NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1712639084|gb|QDU65846|]
View 

2-oxoglutarate oxidoreductase subunit KorA [Planctomycetes bacterium Pla133]

Protein Classification

2-oxoacid:acceptor oxidoreductase subunit alpha( domain architecture ID 11497501)

2-oxoacid:acceptor oxidoreductase subunit alpha such as Mycobacterium tuberculosis 2-oxoglutarate oxidoreductase subunit KorA, which is a component of the enzyme that catalyzes the CoA-dependent oxidative decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
OAFO_sf TIGR03710
2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a ...
18-613 0e+00

2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a C-terminal thiamine diphosphate (TPP) binding domain typical of flavodoxin/ferredoxin oxidoreductases (pfam01855) as well as an N-terminal domain similar to the gamma subunit of the same group of oxidoreductases (pfam01558). The genes represented by this model are always found in association with a neighboring gene for a beta subunit (TIGR02177) which also occurs in a 4-subunit (alpha/beta/gamma/ferredoxin) version of the system. This alpha/gamma plus beta structure was used to define the set of sequences to include in this model. This pair of genes is not consistantly observed in proximity to any electron acceptor genes, but is found next to putative ferredoxins or ferredoxin-domain proteins in Azoarcus sp. EbN1, Bradyrhizobium japonicum USDA 110, Frankia sp. CcI3, Rhodoferax ferrireducens DSM 15236, Rhodopseudomonas palustris BisB5, Os, Sphingomonas wittichii RW1 and Streptomyces clavuligerus. Other potential acceptors are also sporadically observed in close proximity including ferritin-like proteins, reberythrin, peroxiredoxin and a variety of other flavin and iron-sulfur cluster-containing proteins. The phylogenetic distribution of this family encompasses archaea, a number of deeply-branching bacterial clades and only a small number of firmicutes and proteobacteria. The enzyme from Sulfolobus has been characterized with respect to its substrate specificity, which is described as wide, encompassing various 2-oxoacids such as 2-oxoglutarate, 2-oxobutyrate and pyruvate. The enzyme from Hydrogenobacter thermophilus has been shown to have a high specificity towards 2-oxoglutarate and is one of the key enzymes in the reverse TCA cycle in this organism. Furthermore, considering its binding of coenzyme A, it can be reasonably inferred that the product of the reaction is succinyl-CoA. The genes for this enzyme in Prevotella intermedia 17, Persephonella marina EX-H1 and Picrophilus torridus DSM 9790 are in close proximity to a variety of TCA cycle genes. Persephonella marina and P. torridus are believed to encode complete TCA cycles, and none of these contains the lipoate-based 2-oxoglutarate dehydrogenase (E1/E2/E3) system. That system is presumed to be replaced by this one. In fact, the lipoate system is absent in most organisms possessing a member of this family, providing additional circumstantial evidence that many of these enzymes are capable of acting as 2-oxoglutarate dehydrogenases and


:

Pssm-ID: 274738 [Multi-domain]  Cd Length: 562  Bit Score: 723.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  18 SVVIRFAGDSGDGMQITGNQFTSTSAAVGNDLATLPDFPAEIRApvgtrpGVSGFQVRFSSSDIHTPGDAPDVLVAMNPA 97
Cdd:TIGR03710   1 DVVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRG------GHSYFQIRISDEPVRSPGDGVDVLVALNPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  98 ALVVNLKDLKPGGMVILNTGNWKELDLKKARCatdprqdgtldgyrtIEIDINERVKQAltesglspKDVQRCKNFYTLG 177
Cdd:TIGR03710  75 TLKEHLDELRPGGIIIYDSDLFDEEDLEKARV---------------IPVPLTEIAKEA--------KGRKRMKNMVALG 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 178 LMYWLYSRPLEPTLNWLAKKFAKKPDLVAANQTALKAGFNAGdiHEHFQTRYDVPPcTTLEPGTYRNIMGNQALSIGLVA 257
Cdd:TIGR03710 132 ALAALLGLDLEPLEEVIREKFGKKPEIAEANLKALRAGYDYA--EETEKTDYLVLP-APPKDGDRILISGNEAIALGAIA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 258 GAQLagldiFLGSYPITPASDILHELAGF-KNFGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGPGMALKTEAMGLAI 336
Cdd:TIGR03710 209 GGLR-----FLAAYPITPATDILHFLAKHlKKFGVVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAG 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 337 ATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQYMTPVILLSDGYIA 416
Cdd:TIGR03710 284 MTETPLVIVDVQRGGPSTGLPTKTEQSDLLFALYGGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLA 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 417 NGSEPWRLPEMESLKAFPVTF-HTATEGFSPVARDEKLARPWAIPGTPGLEHRIGGLEKDgDTGNISYDAHNHERMSHLR 495
Cdd:TIGR03710 364 NSYATVPPPDLDDLPAIDRGKvLEPEEEYKRYELTEDGISPRAIPGTPGGIHRATGLEHD-ETGHISEDPENRVKMMEKR 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 496 AQKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPM-AKGLDGIFSRFRTVLVPE 574
Cdd:TIGR03710 443 ARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGAIREAVERLRAEGIKVALLHLRLLYPFpKNELAELLEGAKKVIVVE 522
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 1712639084 575 LN-MGQMCRLLRSEFPKHDFASYPKVQGLPFATHELVERI 613
Cdd:TIGR03710 523 QNaTGQLAKLLRAETGIVKVRSILKYDGRPFTPEEIVEAI 562
 
