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Conserved domains on  [gi|664790455|gb|AIF53128|]
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2-oxoglutarate synthase [Pelosinus sp. UFO1]

Protein Classification

thiamine pyrophosphate-dependent enzyme( domain architecture ID 22)

thiamine pyrophosphate (TPP)-dependent enzyme uses thiamine pyrophosphate as a cofactor to catalyze various reactions including reversible decarboxylation

CATH:  3.40.50.1220
Gene Ontology:  GO:0030976|GO:0003824
PubMed:  12735696|15514159
SCOP:  3001790

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 ...
 6-237 1.08e-103

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: 301.29  E-value: 1.08e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455   6 FARPDSLVDVATHYCPGCQHGIIHRLVAEVIDELEIQKTAIGVVPVGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHP 85
Cdd:COG1013    2 LKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  86 DKVVFTYQGDGDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGrqssSAGWPIRLSEML 165
Cdd:COG1013   82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664790455 166 ATlDGAKFIARVCVNDPANMAKaktAIKTAFQvqirGEGFAMVEVLATCPTNWGKSPIEAKKWLKENMIPQF 237
Cdd:COG1013  158 AA-HGATYVARASVGDPKDLKK---KIKKAIE----HKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMWPLY 221
 
Name Accession Description Interval E-value
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 6-237 1.08e-103

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: 301.29  E-value: 1.08e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455   6 FARPDSLVDVATHYCPGCQHGIIHRLVAEVIDELEIQKTAIGVVPVGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHP 85
Cdd:COG1013    2 LKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  86 DKVVFTYQGDGDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGrqssSAGWPIRLSEML 165
Cdd:COG1013   82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664790455 166 ATlDGAKFIARVCVNDPANMAKaktAIKTAFQvqirGEGFAMVEVLATCPTNWGKSPIEAKKWLKENMIPQF 237
Cdd:COG1013  158 AA-HGATYVARASVGDPKDLKK---KIKKAIE----HKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMWPLY 221
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 19-217 7.78e-80

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: 238.19  E-value: 7.78e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  19 YCPGCQHGIIHRLVAEVIDELEIQKTAIGVV-PVGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHPDKVVFTYQGDGD 97
Cdd:cd03375    1 WCPGCGDGSILKALAKALAELGIDPEKVVVVsGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  98 AAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSSAGwPIRLSEMLatldGAKFIARV 177
Cdd:cd03375   81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFN-PLALALAA----GATFVARG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 664790455 178 CVNDPanmAKAKTAIKTAfqvqIRGEGFAMVEVLATCPTN 217
Cdd:cd03375  156 FSGDI---KQLKEIIKKA----IQHKGFSFVEVLSPCPTF 188
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 20-235 1.61e-53

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 174.68  E-value: 1.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  20 CPGCQHGIIHRLVAEVIDELEIQKTAIGVVP-VGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHPDKVVFTYQGDGDA 98
Cdd:PRK05778  21 CPGCGNFGILNAIIQALAELGLDPDKVVVVSgIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVVGGDGDL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  99 AAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSsagwPIRLSEmLATLDGAKFIARVC 178
Cdd:PRK05778 101 ASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEP----PIDPCA-LALAAGATFVARSF 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664790455 179 VNDPANMakaKTAIKTAfqvqIRGEGFAMVEVLATCPTNWG-----KSPIEAKKWLKENMIP 235
Cdd:PRK05778 176 AGDVKQL---VELIKKA----ISHKGFAFIDVLSPCVTFNGrntstKSPAYMREYYKKRVYK 230
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
68-210 2.08e-17

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 76.47  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455   68 AAHGRAPAVATGIKRVHPDKVVFTYQGDGDAAAIGTaEMVHAAARGERITAIFVNNAIYGMTGGQlapTTLVDQVTATSP 147
Cdd:pfam02775  28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVVVLNNGGYGMTRGQ---QTPFGGGRYSGP 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664790455  148 YGRQSSsagwPIRLsEMLATLDGAKFIArvcVNDPANMAKaktAIKTAFQvqirGEGFAMVEV 210
Cdd:pfam02775 104 SGKILP----PVDF-AKLAEAYGAKGAR---VESPEELEE---ALKEALE----HDGPALIDV 151
 
Name Accession Description Interval E-value
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 6-237 1.08e-103

