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Conserved domains on  [gi|118501698|gb|ABK98180|]
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pyruvate flavodoxin/ferredoxin oxidoreductase domain protein [Pelobacter propionicus DSM 2379]

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

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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 ...
12-566 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: 648.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   12 DYAIVLAGEAGQGIQVIESLLTRAFRREGYHVFSSPEFMSRIRGGSNSTLLRIGAEPVRAWSDRCDLCVAFDQKALAHLG 91
Cdd:TIGR03710   1 DVVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRGGHSYFQIRISDEPVRSPGDGVDVLVALNPETLKEHL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   92 DRIGPATLVLGD----GLKGIEGQQFIDVPLARLSEAAGGR-LFANTIAAGMIWGLFHAPPETLEQAVKGVFRGKAaEAI 166
Cdd:TIGR03710  81 DELRPGGIIIYDsdlfDEEDLEKARVIPVPLTEIAKEAKGRkRMKNMVALGALAALLGLDLEPLEEVIREKFGKKP-EIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  167 DHNLVAAKSGMDVGRELRRTGRMSLALPPPDSGRkdLHLTGTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFG 246
Cdd:TIGR03710 160 EANLKALRAGYDYAEETEKTDYLVLPAPPKDGDR--ILISGNEAIALGAIAGGLRFLAAYPITPATDILHFLAKHLKKFG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  247 IIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMSEALSLAGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALH 326
Cdd:TIGR03710 238 VVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAGMTETPLVIVDVQRGGPSTGLPTKTEQSDLLFALY 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  327 AGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVIILTDQYLMDSGVDGEGFQPPDPPFE--STAVAAMPGYRRYAL 404
Cdd:TIGR03710 318 GGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLANSYATVPPPDLDDLPAIdrGKVLEPEEEYKRYEL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  405 TKNGISPRAIPGWGAGLVVCDSHEHNEDGHIDETPSTRTEMVDKRLRKLAAIVENTPPPQWIGPEDATSLVICWGSTREI 484
Cdd:TIGR03710 398 TEDGISPRAIPGTPGGIHRATGLEHDETGHISEDPENRVKMMEKRARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGA 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  485 VLEAvagpgMERL-------AVMHFQQLFPLH-GETGRRLQRVDNLILVEGNASGQLGQLLRGTWGITCRHRILKYNGRQ 556
Cdd:TIGR03710 478 IREA-----VERLraegikvALLHLRLLYPFPkNELAELLEGAKKVIVVEQNATGQLAKLLRAETGIVKVRSILKYDGRP 552
                         570
                  ....*....|
gi 118501698  557 FSVEELRTRL 566
Cdd:TIGR03710 553 FTPEEIVEAI 562
 
