|]
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2-oxoglutarate oxidoreductase [Planctomycetes bacterium RIFCSPHIGHO2_02_FULL_52_58]

Protein Classification

thiamine pyrophosphate-dependent enzyme; pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha( domain architecture ID 10130132)

thiamine pyrophosphate (TPP)-dependent enzyme uses thiamine pyrophosphate as a cofactor to catalyze various reactions including reversible decarboxylation| pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha is part of the thiamine pyrophosphate-dependent enzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 5-243 9.50e-104

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


:

Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 301.68  E-value: 9.50e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800   5 YSAPETLIRTPSHYCPGCGHGIAHRLLAEIIDELGIRGKTIGLAPVGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHP 84
Cdd:COG1013     2 LKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  85 DNIVFTYQGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGrdplTHGYPIRICELL 164
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800 165 ATLeGASFLARTSLSSPKDVsqtKEALKKGfktqIEKKGFSLIEVLSPCPVYWRMSPVESLKFIEEKM------------ 232
Cdd:COG1013   158 AAH-GATYVARASVGDPKDL---KKKIKKA----IEHKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMwplyeydpgekl 229

                         250
                  ....*....|....*..
gi 1088342800 233 ------TQTFPLGVFKD 243
Cdd:COG1013   230 rltyepKDKIPVGEFLK 246
 
Name Accession Description Interval E-value
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 5-243 9.50e-104

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 301.68  E-value: 9.50e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800   5 YSAPETLIRTPSHYCPGCGHGIAHRLLAEIIDELGIRGKTIGLAPVGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHP 84
Cdd:COG1013     2 LKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  85 DNIVFTYQGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGrdplTHGYPIRICELL 164
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800 165 ATLeGASFLARTSLSSPKDVsqtKEALKKGfktqIEKKGFSLIEVLSPCPVYWRMSPVESLKFIEEKM------------ 232
Cdd:COG1013   158 AAH-GATYVARASVGDPKDL---KKKIKKA----IEHKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMwplyeydpgekl 229

                         250
                  ....*....|....*..
gi 1088342800 233 ------TQTFPLGVFKD 243
Cdd:COG1013   230 rltyepKDKIPVGEFLK 246
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 18-241 9.36e-84

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.


Pssm-ID: 239470 [Multi-domain]  Cd Length: 193  Bit Score: 248.59  E-value: 9.36e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  18 YCPGCGHGIAHRLLAEIIDELGI-RGKTIGLAPVGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHPDNIVFTYQGDGD 96
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIdPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  97 LAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGRDPlthgYPIRICElLATLEGASFLART 176
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIE----EPFNPLA-LALAAGATFVARG 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1088342800 177 SLSspkDVSQTKEALKKGfktqIEKKGFSLIEVLSPCPvywrmspveslkfieekmtqTFPLGVF 241
Cdd:cd03375   156 FSG---DIKQLKEIIKKA----IQHKGFSFVEVLSPCP--------------------TFPLGVF 193
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 13-216 9.86e-59

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 188.55  E-value: 9.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  13 RTPSHYCPGCGHGIAHRLLAEIIDELGI-RGKTIGLAPVGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHPDNIVFTY 91
Cdd:PRK05778   15 GLPTTWCPGCGNFGILNAIIQALAELGLdPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  92 QGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGrdplTHGYPIRICELLATLeGAS 171
Cdd:PRK05778   95 GGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYG----NIEPPIDPCALALAA-GAT 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1088342800 172 FLARtSLSSpkDVSQTKEALKKGfktqIEKKGFSLIEVLSPCPVY 216
Cdd:PRK05778  170 FVAR-SFAG--DVKQLVELIKKA----ISHKGFAFIDVLSPCVTF 207
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
67-209 1.95e-21

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 87.26  E-value: 1.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  67 AAHGRPPAIATGIKRVHPDNIVFTYQGDGDLAAIGMaEIVHAASRAENITVIFINNAIYGMTNGQlapTTLLNQRTTTTP 146
Cdd:pfam02775  28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVVVLNNGGYGMTRGQ---QTPFGGGRYSGP 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1088342800 147 EGRDplthGYPIRICELLATLeGASFLartSLSSPKDVsqtKEALKKGfktqIEKKGFSLIEV 209
Cdd:pfam02775 104 SGKI----LPPVDFAKLAEAY-GAKGA---RVESPEEL---EEALKEA----LEHDGPALIDV 151
 
Name Accession Description Interval E-value
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 5-243 9.50e-104

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 301.68  E-value: 9.50e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800   5 YSAPETLIRTPSHYCPGCGHGIAHRLLAEIIDELGIRGKTIGLAPVGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHP 84
Cdd:COG1013     2 LKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  85 DNIVFTYQGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGrdplTHGYPIRICELL 164
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800 165 ATLeGASFLARTSLSSPKDVsqtKEALKKGfktqIEKKGFSLIEVLSPCPVYWRMSPVESLKFIEEKM------------ 232
Cdd:COG1013   158 AAH-GATYVARASVGDPKDL---KKKIKKA----IEHKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMwplyeydpgekl 229

                         250
                  ....*....|....*..
gi 1088342800 233 ------TQTFPLGVFKD 243
Cdd:COG1013   230 rltyepKDKIPVGEFLK 246
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 18-241 9.36e-84

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.