Name Accession Description Interval E-value
OAFO_sf TIGR03710
2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a ...
18-613 0e+00

2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a C-terminal thiamine diphosphate (TPP) binding domain typical of flavodoxin/ferredoxin oxidoreductases (pfam01855) as well as an N-terminal domain similar to the gamma subunit of the same group of oxidoreductases (pfam01558). The genes represented by this model are always found in association with a neighboring gene for a beta subunit (TIGR02177) which also occurs in a 4-subunit (alpha/beta/gamma/ferredoxin) version of the system. This alpha/gamma plus beta structure was used to define the set of sequences to include in this model. This pair of genes is not consistantly observed in proximity to any electron acceptor genes, but is found next to putative ferredoxins or ferredoxin-domain proteins in Azoarcus sp. EbN1, Bradyrhizobium japonicum USDA 110, Frankia sp. CcI3, Rhodoferax ferrireducens DSM 15236, Rhodopseudomonas palustris BisB5, Os, Sphingomonas wittichii RW1 and Streptomyces clavuligerus. Other potential acceptors are also sporadically observed in close proximity including ferritin-like proteins, reberythrin, peroxiredoxin and a variety of other flavin and iron-sulfur cluster-containing proteins. The phylogenetic distribution of this family encompasses archaea, a number of deeply-branching bacterial clades and only a small number of firmicutes and proteobacteria. The enzyme from Sulfolobus has been characterized with respect to its substrate specificity, which is described as wide, encompassing various 2-oxoacids such as 2-oxoglutarate, 2-oxobutyrate and pyruvate. The enzyme from Hydrogenobacter thermophilus has been shown to have a high specificity towards 2-oxoglutarate and is one of the key enzymes in the reverse TCA cycle in this organism. Furthermore, considering its binding of coenzyme A, it can be reasonably inferred that the product of the reaction is succinyl-CoA. The genes for this enzyme in Prevotella intermedia 17, Persephonella marina EX-H1 and Picrophilus torridus DSM 9790 are in close proximity to a variety of TCA cycle genes. Persephonella marina and P. torridus are believed to encode complete TCA cycles, and none of these contains the lipoate-based 2-oxoglutarate dehydrogenase (E1/E2/E3) system. That system is presumed to be replaced by this one. In fact, the lipoate system is absent in most organisms possessing a member of this family, providing additional circumstantial evidence that many of these enzymes are capable of acting as 2-oxoglutarate dehydrogenases and


Pssm-ID: 274738 [Multi-domain]  Cd Length: 562  Bit Score: 723.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  18 SVVIRFAGDSGDGMQITGNQFTSTSAAVGNDLATLPDFPAEIRApvgtrpGVSGFQVRFSSSDIHTPGDAPDVLVAMNPA 97
Cdd:TIGR03710   1 DVVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRG------GHSYFQIRISDEPVRSPGDGVDVLVALNPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  98 ALVVNLKDLKPGGMVILNTGNWKELDLKKARCatdprqdgtldgyrtIEIDINERVKQAltesglspKDVQRCKNFYTLG 177
Cdd:TIGR03710  75 TLKEHLDELRPGGIIIYDSDLFDEEDLEKARV---------------IPVPLTEIAKEA--------KGRKRMKNMVALG 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 178 LMYWLYSRPLEPTLNWLAKKFAKKPDLVAANQTALKAGFNAGdiHEHFQTRYDVPPcTTLEPGTYRNIMGNQALSIGLVA 257
Cdd:TIGR03710 132 ALAALLGLDLEPLEEVIREKFGKKPEIAEANLKALRAGYDYA--EETEKTDYLVLP-APPKDGDRILISGNEAIALGAIA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 258 GAQLagldiFLGSYPITPASDILHELAGF-KNFGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGPGMALKTEAMGLAI 336
Cdd:TIGR03710 209 GGLR-----FLAAYPITPATDILHFLAKHlKKFGVVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAG 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 337 ATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQYMTPVILLSDGYIA 416
Cdd:TIGR03710 284 MTETPLVIVDVQRGGPSTGLPTKTEQSDLLFALYGGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLA 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 417 NGSEPWRLPEMESLKAFPVTF-HTATEGFSPVARDEKLARPWAIPGTPGLEHRIGGLEKDgDTGNISYDAHNHERMSHLR 495
Cdd:TIGR03710 364 NSYATVPPPDLDDLPAIDRGKvLEPEEEYKRYELTEDGISPRAIPGTPGGIHRATGLEHD-ETGHISEDPENRVKMMEKR 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 496 AQKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPM-AKGLDGIFSRFRTVLVPE 574
Cdd:TIGR03710 443 ARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGAIREAVERLRAEGIKVALLHLRLLYPFpKNELAELLEGAKKVIVVE 522
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 1712639084 575 LN-MGQMCRLLRSEFPKHDFASYPKVQGLPFATHELVERI 613
Cdd:TIGR03710 523 QNaTGQLAKLLRAETGIVKVRSILKYDGRPFTPEEIVEAI 562
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
240-618 1.84e-137

