Reviewed, UniProtKB/Swiss-Prot P11960 (ODBA_RAT)

Names and origin

Protein names

Recommended name:
    2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
    EC=1.2.4.4
Alternative name(s):
    Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
      Short name=BCKDH E1-alpha

Gene names

Name:

Bckdha

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	441 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 + CO(2).
Cofactor	Thiamine pyrophosphate.
Subunit structure	Heterotetramer of alpha and beta chains By similarity.
Subcellular location	Mitochondrion matrix.
Miscellaneous	Bound potassium ions stabilize the protein structure By similarity.
Sequence similarities	Belongs to the BCKDHA family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Potassium Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	branched chain family amino acid catabolic process Inferred from sequence or structural similarity. Source: HGNC oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial alpha-ketoglutarate dehydrogenase complex Inferred from sequence or structural similarity. Source: HGNC
Molecular function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC alpha-ketoacid dehydrogenase activity Inferred from sequence or structural similarity. Source: HGNC potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	‹1 – 41	›41	Mitochondrion By similarity
	Chain	42 – 441	400	2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial		PRO_0000020468
Regions
	Region	153 – 155	3	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	202	1	Potassium By similarity
	Metal binding	207	1	Potassium By similarity
	Metal binding	208	1	Potassium By similarity
Amino acid modifications
	Modified residue	333	1	Phosphoserine
	Modified residue	341	1	Phosphotyrosine By similarity
	Modified residue	343	1	Phosphoserine
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P11960-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: FFD7709A94094C8E	FASTA	441	50,164
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a cDNA for the E1 alpha subunit of rat liver branched chain alpha-ketoacid dehydrogenase." Zhang B., Kuntz M.J., Goodwin G.W., Harris R.A., Crabb D.W. J. Biol. Chem. 262:15220-15224(1987) [PubMed: 2822716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed: 16396499] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-343, MASS SPECTROMETRY. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02827 mRNA. Translation: AAA40811.1.
PIR	DERTXA. A29468.
RefSeq	NP_036914.1.
UniGene	Rn.49145
3D structure databases
HSSP	HSSP built from PDB template 1DTW based on UniProtKB P12694.
SMR	P11960. Positions 47-441.
ModBase	Search...
PTM databases
PhosphoSite	P11960.
Genome annotation databases
Ensembl	ENSRNOG00000020607. Rattus norvegicus. [Contig view]
GeneID	25244.
KEGG	rno:25244.
NMPDR	fig|10116.3.peg.1316.
Organism-specific databases
RGD	2196. Bckdha.
Phylogenomic databases
HOVERGEN	P11960.
Gene expression databases
ArrayExpress	P11960.
GermOnline	ENSRNOG00000020607. Rattus norvegicus.
Family and domain databases
InterPro	IPR001017. DHase_E1. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	605839.

Entry information

Entry name

ODBA_RAT

Accession

Primary (citable) accession number: P11960

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	November 25, 2008
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)