Pssm-ID: 239470 [Multi-domain]  Cd Length: 193  Bit Score: 248.59  E-value: 9.36e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  18 YCPGCGHGIAHRLLAEIIDELGI-RGKTIGLAPVGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHPDNIVFTYQGDGD 96
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIdPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  97 LAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGRDPlthgYPIRICElLATLEGASFLART 176
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIE----EPFNPLA-LALAAGATFVARG 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1088342800 177 SLSspkDVSQTKEALKKGfktqIEKKGFSLIEVLSPCPvywrmspveslkfieekmtqTFPLGVF 241
Cdd:cd03375   156 FSG---DIKQLKEIIKKA----IQHKGFSFVEVLSPCP--------------------TFPLGVF 193
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 13-216 9.86e-59

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 188.55  E-value: 9.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  13 RTPSHYCPGCGHGIAHRLLAEIIDELGI-RGKTIGLAPVGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHPDNIVFTY 91
Cdd:PRK05778   15 GLPTTWCPGCGNFGILNAIIQALAELGLdPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  92 QGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGrdplTHGYPIRICELLATLeGAS 171
Cdd:PRK05778   95 GGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYG----NIEPPIDPCALALAA-GAT 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1088342800 172 FLARtSLSSpkDVSQTKEALKKGfktqIEKKGFSLIEVLSPCPVY 216
Cdd:PRK05778  170 FVAR-SFAG--DVKQLVELIKKA----ISHKGFAFIDVLSPCVTF 207
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 17-233 1.58e-54

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 177.34  E-value: 1.58e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  17 HYCPGCGHGIAHRLLAEIIDELGI-RGKTIGLAPVGCSV-LAYnYLDIDMCEAAHGRPPAIATGIKRVHPDNIVFTYQGD 94
Cdd:PRK11867   18 RWCPGCGDGSILAALQRALAELGLdPENVAVVSGIGCSGrLPG-YINTYGFHTIHGRALAIATGLKLANPDLTVIVVTGD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  95 GDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGrdplTHGYPIRICElLATLEGASFLA 174
Cdd:PRK11867   97 GDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYG----SIEPPFNPVE-LALGAGATFVA 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1088342800 175 RTsLSSpkDVSQTKEALKKGfktqIEKKGFSLIEVLSPCPVYwrmSPVESLKFIEEKMT 233
Cdd:PRK11867  172 RG-FDS--DVKQLTELIKAA----INHKGFSFVEILQPCPTF---NNVNTFDWFKERLV 220
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 18-217 6.47e-38

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 134.11  E-value: 6.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  18 YCPGCGHGIAHRLLAEIIDELGIRGKTIGLAP-VGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHPDNIVFTYQGDGD 96
Cdd:PRK11866    9 WCPGCGNYGILEALRKALAELGIPPENVVVVSgIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  97 LAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGR--DPLThgyPIriceLLATLEGASFLA 174
Cdd:PRK11866   89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNieEPFN---PI----ALALAAGATFVA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1088342800 175 RtSLSSpkDVSQTKEALKKGfktqIEKKGFSLIEVLSPCpVYW 217
Cdd:PRK11866  162 R-GFSG--DVKHLKEIIKEA----IKHKGFSFIDVLSPC-VTF 196
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
15-242 5.22e-36

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 129.08  E-value: 5.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  15 PSHYCPGCGHGIAHRLLAEIIDELGIRGKTIGLAP-VGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHPDNIVFTYQG 93
Cdd:PRK09628   15 PTLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSgIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  94 DGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGR-DPlthgyPIRICElLATLEGASF 172
Cdd:PRK09628   95 DGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNiDP-----TFDACK-LATAAGASF 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800 173 LARTSLSSPKDVSQTkeaLKKGFktqiEKKGFSLIEVLSPCPVYW----RM-SPVESLKFI---------------EEKM 232
Cdd:PRK09628  169 VARESVIDPQKLEKL---LVKGF----SHKGFSFFDVFSNCHINLgrknKMgEAVQMLKWIesrtvskrkfdalspEERV 241

                         250
                  ....*....|
gi 1088342800 233 TQtFPLGVFK 242
Cdd:PRK09628  242 GK-FPTGILK 250
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 18-248 4.82e-34

