[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1016/0378-1119(90)90294-2; PubMed=2323578 [NCBI, ExPASy, EBI, Israel, Japan] Ho L., Patel M.S.; "Cloning and cDNA sequence of the beta-subunit component of human pyruvate dehydrogenase complex."; Gene 86:297-302(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). PubMed=1702713 [NCBI, ExPASy, EBI, Israel, Japan] Chun K., MacKay N., Willard H.F., Robinson B.H.; "Isolation, characterization and chromosomal localization of cDNA clones for the E1 beta subunit of the pyruvate dehydrogenase complex."; Eur. J. Biochem. 194:587-592(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-31. PubMed=2376596 [NCBI, ExPASy, EBI, Israel, Japan] Huh T.L., Casazza J.P., Huh J.W., Chi Y.T., Song B.J.; "Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast."; J. Biol. Chem. 265:13320-13326(1990).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). PubMed=2377599 [NCBI, ExPASy, EBI, Israel, Japan] Koike K., Urata Y., Koike M.; "Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene."; Proc. Natl. Acad. Sci. U.S.A. 87:5594-5597(1990).
[5]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-31. PubMed=3422424 [NCBI, ExPASy, EBI, Israel, Japan] Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.; "Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase."; Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). TISSUE=Brain; DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan] Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.; "Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."; Genome Res. 11:422-435(2001).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Lung; 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).
[9]	PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 23-69. DOI=10.1016/0006-291X(88)90714-0; PubMed=2829898 [NCBI, ExPASy, EBI, Israel, Japan] Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C., Mole J.E., Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S.; "Identification of a cDNA clone for the beta-subunit of the pyruvate dehydrogenase component of human pyruvate dehydrogenase complex."; Biochem. Biophys. Res. Commun. 150:904-908(1988).
[10]	PROTEIN SEQUENCE OF 31-43. TISSUE=Heart; DOI=10.1002/elps.11501501209; PubMed=7895732 [NCBI, ExPASy, EBI, Israel, Japan] Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.; "The human myocardial two-dimensional gel protein database: update 1994."; Electrophoresis 15:1459-1465(1994).
[11]	PROTEIN SEQUENCE OF 31-55. PubMed=2295468 [NCBI, ExPASy, EBI, Israel, Japan] Muno D., Kominami E., Ishii H., Usui K., Saifuku K., Sakakibara Y., Namihisa T.; "Isolation of tryptic fragment of antigen from mitochondrial inner membrane proteins reacting with antimitochondrial antibody in sera of patients with primary biliary cirrhosis."; Hepatology 11:16-23(1990).
[12]	X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 32-359 IN COMPLEX WITH THIAMINE PYROPHOSPHATE. DOI=10.1074/jbc.M300339200; PubMed=12651851 [NCBI, ExPASy, EBI, Israel, Japan] Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.; "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase."; J. Biol. Chem. 278:21240-21246(2003).
[13]	VARIANTS PDHE1 DEFICIENCY CYS-132 AND SER-344. DOI=10.1007/s00439-004-1124-8; PubMed=15138885 [NCBI, ExPASy, EBI, Israel, Japan] Brown R.M., Head R.A., Boubriak I.I., Leonard J.V., Thomas N.H., Brown G.K.; "Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency."; Hum. Genet. 115:123-127(2004).

Comments

FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate.
SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
SUBCELLULAR LOCATION: Mitochondrion matrix.

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

Name	1
Isoform ID	P11177-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P11177-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_012675.

DISEASE: Defects in PDHB are a cause of pyruvate dehydrogenase E1 component deficiency (PDHE1 deficiency) [MIM:312170]. PDHE1 deficiency is the most common enzyme defect in patients with primary lactic acidosis. It is associated with variable clinical phenotypes ranging from neonatal death to prolonged survival complicated by developmental delay, seizures, ataxia, apnea, and in some cases to an X-linked form of Leigh syndrome (LS) (Leigh encephalomyelopathy).

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

M34479; AAA36428.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19123; AAA60052.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M54788; AAA60053.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34055; AAA60233.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34056; AAA60054.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D90086; BAA14123.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J03576; AAA88097.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL117618; CAB56017.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541911; CAG46709.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000439; AAH00439.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001924; AAH01924.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57778; CAA40924.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JU0145; DEHUPB.

NP_000916.2; -.

3D structure databases

PDB

1NI4; X-ray; 1.95 A; B/D=32-359.	[ExPASy / RCSB / EBI]
2OZL; X-ray; 1.90 A; B/D=31-359.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1NI4; -.
2OZL; -.

ModBase

P11177.

Protein-protein interaction databases

IntAct

P11177; 8.

PTM databases

PhosphoSite

P11177; -.

Enzyme and pathway databases

Reactome

REACT_1046; Pyruvate metabolism and TCA cycle.

2D gel databases

SWISS-2DPAGE

P11177; -.

HSC-2DPAGE

P11177; -.