Name Accession Description Interval E-value
OAFO_sf TIGR03710
2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a ...
12-566 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: 648.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   12 DYAIVLAGEAGQGIQVIESLLTRAFRREGYHVFSSPEFMSRIRGGSNSTLLRIGAEPVRAWSDRCDLCVAFDQKALAHLG 91
Cdd:TIGR03710   1 DVVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRGGHSYFQIRISDEPVRSPGDGVDVLVALNPETLKEHL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   92 DRIGPATLVLGD----GLKGIEGQQFIDVPLARLSEAAGGR-LFANTIAAGMIWGLFHAPPETLEQAVKGVFRGKAaEAI 166
Cdd:TIGR03710  81 DELRPGGIIIYDsdlfDEEDLEKARVIPVPLTEIAKEAKGRkRMKNMVALGALAALLGLDLEPLEEVIREKFGKKP-EIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  167 DHNLVAAKSGMDVGRELRRTGRMSLALPPPDSGRkdLHLTGTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFG 246
Cdd:TIGR03710 160 EANLKALRAGYDYAEETEKTDYLVLPAPPKDGDR--ILISGNEAIALGAIAGGLRFLAAYPITPATDILHFLAKHLKKFG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  247 IIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMSEALSLAGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALH 326
Cdd:TIGR03710 238 VVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAGMTETPLVIVDVQRGGPSTGLPTKTEQSDLLFALY 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  327 AGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVIILTDQYLMDSGVDGEGFQPPDPPFE--STAVAAMPGYRRYAL 404
Cdd:TIGR03710 318 GGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLANSYATVPPPDLDDLPAIdrGKVLEPEEEYKRYEL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  405 TKNGISPRAIPGWGAGLVVCDSHEHNEDGHIDETPSTRTEMVDKRLRKLAAIVENTPPPQWIGPEDATSLVICWGSTREI 484
Cdd:TIGR03710 398 TEDGISPRAIPGTPGGIHRATGLEHDETGHISEDPENRVKMMEKRARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGA 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  485 VLEAvagpgMERL-------AVMHFQQLFPLH-GETGRRLQRVDNLILVEGNASGQLGQLLRGTWGITCRHRILKYNGRQ 556
Cdd:TIGR03710 478 IREA-----VERLraegikvALLHLRLLYPFPkNELAELLEGAKKVIVVEQNATGQLAKLLRAETGIVKVRSILKYDGRP 552
                         570
                  ....*....|
gi 118501698  557 FSVEELRTRL 566
Cdd:TIGR03710 553 FTPEEIVEAI 562
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
205-574 6.99e-131

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: 387.13  E-value: 6.99e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 205 LTGTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFGIIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALM 284
Cdd:COG0674    6 MDGNEAVALGAIAAGCRVIAAYPITPSTEIAEYLAEWLAELGGVVVQAESEIAAIGAVIGASAAGARAMTATSGPGLSLM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 285 SEALSLAGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALHAGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVI 364
Cdd:COG0674   86 QEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQALYGGHGDTGWIVLAPSSVQEAFDLTIIAFNLAEKYRVPVI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 365 ILTDQYLMDSgvdGEGFQPPDPPfESTAVAAMPGYRRYALTKNgisPRAIPGWGAGLVVCDSHEHNEdghiDETPSTRTE 444
Cdd:COG0674  166 VLFDGFLGSH---EEPVELPDDE-EVKILPRPEEYRPYALDED---PRAIPGTAQPDVYFTGLEHDE----TEDPENAEK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 445 MVDKRLRKLAAIVENTPPPQWIGPEDATSLVICWGSTREIVLEAV-----AGpgmERLAVMHFQQLFPLHGE-TGRRLQR 518
Cdd:COG0674  235 MVEKRMRKFEKIRDELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVdrlreEG---IKVGLLRVRLLRPFPAEaLREALKG 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118501698 519 VDNLILVEGNASGQLGQLLRGTWGIT-CRHRILKYNGRQFSVEELRTRLGEIVAQGE 574
Cdd:COG0674  312 VKKVAVVERNKSGQLALDVRAALGADrVVGGIYGLGGRPFTPEEILAVIEELLKGAP 368
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
207-369 7.52e-60

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: 195.80  E-value: 7.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 207 GTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHG-HDFGIIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMS 285
Cdd:cd07034    1 GNEAVARGALAAGVDVVAAYPITPSTEIAETLAKAVlGELGGVVVQAESEHAAAEAAIGASAAGARAMTATSGPGLNLMA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 286 EALSLAGVTESPMVILLAQRPGPATGLPtRTEQGDLNLALHAGHgdvPRIILAPGNPQQAFDCARDAFRLADAYQVPVII 365
Cdd:cd07034   81 EALYLAAGAELPLVIVVAQRPGPSTGLP-KPDQSDLMAARYGGH---PWPVLAPSSVQEAFDLALEAFELAEKYRLPVIV 156

                 ....
gi 118501698 366 LTDQ 369
Cdd:cd07034  157 LSDG 160
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
214-448 7.32e-55

