Reviewed, UniProtKB/Swiss-Prot P50136 (ODBA_MOUSE)

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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	442 AA.
Sequence status	Complete.
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 CO2. 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 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 positive regulation of transcription, DNA-dependent Inferred from direct assay. Source: MGI
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 cyclin-dependent protein kinase 5 activator regulator activity Inferred from direct assay. Source: MGI 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 – 42	42	Mitochondrion By similarity
	Chain	43 – 442	400	2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial		PRO_0000020467
Regions
	Region	154 – 156	3	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	203	1	Potassium By similarity
	Metal binding	208	1	Potassium By similarity
	Metal binding	209	1	Potassium By similarity
Amino acid modifications
	Modified residue	334	1	Phosphoserine Ref.3 Ref.5
	Modified residue	342	1	Phosphotyrosine By similarity
	Modified residue	344	1	Phosphoserine Ref.2 Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P50136-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 3388213D88BC7C92	FASTA	442	50,371
	10 20 30 40 50 60 MSAAKIWRPS RGLRQAALLL LGRSGVRGLA RSHPSRQQQQ QFPSLDDKPQ FPGASAEFVD 70 80 90 100 110 120 KLEFIQPNVI SGIPIYRVMD RQGQIINPSE DPHLPQEEVL KFYRSMTLLN TMDRILYESQ 130 140 150 160 170 180 REGRISFYMT NYGEEGTHVG SAAALERTDL VFGQYREAGV LMYRDYPLEL FMSQCYGNVN 190 200 210 220 230 240 DPGKGRQMPV HYGCKERHFV TISSPLATQI PQAVGAAYAA KRANANRIVI CYFGEGAASE 250 260 270 280 290 300 GDAHAGFNFA ATLECPIIFF CRNNGYAIST PTSEQYRGDG IAARGPGYGI KSIRVDGNDV 310 320 330 340 350 360 FAVYNATKEA RRRAVAENQP FLIEAMTYRI GHHSTSDDSS AYRSVDEVNY WDKQDHPISR 370 380 390 400 410 420 LRQYLLNQGW WDEEQEKAWR KQSRKKVMEA FEQAERKLKP NPSLLFSDVY QEMPAQLRRQ 430 440 QESLARHLQT YGEHYPLDHF EK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Effects of insulin on the regulation of branched-chain alpha-keto acid dehydrogenase E1 alpha subunit gene expression." Costeas P.A., Chinsky J.M. Biochem. J. 318:85-92(1996) [PubMed: 8761456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J. Tissue: Liver.
[2]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, MASS SPECTROMETRY. Tissue: Liver.
[3]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L47335 mRNA. Translation: AAB38422.1.
IPI	IPI00331555.
PIR	S71881.
UniGene	Mm.25848
3D structure databases
HSSP	HSSP built from PDB template 1DTW based on UniProtKB P12694.
SMR	P50136. Positions 48-442.
ModBase	Search...
Protein-protein interaction databases
STRING	P50136.
2-D gel databases
SWISS-2DPAGE	P50136.
Proteomic databases
PRIDE	P50136.
Genome annotation databases
Ensembl	ENSMUST00000071329; ENSMUSP00000071292; ENSMUSG00000060376; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:107701. Bckdha.
Phylogenomic databases
HOVERGEN	P50136.
Enzyme and pathway databases
BRENDA	1.2.4.4. 244.
Gene expression databases
ArrayExpress	P50136.
Bgee	P50136.
Genevestigator	P50136.
GermOnline	ENSMUSG00000060376. Mus musculus.
Family and domain databases
InterPro	IPR001017. DH_E1. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

ODBA_MOUSE

Accession

Primary (citable) accession number: P50136

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	October 13, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)