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Conserved domains on  [gi|364507714|gb|AEW51238|]
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2-oxoglutarate ferredoxin oxidoreductase alpha subunit [Legionella pneumophila subsp. pneumophila ATCC 43290]

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 ...
7-595 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: 684.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714    7 IVVRITGDSGDGVQLVGEQLTISAALTGRDVRTMPDFPAEIRApagtvaGVSGFQLAMAERAIFTAGESLDVLVALNPAA 86
Cdd:TIGR03710   2 VVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRG------GHSYFQIRISDEPVRSPGDGVDVLVALNPET 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714   87 LKNSLQHLNQGGLLIINEDSFQERDWQKagidksfldncrehYHIVAFPLiTQTIQAVESINLTKpqavktkNFYILGLV 166
Cdd:TIGR03710  76 LKEHLDELRPGGIIIYDSDLFDEEDLEK--------------ARVIPVPL-TEIAKEAKGRKRMK-------NMVALGAL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  167 LWLFDLPTETCQAFIAKKFKTNQAIAKANELALLAGYNYAMTLELsrRDYMLGEVNRHSGEYRQITGVEAVGLALATLAT 246
Cdd:TIGR03710 134 AALLGLDLEPLEEVIREKFGKKPEIAEANLKALRAGYDYAEETEK--TDYLVLPAPPKDGDRILISGNEAIALGAIAGGL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  247 QtqvplLVSGYPITPASAILHECA-RLSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTE 325
Cdd:TIGR03710 212 R-----FLAAYPITPATDILHFLAkHLKKFGVVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAGMTE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  326 LPLVLVDVQRAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLANAA 405
Cdd:TIGR03710 287 TPLVIVDVQRGGPSTGLPTKTEQSDLLFALYGGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLANSY 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  406 EPWEIPALDSLNI--------PKPEFnrftKPYHRDEFLSRSWNVPGTSGFIHQIGGLEKqGDEGRVSYDAENHQKMVIT 477
Cdd:TIGR03710 367 ATVPPPDLDDLPAidrgkvlePEEEY----KRYELTEDGISPRAIPGTPGGIHRATGLEH-DETGHISEDPENRVKMMEK 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  478 RAEKIKGIARDYPALVLEGDMTAPTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLP-DDLGSLLKKYDKVLVA 556
Cdd:TIGR03710 442 RARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGAIREAVERLRAEGIKVALLHLRLLYPFPkNELAELLEGAKKVIVV 521
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 364507714  557 ELN-SGQLCQLIRAVY-LVDAQSISQCNGQPFSVNPLVSAI 595
Cdd:TIGR03710 522 EQNaTGQLAKLLRAETgIVKVRSILKYDGRPFTPEEIVEAI 562
 
Name Accession Description Interval E-value
OAFO_sf TIGR03710
2-oxoacid:acceptor oxidoreductase, alpha subunit; This family of proteins contains a ...
7-595 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: 684.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714    7 IVVRITGDSGDGVQLVGEQLTISAALTGRDVRTMPDFPAEIRApagtvaGVSGFQLAMAERAIFTAGESLDVLVALNPAA 86
Cdd:TIGR03710   2 VVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRG------GHSYFQIRISDEPVRSPGDGVDVLVALNPET 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714   87 LKNSLQHLNQGGLLIINEDSFQERDWQKagidksfldncrehYHIVAFPLiTQTIQAVESINLTKpqavktkNFYILGLV 166
Cdd:TIGR03710  76 LKEHLDELRPGGIIIYDSDLFDEEDLEK--------------ARVIPVPL-TEIAKEAKGRKRMK-------NMVALGAL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  167 LWLFDLPTETCQAFIAKKFKTNQAIAKANELALLAGYNYAMTLELsrRDYMLGEVNRHSGEYRQITGVEAVGLALATLAT 246
Cdd:TIGR03710 134 AALLGLDLEPLEEVIREKFGKKPEIAEANLKALRAGYDYAEETEK--TDYLVLPAPPKDGDRILISGNEAIALGAIAGGL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  247 QtqvplLVSGYPITPASAILHECA-RLSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTE 325
Cdd:TIGR03710 212 R-----FLAAYPITPATDILHFLAkHLKKFGVVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAGMTE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  326 LPLVLVDVQRAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLANAA 405
Cdd:TIGR03710 287 TPLVIVDVQRGGPSTGLPTKTEQSDLLFALYGGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLANSY 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  406 EPWEIPALDSLNI--------PKPEFnrftKPYHRDEFLSRSWNVPGTSGFIHQIGGLEKqGDEGRVSYDAENHQKMVIT 477
Cdd:TIGR03710 367 ATVPPPDLDDLPAidrgkvlePEEEY----KRYELTEDGISPRAIPGTPGGIHRATGLEH-DETGHISEDPENRVKMMEK 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  478 RAEKIKGIARDYPALVLEGDMTAPTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLP-DDLGSLLKKYDKVLVA 556
Cdd:TIGR03710 442 RARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGAIREAVERLRAEGIKVALLHLRLLYPFPkNELAELLEGAKKVIVV 521
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 364507714  557 ELN-SGQLCQLIRAVY-LVDAQSISQCNGQPFSVNPLVSAI 595
Cdd:TIGR03710 522 EQNaTGQLAKLLRAETgIVKVRSILKYDGRPFTPEEIVEAI 562
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
226-596 2.63e-130