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: 185.15  E-value: 7.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  214 GAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFG---IIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMSEALSL 290
Cdd:pfam01855   1 AAIAAGVDVIAAYPITPSSEIAEEAAEWAANGEkgdVVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  291 AGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALhaghgDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVIILTDQY 370
Cdd:pfam01855  81 AAGERLPVVIHVVARAGPSPGLSIFGDHSDVMAAR-----DTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  371 LMDSGVdgEGFQPPDPPFESTAVAA-MPGYRRYaltKNGISPRAIPGWGAGLVVCDSHEHNEDGHID-ETPSTRTEMVDK 448
Cdd:pfam01855 156 RTSHER--EKVELPPDEDEKDLIDEfLPPYKRK---RYGLDPEMPIARGTAQNPDTYFEHREYGNPAyDAAEVVIEEVMK 230
PRK08659 PRK08659
2-oxoacid:acceptor oxidoreductase subunit alpha;
205-562 8.13e-55

2-oxoacid:acceptor oxidoreductase subunit alpha;


Pssm-ID: 181526 [Multi-domain]  Cd Length: 376  Bit Score: 190.07  E-value: 8.13e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 205 LTGTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFGIIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALM 284
Cdd:PRK08659   7 LQGNEACAEGAIAAGCRFFAGYPITPSTEIAEVMARELPKVGGVFIQMEDEIASMAAVIGASWAGAKAMTATSGPGFSLM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 285 SEALSLAGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALHAGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVI 364
Cdd:PRK08659  87 QENIGYAAMTETPCVIVNVQRGGPSTGQPTKPAQGDMMQARWGTHGDHPIIALSPSSVQECFDLTIRAFNLAEKYRTPVI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 365 ILTDQYLmdsGVDGEGFQPPDPP----FESTAVAAMP-GYRRYALTKNGISPRAIPGWGA-----GLVvcdsheHNEDGH 434
Cdd:PRK08659 167 VLADEVV---GHMREKVVLPEPDeieiIERKLPKVPPeAYKPFDDPEGGVPPMPAFGDGYrfhvtGLT------HDERGF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 435 idetPSTRTEMVDKRLRKLAAIVENTPPP----QWIGPEDATSLVICWGSTREIVLEAVAGPGMERLAVMHFQ--QLFPL 508
Cdd:PRK08659 238 ----PTTDPETHEKLVRRLVRKIEKNRDDivlyEEYMLEDAEVVVVAYGSVARSARRAVKEAREEGIKVGLFRliTVWPF 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 118501698 509 HGETGRRL-QRVDNLILVEGNasgqLGQLLRGTWGITCRHR----ILKYNGRQFSVEEL 562
Cdd:PRK08659 314 PEEAIRELaKKVKAIVVPEMN----LGQMSLEVERVVNGRAkvegINKIGGELITPEEI 368
 
