[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1016/0167-4781(93)90023-7; PubMed=8268236 [NCBI, ExPASy, EBI, Israel, Japan] Chinsky J.M., Costeas P.A.; "Molecular cloning and analysis of the expression of the E1 beta subunit of branched chain alpha-ketoacid dehydrogenase in mice."; Biochim. Biophys. Acta 1216:499-503(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). STRAIN=C57BL/6J; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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.
SUBUNIT: Heterodimer of an alpha and a beta chain.
SUBCELLULAR LOCATION: Mitochondrion matrix.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q6P3A8-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q6P3A8-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_029841.

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

L16992; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]
BC064099; AAH64099.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_954665.1; -.
XP_001481012.1; -.

UniGene

Mm.12819

3D structure databases

SMR

Q6P3A8; 1-322.

ModBase

Q6P3A8.

Organism-specific databases

MGI

MGI:88137; Bckdhb.

Gene expression databases

ArrayExpress

Q6P3A8; -.

Ontologies

GO:0005947;	Cellular component: mitochondrial alpha-ketoglutarate dehydrogenase complex (inferred from sequence or structural similarity from HGNC).
GO:0005743;	Cellular component: mitochondrial inner membrane (traceable author statement from MGI).
GO:0003826;	Molecular function: alpha-ketoacid dehydrogenase activity (inferred from direct assay from MGI).
GO:0009083;	Biological process: branched chain family amino acid catabolic process (inferred from sequence or structural similarity from HGNC).
QuickGo view.

Family and domain databases

InterPro

IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.920; Transketo_C_like; 2.

Pfam

PF02779; Transket_pyr; 2.
PF02780; Transketolase_C; 2.
Pfam graphical view of domain structure.

BLOCKS

Q6P3A8.

Genome annotation databases

Ensembl

ENSMUSG00000032263; Mus musculus. [Contig view]

GeneID

100048676; -.
12040; -.

KEGG

mmu:100048676; -.
mmu:12040; -.

Phylogenomic databases

HOGENOM

Q6P3A8; -.

HOVERGEN

Q6P3A8; -.

Other

SOURCE

Bckdhb; Mus musculus.

ProtoNet

Q6P3A8.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 48`	`48`	`Mitochondrion (Potential).`
`CHAIN`	`49 390`	`342`	`2-oxoisovalerate dehydrogenase subunit beta, mitochondrial.`	`PRO_0000312367`
`VAR_SEQ`	`1 68`		`Missing (in isoform 2).`	`VSP_029841`

Sequence information

Length: 390 AA [This is the length of the unprocessed precursor]

Molecular weight: 42880 Da [This is the MW of the unprocessed precursor]

CRC64: 507E04F01BCCD298 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVAARAGG LLWLRAAGAE RRRCGLRCAA LVQGFLQPGG EDTAQKRRVA HFTFHPDPES 

        70         80         90        100        110        120 
LQYGQTQKMN LFQSITSALD NSLAKDPTAV IFGEDVAFGG VFRCTVGLRD KYGKDRVFNT 

       130        140        150        160        170        180 
PLCEQGIVGF GIGIAVTGAT AIAEIQFADY IFPAFDQIVN EAAKYRYRSG DLFNCGSLTI 

       190        200        210        220        230        240 
RAPWGCVGHG ALYHSQSPEA FFAHCPGIKV VIPRSPFQAK GLLLSCIEDK NPCIFFEPKI 

       250        260        270        280        290        300 
LYRAAVEQVP VEPYKIPLSQ AEVIQEGSDV TLVAWGTQVH VIREVASMAQ EKLGVSCEVI 

       310        320        330        340        350        360 
DLRTIVPWDV DTVCKSVIKT GRLLISHEAP LTGGFASEIS STVQEECFLN LEAPISRVCG 

       370        380        390 
YDTPFPHIFE PFYIPDKWKC YDALRKMINY

Q6P3A8 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