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: 386.74  E-value: 2.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 226 GEYRQITGVEAVGLALATLATQtqvplLVSGYPITPASAILHECA-RLSDYGVQLIQAEDEIAAICSCIGAAYGGRLALT 304
Cdd:COG0674    1 GKRVLMDGNEAVALGAIAAGCR-----VIAAYPITPSTEIAEYLAeWLAELGGVVVQAESEIAAIGAVIGASAAGARAMT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 305 CTSGPGLDLKCESLGLAVVTELPLVLVDVQRAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFR 384
Cdd:COG0674   76 ATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQALYGGHGDTGWIVLAPSSVQEAFDLTIIAFN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 385 IAIKYMTPVIVLLDAYLANAAEPWEIPALDSLNIPKPEFNRftKPYHRDEflsRSWNVPGTSGFIHQIGGLEKqgdegRV 464
Cdd:COG0674  156 LAEKYRVPVIVLFDGFLGSHEEPVELPDDEEVKILPRPEEY--RPYALDE---DPRAIPGTAQPDVYFTGLEH-----DE 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 465 SYDAENHQKMVITRAEKIKGIARDYPALVLEGDMTAPTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLP-DDL 543
Cdd:COG0674  226 TEDPENAEKMVEKRMRKFEKIRDELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFPaEAL 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 364507714 544 GSLLKKYDKVLVAELN-SGQLCQLIRAVYLVDA--QSISQCNGQPFSVNPLVSAIK 596
Cdd:COG0674  306 REALKGVKKVAVVERNkSGQLALDVRAALGADRvvGGIYGLGGRPFTPEEILAVIE 361
PRK08659 PRK08659
2-oxoacid:acceptor oxidoreductase subunit alpha;
256-599 4.92e-77

2-oxoacid:acceptor oxidoreductase subunit alpha;


Pssm-ID: 181526 [Multi-domain]  Cd Length: 376  Bit Score: 249.39  E-value: 4.92e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 256 GYPITPASAILHECA-RLSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTELPLVLVDVQ 334
Cdd:PRK08659  27 GYPITPSTEIAEVMArELPKVGGVFIQMEDEIASMAAVIGASWAGAKAMTATSGPGFSLMQENIGYAAMTETPCVIVNVQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 335 RAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLANAAEPWEIPALD 414
Cdd:PRK08659 107 RGGPSTGQPTKPAQGDMMQARWGTHGDHPIIALSPSSVQECFDLTIRAFNLAEKYRTPVIVLADEVVGHMREKVVLPEPD 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 415 SLNI-----PKPEFNRFtKPYHRDEFLSRSWNVPGTSGFIHqIGGLEKqgDE-GRVSYDAENHQKMVITRAEKIKGIARD 488
Cdd:PRK08659 187 EIEIierklPKVPPEAY-KPFDDPEGGVPPMPAFGDGYRFH-VTGLTH--DErGFPTTDPETHEKLVRRLVRKIEKNRDD 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 489 YpALVlEGDMT--APTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLPDD-LGSLLKKYDKVLVAELNSGQLCQ 565
Cdd:PRK08659 263 I-VLY-EEYMLedAEVVVVAYGSVARSARRAVKEAREEGIKVGLFRLITVWPFPEEaIRELAKKVKAIVVPEMNLGQMSL 340
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 364507714 566 LIRAVYLVDAQ--SISQCNGQPFSVNPLVSAIKAEA 599
Cdd:PRK08659 341 EVERVVNGRAKveGINKIGGELITPEEILEKIKEVA 376
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
254-432 5.78e-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: 186.31  E-value: 5.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  254 VSGYPITPASAILHECARLSDYG----VQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTELPLV 329
Cdd:pfam01855  10 IAAYPITPSSEIAEEAAEWAANGekgdVVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLGKAAGERLPVV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  330 LVDVQRAGASTGLPTKTSQSDLKQALygrhgEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLA-NAAEPW 408
Cdd:pfam01855  90 IHVVARAGPSPGLSIFGDHSDVMAAR-----DTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGFRTsHEREKV 164
                         170       180
                  ....*....|....*....|....
gi 364507714  409 EIPALDslnIPKPEFNRFTKPYHR 432
Cdd:pfam01855 165 ELPPDE---DEKDLIDEFLPPYKR 185
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
233-399 9.02e-54

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: 180.39  E-value: 9.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 233 GVEAVGLAlATLATqtqvPLLVSGYPITPASAILHECAR--LSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPG 310
Cdd:cd07034    1 GNEAVARG-ALAAG----VDVVAAYPITPSTEIAETLAKavLGELGGVVVQAESEHAAAEAAIGASAAGARAMTATSGPG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 311 LDLKCESLGLAVVTELPLVLVDVQRAGASTGLPtKTSQSDLKQALYGRHgeaPLPVIAAQSPADCFNTIIEAFRIAIKYM 390
Cdd:cd07034   76 LNLMAEALYLAAGAELPLVIVVAQRPGPSTGLP-KPDQSDLMAARYGGH---PWPVLAPSSVQEAFDLALEAFELAEKYR 151

                 ....*....
gi 364507714 391 TPVIVLLDA 399
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 ...
7-595 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: 684.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714    7 IVVRITGDSGDGVQLVGEQLTISAALTGRDVRTMPDFPAEIRApagtvaGVSGFQLAMAERAIFTAGESLDVLVALNPAA 86
Cdd:TIGR03710   2 VVIRIGGAAGDGIQTAGEIFAKALARAGYYVFTFRDYPSRIRG------GHSYFQIRISDEPVRSPGDGVDVLVALNPET 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714   87 LKNSLQHLNQGGLLIINEDSFQERDWQKagidksfldncrehYHIVAFPLiTQTIQAVESINLTKpqavktkNFYILGLV 166
Cdd:TIGR03710  76 LKEHLDELRPGGIIIYDSDLFDEEDLEK--------------ARVIPVPL-TEIAKEAKGRKRMK-------NMVALGAL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  167 LWLFDLPTETCQAFIAKKFKTNQAIAKANELALLAGYNYAMTLELsrRDYMLGEVNRHSGEYRQITGVEAVGLALATLAT 246
Cdd:TIGR03710 134 AALLGLDLEPLEEVIREKFGKKPEIAEANLKALRAGYDYAEETEK--TDYLVLPAPPKDGDRILISGNEAIALGAIAGGL 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  247 QtqvplLVSGYPITPASAILHECA-RLSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTE 325
Cdd:TIGR03710 212 R-----FLAAYPITPATDILHFLAkHLKKFGVVVVQAEDEIAAINMAIGASYAGARAMTATSGPGFALMSEALGLAGMTE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  326 LPLVLVDVQRAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLANAA 405
Cdd:TIGR03710 287 TPLVIVDVQRGGPSTGLPTKTEQSDLLFALYGGHGEFPRIVLAPGSPEECFYLAAEAFNLAEKYQTPVIVLSDQYLANSY 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  406 EPWEIPALDSLNI--------PKPEFnrftKPYHRDEFLSRSWNVPGTSGFIHQIGGLEKqGDEGRVSYDAENHQKMVIT 477
Cdd:TIGR03710 367 ATVPPPDLDDLPAidrgkvlePEEEY----KRYELTEDGISPRAIPGTPGGIHRATGLEH-DETGHISEDPENRVKMMEK 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  478 RAEKIKGIARDYPALVLEGDMTAPTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLP-DDLGSLLKKYDKVLVA 556
Cdd:TIGR03710 442 RARKLETIAKEIPEPEVYGDEDADVLIIGWGSTYGAIREAVERLRAEGIKVALLHLRLLYPFPkNELAELLEGAKKVIVV 521
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 364507714  557 ELN-SGQLCQLIRAVY-LVDAQSISQCNGQPFSVNPLVSAI 595
Cdd:TIGR03710 522 EQNaTGQLAKLLRAETgIVKVRSILKYDGRPFTPEEIVEAI 562
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
226-596 2.63e-130