Name Accession Description Interval E-value
OAFO_sf TIGR03710
2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a ...
12-566 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: 648.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   12 DYAIVLAGEAGQGIQVIESLLTRAFRREGYHVFSSPEFMSRIRGGSNSTLLRIGAEPVRAWSDRCDLCVAFDQKALAHLG 91
Cdd:TIGR03710   1 DVVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRGGHSYFQIRISDEPVRSPGDGVDVLVALNPETLKEHL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   92 DRIGPATLVLGD----GLKGIEGQQFIDVPLARLSEAAGGR-LFANTIAAGMIWGLFHAPPETLEQAVKGVFRGKAaEAI 166
Cdd:TIGR03710  81 DELRPGGIIIYDsdlfDEEDLEKARVIPVPLTEIAKEAKGRkRMKNMVALGALAALLGLDLEPLEEVIREKFGKKP-EIA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  167 DHNLVAAKSGMDVGRELRRTGRMSLALPPPDSGRkdLHLTGTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFG 246
Cdd:TIGR03710 160 EANLKALRAGYDYAEETEKTDYLVLPAPPKDGDR--ILISGNEAIALGAIAGGLRFLAAYPITPATDILHFLAKHLKKFG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  247 IIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMSEALSLAGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALH 326
Cdd:TIGR03710 238 VVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAGMTETPLVIVDVQRGGPSTGLPTKTEQSDLLFALY 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  327 AGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVIILTDQYLMDSGVDGEGFQPPDPPFE--STAVAAMPGYRRYAL 404
Cdd:TIGR03710 318 GGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLANSYATVPPPDLDDLPAIdrGKVLEPEEEYKRYEL 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  405 TKNGISPRAIPGWGAGLVVCDSHEHNEDGHIDETPSTRTEMVDKRLRKLAAIVENTPPPQWIGPEDATSLVICWGSTREI 484
Cdd:TIGR03710 398 TEDGISPRAIPGTPGGIHRATGLEHDETGHISEDPENRVKMMEKRARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGA 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  485 VLEAvagpgMERL-------AVMHFQQLFPLH-GETGRRLQRVDNLILVEGNASGQLGQLLRGTWGITCRHRILKYNGRQ 556
Cdd:TIGR03710 478 IREA-----VERLraegikvALLHLRLLYPFPkNELAELLEGAKKVIVVEQNATGQLAKLLRAETGIVKVRSILKYDGRP 552
                         570
                  ....*....|
gi 118501698  557 FSVEELRTRL 566
Cdd:TIGR03710 553 FTPEEIVEAI 562
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
205-574 6.99e-131

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: 387.13  E-value: 6.99e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 205 LTGTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFGIIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALM 284
Cdd:COG0674    6 MDGNEAVALGAIAAGCRVIAAYPITPSTEIAEYLAEWLAELGGVVVQAESEIAAIGAVIGASAAGARAMTATSGPGLSLM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 285 SEALSLAGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALHAGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVI 364
Cdd:COG0674   86 QEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQALYGGHGDTGWIVLAPSSVQEAFDLTIIAFNLAEKYRVPVI 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 365 ILTDQYLMDSgvdGEGFQPPDPPfESTAVAAMPGYRRYALTKNgisPRAIPGWGAGLVVCDSHEHNEdghiDETPSTRTE 444
Cdd:COG0674  166 VLFDGFLGSH---EEPVELPDDE-EVKILPRPEEYRPYALDED---PRAIPGTAQPDVYFTGLEHDE----TEDPENAEK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 445 MVDKRLRKLAAIVENTPPPQWIGPEDATSLVICWGSTREIVLEAV-----AGpgmERLAVMHFQQLFPLHGE-TGRRLQR 518
Cdd:COG0674  235 MVEKRMRKFEKIRDELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVdrlreEG---IKVGLLRVRLLRPFPAEaLREALKG 311
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118501698 519 VDNLILVEGNASGQLGQLLRGTWGIT-CRHRILKYNGRQFSVEELRTRLGEIVAQGE 574
Cdd:COG0674  312 VKKVAVVERNKSGQLALDVRAALGADrVVGGIYGLGGRPFTPEEILAVIEELLKGAP 368
PorG COG1014
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma ...
10-420 6.08e-64

