[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-24. STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; PubMed=8550425 [NCBI, ExPASy, EBI, Israel, Japan] Kletzin A., Adams M.W.W.; "Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima."; J. Bacteriol. 178:248-257(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.; "The complete sequence of the Pyrococcus furiosus genome."; Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[3]	CHARACTERIZATION. STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; DOI=10.1016/0167-4838(93)90190-3; PubMed=8380721 [NCBI, ExPASy, EBI, Israel, Japan] Blamey J.M., Adams M.W.W.; "Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus."; Biochim. Biophys. Acta 1161:19-27(1993).

Comments

CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO₂ + 2 reduced ferredoxin + 2 H⁺.
SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma chain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X85250; CAA59506.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE010209; AAL81089.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T45089; T45089.

RefSeq

NP_578694.1; -.

3D structure databases

HSSP

P94692; 1KEK. [HSSP ENTRY / PDB]

ModBase

Q51805.

Ontologies

GO:0019164;	Molecular function: pyruvate synthase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011766; TPP_enzyme_bd_C.
Graphical view of domain structure.

Pfam

PF02775; TPP_enzyme_C; 1.
Pfam graphical view of domain structure.

Genome annotation databases

1468830; -.

AE009950_GR; PF0965.

pfu:PF0965; -.

fig|186497.1.peg.1001; -.

Phylogenomic databases

HOGENOM

Q51805; -.

Genome annotation databases

CMR

Q51805; PF0965.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Direct protein sequencing; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 331`	`330`	`Pyruvate synthase subunit porB.`	`PRO_0000099907`

Sequence information

Length: 331 AA [This is the length of the unprocessed precursor]

Molecular weight: 36261 Da [This is the MW of the unprocessed precursor]

CRC64: 1523640D21AB7D12 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVRKPPITT REYWAPGHAA CAGCGCATAL RLATKALSEA MEEKYGDPNA FAIAHATGCM 

        70         80         90        100        110        120 
EVVSAVFPYT AWKAPWIHVA FENAAAVASG IEAAWKKLGR KGKILAIGGD GGTADIGLQA 

       130        140        150        160        170        180 
LSGMLERWHN VLYLMYDNEA YMNTGIQRSS STPYGAWTTT SPPGKYSVGE DKPKKWVALI 

       190        200        210        220        230        240 
AAAHQIPYVA TASIGNPLDF VRKIKKAGKI DGPAFVQVLC TCPTGWRSPL EKGVEIARLA 

       250        260        270        280        290        300 
IETGIWPLFE IENGDIWNIK IQPPGGGAKV YKEGNRVVRI EFKKPIEEYL KLQGRFKHLF 

       310        320        330 
KRPEAIEELR NQVKAMWKVL GVEAILPRPE E

Q51805 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools