[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2365818 [NCBI, ExPASy, EBI, Israel, Japan] Matsuda I., Asaka J., Akaboshi I., Endo F., Mitsubuchi H., Nobukuni Y.; "Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease."; J. Clin. Invest. 86:242-247(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Placenta; PubMed=8651316 [NCBI, ExPASy, EBI, Israel, Japan] Chuang J.L., Cox R.P., Chuang D.T.; "Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences."; Am. J. Hum. Genet. 58:1373-1377(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Eye; 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).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 20-392. DOI=10.1016/0014-5793(90)80215-5; PubMed=2335211 [NCBI, ExPASy, EBI, Israel, Japan] Chuang J.L., Cox R.P., Chuang D.T.; "Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex."; FEBS Lett. 262:305-309(1990).
[5]	PROTEIN SEQUENCE OF 36-62. DOI=10.1016/0304-4165(94)90161-9; PubMed=7918575 [NCBI, ExPASy, EBI, Israel, Japan] Wynn R.M., Kochi H., Cox R.P., Chuang D.T.; "Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence."; Biochim. Biophys. Acta 1201:125-128(1994).
[6]	VARIANT MSUD1B ARG-206. PubMed=8161368 [NCBI, ExPASy, EBI, Israel, Japan] Nobukuni Y., Mitsubuchi H., Hayashida Y., Ohta K., Indo Y., Ichiba Y., Endo F., Matsuda I.; "Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex."; Biochim. Biophys. Acta 1225:64-70(1993).
[7]	VARIANTS MSUD1B PRO-183 AND SER-278. DOI=10.1086/323677; PubMed=11509994 [NCBI, ExPASy, EBI, Israel, Japan] Edelmann L., Wasserstein M.P., Kornreich R., Sansaricq C., Snyderman S.E., Diaz G.A.; "Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population."; Am. J. Hum. Genet. 69:863-868(2001).

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.
INTERACTION:
P12694:BCKDHA; NbExp=4; IntAct=EBI-1029067, EBI-1029053;
SUBCELLULAR LOCATION: Mitochondrion matrix.
DISEASE: Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:248600]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=BCKDHB";.

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

M55575; AAA51812.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D90391; BAA14389.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC040139; AAH40139.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U50708; AAB16763.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52446; CAA36685.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A37157; A37157.

RefSeq

NP_000047.1; -.
NP_898871.1; -.

UniGene

Hs.654441

3D structure databases

PDB

1DTW; X-ray; 2.70 A; B=51-392.	[ExPASy / RCSB / EBI]
1OLS; X-ray; 1.85 A; B=51-392.	[ExPASy / RCSB / EBI]
1OLU; X-ray; 1.90 A; B=51-392.	[ExPASy / RCSB / EBI]
1OLX; X-ray; 2.25 A; B=51-392.	[ExPASy / RCSB / EBI]
1U5B; X-ray; 1.83 A; B=51-392.	[ExPASy / RCSB / EBI]
1V11; X-ray; 1.95 A; B=51-392.	[ExPASy / RCSB / EBI]
1V16; X-ray; 1.90 A; B=51-392.	[ExPASy / RCSB / EBI]
1V1M; X-ray; 2.00 A; B=51-392.	[ExPASy / RCSB / EBI]
1V1R; X-ray; 1.80 A; B=51-392.	[ExPASy / RCSB / EBI]
1WCI; X-ray; 1.84 A; B=51-392.	[ExPASy / RCSB / EBI]
1X7W; X-ray; 1.73 A; B=51-392.	[ExPASy / RCSB / EBI]
1X7X; X-ray; 2.10 A; B=51-392.	[ExPASy / RCSB / EBI]
1X7Y; X-ray; 1.57 A; B=51-392.	[ExPASy / RCSB / EBI]
1X7Z; X-ray; 1.72 A; B=51-392.	[ExPASy / RCSB / EBI]
1X80; X-ray; 2.00 A; B=51-392.	[ExPASy / RCSB / EBI]
2BEU; X-ray; 1.89 A; B=51-392.	[ExPASy / RCSB / EBI]
2BEV; X-ray; 1.80 A; B=51-392.	[ExPASy / RCSB / EBI]
2BEW; X-ray; 1.79 A; B=51-392.	[ExPASy / RCSB / EBI]
2BFB; X-ray; 1.77 A; B=51-392.	[ExPASy / RCSB / EBI]
2BFC; X-ray; 1.64 A; B=51-392.	[ExPASy / RCSB / EBI]
2BFD; X-ray; 1.39 A; B=51-392.	[ExPASy / RCSB / EBI]
2BFE; X-ray; 1.69 A; B=51-392.	[ExPASy / RCSB / EBI]
2BFF; X-ray; 1.46 A; B=51-392.	[ExPASy / RCSB / EBI]
2J9F; X-ray; 1.88 A; B/D=51-392.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DTW; -.
1OLS; -.
1OLU; -.
1OLX; -.
1U5B; -.
1V11; -.
1V16; -.
1V1M; -.
1V1R; -.
1WCI; -.
1X7W; -.
1X7X; -.
1X7Y; -.
1X7Z; -.
1X80; -.
2BEU; -.
2BEV; -.
2BEW; -.
2BFB; -.
2BFC; -.
2BFD; -.
2BFE; -.
2BFF; -.
2J9F; -.

ModBase

P21953.