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


Pssm-ID: 440438 [Multi-domain]  Cd Length: 372  Bit Score: 405.62  E-value: 1.84e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 240 GTYRNIMGNQALSIGLVAgaqlAGLDiFLGSYPITPASDILHELAGFK-NFGVRTFQAEDEIAAICSAIGASFAGHLGLT 318
Cdd:COG0674     1 GKRVLMDGNEAVALGAIA----AGCR-VIAAYPITPSTEIAEYLAEWLaELGGVVVQAESEIAAIGAVIGASAAGARAMT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 319 TTSGPGMALKTEAMGLAIATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVR 398
Cdd:COG0674    76 ATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQALYGGHGDTGWIVLAPSSVQEAFDLTIIAFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 399 IAVQYMTPVILLSDGYIANGSEPWRLPEMESLKAFPvtfhtATEGFSPVARDEklaRPWAIPGTPGLEHRIGGLEKDgdt 478
Cdd:COG0674   156 LAEKYRVPVIVLFDGFLGSHEEPVELPDDEEVKILP-----RPEEYRPYALDE---DPRAIPGTAQPDVYFTGLEHD--- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 479 gnISYDAHNHERMSHLRAQKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPM-A 557
Cdd:COG0674   225 --ETEDPENAEKMVEKRMRKFEKIRDELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFpA 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712639084 558 KGLDGIFSRFRTVLVPELNM-GQMCRLLRSEFPKHDFA-SYPKVQGLPFATHELVERIEDLLK 618
Cdd:COG0674   303 EALREALKGVKKVAVVERNKsGQLALDVRAALGADRVVgGIYGLGGRPFTPEEILAVIEELLK 365
PRK08659 PRK08659
2-oxoacid:acceptor oxidoreductase subunit alpha;
245-617 7.78e-74

2-oxoacid:acceptor oxidoreductase subunit alpha;


Pssm-ID: 181526 [Multi-domain]  Cd Length: 376  Bit Score: 241.30  E-value: 7.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 245 IMGNQALsiglVAGAQLAGLDIFLGsYPITPASDILHELAG-FKNFGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGP 323
Cdd:PRK08659    7 LQGNEAC----AEGAIAAGCRFFAG-YPITPSTEIAEVMAReLPKVGGVFIQMEDEIASMAAVIGASWAGAKAMTATSGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 324 GMALKTEAMGLAIATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQY 403
Cdd:PRK08659   82 GFSLMQENIGYAAMTETPCVIVNVQRGGPSTGQPTKPAQGDMMQARWGTHGDHPIIALSPSSVQECFDLTIRAFNLAEKY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 404 MTPVILLSDGYIANGSEPWRLPEMESLKAFPVTFHTAT-EGFSPVARDEKLARPWAIPGTpGLEHRIGGLEKDgDTGNIS 482
Cdd:PRK08659  162 RTPVIVLADEVVGHMREKVVLPEPDEIEIIERKLPKVPpEAYKPFDDPEGGVPPMPAFGD-GYRFHVTGLTHD-ERGFPT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 483 YDAHNHERMSHLRAQKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPMA-KGLD 561
Cdd:PRK08659  240 TDPETHEKLVRRLVRKIEKNRDDIVLYEEYMLEDAEVVVVAYGSVARSARRAVKEAREEGIKVGLFRLITVWPFPeEAIR 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1712639084 562 GIFSRFRTVLVPELNMGQMCRLL-RSEFPKHDFASYPKVQGLPFATHELVERIEDLL 617
Cdd:PRK08659  320 ELAKKVKAIVVPEMNLGQMSLEVeRVVNGRAKVEGINKIGGELITPEEILEKIKEVA 376
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
258-473 1.16e-57

Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N terminal structural domain of the pyruvate ferredoxin oxidoreductase. This domain binds thiamine diphosphate, and along with domains II and IV, is involved in inter subunit contacts. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited.


Pssm-ID: 396432  Cd Length: 230  Bit Score: 193.63  E-value: 1.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 258 GAQLAGLDiFLGSYPITPASDILHELAGFK-NFGVRT---FQAEDEIAAICSAIGASFAGHLGLTTTSGPGMALKTEAMG 333
Cdd:pfam01855   1 AAIAAGVD-VIAAYPITPSSEIAEEAAEWAaNGEKGDvvvIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 334 LAIATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVlgrngDAPMPVVSCSTPSDCFETAIEAVRIAVQYMTPVILLSDG 413
Cdd:pfam01855  80 KAAGERLPVVIHVVARAGPSPGLSIFGDHSDVMAAR-----DTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712639084 414 YIA-NGSEPWRLPEMESLKA----FPVTFHTATEGFSPvarDEKLARPWAIPGTPGLEHRIGGLE 473
Cdd:pfam01855 155 FRTsHEREKVELPPDEDEKDlideFLPPYKRKRYGLDP---EMPIARGTAQNPDTYFEHREYGNP 216
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
247-413 4.85e-55

Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.