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: 215.71  E-value: 6.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  10 ARDYAIVLAGEAGQGIQVIESLLTRAFRREGYHVFSSPEFMSRIRGGSNSTLLRIGAEPVRA-WSDRCDLCVAFDQKALA 88
Cdd:COG1014    2 AMDLEIRIAGVGGQGVVTAGKILAKAAMREGYYVQGYPSYGSEQRGGPVVSHVRISDEPIRSpLIDEADVLIALDPEELD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  89 HLGDRIGPATLVLGD-----------GLKGIEGQ--QFIDVPLARLS-EAAGGRLFANTIAAGMIWGLFHAPPETLEQAV 154
Cdd:COG1014   82 RVLDGLKPGGVLIVNsslvppevwrlPQEALERKdiRVYVIDATKIAkELLGNARVANTVMLGALAALLGLPLEALEEAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 155 KGVFRGKAAEAIDHNLVAAKSGMDVGRELRRtgrmslalpPPDSGRKDLHLTGTEAIALGAMAGGCNFVSFYPMSPSTGV 234
Cdd:COG1014  162 EETFGKKGEKVVELNLKAFEAGYEAAKEVFA---------LAAAPAPLVLLAGNAAAALGAAAGGAAFAAAYPITPSTSL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 235 ASFLAKHGHDFGIIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMSEALSLAGVTESPMVILLAQRPGPATGLPT 314
Cdd:COG1014  233 IEAAAAAAAKVGGVVAEEEAAAAAAAAAAAAAAAGAAAAAAGGGGGAALATEGLGLAGMTETPVVAVAAPRPGPGTGTPT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 315 RTEQGDLNLALHAGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVIILTDQYLMDSGVDGEGFQPPDPPFESTAVA 394
Cdd:COG1014  313 EEEQGLLLLAAGGGGGEAPALALAPDTEEELLFAAAAAFALAEYAQALLLLLLLQLLVLLLTDLLLLLLDLLRRRAGLGA 392
                        410       420
                 ....*....|....*....|....*.
gi 118501698 395 AMPGYRRYALTKNGISPRAIPGWGAG 420
Cdd:COG1014  393 EEAEARRKLLAAEGRAARAAGGGGGG 418
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
207-369 7.52e-60

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: 195.80  E-value: 7.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 207 GTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHG-HDFGIIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMS 285
Cdd:cd07034    1 GNEAVARGALAAGVDVVAAYPITPSTEIAETLAKAVlGELGGVVVQAESEHAAAEAAIGASAAGARAMTATSGPGLNLMA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 286 EALSLAGVTESPMVILLAQRPGPATGLPtRTEQGDLNLALHAGHgdvPRIILAPGNPQQAFDCARDAFRLADAYQVPVII 365
Cdd:cd07034   81 EALYLAAGAELPLVIVVAQRPGPSTGLP-KPDQSDLMAARYGGH---PWPVLAPSSVQEAFDLALEAFELAEKYRLPVIV 156

                 ....
gi 118501698 366 LTDQ 369
Cdd:cd07034  157 LSDG 160
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
214-448 7.32e-55

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: 185.15  E-value: 7.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  214 GAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFG---IIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMSEALSL 290
Cdd:pfam01855   1 AAIAAGVDVIAAYPITPSSEIAEEAAEWAANGEkgdVVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  291 AGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALhaghgDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVIILTDQY 370
Cdd:pfam01855  81 AAGERLPVVIHVVARAGPSPGLSIFGDHSDVMAAR-----DTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  371 LMDSGVdgEGFQPPDPPFESTAVAA-MPGYRRYaltKNGISPRAIPGWGAGLVVCDSHEHNEDGHID-ETPSTRTEMVDK 448
Cdd:pfam01855 156 RTSHER--EKVELPPDEDEKDLIDEfLPPYKRK---RYGLDPEMPIARGTAQNPDTYFEHREYGNPAyDAAEVVIEEVMK 230
PRK08659 PRK08659
2-oxoacid:acceptor oxidoreductase subunit alpha;
205-562 8.13e-55

2-oxoacid:acceptor oxidoreductase subunit alpha;