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: 386.74  E-value: 2.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 226 GEYRQITGVEAVGLALATLATQtqvplLVSGYPITPASAILHECA-RLSDYGVQLIQAEDEIAAICSCIGAAYGGRLALT 304
Cdd:COG0674    1 GKRVLMDGNEAVALGAIAAGCR-----VIAAYPITPSTEIAEYLAeWLAELGGVVVQAESEIAAIGAVIGASAAGARAMT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 305 CTSGPGLDLKCESLGLAVVTELPLVLVDVQRAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFR 384
Cdd:COG0674   76 ATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQALYGGHGDTGWIVLAPSSVQEAFDLTIIAFN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 385 IAIKYMTPVIVLLDAYLANAAEPWEIPALDSLNIPKPEFNRftKPYHRDEflsRSWNVPGTSGFIHQIGGLEKqgdegRV 464
Cdd:COG0674  156 LAEKYRVPVIVLFDGFLGSHEEPVELPDDEEVKILPRPEEY--RPYALDE---DPRAIPGTAQPDVYFTGLEH-----DE 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 465 SYDAENHQKMVITRAEKIKGIARDYPALVLEGDMTAPTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLP-DDL 543
Cdd:COG0674  226 TEDPENAEKMVEKRMRKFEKIRDELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFPaEAL 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 364507714 544 GSLLKKYDKVLVAELN-SGQLCQLIRAVYLVDA--QSISQCNGQPFSVNPLVSAIK 596
Cdd:COG0674  306 REALKGVKKVAVVERNkSGQLALDVRAALGADRvvGGIYGLGGRPFTPEEILAVIE 361
PRK08659 PRK08659
2-oxoacid:acceptor oxidoreductase subunit alpha;
256-599 4.92e-77

2-oxoacid:acceptor oxidoreductase subunit alpha;


Pssm-ID: 181526 [Multi-domain]  Cd Length: 376  Bit Score: 249.39  E-value: 4.92e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 256 GYPITPASAILHECA-RLSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTELPLVLVDVQ 334
Cdd:PRK08659  27 GYPITPSTEIAEVMArELPKVGGVFIQMEDEIASMAAVIGASWAGAKAMTATSGPGFSLMQENIGYAAMTETPCVIVNVQ 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 335 RAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLANAAEPWEIPALD 414
Cdd:PRK08659 107 RGGPSTGQPTKPAQGDMMQARWGTHGDHPIIALSPSSVQECFDLTIRAFNLAEKYRTPVIVLADEVVGHMREKVVLPEPD 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 415 SLNI-----PKPEFNRFtKPYHRDEFLSRSWNVPGTSGFIHqIGGLEKqgDE-GRVSYDAENHQKMVITRAEKIKGIARD 488
Cdd:PRK08659 187 EIEIierklPKVPPEAY-KPFDDPEGGVPPMPAFGDGYRFH-VTGLTH--DErGFPTTDPETHEKLVRRLVRKIEKNRDD 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 489 YpALVlEGDMT--APTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLPDD-LGSLLKKYDKVLVAELNSGQLCQ 565
Cdd:PRK08659 263 I-VLY-EEYMLedAEVVVVAYGSVARSARRAVKEAREEGIKVGLFRLITVWPFPEEaIRELAKKVKAIVVPEMNLGQMSL 340
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 364507714 566 LIRAVYLVDAQ--SISQCNGQPFSVNPLVSAIKAEA 599
Cdd:PRK08659 341 EVERVVNGRAKveGINKIGGELITPEEILEKIKEVA 376
oorA PRK09627
2-oxoglutarate synthase subunit alpha;
255-596 2.58e-62