Pssm-ID: 132917 [Multi-domain]  Cd Length: 160  Bit Score: 183.86  E-value: 4.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 247 GNQALSIGLVAgaqlAGLDiFLGSYPITPASDILHELAGFKN--FGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGPG 324
Cdd:cd07034     1 GNEAVARGALA----AGVD-VVAAYPITPSTEIAETLAKAVLgeLGGVVVQAESEHAAAEAAIGASAAGARAMTATSGPG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 325 MALKTEAMGLAIATELPLVIVDIQRAGPSTGMPtKTEQSDLYQAvlgRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQYM 404
Cdd:cd07034    76 LNLMAEALYLAAGAELPLVIVVAQRPGPSTGLP-KPDQSDLMAA---RYGGHPWPVLAPSSVQEAFDLALEAFELAEKYR 151

                  ....*....
gi 1712639084 405 TPVILLSDG 413
Cdd:cd07034   152 LPVIVLSDG 160
 
Name Accession Description Interval E-value
OAFO_sf TIGR03710
2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a ...
18-613 0e+00

2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a C-terminal thiamine diphosphate (TPP) binding domain typical of flavodoxin/ferredoxin oxidoreductases (pfam01855) as well as an N-terminal domain similar to the gamma subunit of the same group of oxidoreductases (pfam01558). The genes represented by this model are always found in association with a neighboring gene for a beta subunit (TIGR02177) which also occurs in a 4-subunit (alpha/beta/gamma/ferredoxin) version of the system. This alpha/gamma plus beta structure was used to define the set of sequences to include in this model. This pair of genes is not consistantly observed in proximity to any electron acceptor genes, but is found next to putative ferredoxins or ferredoxin-domain proteins in Azoarcus sp. EbN1, Bradyrhizobium japonicum USDA 110, Frankia sp. CcI3, Rhodoferax ferrireducens DSM 15236, Rhodopseudomonas palustris BisB5, Os, Sphingomonas wittichii RW1 and Streptomyces clavuligerus. Other potential acceptors are also sporadically observed in close proximity including ferritin-like proteins, reberythrin, peroxiredoxin and a variety of other flavin and iron-sulfur cluster-containing proteins. The phylogenetic distribution of this family encompasses archaea, a number of deeply-branching bacterial clades and only a small number of firmicutes and proteobacteria. The enzyme from Sulfolobus has been characterized with respect to its substrate specificity, which is described as wide, encompassing various 2-oxoacids such as 2-oxoglutarate, 2-oxobutyrate and pyruvate. The enzyme from Hydrogenobacter thermophilus has been shown to have a high specificity towards 2-oxoglutarate and is one of the key enzymes in the reverse TCA cycle in this organism. Furthermore, considering its binding of coenzyme A, it can be reasonably inferred that the product of the reaction is succinyl-CoA. The genes for this enzyme in Prevotella intermedia 17, Persephonella marina EX-H1 and Picrophilus torridus DSM 9790 are in close proximity to a variety of TCA cycle genes. Persephonella marina and P. torridus are believed to encode complete TCA cycles, and none of these contains the lipoate-based 2-oxoglutarate dehydrogenase (E1/E2/E3) system. That system is presumed to be replaced by this one. In fact, the lipoate system is absent in most organisms possessing a member of this family, providing additional circumstantial evidence that many of these enzymes are capable of acting as 2-oxoglutarate dehydrogenases and


Pssm-ID: 274738 [Multi-domain]  Cd Length: 562  Bit Score: 723.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  18 SVVIRFAGDSGDGMQITGNQFTSTSAAVGNDLATLPDFPAEIRApvgtrpGVSGFQVRFSSSDIHTPGDAPDVLVAMNPA 97
Cdd:TIGR03710   1 DVVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRG------GHSYFQIRISDEPVRSPGDGVDVLVALNPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  98 ALVVNLKDLKPGGMVILNTGNWKELDLKKARCatdprqdgtldgyrtIEIDINERVKQAltesglspKDVQRCKNFYTLG 177
Cdd:TIGR03710  75 TLKEHLDELRPGGIIIYDSDLFDEEDLEKARV---------------IPVPLTEIAKEA--------KGRKRMKNMVALG 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 178 LMYWLYSRPLEPTLNWLAKKFAKKPDLVAANQTALKAGFNAGdiHEHFQTRYDVPPcTTLEPGTYRNIMGNQALSIGLVA 257
Cdd:TIGR03710 132 ALAALLGLDLEPLEEVIREKFGKKPEIAEANLKALRAGYDYA--EETEKTDYLVLP-APPKDGDRILISGNEAIALGAIA 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 258 GAQLagldiFLGSYPITPASDILHELAGF-KNFGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGPGMALKTEAMGLAI 336
Cdd:TIGR03710 209 GGLR-----FLAAYPITPATDILHFLAKHlKKFGVVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAG 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 337 ATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQYMTPVILLSDGYIA 416
Cdd:TIGR03710 284 MTETPLVIVDVQRGGPSTGLPTKTEQSDLLFALYGGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLA 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 417 NGSEPWRLPEMESLKAFPVTF-HTATEGFSPVARDEKLARPWAIPGTPGLEHRIGGLEKDgDTGNISYDAHNHERMSHLR 495
Cdd:TIGR03710 364 NSYATVPPPDLDDLPAIDRGKvLEPEEEYKRYELTEDGISPRAIPGTPGGIHRATGLEHD-ETGHISEDPENRVKMMEKR 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 496 AQKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPM-AKGLDGIFSRFRTVLVPE 574
Cdd:TIGR03710 443 ARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGAIREAVERLRAEGIKVALLHLRLLYPFpKNELAELLEGAKKVIVVE 522
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|
gi 1712639084 575 LN-MGQMCRLLRSEFPKHDFASYPKVQGLPFATHELVERI 613
Cdd:TIGR03710 523 QNaTGQLAKLLRAETGIVKVRSILKYDGRPFTPEEIVEAI 562
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
240-618 1.84e-137