Pssm-ID: 181526 [Multi-domain]  Cd Length: 376  Bit Score: 190.07  E-value: 8.13e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 205 LTGTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFGIIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALM 284
Cdd:PRK08659   7 LQGNEACAEGAIAAGCRFFAGYPITPSTEIAEVMARELPKVGGVFIQMEDEIASMAAVIGASWAGAKAMTATSGPGFSLM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 285 SEALSLAGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALHAGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPVI 364
Cdd:PRK08659  87 QENIGYAAMTETPCVIVNVQRGGPSTGQPTKPAQGDMMQARWGTHGDHPIIALSPSSVQECFDLTIRAFNLAEKYRTPVI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 365 ILTDQYLmdsGVDGEGFQPPDPP----FESTAVAAMP-GYRRYALTKNGISPRAIPGWGA-----GLVvcdsheHNEDGH 434
Cdd:PRK08659 167 VLADEVV---GHMREKVVLPEPDeieiIERKLPKVPPeAYKPFDDPEGGVPPMPAFGDGYrfhvtGLT------HDERGF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 435 idetPSTRTEMVDKRLRKLAAIVENTPPP----QWIGPEDATSLVICWGSTREIVLEAVAGPGMERLAVMHFQ--QLFPL 508
Cdd:PRK08659 238 ----PTTDPETHEKLVRRLVRKIEKNRDDivlyEEYMLEDAEVVVVAYGSVARSARRAVKEAREEGIKVGLFRliTVWPF 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 118501698 509 HGETGRRL-QRVDNLILVEGNasgqLGQLLRGTWGITCRHR----ILKYNGRQFSVEEL 562
Cdd:PRK08659 314 PEEAIRELaKKVKAIVVPEMN----LGQMSLEVERVVNGRAkvegINKIGGELITPEEI 368
oorA PRK09627
2-oxoglutarate synthase subunit alpha;
206-569 2.73e-39

2-oxoglutarate synthase subunit alpha;


Pssm-ID: 182002 [Multi-domain]  Cd Length: 375  Bit Score: 147.55  E-value: 2.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 206 TGTEAIALGAMAGGCNFVSFYPMSPSTGVA----SFLAKHGHDFgiIveQAEDEICAATMVLGAWYAGARALTTTSGGGF 281
Cdd:PRK09627   7 TGNELVAKAAIECGCRFFGGYPITPSSEIAhemsVLLPKCGGTF--I--QMEDEISGISVALGASMSGVKSMTASSGPGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 282 ALMSEALSLAGVTESPMVILLAQRPGPATGLPTRTEQGDLNLALHAGHGDVPRIILAPGNPQQAFDCARDAFRLADAYQV 361
Cdd:PRK09627  83 SLKAEQIGLGFIAEIPLVIVNVMRGGPSTGLPTRVAQGDVNQAKNPTHGDFKSIALAPGSLEEAYTETVRAFNLAERFMT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 362 PVIILTDQYL--MDSGV--------------------DGEGFQPPDPPFESTAV--AAMPGYrRYALTkngispraipgw 417
Cdd:PRK09627 163 PVFLLLDETVghMYGKAvipdleevqkmiinrkefdgDKKDYKPYGVAQDEPAVlnPFFKGY-RYHVT------------ 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 418 gaGLvvcdsHeHNEDGHidetPSTRTEMVDKRLRKLAAIVENTPPPQWIGPE----DATSLVICWGSTREIVLEAVAGPG 493
Cdd:PRK09627 230 --GL-----H-HGPIGF----PTEDAKICGKLIDRLFNKIESHQDEIEEYEEymldDAEILIIAYGSVSLSAKEAIKRLR 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 494 MERLAVMHFQ--QLFPLHGETGRRL-QRVDNLILVEGNasgqLGQLLRGTWGITCR---HRILKYNGRQFSVEELRTRLG 567
Cdd:PRK09627 298 EEGIKVGLFRpiTLWPSPAKKLKEIgDKFEKILVIELN----MGQYLEEIERVMQRddfHFLGKANGRPISPSEIIAKVK 373

                 ..
gi 118501698 568 EI 569
Cdd:PRK09627 374 EL 375
PRK07119 PRK07119
2-ketoisovalerate ferredoxin reductase; Validated
207-368 1.92e-34

