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Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHE1-B) (EC 1.2.4.1)

 ODPB_HUMAN              Reviewed;         359 AA.
P11177; B2R7L0; B4DDD7; Q6FH45; Q9BQ27; Q9UFK3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 3.
25-OCT-2017, entry version 207.
RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
Short=PDHE1-B;
EC=1.2.4.1;
Flags: Precursor;
Name=PDHB; Synonyms=PHE1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2323578; DOI=10.1016/0378-1119(90)90294-2;
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; DOI=10.1111/j.1432-1033.1990.tb15656.x;
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;
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; DOI=10.1073/pnas.87.15.5594;
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; DOI=10.1073/pnas.85.1.41;
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;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
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] (ISOFORMS 1 AND 3).
TISSUE=Brain cortex;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[12]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 23-69.
PubMed=2829898; DOI=10.1016/0006-291X(88)90714-0;
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).
[13]
PROTEIN SEQUENCE OF 31-43.
TISSUE=Heart;
PubMed=7895732; DOI=10.1002/elps.11501501209;
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).
[14]
PROTEIN SEQUENCE OF 31-55.
PubMed=2295468; DOI=10.1002/hep.1840110105;
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).
[15]
SUBUNIT.
PubMed=14638692; DOI=10.1074/jbc.M308172200;
Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.;
"Organization of the cores of the mammalian pyruvate dehydrogenase
complex formed by E2 and E2 plus the E3-binding protein and their
capacities to bind the E1 and E3 components.";
J. Biol. Chem. 279:6921-6933(2004).
[16]
INTERACTION WITH DLAT, AND MUTAGENESIS OF GLU-259; GLU-262; GLU-264;
ASP-319 AND ILE-359.
PubMed=20160912; DOI=10.1016/j.molcatb.2009.05.001;
Patel M.S., Korotchkina L.G., Sidhu S.;
"Interaction of E1 and E3 components with the core proteins of the
human pyruvate dehydrogenase complex.";
J. Mol. Catal., B Enzym. 61:2-6(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 32-359 IN COMPLEX WITH
THIAMINE PYROPHOSPHATE, AND COFACTOR.
PubMed=12651851; DOI=10.1074/jbc.M300339200;
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).
[21]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 32-359, SUBUNIT, AND
FUNCTION.
PubMed=17474719; DOI=10.1021/bi700083z;
Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M.,
Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.;
"Phosphorylation of serine 264 impedes active site accessibility in
the E1 component of the human pyruvate dehydrogenase multienzyme
complex.";
Biochemistry 46:6277-6287(2007).
[22]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 31-359, CATALYTIC ACTIVITY,
SUBUNIT, COFACTOR, AND FUNCTION.
PubMed=19081061; DOI=10.1016/j.str.2008.10.010;
Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J.,
Chuang D.T.;
"Structural basis for inactivation of the human pyruvate dehydrogenase
complex by phosphorylation: role of disordered phosphorylation
loops.";
Structure 16:1849-1859(2008).
[23]
VARIANTS PDHBD CYS-132 AND SER-344.
PubMed=15138885; DOI=10.1007/s00439-004-1124-8;
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).
-!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
conversion of pyruvate to acetyl-CoA and CO(2), and thereby links
the glycolytic pathway to the tricarboxylic cycle.
{ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061}.
-!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
{ECO:0000269|PubMed:19081061}.
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Evidence={ECO:0000269|PubMed:12651851,
ECO:0000269|PubMed:19081061};
-!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits
(PubMed:12651851, PubMed:17474719, PubMed:19081061). The
heterotetramer interacts with DLAT, and is part of the multimeric
pyruvate dehydrogenase complex that contains multiple copies of
pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase
(DLAT, E2) and lipoamide dehydrogenase (DLD, E3)
(PubMed:14638692). These subunits are bound to an inner core
composed of about 48 DLAT and 12 PDHX molecules (PubMed:14638692).
Interacts with DLAT (PubMed:20160912).
{ECO:0000269|PubMed:12651851, ECO:0000269|PubMed:14638692,
ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061,
ECO:0000269|PubMed:20160912}.
-!- INTERACTION:
P10515:DLAT; NbExp=7; IntAct=EBI-1035872, EBI-2959723;
P08559:PDHA1; NbExp=3; IntAct=EBI-1035872, EBI-715747;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P11177-1; Sequence=Displayed;
Name=2;
IsoId=P11177-2; Sequence=VSP_012675;
Note=No experimental confirmation available.;
Name=3;
IsoId=P11177-3; Sequence=VSP_043364;
Note=No experimental confirmation available.;
-!- DISEASE: Pyruvate dehydrogenase E1-beta deficiency (PDHBD)
[MIM:614111]: An enzymatic defect causing primary lactic acidosis
in children. It is associated with a broad clinical spectrum
ranging from fatal lactic acidosis in the newborn to chronic
neurologic dysfunction with structural abnormalities in the
central nervous system without systemic acidosis.
{ECO:0000269|PubMed:15138885}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; M34479; AAA36428.1; -; mRNA.
EMBL; M19123; AAA60052.1; ALT_SEQ; mRNA.
EMBL; M54788; AAA60053.1; -; mRNA.
EMBL; M34055; AAA60233.1; -; mRNA.
EMBL; M34056; AAA60054.1; -; mRNA.
EMBL; D90086; BAA14123.1; -; Genomic_DNA.
EMBL; J03576; AAA88097.1; -; mRNA.