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


Pssm-ID: 440438 [Multi-domain]  Cd Length: 372  Bit Score: 405.62  E-value: 1.84e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 240 GTYRNIMGNQALSIGLVAgaqlAGLDiFLGSYPITPASDILHELAGFK-NFGVRTFQAEDEIAAICSAIGASFAGHLGLT 318
Cdd:COG0674     1 GKRVLMDGNEAVALGAIA----AGCR-VIAAYPITPSTEIAEYLAEWLaELGGVVVQAESEIAAIGAVIGASAAGARAMT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 319 TTSGPGMALKTEAMGLAIATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVR 398
Cdd:COG0674    76 ATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQALYGGHGDTGWIVLAPSSVQEAFDLTIIAFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 399 IAVQYMTPVILLSDGYIANGSEPWRLPEMESLKAFPvtfhtATEGFSPVARDEklaRPWAIPGTPGLEHRIGGLEKDgdt 478
Cdd:COG0674   156 LAEKYRVPVIVLFDGFLGSHEEPVELPDDEEVKILP-----RPEEYRPYALDE---DPRAIPGTAQPDVYFTGLEHD--- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 479 gnISYDAHNHERMSHLRAQKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPM-A 557
Cdd:COG0674   225 --ETEDPENAEKMVEKRMRKFEKIRDELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFpA 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712639084 558 KGLDGIFSRFRTVLVPELNM-GQMCRLLRSEFPKHDFA-SYPKVQGLPFATHELVERIEDLLK 618
Cdd:COG0674   303 EALREALKGVKKVAVVERNKsGQLALDVRAALGADRVVgGIYGLGGRPFTPEEILAVIEELLK 365
PRK08659 PRK08659
2-oxoacid:acceptor oxidoreductase subunit alpha;
245-617 7.78e-74

2-oxoacid:acceptor oxidoreductase subunit alpha;


Pssm-ID: 181526 [Multi-domain]  Cd Length: 376  Bit Score: 241.30  E-value: 7.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 245 IMGNQALsiglVAGAQLAGLDIFLGsYPITPASDILHELAG-FKNFGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGP 323
Cdd:PRK08659    7 LQGNEAC----AEGAIAAGCRFFAG-YPITPSTEIAEVMAReLPKVGGVFIQMEDEIASMAAVIGASWAGAKAMTATSGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 324 GMALKTEAMGLAIATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQY 403
Cdd:PRK08659   82 GFSLMQENIGYAAMTETPCVIVNVQRGGPSTGQPTKPAQGDMMQARWGTHGDHPIIALSPSSVQECFDLTIRAFNLAEKY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 404 MTPVILLSDGYIANGSEPWRLPEMESLKAFPVTFHTAT-EGFSPVARDEKLARPWAIPGTpGLEHRIGGLEKDgDTGNIS 482
Cdd:PRK08659  162 RTPVIVLADEVVGHMREKVVLPEPDEIEIIERKLPKVPpEAYKPFDDPEGGVPPMPAFGD-GYRFHVTGLTHD-ERGFPT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 483 YDAHNHERMSHLRAQKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPMA-KGLD 561
Cdd:PRK08659  240 TDPETHEKLVRRLVRKIEKNRDDIVLYEEYMLEDAEVVVVAYGSVARSARRAVKEAREEGIKVGLFRLITVWPFPeEAIR 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1712639084 562 GIFSRFRTVLVPELNMGQMCRLL-RSEFPKHDFASYPKVQGLPFATHELVERIEDLL 617
Cdd:PRK08659  320 ELAKKVKAIVVPEMNLGQMSLEVeRVVNGRAKVEGINKIGGELITPEEILEKIKEVA 376
oorA PRK09627
2-oxoglutarate synthase subunit alpha;
267-616 3.03e-62

2-oxoglutarate synthase subunit alpha;