2-ketoisovalerate ferredoxin reductase; Validated


Pssm-ID: 235942 [Multi-domain]  Cd Length: 352  Bit Score: 133.45  E-value: 1.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 207 GTEAIALGAMAGGCNFVSFYPMSPSTGVASFLAKHGHDFGIIVEQAEDEICAATMVLGAWYAGARALTTTSGGGFALMSE 286
Cdd:PRK07119   9 GNEAIAEAAIRAGCRCYFGYPITPQSEIPEYMSRRLPEVGGVFVQAESEVAAINMVYGAAATGKRVMTSSSSPGISLKQE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 287 ALS-LAGvTESPMVILLAQRPGPatGLPT-RTEQGDLNLALHA-GHGDVPRIILAPGNPQQAFDCARDAFRLADAYQVPV 363
Cdd:PRK07119  89 GISyLAG-AELPCVIVNIMRGGP--GLGNiQPSQGDYFQAVKGgGHGDYRLIVLAPSSVQEMVDLTMLAFDLADKYRNPV 165

                 ....*
gi 118501698 364 IILTD 368
Cdd:PRK07119 166 MVLGD 170
POR pfam01558
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large ...
21-178 2.13e-33

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: 125.11  E-value: 2.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   21 AGQGIQVIESLLTRAFRREGYHVFSSPEFMSRIRGGSNSTLLRIGAEPVRAWS--DRCDLCVAFDQKALAHLGDRIGPAT 98
Cdd:pfam01558   1 GGQGVVTAGKILAKAAARAGYYVQATPEYGSEIRGGPVVSHVRISDEPIVPAIpvGEADLLVALDPETLDRHLDGLKPGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   99 LVLGD------------GLKGIEGQQFIDVPLARLSEAAGG-RLFANTIAAGMIWGLFHAPPETLEQAVKGVFRGKaAEA 165
Cdd:pfam01558  81 IIIYNssevppellekdLPAYPRLARVYGVPATEIAKEAGGnSRAANTVMLGALAALLGLPLEALEEAIKKRFPGK-AKV 159
                         170
                  ....*....|...
gi 118501698  166 IDHNLVAAKSGMD 178
Cdd:pfam01558 160 IELNLKAFRAGYE 172
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
223-371 5.92e-13

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 70.95  E-value: 5.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 223 VSFYPMSPST----GVASFLAkHGHDFGIIVeQAEDEICAATMVLGAWYAGARALTTTSGGGFALMSEALSLAGVTESPM 298
Cdd:PRK09622  31 VAAYPITPSTpivqNYGSFKA-NGYVDGEFV-MVESEHAAMSACVGAAAAGGRVATATSSQGLALMVEVLYQASGMRLPI 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118501698 299 VILLAQRpGPATGLPTRTEQGDLNLALHAGHgdvprIILAPGNPQQAFDCARDAFRLADAYQV--PVIILTDQYL 371
Cdd:PRK09622 109 VLNLVNR-ALAAPLNVNGDHSDMYLSRDSGW-----ISLCTCNPQEAYDFTLMAFKIAEDQKVrlPVIVNQDGFL 177
vorA PRK08366
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed
205-392 4.18e-10

2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed


Pssm-ID: 169406 [Multi-domain]  Cd Length: 390  Bit Score: 61.94  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 205 LTGTEAIALGAMAGGCNFVSFYPMSPSTGV----ASFLAKHGHDFGIIVEQAEDEICAATmvLGAWYAGARALTTTSGGG 280
Cdd:PRK08366   6 VSGNYAAAYAALHARVQVVAAYPITPQTSIiekiAEFIANGEADIQYVPVESEHSAMAAC--IGASAAGARAFTATSAQG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698 281 FALMSEALSLAGVTESPMVILLAQRpGPATGLPTRTEQGDlNLAlhagHGDVPRIILAPGNPQQAFDCARDAFRLADAYQ 360
Cdd:PRK08366  84 LALMHEMLHWAAGARLPIVMVDVNR-AMAPPWSVWDDQTD-SLA----QRDTGWMQFYAENNQEVYDGVLMAFKVAETVN 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 118501698 361 VPVIILTDQYLMDSGVD---------GEGFQPPDPPFESTA 392
Cdd:PRK08366 158 LPAMVVESAFILSHTYDvvemipqelVDEFLPPRKPLYSLA 198
PRK06853 PRK06853
indolepyruvate oxidoreductase subunit beta; Reviewed
13-184 2.05e-07

