NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3379058 [NCBI, ExPASy, EBI, Israel, Japan]
Hu C.-W.C., Lau K.S., Griffin T.A., Chuang J.L., Fisher C.W., Cox R.P., Chuang D.T.;
"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.";
J. Biol. Chem. 263:9007-9014(1988).

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

J03759; AAA30595.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A28073; DEBOXA.

NP_776931.1; -.

3D structure databases

HSSP

P12694; 1DTW. [HSSP ENTRY / PDB]

SMR

P11178; 61-455.

ModBase

P11178.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003863;	Molecular function: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity (inferred from electronic annotation from EC).
GO:0030955;	Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

Ensembl

ENSBTAG00000016037; Bos taurus. [Contig view]

GeneID

282149; -.

KEGG

bta:282149; -.

Phylogenomic databases

HOVERGEN

P11178; -.

Other

ProtoNet

P11178.

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 55`	`55`	`Mitochondrion.`
`CHAIN`	`56 455`	`400`	`2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial.`	`PRO_0000020464`
`REGION`	`167 169`	`3`	`Thiamine pyrophosphate binding (By similarity).`
`METAL`	`216 216`		`Potassium (By similarity).`
`METAL`	`221 221`		`Potassium (By similarity).`
`METAL`	`222 222`		`Potassium (By similarity).`
`MOD_RES`	`347 347`		`Phosphoserine (By similarity).`
`MOD_RES`	`355 355`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`357 357`		`Phosphoserine (By similarity).`

Sequence information

Length: 455 AA [This is the length of the unprocessed precursor]

Molecular weight: 51678 Da [This is the MW of the unprocessed precursor]

CRC64: 66A7CA6003E0B846 [This is a checksum on the sequence]

        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

P11178 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