Pssm-ID: 182002 [Multi-domain]  Cd Length: 375  Bit Score: 210.72  E-value: 3.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 267 FLGSYPITPASDILHELAG-FKNFGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGPGMALKTEAMGLAIATELPLVIV 345
Cdd:PRK09627   23 FFGGYPITPSSEIAHEMSVlLPKCGGTFIQMEDEISGISVALGASMSGVKSMTASSGPGISLKAEQIGLGFIAEIPLVIV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 346 DIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQYMTPVILLSDGYIANGSEPWRLP 425
Cdd:PRK09627  103 NVMRGGPSTGLPTRVAQGDVNQAKNPTHGDFKSIALAPGSLEEAYTETVRAFNLAERFMTPVFLLLDETVGHMYGKAVIP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 426 EMESLKAFPV---TFHTATEGFSP--VARDEKlarpwAI--PGTPGLEHRIGGLEKdGDTGNISYDA----HNHERMshl 494
Cdd:PRK09627  183 DLEEVQKMIInrkEFDGDKKDYKPygVAQDEP-----AVlnPFFKGYRYHVTGLHH-GPIGFPTEDAkicgKLIDRL--- 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 495 rAQKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPM-AKGLDGIFSRFRTVLVP 573
Cdd:PRK09627  254 -FNKIESHQDEIEEYEEYMLDDAEILIIAYGSVSLSAKEAIKRLREEGIKVGLFRPITLWPSpAKKLKEIGDKFEKILVI 332
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1712639084 574 ELNMGQMCRLLRSEFPKHDFASYPKVQGLPFATHELVERIEDL 616
Cdd:PRK09627  333 ELNMGQYLEEIERVMQRDDFHFLGKANGRPISPSEIIAKVKEL 375
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
258-473 1.16e-57

Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N terminal structural domain of the pyruvate ferredoxin oxidoreductase. This domain binds thiamine diphosphate, and along with domains II and IV, is involved in inter subunit contacts. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited.


Pssm-ID: 396432  Cd Length: 230  Bit Score: 193.63  E-value: 1.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 258 GAQLAGLDiFLGSYPITPASDILHELAGFK-NFGVRT---FQAEDEIAAICSAIGASFAGHLGLTTTSGPGMALKTEAMG 333
Cdd:pfam01855   1 AAIAAGVD-VIAAYPITPSSEIAEEAAEWAaNGEKGDvvvIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 334 LAIATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVlgrngDAPMPVVSCSTPSDCFETAIEAVRIAVQYMTPVILLSDG 413
Cdd:pfam01855  80 KAAGERLPVVIHVVARAGPSPGLSIFGDHSDVMAAR-----DTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712639084 414 YIA-NGSEPWRLPEMESLKA----FPVTFHTATEGFSPvarDEKLARPWAIPGTPGLEHRIGGLE 473
Cdd:pfam01855 155 FRTsHEREKVELPPDEDEKDlideFLPPYKRKRYGLDP---EMPIARGTAQNPDTYFEHREYGNP 216
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
247-413 4.85e-55

Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.


Pssm-ID: 132917 [Multi-domain]  Cd Length: 160  Bit Score: 183.86  E-value: 4.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 247 GNQALSIGLVAgaqlAGLDiFLGSYPITPASDILHELAGFKN--FGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGPG 324
Cdd:cd07034     1 GNEAVARGALA----AGVD-VVAAYPITPSTEIAETLAKAVLgeLGGVVVQAESEHAAAEAAIGASAAGARAMTATSGPG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 325 MALKTEAMGLAIATELPLVIVDIQRAGPSTGMPtKTEQSDLYQAvlgRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQYM 404
Cdd:cd07034    76 LNLMAEALYLAAGAELPLVIVVAQRPGPSTGLP-KPDQSDLMAA---RYGGHPWPVLAPSSVQEAFDLALEAFELAEKYR 151

                  ....*....
gi 1712639084 405 TPVILLSDG 413
Cdd:cd07034   152 LPVIVLSDG 160
PRK07119 PRK07119
2-ketoisovalerate ferredoxin reductase; Validated
247-580 3.52e-49

2-ketoisovalerate ferredoxin reductase; Validated


Pssm-ID: 235942 [Multi-domain]  Cd Length: 352  Bit Score: 174.66  E-value: 3.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 247 GNQALSIGLVAgaqlAGLDIFLGsYPITPASDILHELAGFKNFGVRTF-QAEDEIAAICSAIGASFAGHLGLTTTSGPGM 325
Cdd:PRK07119    9 GNEAIAEAAIR----AGCRCYFG-YPITPQSEIPEYMSRRLPEVGGVFvQAESEVAAINMVYGAAATGKRVMTSSSSPGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 326 ALKTEAMGLAIATELPLVIVDIQRAGPSTG--MPtktEQSDLYQAVLGR-NGDAPMPVVSCSTPSDCFETAIEAVRIAVQ 402
Cdd:PRK07119   84 SLKQEGISYLAGAELPCVIVNIMRGGPGLGniQP---SQGDYFQAVKGGgHGDYRLIVLAPSSVQEMVDLTMLAFDLADK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 403 YMTPVILLSDGYIANGSEPWRLPEMeslkafpvtfhtategfspvARDEKLARPWAIPGTPGLEHRI--------GGLEK 474
Cdd:PRK07119  161 YRNPVMVLGDGVLGQMMEPVEFPPR--------------------KKRPLPPKDWAVTGTKGRRKNIitslfldpEELEK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 475 dgdtgnisydaHNHermsHLRAqKVMNVQETIPDPEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAvhLRHI- 553
Cdd:PRK07119  221 -----------HNL----RLQE-KYAKIEENEVRYEEYNTEDAELVLVAYGTSARIAKSAVDMAREEGIKVGL--FRPIt 282
                         330       340
                  ....*....|....*....|....*....
gi 1712639084 554 -WPM-AKGLDGIFSRFRTVLVPELNMGQM 580
Cdd:PRK07119  283 lWPFpEKALEELADKGKGFLSVEMSMGQM 311
PorG COG1014
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma ...
21-464 8.67e-30