2-oxoglutarate synthase subunit alpha;


Pssm-ID: 182002 [Multi-domain]  Cd Length: 375  Bit Score: 210.72  E-value: 2.58e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 255 SGYPITPASAILHECAR-LSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTELPLVLVDV 333
Cdd:PRK09627  25 GGYPITPSSEIAHEMSVlLPKCGGTFIQMEDEISGISVALGASMSGVKSMTASSGPGISLKAEQIGLGFIAEIPLVIVNV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 334 QRAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLANAAEPWEIPAL 413
Cdd:PRK09627 105 MRGGPSTGLPTRVAQGDVNQAKNPTHGDFKSIALAPGSLEEAYTETVRAFNLAERFMTPVFLLLDETVGHMYGKAVIPDL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 414 DSLN---IPKPEFN---RFTKPYHRDEFLSRSWNvPGTSGFIHQIGGLEkQGDEGRVSYDAENHQKMVITRAEKIKGIAR 487
Cdd:PRK09627 185 EEVQkmiINRKEFDgdkKDYKPYGVAQDEPAVLN-PFFKGYRYHVTGLH-HGPIGFPTEDAKICGKLIDRLFNKIESHQD 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 488 D---YPALVLEGdmtAPTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLPDD-LGSLLKKYDKVLVAELNSGQL 563
Cdd:PRK09627 263 EieeYEEYMLDD---AEILIIAYGSVSLSAKEAIKRLREEGIKVGLFRPITLWPSPAKkLKEIGDKFEKILVIELNMGQY 339
                        330       340       350
                 ....*....|....*....|....*....|....
gi 364507714 564 CQLI-RAVYLVDAQSISQCNGQPFSVNPLVSAIK 596
Cdd:PRK09627 340 LEEIeRVMQRDDFHFLGKANGRPISPSEIIAKVK 373
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
254-432 5.78e-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: 186.31  E-value: 5.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  254 VSGYPITPASAILHECARLSDYG----VQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTELPLV 329
Cdd:pfam01855  10 IAAYPITPSSEIAEEAAEWAANGekgdVVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLGKAAGERLPVV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  330 LVDVQRAGASTGLPTKTSQSDLKQALygrhgEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLA-NAAEPW 408
Cdd:pfam01855  90 IHVVARAGPSPGLSIFGDHSDVMAAR-----DTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGFRTsHEREKV 164
                         170       180
                  ....*....|....*....|....
gi 364507714  409 EIPALDslnIPKPEFNRFTKPYHR 432
Cdd:pfam01855 165 ELPPDE---DEKDLIDEFLPPYKR 185
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
233-399 9.02e-54

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: 180.39  E-value: 9.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 233 GVEAVGLAlATLATqtqvPLLVSGYPITPASAILHECAR--LSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPG 310
Cdd:cd07034    1 GNEAVARG-ALAAG----VDVVAAYPITPSTEIAETLAKavLGELGGVVVQAESEHAAAEAAIGASAAGARAMTATSGPG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 311 LDLKCESLGLAVVTELPLVLVDVQRAGASTGLPtKTSQSDLKQALYGRHgeaPLPVIAAQSPADCFNTIIEAFRIAIKYM 390
Cdd:cd07034   76 LNLMAEALYLAAGAELPLVIVVAQRPGPSTGLP-KPDQSDLMAARYGGH---PWPVLAPSSVQEAFDLALEAFELAEKYR 151

                 ....*....
gi 364507714 391 TPVIVLLDA 399
Cdd:cd07034  152 LPVIVLSDG 160
PRK07119 PRK07119
2-ketoisovalerate ferredoxin reductase; Validated
256-568 5.23e-37