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 124.12  E-value: 4.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  18 YCPGCGHGIAHRLLAEIIDELGIRGKTIGL-APVGCSVLAYNYLDIDMCEAAHGRPPAIATGIKRVHPDNIVFTYQGDGD 96
Cdd:PRK11869   10 WCPGCGNFGIRNALMKALSELNLKPRQVVIvSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAEGGDGD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  97 LAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEG--RDPLThgyPIRicelLATLEGASFLA 174
Cdd:PRK11869   90 MYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGvfEEPFN---PIA----LAIALDASFVA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800 175 RTSLSspkDVSQTKEALKKGfktqIEKKGFSLIEVLSPCPVYWRMSPVE-----------------SLKFIEEKMTQTFP 237
Cdd:PRK11869  163 RTFSG---DIEETKEILKEA----IKHKGLAIVDIFQPCVSFNKVNTYQwyrentyylkdhdptdrELAFKRALETEKLP 235

                         250
                  ....*....|.
gi 1088342800 238 LGVFKDWEKTV 248
Cdd:PRK11869  236 LGIFYINEKPT 246
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
19-242 3.06e-22

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 92.85  E-value: 3.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  19 CPGCGHGIAHRLLAEIIDElgirgKTIGLAPVGCS-VLA----YNYLDIDMCEAAHGRPPAIATGIKRV-----HPDNIV 88
Cdd:PRK11864   21 CPGCGAPLGLRYLLKALGE-----KTVLVIPASCStVIQgdtpKSPLTVPVLHTAFAATAAVASGIEEAlkargEKGVIV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  89 FTYQGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGRDPlthgyPIRICELLATLE 168
Cdd:PRK11864   96 VGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKRE-----HKKPVPDIMAAH 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800 169 GASFLARTSLSSPKDVsqtKEALKKGFKTqiekKGFSLIEVLSPCPVYWRMSP---VESLKFIEEkmTQTFPL-----GV 240
Cdd:PRK11864  171 KVPYVATASIAYPEDF---IRKLKKAKEI----RGFKFIHLLAPCPPGWRFDPdktIEIARLAVE--TGVWPLfeyenGK 241


                  ..
gi 1088342800 241 FK 242
Cdd:PRK11864  242 FK 243
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
67-209 1.95e-21

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 87.26  E-value: 1.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  67 AAHGRPPAIATGIKRVHPDNIVFTYQGDGDLAAIGMaEIVHAASRAENITVIFINNAIYGMTNGQlapTTLLNQRTTTTP 146
Cdd:pfam02775  28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVVVLNNGGYGMTRGQ---QTPFGGGRYSGP 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1088342800 147 EGRDplthGYPIRICELLATLeGASFLartSLSSPKDVsqtKEALKKGfktqIEKKGFSLIEV 209
Cdd:pfam02775 104 SGKI----LPPVDFAKLAEAY-GAKGA---RVESPEEL---EEALKEA----LEHDGPALIDV 151
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 14-238 1.27e-20

Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.


Pssm-ID: 239471 [Multi-domain]  Cd Length: 235  Bit Score: 87.29  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  14 TPSH-YCPGCGHGIAHRLLAEIIDElgirgKTIGLAPVGCSVLA-----YNYLDIDMCEAAHGRPPAIATGIKRV----- 82
Cdd:cd03376     2 APGHrACAGCGAALALRHVLKALGP-----DTVVVNPTGCLEVIttpypYTAWRVPWIHVAFENAAAVASGIEAAlkalg 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  83 -HPDNIVFTYQGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGRDPLTHGYPIRIC 161
Cdd:cd03376    77 rGKDITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSFGKKQPKKDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088342800 162 ELLATLEGASFLARTSLSSPKDvsqtkeaLKKGFKTQIEKKGFSLIEVLSPCPVYWRMSPVESLKfIEEKMTQT--FPL 238
Cdd:cd03376   157 PLIMAAHNIPYVATASVAYPED-------LYKKVKKALSIEGPAYIHILSPCPTGWRFDPSKTIE-IARLAVETgfWPL 227
PRK11865 PRK11865
pyruvate synthase subunit beta;
15-221 6.23e-19

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 83.99  E-value: 6.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  15 PSHY-CPGCGHGIAHRLLAEIIDElgirgKTIGLAPVGCSVL--------AYNYLDIDMC-EAAhgrpPAIATGI----K 80
Cdd:PRK11865   16 PGHRaCAGCGAAIAMRLALKALGK-----NTVIVVATGCLEVittpypetAWNVPWIHVAfENA----AAVASGIeravK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  81 RVHPDNIVFTYQGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGRDPLTHGYPIRI 160
Cdd:PRK11865   87 ALGKKVNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRGEDRPKKN 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1088342800 161 CELLATLEGASFLARTSLSSPKD-VSQTKEALkkgfktqiEKKGFSLIEVLSPCPVYWRMSP 221
Cdd:PRK11865  167 MPLIMAAHGIPYVATASIGYPEDfMEKVKKAK--------EVEGPAYIQVLQPCPTGWGFPP 220
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 19-217 2.21e-18

Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238976 [Multi-domain]  Cd Length: 237  Bit Score: 81.38  E-value: 2.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  19 CPGCGHGIAHRLlaeIIDELGIRGKTIGLAPVGCSVLA-----YNYLDIDMCEAAHGRPPAIATGIKRV----------- 82
Cdd:cd02018     8 CAGCGEVTAVRV---VLAALPAPEDTVIANSTGCSSVYastapFNSWAVPWVNSLFEDANAVASGLKRGlkarfpkdrel 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  83 --HPDNIVFTyqGDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTP----EGRDPLThgy 156
Cdd:cd02018    85 dkKKDVVVIG--GDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPagkkEDKKDLV--- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1088342800 157 piriceLLATLEGASFLARTSLSSPKDVSQT-KEALKKGFktqiekkGFSLIEVLSPCPVYW 217
Cdd:cd02018   160 ------LIAATHGCVYVARLSPALKKHFLKVvKEAISRTD-------GPTFIHAYTPCITEW 208
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 15-213 3.44e-11

Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.


Pssm-ID: 238966 [Multi-domain]  Cd Length: 178  Bit Score: 60.37  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  15 PSHYCPGCGHgiahRLLAEIIDeLGIRGKTIGLAPVGCSVLAYN--YLDIDMCeAAHGRPPAIATGIKRVHPDNIVFTYQ 92
Cdd:cd02008     3 PPGLCPGCPH----RPSFYALR-KAFKKDSIVSGDIGCYTLGALppLNAIDTC-TCMGASIGVAIGMAKASEDKKVVAVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  93 GDGDLAAIGMAEIVHAASRAENITVIFINNAIYGMTNGQLAPTTLLNQRTTTTPEGRDPLTHGypiricellatlEGASF 172
Cdd:cd02008    77 GDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTVIDIEALVRA------------IGVKR 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1088342800 173 LARTslsSPKDVSQTKEALKKgfktQIEKKGFSLIEVLSPC 213
Cdd:cd02008   145 VVVV---DPYDLKAIREELKE----ALAVPGVSVIIAKRPC 178
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 72-209 5.90e-05

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 42.24  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088342800  72 PPAiATGIKRVHPDNIVFTYQGDGDLAAiGMAEIVHAASRAENITVIFINNAIYGMTNGQlapttllnQRTTTtpEGRDP 151
Cdd:cd00568    52 LPA-AIGAALAAPDRPVVCIAGDGGFMM-TGQELATAVRYGLPVIVVVFNNGGYGTIRMH--------QEAFY--GGRVS 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1088342800 152 LTHGYPIRICELLATLEGASFLARtslsspkdvsqTKEALKKGFKTQIEKKGFSLIEV 209
Cdd:cd00568   120 GTDLSNPDFAALAEAYGAKGVRVE-----------DPEDLEAALAEALAAGGPALIEV 166
PRK06163 PRK06163
hypothetical protein; Provisional
 75-135 5.12e-04

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 40.20  E-value: 5.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1088342800  75 IATGIKRVHPDNIVFTYQGDGDL-AAIGMAEIVhAASRAENITVIFINNAIYGMTNGQLAPT 135
Cdd:PRK06163   65 IALGVALAQPKRRVIALEGDGSLlMQLGALGTI-AALAPKNLTIIVMDNGVYQITGGQPTLT 125
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 74-136 1.70e-03

Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.


Pssm-ID: 239468 [Multi-domain]  Cd Length: 188  Bit Score: 38.45  E-value: 1.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1088342800  74 AIATGIKRVHPDNIVFTYQGDGdlAAI----GMAEIvhAASRAENITVIFINNAIYGMTNGQlaPTT 136
Cdd:cd03371    55 QIALGIALARPDRKVVCIDGDG--AALmhmgGLATI--GGLAPANLIHIVLNNGAHDSVGGQ--PTV 115
PRK08199 PRK08199
thiamine pyrophosphate protein; Validated
 70-126 2.95e-03

thiamine pyrophosphate protein; Validated


Pssm-ID: 181285 [Multi-domain]  Cd Length: 557  Bit Score: 38.70  E-value: 2.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1088342800  70 GRPPAIATgiKRVHPDNIVFTYQGDGDLAAIGmAEIVHAASRAENITVIFINNAIYG 126
Cdd:PRK08199  420 GLPAAIAA--KLLFPERTVVAFAGDGCFLMNG-QELATAVQYGLPIIVIVVNNGMYG 473
 
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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