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


Pssm-ID: 440638 [Multi-domain]  Cd Length: 424  Bit Score: 122.11  E-value: 8.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  21 IRFAGDSGDGMQITGNQFTSTSAAVGNDLATLPDFPAEIRapvGtrpGVSGFQVRFSSSDIHTP-GDAPDVLVAMNPAAL 99
Cdd:COG1014     7 IRIAGVGGQGVVTAGKILAKAAMREGYYVQGYPSYGSEQR---G---GPVVSHVRISDEPIRSPlIDEADVLIALDPEEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 100 VVNLKDLKPGGMVILNTgnwkelDLKKARCATDPRQDGTLDGYRTIEIDINERVKQALTESglspkdvqRCKN------- 172
Cdd:COG1014    81 DRVLDGLKPGGVLIVNS------SLVPPEVWRLPQEALERKDIRVYVIDATKIAKELLGNA--------RVANtvmlgal 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 173 FYTLGLmywlysrPLEPTLNWLAKKFAKK-PDLVAANQTALKAGFNAgdIHEHFqtryDVPPcttlEPGTYRNIMGNQAL 251
Cdd:COG1014   147 AALLGL-------PLEALEEAIEETFGKKgEKVVELNLKAFEAGYEA--AKEVF----ALAA----APAPLVLLAGNAAA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 252 SIGLVAGAQLAGldiflGSYPITPASDILHELAGFKN-FGVRTFQAEDEIAAICSAIGASFAGHLGLTTTSGPGMALKTE 330
Cdd:COG1014   210 ALGAAAGGAAFA-----AAYPITPSTSLIEAAAAAAAkVGGVVAEEEAAAAAAAAAAAAAAAGAAAAAAGGGGGAALATE 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 331 AMGLAIATELPLVIVDIQRAGPSTGMPTKTEQSDLYQAVLGRNGDAPMPVVSCSTPSDCFETAIEAVRIAVQYMTPVILL 410
Cdd:COG1014   285 GLGLAGMTETPVVAVAAPRPGPGTGTPTEEEQGLLLLAAGGGGGEAPALALAPDTEEELLFAAAAAFALAEYAQALLLLL 364
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1712639084 411 SDGYIANGSEPWRLPEMESLKAFPVTFHTATEGFSPVARDEKLARPWAIPGTPG 464
Cdd:COG1014   365 LLQLLVLLLTDLLLLLLDLLRRRAGLGAEEAEARRKLLAAEGRAARAAGGGGGG 418
POR pfam01558
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large ...
28-217 1.09e-22

Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large protein pyruvate-flavodoxin oxidoreductase and the whole pyruvate ferredoxin oxidoreductase gamma subunit protein. It is not known whether the gamma subunit has a catalytic or regulatory role. Pyruvate oxidoreductase (POR) catalyzes the final step in the fermentation of carbohydrates in anaerobic microorganizms. This involves the oxidative decarboxylation of pyruvate with the participation of thiamine followed by the transfer of an acetyl moiety to coenzyme A for the synthesis of acetyl-CoA. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited.


Pssm-ID: 426323 [Multi-domain]  Cd Length: 172  Bit Score: 95.45  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  28 GDGMQITGNQFTSTSAAVGNDLATLPDFPAEIRApvgtrpGVSGFQVRFSSSDI--HTPGDAPDVLVAMNPAALVVNLKD 105
Cdd:pfam01558   2 GQGVVTAGKILAKAAARAGYYVQATPEYGSEIRG------GPVVSHVRISDEPIvpAIPVGEADLLVALDPETLDRHLDG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 106 LKPGGMVILNTGNWKELDLKKARCATDPRQdgtldgyRTIEIDINERVKQALtesglspkDVQRCKNFYTLGLMYWLYSR 185
Cdd:pfam01558  76 LKPGGIIIYNSSEVPPELLEKDLPAYPRLA-------RVYGVPATEIAKEAG--------GNSRAANTVMLGALAALLGL 140
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1712639084 186 PLEPTLNWLAKKFAKKPDLVAANQTALKAGFN 217
Cdd:pfam01558 141 PLEALEEAIKKRFPGKAKVIELNLKAFRAGYE 172
vorA PRK08366
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed
268-563 3.35e-11