indolepyruvate oxidoreductase subunit beta; Reviewed


Pssm-ID: 180732 [Multi-domain]  Cd Length: 197  Bit Score: 51.40  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  13 YAIVLAGEAGQGIQVIESLLTRAFRREGYHVFSSpEF--MSRiRGGSNSTLLRIGAEpvrAWSD-----RCDLCVAFDQ- 84
Cdd:PRK06853   4 TNILIVGVGGQGILLASKILGEAALAAGYDVKVS-EVhgMSQ-RGGSVVSHVRFGDE---VYSPlipegKADLLLAFEPl 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  85 KALAHLG------------DRIGPATLVLG--------DGLKGIE--GQQFIDVPLARLSEAAGGRLFANTIAAGMIWGL 142
Cdd:PRK06853  79 EALRYLPylkkggkvvvntQPIVPVPVSLGlakypedeEILEELKklGIKVYVIDAEKIAKEAGNIKAANVVLLGALAKF 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 118501698 143 FHAPPETLEQAVKGVFRGKAAEAidhNLVAAKSGMDVGRELR 184
Cdd:PRK06853 159 LPIDEETLEEAIKERVPPKFVEV---NLKAFEAGREAAEKLA 197
PorC_KorC TIGR02175
2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number ...
13-176 5.15e-06

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: 46.96  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   13 YAIVLAGEAGQGIQVIESLLTRAFRREGYHVFSSPEFMSRIRGGSNSTLLRIGAEPVRAWSD--RCDLCVAFDQKALahl 90
Cdd:TIGR02175   2 IEIRFHGRGGQGAVTASQLLAEAAFLEGKYAQAFPEFGAERRGAPVRAFLRISDRPIRVHSQiyEPDYVVVLDPTLL--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698   91 gdrigpATLVLGDGLKGiEGQQFIDVPLA----------------RLSEAAGGRLFANTIAAGMIWGLFHAPP-ETLEQA 153
Cdd:TIGR02175  79 ------KTVNVTAGLKE-DGILIVNTKKDpeelrkelkvytvdatKIALVVLGRPIVNTPMLGAFAKVTGLVSlESLEKA 151
                         170       180
                  ....*....|....*....|...
gi 118501698  154 VKGVFRGKAAEAidhNLVAAKSG 176
Cdd:TIGR02175 152 IEESFPGKLAEA---NAKAVERA 171
PRK08338 PRK08338
2-oxoacid:ferredoxin oxidoreductase subunit gamma;
15-182 6.96e-06

2-oxoacid:ferredoxin oxidoreductase subunit gamma;


Pssm-ID: 181394 [Multi-domain]  Cd Length: 170  Bit Score: 46.46  E-value: 6.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  15 IVLAGEAGQGIQVIESLLTRAFRREGYHVFSSPEFMSRIRGGSNSTLLRIGAEPV-RAWSDRCDLCVAFDQKALAHLGDR 93
Cdd:PRK08338   3 IRFAGIGGQGVVLAGVILGEAAAIEGLNVLQTQDYSSASRGGHSIADVIISKEPIyDVMVTKADVLVALHQLGYETAKSS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118501698  94 IGPATLVLGDGLKGIEGQQFIDVPLARLSEAAGG-RLFANTIAAGMIWGLFH-APPETLEQAVKGVFRgKAAEAIdhNLV 171
Cdd:PRK08338  83 LKEDGLLIIDTDLVKPDRDYIGAPFTRIAEETTGlALTVNMVALGYLVAKTGvVKKESVEEAIRRRVP-KGTEEI--NIK 159
                        170
                 ....*....|.
gi 118501698 172 AAKSGMDVGRE 182
Cdd:PRK08338 160 AFRKGYEEGLK 170
 
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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