Reviewed, UniProtKB/Swiss-Prot P11178 (ODBA_BOVIN)

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC 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 – 55	55	Mitochondrion
	Chain	56 – 455	400	2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial		PRO_0000020464
Regions
	Region	167 – 169	3	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	216	1	Potassium By similarity
	Metal binding	221	1	Potassium By similarity
	Metal binding	222	1	Potassium By similarity
Amino acid modifications
	Modified residue	347	1	Phosphoserine By similarity
	Modified residue	355	1	Phosphotyrosine By similarity
	Modified residue	357	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P11178-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 66A7CA6003E0B846	FASTA	455	51,678
	10 20 30 40 50 60 MQGSAKMAMA VAVAVARVWR PSRGLGRTGL PLLRLLGARG LARFHPHRWQ QQQHFSSLDD 70 80 90 100 110 120 KPQFPGASAE FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPQE KVLKFYKSMT 130 140 150 160 170 180 LLNTMDRILY ESQRQGRISF YMTNYGEEGT HVGSAAALDD TDLVFGQYRE AGVLMYRDYP 190 200 210 220 230 240 LELFMAQCYG NVSDLGKGRQ MPVHYGCRER HFVTISSPLA TQIPQAVGAA YAAKRANANR 250 260 270 280 290 300 VVICYFGEGA ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG 310 320 330 340 350 360 YGILSIRVDG NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE 370 380 390 400 410 420 VNYWDKQDHP ISRLRHHLQS RGWWDDEQEK AWRKQSRKKV MEAFEQAERK LKPNPSLIFS 430 440 450 DVYQEMPAQL RKQQESLARH LQTYGEHYPL DHFEK

References

[1]

"Isolation and sequencing of a cDNA encoding the decarboxylase (E1)alpha precursor of bovine branched-chain alpha-keto acid dehydrogenase complex. Expression of E1 alpha mRNA and subunit in maple-syrup-urine-disease and 3T3-L1 cells." Hu C.-W.C., Lau K.S., Griffin T.A., Chuang J.L., Fisher C.W., Cox R.P., Chuang D.T. J. Biol. Chem. 263:9007-9014(1988) [PubMed: 3379058] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03759 mRNA. Translation: AAA30595.1.
PIR	DEBOXA. A28073.
RefSeq	NP_776931.1.
UniGene	Bt.5287
3D structure databases
HSSP	HSSP built from PDB template 1DTW based on UniProtKB P12694.
SMR	P11178. Positions 61-455.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000016037. Bos taurus. [Contig view]
GeneID	282149.
KEGG	bta:282149.
Phylogenomic databases
HOVERGEN	P11178.
Family and domain databases
InterPro	IPR001017. DHase_E1. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODBA_BOVIN

Accession

Primary (citable) accession number: P11178

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	November 4, 2008
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)