2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed


Pssm-ID: 169406 [Multi-domain]  Cd Length: 390  Bit Score: 65.40  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 268 LGSYPITPASDILHELAGFKNFGVRTFQ---AEDEIAAICSAIGASFAGHLGLTTTSGPGMALKTEAMGLAIATELPLVI 344
Cdd:PRK08366   24 VAAYPITPQTSIIEKIAEFIANGEADIQyvpVESEHSAMAACIGASAAGARAFTATSAQGLALMHEMLHWAAGARLPIVM 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 345 VDIQRAGPstgmPTKTEQSDLYQAVLGRngDAPMPVVSCSTPSDCFETAIEAVRIAVQYMTPVILLSDGYIAngSEPWRL 424
Cdd:PRK08366  104 VDVNRAMA----PPWSVWDDQTDSLAQR--DTGWMQFYAENNQEVYDGVLMAFKVAETVNLPAMVVESAFIL--SHTYDV 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 425 PEM---ESLKAF-----PVtfHTATEGFSPVArdeklarpwaipgtpglehrIGGLEKDGDTGNISYD-AHNHErmshlR 495
Cdd:PRK08366  176 VEMipqELVDEFlpprkPL--YSLADFDNPIS--------------------VGALATPADYYEFRYKiAKAME-----E 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 496 AQKVM-------------NVQETIpdpEVFGAESGDVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWP------- 555
Cdd:PRK08366  229 AKKVIkevgkefgerfgrDYSQMI---ETYYTDDADFVFMGMGSLMGTVKEAVDLLRKEGYKVGYAKVRWFRPfpkeely 305

                  ....*....
gi 1712639084 556 -MAKGLDGI 563
Cdd:PRK08366  306 eIAESVKGI 314
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
247-415 6.05e-08

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 55.16  E-value: 6.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 247 GNQALSIGLvagaQLAGLDIfLGSYPITPASDILHELAGFKNFGV---RTFQAEDEIAAICSAIGASFAGHLGLTTTSGP 323
Cdd:PRK09622   15 GNTAASNAL----RQAQIDV-VAAYPITPSTPIVQNYGSFKANGYvdgEFVMVESEHAAMSACVGAAAAGGRVATATSSQ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084 324 GMALKTEAMGLAIATELPLVIVDIQRAGPSTgMPTKTEQSDLYqavLGRngDAPMPVVSCSTPSDCFETAIEAVRIAVQY 403
Cdd:PRK09622   90 GLALMVEVLYQASGMRLPIVLNLVNRALAAP-LNVNGDHSDMY---LSR--DSGWISLCTCNPQEAYDFTLMAFKIAEDQ 163
                         170
                  ....*....|....
gi 1712639084 404 MT--PVILLSDGYI 415
Cdd:PRK09622  164 KVrlPVIVNQDGFL 177
PFOR_II pfam17147
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ...
518-580 1.67e-05

Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV.


Pssm-ID: 407280 [Multi-domain]  Cd Length: 102  Bit Score: 43.79  E-value: 1.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712639084 518 DVLVCGWGSTAGSIRSAVEICAGRGLSVGAVHLRHIWPM-AKGLDGIFSRFRTVLVPELNM-----GQM 580
Cdd:pfam17147   2 EVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFpEEELKELLAGVKKVVVLDRNIsfgspGQL 70
PRK14029 PRK14029
pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional
21-128 5.15e-05

pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional


Pssm-ID: 172523 [Multi-domain]  Cd Length: 185  Bit Score: 44.24  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  21 IRFAGDSGDGMQITGNQFTSTSAAVGNDLATLPDFPAEIR-APVGTRPGVSGFQVRfsssdIHTPGDAPDVLVAMNPAAL 99
Cdd:PRK14029    4 IRFHGRGGQGAVTAANILAEAAFLEGKYVQAFPFFGVERRgAPVTAFTRIDEKPIR-----IKTQIYEPDVVVVLDPSLL 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1712639084 100 --VVNLKDLKPGGMVILNTGNWKELDLKKAR 128
Cdd:PRK14029   79 dtVDVTAGLKDGGIVIVNTEKSKEEVLEKLK 109
PorC_KorC TIGR02175
2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number ...
21-131 5.88e-04

2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins (H. pylori) used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes the gamma subunit. In Pyrococcus furious, enzymes active on pyruvate and 2-ketoisovalerate share a common gamma subunit.


Pssm-ID: 274014 [Multi-domain]  Cd Length: 177  Bit Score: 41.18  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712639084  21 IRFAGDSGDGMqITGNQFTSTSAAVGNDLA-TLPDFPAEIR-APVGTRPGVSGFQVRfsssdIHTPGDAPDVLVAMNPAA 98
Cdd:TIGR02175   4 IRFHGRGGQGA-VTASQLLAEAAFLEGKYAqAFPEFGAERRgAPVRAFLRISDRPIR-----VHSQIYEPDYVVVLDPTL 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1712639084  99 L-VVNLKD-LKPGGMVILNTGNWKELDLKKARCAT 131
Cdd:TIGR02175  78 LkTVNVTAgLKEDGILIVNTKKDPEELRKELKVYT 112
PRK06853 PRK06853
indolepyruvate oxidoreductase subunit beta; Reviewed
73-116 2.15e-03

indolepyruvate oxidoreductase subunit beta; Reviewed


Pssm-ID: 180732 [Multi-domain]  Cd Length: 197  Bit Score: 39.85  E-value: 2.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1712639084  73 QVRFS---SSDIHTPGDApDVLVAMNPAALVVNLKDLKPGGMVILNT 116
Cdd:PRK06853   52 HVRFGdevYSPLIPEGKA-DLLLAFEPLEALRYLPYLKKGGKVVVNT 97
 
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