[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2822716 [NCBI, ExPASy, EBI, Israel, Japan] Zhang B., Kuntz M.J., Goodwin G.W., Harris R.A., Crabb D.W.; "Molecular cloning of a cDNA for the E1 alpha subunit of rat liver branched chain alpha-ketoacid dehydrogenase."; J. Biol. Chem. 262:15220-15224(1987).
[2]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-343, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr0503073; PubMed=16396499 [NCBI, ExPASy, EBI, Israel, Japan] Moser K., White F.M.; "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; J. Proteome Res. 5:98-104(2006).

Comments

FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate.
SUBUNIT: Heterotetramer of alpha and beta chains (By similarity).
SUBCELLULAR LOCATION: Mitochondrion matrix.
MISCELLANEOUS: Bound potassium ions stabilize the protein structure (By similarity).
SIMILARITY: Belongs to the BCKDHA family.

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

J02827; AAA40811.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A29468; DERTXA.

NP_036914.1; -.

3D structure databases

HSSP

P12694; 1DTW. [HSSP ENTRY / PDB]

SMR

P11960; 47-441.

ModBase

P11960.

Protein-protein interaction databases

IntAct

P11960; -.

PTM databases

PhosphoSite

P11960; -.

Organism-specific databases

RGD

2196; Bckdha.

Gene expression databases

ArrayExpress

P11960; -.

GermOnline

ENSRNOG00000020607; Rattus norvegicus.

Ontologies

GO:0005947;	Cellular component: mitochondrial alpha-ketoglutarate dehydrogenase complex (inferred from sequence or structural similarity from HGNC).
GO:0003826;	Molecular function: alpha-ketoacid dehydrogenase activity (inferred from sequence or structural similarity from HGNC).
GO:0009083;	Biological process: branched chain family amino acid catabolic process (inferred from sequence or structural similarity from HGNC).
QuickGo view.

Family and domain databases

InterPro

IPR001017; DHase_E1.
Graphical view of domain structure.

Pfam

PF00676; E1_dh; 1.
Pfam graphical view of domain structure.

BLOCKS

P11960.

Genome annotation databases

Ensembl

ENSRNOG00000020607; Rattus norvegicus. [Contig view]

GeneID

25244; -.

KEGG

rno:25244; -.

NMPDR

fig|10116.3.peg.1316; -.

Phylogenomic databases

HOVERGEN

P11960; -.

Other

ProtoNet

P11960.

UniRef

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

Keywords

Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein; Potassium; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 41`	`>41`	`Mitochondrion (By similarity).`
`CHAIN`	`42 441`	`400`	`2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial.`	`PRO_0000020468`
`REGION`	`153 155`	`3`	`Thiamine pyrophosphate binding (By similarity).`
`METAL`	`202 202`		`Potassium (By similarity).`
`METAL`	`207 207`		`Potassium (By similarity).`
`METAL`	`208 208`		`Potassium (By similarity).`
`MOD_RES`	`333 333`		`Phosphoserine.`
`MOD_RES`	`341 341`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`343 343`		`Phosphoserine.`
`NON_TER`	`1 1`

Sequence information

Length: 441 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 50164 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: FFD7709A94094C8E [This is a checksum on the sequence]

        10         20         30         40         50         60 
SAAKIWRPSR GLRQAALLLL GRPGARGLAR FHPSRQQQQQ FPSLDDKPQF PGASAEFVDK 

        70         80         90        100        110        120 
LEFIQPNVIS GIPIYRVMDR QGQIINPSED PHLPQEEVLK LYRSMTLLNT MDRILYESQR 

       130        140        150        160        170        180 
QGRISFYMTN YGEEGTHVGS AAALERTDLV FGQYREAGVL MYRDYPLELF MAQCYGNVSD 

       190        200        210        220        230        240 
PGKGRQMPVH YGCKERHFVT ISSPLATQIP QAVGAAYAAK RANANQIVIC YFGEGAASEG 

       250        260        270        280        290        300 
DAHAGFNFAA TLECPIIFFC RNNGYAISTP TSEQYRGDGI AARGPGYGIM SIRVDGNDVF 

       310        320        330        340        350        360 
AVYNATKEAR RRAVAENQPF LIEAMTYRIG HHSTSDDSSA YRSVDEVNYW DKQDHPISRL 

       370        380        390        400        410        420 
RQYLLNQGWW DEEQEKAWRK QSRKKVMEAF EQAERKLKPN PSLLFSDVYQ EMPAQLRRQQ 

       430        440 
ESLARHLQTY GEHYPLDHFD K

P11960 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