Protein-protein interaction databases

DIP

DIP:6147N; -.

IntAct

P21953; -.

PTM databases

PhosphoSite

P21953; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12006; -.

Reactome

REACT_13; Metabolism of amino acids.

2D gel databases

REPRODUCTION-2DPAGE

IPI00011276; -.

Organism-specific databases

HIX0025076; -.

HGNC:987; BCKDHB.

248600; phenotype. [NCBI / EBI]
248611; gene. [NCBI / EBI]

Orphanet

511; Leucinosis.
2394; Lipoamide dehydrogenase deficiency.

PharmGKB

PA25298; -.

GeneCards

P21953.

Gene expression databases

ArrayExpress

P21953; -.

CleanEx

HS_BCKDHB; -.

GermOnline

ENSG00000083123; Homo sapiens.

Ontologies

GO:0005947;	Cellular component: mitochondrial alpha-ketoglutarate dehydrogenase complex (inferred from mutant phenotype from HGNC).
GO:0003863;	Molecular function: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity (traceable author statement from ProtInc).
GO:0016831;	Molecular function: carboxy-lyase activity (traceable author statement from HGNC).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0009083;	Biological process: branched chain family amino acid catabolic process (inferred from mutant phenotype 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; 1.

Pfam

PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.

BLOCKS

P21953.

Proteomic databases

PeptideAtlas

P21953; -.

Genome annotation databases

Ensembl

ENSG00000083123; Homo sapiens. [Contig view]

GeneID

594; -.

KEGG

hsa:594; -.

Phylogenomic databases

HOGENOM

P21953; -.

HOVERGEN

P21953; -.

Other

SOURCE

BCKDHB; Homo sapiens.

ProtoNet

P21953.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; Disease mutation; Maple syrup urine disease; Mitochondrion; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 50`	`50`	`Mitochondrion.`
`CHAIN`	`51 392`	`342`	`2-oxoisovalerate dehydrogenase subunit beta, mitochondrial.`	`PRO_0000020470`
`VARIANT`	`183 183`	`1`	`R -> P (in MSUD1B; dbSNP:rs28934895 [NCBI]).`	`VAR_024851 [3D]`
`VARIANT`	`206 206`	`1`	`H -> R (in MSUD1B).`	`VAR_004974 [3D]`
`VARIANT`	`278 278`	`1`	`G -> S (in MSUD1B).`	`VAR_024852 [3D]`
`CONFLICT`	`20 23`		`EGHW -> RLPP (in Ref. 4).`
`CONFLICT`	`322 322`		`T -> S (in Ref. 4; CAA36685).`
`STRAND`	`68 71`	`4`
`HELIX`	`73 87`	`15`
`STRAND`	`92 95`	`4`
`TURN`	`96 101`	`6`
`TURN`	`106 109`	`4`
`HELIX`	`110 114`	`5`
`TURN`	`116 118`	`3`
`STRAND`	`119 121`	`3`
`HELIX`	`126 138`	`13`
`STRAND`	`143 146`	`4`
`HELIX`	`150 152`	`3`
`HELIX`	`154 156`	`3`
`HELIX`	`157 161`	`5`
`HELIX`	`164 166`	`3`
`HELIX`	`167 170`	`4`
`TURN`	`171 173`	`3`
`STRAND`	`180 187`	`8`
`HELIX`	`193 195`	`3`
`HELIX`	`201 205`	`5`
`STRAND`	`211 213`	`3`
`HELIX`	`218 230`	`13`
`STRAND`	`231 233`	`3`
`STRAND`	`235 240`	`6`
`HELIX`	`241 243`	`3`
`STRAND`	`249 254`	`6`
`STRAND`	`264 267`	`4`
`STRAND`	`270 276`	`7`
`HELIX`	`280 295`	`16`
`STRAND`	`299 303`	`5`
`STRAND`	`306 309`	`4`
`HELIX`	`312 322`	`11`
`STRAND`	`325 333`	`9`
`HELIX`	`337 349`	`13`
`HELIX`	`350 352`	`3`
`STRAND`	`358 362`	`5`
`HELIX`	`372 375`	`4`
`HELIX`	`379 390`	`12`

Sequence information

Length: 392 AA [This is the length of the unprocessed precursor]

Molecular weight: 43122 Da [This is the MW of the unprocessed precursor]

CRC64: D78097834D063BB7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVVAAAAGW LLRLRAAGAE GHWRRLPGAG LARGFLHPAA TVEDAAQRRQ VAHFTFQPDP 

        70         80         90        100        110        120 
EPREYGQTQK MNLFQSVTSA LDNSLAKDPT AVIFGEDVAF GGVFRCTVGL RDKYGKDRVF 

       130        140        150        160        170        180 
NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL 

       190        200        210        220        230        240 
TIRSPWGCVG HGALYHSQSP EAFFAHCPGI KVVIPRSPFQ AKGLLLSCIE DKNPCIFFEP 

       250        260        270        280        290        300 
KILYRAAAEE VPIEPYNIPL SQAEVIQEGS DVTLVAWGTQ VHVIREVASM AKEKLGVSCE 

       310        320        330        340        350        360 
VIDLRTIIPW DVDTICKSVI KTGRLLISHE APLTGGFASE ISSTVQEECF LNLEAPISRV 

       370        380        390 
CGYDTPFPHI FEPFYIPDKW KCYDALRKMI NY

P21953 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