[1]	PROTEIN SEQUENCE. PubMed=9108258 [NCBI, ExPASy, EBI, Israel, Japan] Tersteegen A., Linder D., Thauer R.K., Hedderich R.; "Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum."; Eur. J. Biochem. 244:862-868(1997).

Comments

CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO₂ + 2 reduced ferredoxin + 2 H⁺.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 10.0;
Temperature dependence: Optimum temperature is 80 degrees Celsius;
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

3D structure databases
ModBase	P80901.
Family and domain databases
BLOCKS	P80901.
Other
ProtoNet	P80901.
UniRef	View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >10`	`>10`	`Pyruvate synthase subunit porB.`	`PRO_0000099905`
`NON_TER`	`10 10`

Sequence information

Length: 10 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 1236 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 167011DAF6DB0760 [This is a checksum on the sequence]

        10 
XXIPEQXFLR

	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