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: 301.29  E-value: 1.08e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455   6 FARPDSLVDVATHYCPGCQHGIIHRLVAEVIDELEIQKTAIGVVPVGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHP 85
Cdd:COG1013    2 LKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  86 DKVVFTYQGDGDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGrqssSAGWPIRLSEML 165
Cdd:COG1013   82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG----KPEPPKDPAEIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664790455 166 ATlDGAKFIARVCVNDPANMAKaktAIKTAFQvqirGEGFAMVEVLATCPTNWGKSPIEAKKWLKENMIPQF 237
Cdd:COG1013  158 AA-HGATYVARASVGDPKDLKK---KIKKAIE----HKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMWPLY 221
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 19-217 7.78e-80

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: 238.19  E-value: 7.78e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  19 YCPGCQHGIIHRLVAEVIDELEIQKTAIGVV-PVGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHPDKVVFTYQGDGD 97
Cdd:cd03375    1 WCPGCGDGSILKALAKALAELGIDPEKVVVVsGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  98 AAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSSAGwPIRLSEMLatldGAKFIARV 177
Cdd:cd03375   81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFN-PLALALAA----GATFVARG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 664790455 178 CVNDPanmAKAKTAIKTAfqvqIRGEGFAMVEVLATCPTN 217
Cdd:cd03375  156 FSGDI---KQLKEIIKKA----IQHKGFSFVEVLSPCPTF 188
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 20-235 1.61e-53

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 174.68  E-value: 1.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  20 CPGCQHGIIHRLVAEVIDELEIQKTAIGVVP-VGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHPDKVVFTYQGDGDA 98
Cdd:PRK05778  21 CPGCGNFGILNAIIQALAELGLDPDKVVVVSgIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVVGGDGDL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  99 AAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSsagwPIRLSEmLATLDGAKFIARVC 178
Cdd:PRK05778 101 ASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEP----PIDPCA-LALAAGATFVARSF 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664790455 179 VNDPANMakaKTAIKTAfqvqIRGEGFAMVEVLATCPTNWG-----KSPIEAKKWLKENMIP 235
Cdd:PRK05778 176 AGDVKQL---VELIKKA----ISHKGFAFIDVLSPCVTFNGrntstKSPAYMREYYKKRVYK 230
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 1-235 1.90e-50

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 166.17  E-value: 1.90e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455   1 MVEKLFARPDSLVDVATHYCPGCQHGIIHRLVAEVIDELEIQKTAIGVVP-VGCSV-LAYnYFNVDTQQAAHGRAPAVAT 78
Cdd:PRK11867   1 MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSgIGCSGrLPG-YINTYGFHTIHGRALAIAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  79 GIKRVHPDKVVFTYQGDGDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGrqssSAGWP 158
Cdd:PRK11867  80 GLKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYG----SIEPP 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664790455 159 IRLSEmLATLDGAKFIARVCVNDPANMAKaktAIKTAfqvqIRGEGFAMVEVLATCPTNwgkSPIEAKKWLKENMIP 235
Cdd:PRK11867 156 FNPVE-LALGAGATFVARGFDSDVKQLTE---LIKAA----INHKGFSFVEILQPCPTF---NNVNTFDWFKERLVK 221
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 19-243 5.42e-37

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 131.42  E-value: 5.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  19 YCPGCQHGIIHRLVAEVIDELEIQKTAIGVVP-VGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHPDKVVFTYQGDGD 97
Cdd:PRK11866   9 WCPGCGNYGILEALRKALAELGIPPENVVVVSgIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  98 AAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSSAGwPIRLseMLATldGAKFIARV 177
Cdd:PRK11866  89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFN-PIAL--ALAA--GATFVARG 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664790455 178 CVNDPANMakaKTAIKTAfqvqIRGEGFAMVEVLATCPTnwgkspieakkWLKENMIPQFPLNVYK 243
Cdd:PRK11866 164 FSGDVKHL---KEIIKEA----IKHKGFSFIDVLSPCVT-----------FNKLNTYDWFRPRVYK 211
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
17-236 2.95e-36

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 129.47  E-value: 2.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  17 THYCPGCQHGIIHRLVAEVIDELEIQKTAIGVVP-VGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHPDKVVFTYQGD 95
Cdd:PRK09628  16 TLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSgIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  96 GDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSssagwPIRLSEMLATLDGAKFIA 175
Cdd:PRK09628  96 GDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNID-----PTFDACKLATAAGASFVA 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664790455 176 RVCVNDPANMAKaktAIKTAFQvqirGEGFAMVEVLATCPTNWGK-----SPIEAKKWLKENMIPQ 236
Cdd:PRK09628 171 RESVIDPQKLEK---LLVKGFS----HKGFSFFDVFSNCHINLGRknkmgEAVQMLKWIESRTVSK 229
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 8-232 5.86e-27

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 104.86  E-value: 5.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455   8 RPDSLvDVAthYCPGCQHGIIHRLVAEVIDELEIQKTAIGVVP-VGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRVHPD 86
Cdd:PRK11869   2 RPEKY-DIA--WCPGCGNFGIRNALMKALSELNLKPRQVVIVSgIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  87 KVVFTYQGDGDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSSAGwPIRLSEMLa 166
Cdd:PRK11869  79 LTVIAEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFN-PIALAIAL- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664790455 167 tldGAKFIARVCVNDpanMAKAKTAIKTAfqvqIRGEGFAMVEVLATCPTNwgkSPIEAKKWLKEN 232
Cdd:PRK11869 157 ---DASFVARTFSGD---IEETKEILKEA----IKHKGLAIVDIFQPCVSF---NKVNTYQWYREN 209
PRK11865 PRK11865
pyruvate synthase subunit beta;
20-222 6.97e-23

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 94.39  E-value: 6.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  20 CPGCQHGIIHRLVAEVIDELEIQKTAIGVVPVGCSVLAYNYFNVDTQQAAHGRAPAVATGI----KRVHPDKVVFTYQGD 95
Cdd:PRK11865  21 CAGCGAAIAMRLALKALGKNTVIVVATGCLEVITTPYPETAWNVPWIHVAFENAAAVASGIeravKALGKKVNVVAIGGD 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  96 GDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSSAGWPIRLSEMLATLDGAKFIA 175
Cdd:PRK11865 101 GGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRGEDRPKKNMPLIMAAHGIPYVA 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 664790455 176 RVCVNDPAN-MAKAKTAIKTafqvqirgEGFAMVEVLATCPTNWGKSP 222
Cdd:PRK11865 181 TASIGYPEDfMEKVKKAKEV--------EGPAYIQVLQPCPTGWGFPP 220
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 20-237 6.80e-22

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: 90.62  E-value: 6.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  20 CPGCQHGIIHRLVAEVIDELE--IQKTAIGVVPVGCSVLAYNYFNVDTQQAAHGRAPAVATGIKRV-------------H 84
Cdd:cd02018    8 CAGCGEVTAVRVVLAALPAPEdtVIANSTGCSSVYASTAPFNSWAVPWVNSLFEDANAVASGLKRGlkarfpkdreldkK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  85 PDKVVFTyqGDGDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSSagwpIRLSEM 164
Cdd:cd02018   88 KDVVVIG--GDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDK----KDLVLI 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 664790455 165 LATlDGAKFIARVCVNDPANMAKAKTAIKTAFqvqirgEGFAMVEVLATCPTNWG----KSPIEAKKWLKENMIPQF 237
Cdd:cd02018  162 AAT-HGCVYVARLSPALKKHFLKVVKEAISRT------DGPTFIHAYTPCITEWGigsgKSLELARKAVKSRMFPLF 231
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 20-219 3.47e-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: 85.75  E-value: 3.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  20 CPGCQHGIIHRLVAEVIDEleiqKTAIgVVPVGCSVLA-----YNYFNVDTQQAAHGRAPAVATGIKRV-----HPDKV- 88
Cdd:cd03376    8 CAGCGAALALRHVLKALGP----DTVV-VNPTGCLEVIttpypYTAWRVPWIHVAFENAAAVASGIEAAlkalgRGKDIt 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  89 VFTYQGDGDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSSSAGWPIRLSEMLATL 168
Cdd:cd03376   83 VVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSFGKKQPKKDLPLIMAA 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 664790455 169 DGAKFIARVCVNDPANM-AKAKTAIKTafqvqirgEGFAMVEVLATCPTNWG 219
Cdd:cd03376  163 HNIPYVATASVAYPEDLyKKVKKALSI--------EGPAYIHILSPCPTGWR 206
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
68-210 2.08e-17

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 76.47  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455   68 AAHGRAPAVATGIKRVHPDKVVFTYQGDGDAAAIGTaEMVHAAARGERITAIFVNNAIYGMTGGQlapTTLVDQVTATSP 147
Cdd:pfam02775  28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVVVLNNGGYGMTRGQ---QTPFGGGRYSGP 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664790455  148 YGRQSSsagwPIRLsEMLATLDGAKFIArvcVNDPANMAKaktAIKTAFQvqirGEGFAMVEV 210
Cdd:pfam02775 104 SGKILP----PVDF-AKLAEAYGAKGAR---VESPEELEE---ALKEALE----HDGPALIDV 151
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
20-244 1.35e-13

