A5A6H9 (ODBA_PANTR) Reviewed, UniProtKB/Swiss-Prot

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=BCKDE1A
Short name=BCKDH E1-alpha

Gene names

Name:

BCKDHA

Organism

Pan troglodytes (Chimpanzee)

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan

Protein attributes

Sequence length	445 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 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 By similarity.
Subunit structure	Heterotetramer of alpha and beta chains By similarity.
Subcellular location	Mitochondrion matrix By similarity.
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)
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 metal 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 – 45	45	Mitochondrion By similarity
	Chain	46 – 445	400	2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial		PRO_0000296643
Regions
	Region	157 – 159	3	Thiamine pyrophosphate binding By similarity
Sites
	Metal binding	206	1	Potassium By similarity
	Metal binding	211	1	Potassium By similarity
	Metal binding	212	1	Potassium By similarity
Amino acid modifications
	Modified residue	337	1	Phosphoserine By similarity
	Modified residue	345	1	Phosphotyrosine By similarity
	Modified residue	347	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5A6H9 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: 40DAB94B2BA6C074	FASTA	445	50,516
	10 20 30 40 50 60 MAVAIAAARV WRLNRGLSQA ALLLLRRPGA RGLARSHPRR QQQQFSSLDD KPQFPGASAE 70 80 90 100 110 120 FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPKE KVLKLYKSMT LLNTMDRILY 130 140 150 160 170 180 ESQRQGRISF YMTNYGEEGT HVGSAAALDN TDLVFGQYRE AGVLMYRDYP LELFMAQCYG 190 200 210 220 230 240 NISDLGKGRQ MPVHYGCKER HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA 250 260 270 280 290 300 ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG YGIMSIRVDG 310 320 330 340 350 360 NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE VNYWDKQDHP 370 380 390 400 410 420 VSRLRHYLLS QGWWDEEQEK AWRKQSRKKV MEAFEQAERK PKPNPNLLFS DVYQEMPAQL 430 440 RKQQESLARH LQTYGEHYPL DHFDK

References

[1]

"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome." Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M. Gene 399:1-10(2007) [PubMed: 17574350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cerebellum.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB222107 mRNA. Translation: BAF62352.1.
RefSeq	NP_001092034.1. NM_001098564.1.
UniGene	Ptr.894.
3D structure databases
ProteinModelPortal	A5A6H9.
SMR	A5A6H9. Positions 51-445.
ModBase	Search...
Protein-protein interaction databases
STRING	A5A6H9.
Proteomic databases
PRIDE	A5A6H9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	468889.
KEGG	ptr:468889.
Organism-specific databases
CTD	593.
Phylogenomic databases
eggNOG	prNOG05655.
GeneTree	ENSGT00530000063174.
HOVERGEN	HBG002459.
Family and domain databases
InterPro	IPR001017. DH_E1. [Graphical view]
KO	K00166.
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODBA_PANTR

Accession

Primary (citable) accession number: A5A6H9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	June 12, 2007
Last modified:	November 16, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program