REPRODUCTION-2DPAGE

IPI00549885; -.

Organism-specific databases

GC03M058388; -.

HIX0003404; -.

HGNC:8808; PDHB.

179060; gene+phenotype. [NCBI / EBI]
312170; phenotype. [NCBI / EBI]

Orphanet

765; Pyruvate dehydrogenase deficiency.

PharmGKB

PA33152; -.

GeneCards

P11177.

Gene expression databases

ArrayExpress

P11177; -.

CleanEx

HS_PDHB; -.

GermOnline

ENSG00000168291; Homo sapiens.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004739;	Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (traceable author statement from ProtInc).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (traceable author statement from ProtInc).
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.

Proteomics databases

PRIDE

P11177; -.

Genome annotation databases

Ensembl

ENSG00000168291; Homo sapiens. [Contig view]

GeneID

5162; -.

KEGG

hsa:5162; -.

Phylogenomic databases

HOGENOM

P11177; -.

HOVERGEN

P11177; -.

Other

DrugBank

DB00157; NADH.
DB00119; Pyruvic acid.

19970; -.

PDHB; Homo sapiens.

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

Keywords

3D-structure; Alternative splicing; Direct protein sequencing; Disease mutation; Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Polymorphism; Pyruvate; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 30`	`30`	`Mitochondrion.`
`CHAIN`	`31 359`	`329`	`Pyruvate dehydrogenase E1 component subunit beta, mitochondrial.`	`PRO_0000020457`
`BINDING`	`89 89`		`Thiamine pyrophosphate.`
`MOD_RES`	`67 67`		`Phosphotyrosine (By similarity).`
`VAR_SEQ`	`16 33`		`Missing (in isoform 2).`	`VSP_012675`
`VARIANT`	`31 31`	`1`	`L -> V.`	`VAR_004967 [3D]`
`VARIANT`	`132 132`	`1`	`Y -> C (in PDHE1 deficiency; dbSNP:rs28935769 [NCBI]).`	`VAR_030954 [3D]`
`VARIANT`	`344 344`	`1`	`P -> S (in PDHE1 deficiency; dbSNP:rs28933391 [NCBI]).`	`VAR_021058 [3D]`
`CONFLICT`	`9 13`		`RRPLR -> AETPS (in Ref. 5).`
`CONFLICT`	`43 43`		`M -> G (in Ref. 10; AA sequence).`
`CONFLICT`	`160 160`		`Q -> G (in Ref. 5).`
`CONFLICT`	`213 221`		`PPEAQSKDF -> LRKLSQKIL (in Ref. 5).`
`CONFLICT`	`213 213`		`P -> L (in Ref. 4; AAA88097/BAA14123).`
`CONFLICT`	`310 312`		`MEG -> NGS (in Ref. 5).`
`STRAND`	`32 34`	`3`
`HELIX`	`35 49`	`15`
`STRAND`	`53 57`	`5`
`TURN`	`69 72`	`4`
`HELIX`	`73 77`	`5`
`TURN`	`79 81`	`3`
`STRAND`	`82 84`	`3`
`HELIX`	`89 101`	`13`
`STRAND`	`105 109`	`5`
`HELIX`	`113 119`	`7`
`HELIX`	`120 125`	`6`
`TURN`	`126 128`	`3`
`HELIX`	`130 133`	`4`
`STRAND`	`143 147`	`5`
`HELIX`	`156 158`	`3`
`HELIX`	`163 167`	`5`
`STRAND`	`173 175`	`3`
`HELIX`	`180 192`	`13`
`STRAND`	`193 195`	`3`
`STRAND`	`197 201`	`5`
`HELIX`	`203 205`	`3`
`STRAND`	`209 211`	`3`
`HELIX`	`214 217`	`4`
`STRAND`	`229 232`	`4`
`STRAND`	`235 241`	`7`
`HELIX`	`245 257`	`13`
`TURN`	`258 260`	`3`
`STRAND`	`263 267`	`5`
`STRAND`	`270 272`	`3`
`HELIX`	`276 286`	`11`
`STRAND`	`289 292`	`4`
`HELIX`	`301 311`	`11`
`HELIX`	`313 317`	`5`
`STRAND`	`323 325`	`3`
`HELIX`	`336 340`	`5`
`HELIX`	`346 356`	`11`

Sequence information

Length: 359 AA [This is the length of the unprocessed precursor]

Molecular weight: 39233 Da [This is the MW of the unprocessed precursor]

CRC64: AB459B1259FBDBD3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD EKVFLLGEEV 

        70         80         90        100        110        120 
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 

       130        140        150        160        170        180 
DQVINSAAKT YYMSGGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS 

       190        200        210        220        230        240 
EDAKGLIKSA IRDNNPVVVL ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV 

       250        260        270        280        290        300 
SHSRPVGHCL EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG 

       310        320        330        340        350 
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI

P11177 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