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 68.58  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  20 CPGCQHGIIHRLVAEVIDEleiqKTaIGVVPVGCS-VLA----YNYFNVDTQQAAHGRAPAVATGIKRV-----HPDKVV 89
Cdd:PRK11864  21 CPGCGAPLGLRYLLKALGE----KT-VLVIPASCStVIQgdtpKSPLTVPVLHTAFAATAAVASGIEEAlkargEKGVIV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  90 FTYQGDGDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSPYGRQSssagWPIRLSEMLATlD 169
Cdd:PRK11864  96 VGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKRE----HKKPVPDIMAA-H 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664790455 170 GAKFIARVCVNDPANM-AKAKTAIKTafqvqirgEGFAMVEVLATCPTNWGKSP---IEAKKWLKENMIpqFPLNVYKN 244
Cdd:PRK11864 171 KVPYVATASIAYPEDFiRKLKKAKEI--------RGFKFIHLLAPCPPGWRFDPdktIEIARLAVETGV--WPLFEYEN 239
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 18-198 8.31e-07

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: 47.66  E-value: 8.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  18 HYCPGCQHgiihRLVAEVIDELEIQKTAIGVvPVGCSVLAYN--YFNVDTQqAAHGRAPAVATGIKRVHPDKVVFTYQGD 95
Cdd:cd02008    5 GLCPGCPH----RPSFYALRKAFKKDSIVSG-DIGCYTLGALppLNAIDTC-TCMGASIGVAIGMAKASEDKKVVAVIGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  96 GDAAAIGTAEMVHAAARGERITAIFVNNAIYGMTGGQLAPTTLVDQVTATSpygrqsssagwPIRLSEMLATLDgakfIA 175
Cdd:cd02008   79 STFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTT-----------VIDIEALVRAIG----VK 143

                        170       180
                 ....*....|....*....|...
gi 664790455 176 RVCVNDPANMAKAKTAIKTAFQV 198
Cdd:cd02008  144 RVVVVDPYDLKAIREELKEALAV 166
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 57-197 6.37e-06

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: 45.38  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  57 AYNYFNVDtqqaAHGRAPAVATGIKRVHPDKVVFTYqgDGDAAAI---GTAEMVhAAARGERITAIFVNNAIYGMTGGQl 133
Cdd:cd03371   41 AQDFLTVG----SMGHASQIALGIALARPDRKVVCI--DGDGAALmhmGGLATI-GGLAPANLIHIVLNNGAHDSVGGQ- 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664790455 134 aPTTLVD----QVTATSPYgRQSSSAGWPIRLSEMLATL---DGAKFIA-RVCVNDPANMAKAKT---AIKTAFQ 197
Cdd:cd03371  113 -PTVSFDvslpAIAKACGY-RAVYEVPSLEELVAALAKAlaaDGPAFIEvKVRPGSRSDLGRPTTspiENKERFM 185
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 61-132 1.40e-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: 44.17  E-value: 1.40e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664790455  61 FNVDTQQAAHGRAPAVATGIKRVHPDKVVFTYQGDGDAAAIGtAEMVHAAARGERITAIFVNNAIYGMTGGQ 132
Cdd:cd00568   39 FLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMMTG-QELATAVRYGLPVIVVVFNNGGYGTIRMH 109
PRK06163 PRK06163
hypothetical protein; Provisional
 71-205 2.44e-04

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 40.97  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664790455  71 GRAPAVATGIKRVHPDKVVFTYQGDGD----AAAIGTAemvhAAARGERITAIFVNNAIYGMTGGQLAPT-TLVDQVTAT 145
Cdd:PRK06163  60 GLAFPIALGVALAQPKRRVIALEGDGSllmqLGALGTI----AALAPKNLTIIVMDNGVYQITGGQPTLTsQTVDVVAIA 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 664790455 146 SPYGRQSSSagWPI------RLSEMLATLDGAKFIARVCVNDPANMAKAKTAiktafqVQIRgEGF 205
Cdd:PRK06163 136 RGAGLENSH--WAAdeahfeALVDQALSGPGPSFIAVRIDDKPGVGTTERDP------AQIR-ERF 192
 
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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