[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: 3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO₂ + 2 reduced ferredoxin + H⁺.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 9.7;
Temperature dependence: Optimum temperature is 75 degrees Celsius;
SUBUNIT: Heterotrimer of the vorA, vorB and vorC subunits.

Copyright

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Cross-references

3D structure databases

Ontologies

GO:0043807;	Molecular function: 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity (inferred from electronic annotation from EC).
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Family and domain databases

Other

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 >35`	`>35`	`Ketoisovalerate oxidoreductase subunit vorB.`	`PRO_0000099955`
`NON_TER`	`35 35`

Sequence information

Length: 35 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 3670 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: C2AF6C43DE8629BA [This is a checksum on the sequence]

        10         20         30 
ATQMVXGNTA VIIGAMYAGX DXYFGYPITP ASEIL

	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