2-ketoisovalerate ferredoxin reductase; Validated


Pssm-ID: 235942 [Multi-domain]  Cd Length: 352  Bit Score: 141.15  E-value: 5.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 256 GYPITPASAILHECAR-LSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLGLAVVTELPLVLVDVQ 334
Cdd:PRK07119  27 GYPITPQSEIPEYMSRrLPEVGGVFVQAESEVAAINMVYGAAATGKRVMTSSSSPGISLKQEGISYLAGAELPCVIVNIM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 335 RAGAstGLPT-KTSQSDLKQALYGR-HGEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDAYLANAAEPWEIPa 412
Cdd:PRK07119 107 RGGP--GLGNiQPSQGDYFQAVKGGgHGDYRLIVLAPSSVQEMVDLTMLAFDLADKYRNPVMVLGDGVLGQMMEPVEFP- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 413 ldslnipkpefnrftkPYHRDEFLSRSWNVPGTSGFIHQI--------GGLEKQGDEGRVSYDA--ENHQkmvitRAEKI 482
Cdd:PRK07119 184 ----------------PRKKRPLPPKDWAVTGTKGRRKNIitslfldpEELEKHNLRLQEKYAKieENEV-----RYEEY 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 483 KgiardypalvLEGdmtAPTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLPDD-LGSLLKKYDKVLVAELNSG 561
Cdd:PRK07119 243 N----------TED---AELVLVAYGTSARIAKSAVDMAREEGIKVGLFRPITLWPFPEKaLEELADKGKGFLSVEMSMG 309

                 ....*..
gi 364507714 562 QLCQLIR 568
Cdd:PRK07119 310 QMVEDVR 316
PorG COG1014
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma ...
3-401 3.17e-35

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: 137.90  E-value: 3.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714   3 TTDVIVVRITGDSGDGVQLVGEQLTISAALTGRDVRTMPDFPAEIRapaGtvaGVSGFQLAMAERAIF-TAGESLDVLVA 81
Cdd:COG1014    1 MAMDLEIRIAGVGGQGVVTAGKILAKAAMREGYYVQGYPSYGSEQR---G---GPVVSHVRISDEPIRsPLIDEADVLIA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  82 LNPAALKNSLQHLNQGGLLIINEDSFQERDWQkagIDKSFLDncREHYHIVAFPLitQTIqAVESINltkpqAVKTKNFY 161
Cdd:COG1014   75 LDPEELDRVLDGLKPGGVLIVNSSLVPPEVWR---LPQEALE--RKDIRVYVIDA--TKI-AKELLG-----NARVANTV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 162 ILGLVLWLFDLPTETCQAFIAKKF-KTNQAIAKANELALLAGYNYAMTLElsrrdymlgEVNRHSGEYRQITGVEAVGLA 240
Cdd:COG1014  142 MLGALAALLGLPLEALEEAIEETFgKKGEKVVELNLKAFEAGYEAAKEVF---------ALAAAPAPLVLLAGNAAAALG 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 241 LATLATQTQVPllvsgYPITPASA-ILHECARLSDYGVQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCESLG 319
Cdd:COG1014  213 AAAGGAAFAAA-----YPITPSTSlIEAAAAAAAKVGGVVAEEEAAAAAAAAAAAAAAAGAAAAAAGGGGGAALATEGLG 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 320 LAVVTELPLVLVDVQRAGASTGLPTKTSQSDLKQALYGRHGEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVLLDA 399
Cdd:COG1014  288 LAGMTETPVVAVAAPRPGPGTGTPTEEEQGLLLLAAGGGGGEAPALALAPDTEEELLFAAAAAFALAEYAQALLLLLLLQ 367

                 ..
gi 364507714 400 YL 401
Cdd:COG1014  368 LL 369
vorA PRK08366
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed
240-559 7.94e-21

2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed


Pssm-ID: 169406 [Multi-domain]  Cd Length: 390  Bit Score: 95.07  E-value: 7.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 240 ALATLATQTQVpllVSGYPITPASAILHECARLSDYG---VQLIQAEDEIAAICSCIGAAYGGRLALTCTSGPGLDLKCE 316
Cdd:PRK08366  13 AYAALHARVQV---VAAYPITPQTSIIEKIAEFIANGeadIQYVPVESEHSAMAACIGASAAGARAFTATSAQGLALMHE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 317 SLGLAVVTELPLVLVDVQRAGAstglPTKTSQSDLKQALYGRhgEAPLPVIAAQSPADCFNTIIEAFRIAIKYMTPVIVL 396
Cdd:PRK08366  90 MLHWAAGARLPIVMVDVNRAMA----PPWSVWDDQTDSLAQR--DTGWMQFYAENNQEVYDGVLMAFKVAETVNLPAMVV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 397 LDAYLanAAEPWEIPALdslnIPKPEFNRFTKPyhRDEFLSRS-WNVPGTsgfihqIGGLEKQGDEGRVSYD---AENHQ 472
Cdd:PRK08366 164 ESAFI--LSHTYDVVEM----IPQELVDEFLPP--RKPLYSLAdFDNPIS------VGALATPADYYEFRYKiakAMEEA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 473 KMVITRAEKIKG--IARDYPALVLEGDMTAPTLV-IGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLP-DDLGSLLK 548
Cdd:PRK08366 230 KKVIKEVGKEFGerFGRDYSQMIETYYTDDADFVfMGMGSLMGTVKEAVDLLRKEGYKVGYAKVRWFRPFPkEELYEIAE 309
                        330
                 ....*....|.
gi 364507714 549 KYDKVLVAELN 559
Cdd:PRK08366 310 SVKGIAVLDRN 320
POR pfam01558
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large ...
16-204 8.97e-19

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: 83.89  E-value: 8.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714   16 GDGVQLVGEQLTISAALTGRDVRTMPDFPAEIRapagtvAGVSGFQLAMAERAIFTAG--ESLDVLVALNPAALKNSLQH 93
Cdd:pfam01558   2 GQGVVTAGKILAKAAARAGYYVQATPEYGSEIR------GGPVVSHVRISDEPIVPAIpvGEADLLVALDPETLDRHLDG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714   94 LNQGGLLIINEDSFQERDWQKagiDKSFLDNCREHYHIVAFPLitqtiqAVESINltkpqAVKTKNFYILGLVLWLFDLP 173
Cdd:pfam01558  76 LKPGGIIIYNSSEVPPELLEK---DLPAYPRLARVYGVPATEI------AKEAGG-----NSRAANTVMLGALAALLGLP 141
                         170       180       190
                  ....*....|....*....|....*....|.
gi 364507714  174 TETCQAFIAKKFKTNQAIAKANELALLAGYN 204
Cdd:pfam01558 142 LEALEEAIKKRFPGKAKVIELNLKAFRAGYE 172
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
247-548 6.48e-11

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 64.40  E-value: 6.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 247 QTQVPLlVSGYPITPASAILHECARLSDYGV---QLIQAEDEIAAICSCIGA-AYGGRLAlTCTSGPGLDLKCESLGLAV 322
Cdd:PRK09622  25 QAQIDV-VAAYPITPSTPIVQNYGSFKANGYvdgEFVMVESEHAAMSACVGAaAAGGRVA-TATSSQGLALMVEVLYQAS 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 323 VTELPLVLVDVQRAGASTgLPTKTSQSDLkqaLYGRhgEAPLPVIAAQSPADCFNTIIEAFRIA--IKYMTPVIVLLDAY 400
Cdd:PRK09622 103 GMRLPIVLNLVNRALAAP-LNVNGDHSDM---YLSR--DSGWISLCTCNPQEAYDFTLMAFKIAedQKVRLPVIVNQDGF 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714 401 LANAAEPWEIPALDSLN-------IPKPEFNRFTKPYHRDEFLSRSWNvpgtsgfihqiggLEKQGDEGRVSYDAENHQK 473
Cdd:PRK09622 177 LCSHTAQNVRPLSDEVAyqfvgeyQTKNSMLDFDKPVTYGAQTEEDWH-------------FEHKAQLHHALMSSSSVIE 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 364507714 474 MVITRAEKIKGiaRDYpALVLEGDMT-APTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLP-DDLGSLLK 548
Cdd:PRK09622 244 EVFNDFAKLTG--RKY-NLVETYQLEdAEVAIVALGTTYESAIVAAKEMRKEGIKAGVATIRVLRPFPyERLGQALK 317
PFOR_II pfam17147
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ...
500-588 3.26e-08

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: 51.49  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 364507714  500 APTLVIGWGSTFGSLKSAVQQCLEQGLPVAYLHLRHLNPLP-DDLGSLLKKYDKVLVAELN-----SGQLCQLIR-AVYL 572
Cdd:pfam17147   1 AEVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPeEELKELLAGVKKVVVLDRNisfgsPGQLGTEVKaALYD 80
                          90
                  ....*....|....*....
gi 364507714  573 VDAQS---ISQCNGQPFSV 588
Cdd:pfam17147  81 SDPPVvnfIAGLGGRDITP 99
 
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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