EMBL; AL117618; CAB56017.1; -; mRNA.
EMBL; CR541911; CAG46709.1; -; mRNA.
EMBL; AK293153; BAG56698.1; -; mRNA.
EMBL; AK313022; BAG35857.1; -; mRNA.
EMBL; AC135507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW65371.1; -; Genomic_DNA.
EMBL; BC000439; AAH00439.1; -; mRNA.
EMBL; BC001924; AAH01924.1; -; mRNA.
EMBL; X57778; CAA40924.1; -; mRNA.
CCDS; CCDS2890.1; -. [P11177-1]
CCDS; CCDS54602.1; -. [P11177-3]
CCDS; CCDS82795.1; -. [P11177-2]
PIR; JU0145; DEHUPB.
RefSeq; NP_000916.2; NM_000925.3. [P11177-1]
RefSeq; NP_001166939.1; NM_001173468.1. [P11177-3]
RefSeq; NP_001302465.1; NM_001315536.1. [P11177-2]
UniGene; Hs.161357; -.
PDB; 1NI4; X-ray; 1.95 A; B/D=31-359.
PDB; 2OZL; X-ray; 1.90 A; B/D=32-359.
PDB; 3EXE; X-ray; 1.98 A; B/D/F/H=31-359.
PDB; 3EXF; X-ray; 3.00 A; B/D/F/H=31-359.
PDB; 3EXG; X-ray; 3.01 A; 2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z=31-359.
PDB; 3EXH; X-ray; 2.44 A; B/D/F/H=31-359.
PDB; 3EXI; X-ray; 2.20 A; B=31-359.
PDBsum; 1NI4; -.
PDBsum; 2OZL; -.
PDBsum; 3EXE; -.
PDBsum; 3EXF; -.
PDBsum; 3EXG; -.
PDBsum; 3EXH; -.
PDBsum; 3EXI; -.
ProteinModelPortal; P11177; -.
SMR; P11177; -.
BioGrid; 111188; 65.
DIP; DIP-37651N; -.
IntAct; P11177; 24.
MINT; MINT-3007546; -.
STRING; 9606.ENSP00000307241; -.
DrugBank; DB00157; NADH.
DrugBank; DB00119; Pyruvic acid.
iPTMnet; P11177; -.
PhosphoSitePlus; P11177; -.
SwissPalm; P11177; -.
BioMuta; PDHB; -.
DMDM; 134044259; -.
REPRODUCTION-2DPAGE; IPI00549885; -.
SWISS-2DPAGE; P11177; -.
UCD-2DPAGE; P11177; -.
EPD; P11177; -.
MaxQB; P11177; -.
PaxDb; P11177; -.
PeptideAtlas; P11177; -.
PRIDE; P11177; -.
TopDownProteomics; P11177-1; -. [P11177-1]
DNASU; 5162; -.
Ensembl; ENST00000302746; ENSP00000307241; ENSG00000168291. [P11177-1]
Ensembl; ENST00000383714; ENSP00000373220; ENSG00000168291. [P11177-2]
Ensembl; ENST00000485460; ENSP00000417267; ENSG00000168291. [P11177-3]
GeneID; 5162; -.
KEGG; hsa:5162; -.
UCSC; uc003dkf.4; human. [P11177-1]
CTD; 5162; -.
DisGeNET; 5162; -.
EuPathDB; HostDB:ENSG00000168291.12; -.
GeneCards; PDHB; -.
HGNC; HGNC:8808; PDHB.
HPA; CAB033794; -.
HPA; HPA036744; -.
HPA; HPA036745; -.
MalaCards; PDHB; -.
MIM; 179060; gene.
MIM; 614111; phenotype.
neXtProt; NX_P11177; -.
OpenTargets; ENSG00000168291; -.
Orphanet; 255138; Pyruvate dehydrogenase E1-beta deficiency.
PharmGKB; PA33152; -.
eggNOG; KOG0524; Eukaryota.
eggNOG; COG0022; LUCA.
GeneTree; ENSGT00530000063423; -.
HOGENOM; HOG000281450; -.
HOVERGEN; HBG000917; -.
InParanoid; P11177; -.
KO; K00162; -.
OMA; SRMRHHC; -.
OrthoDB; EOG091G0D37; -.
PhylomeDB; P11177; -.
TreeFam; TF105674; -.
BioCyc; MetaCyc:HS09727-MONOMER; -.
Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
Reactome; R-HSA-70268; Pyruvate metabolism.
SABIO-RK; P11177; -.
ChiTaRS; PDHB; human.
EvolutionaryTrace; P11177; -.
GeneWiki; Pyruvate_dehydrogenase_(lipoamide)_beta; -.
GenomeRNAi; 5162; -.
PRO; PR:P11177; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000168291; -.
CleanEx; HS_PDHB; -.
ExpressionAtlas; P11177; baseline and differential.
Genevisible; P11177; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; TAS:ProtInc.
GO; GO:0004738; F:pyruvate dehydrogenase activity; IDA:UniProtKB.
GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:UniProtKB.
GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; IC:MGI.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
GO; GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
GO; GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB.
Gene3D; 3.40.50.920; -; 1.
InterPro; IPR029061; THDP-binding.
InterPro; IPR009014; Transketo_C/PFOR_II.
InterPro; IPR005475; Transketolase-like_Pyr-bd.
InterPro; IPR033248; Transketolase_C.
Pfam; PF02779; Transket_pyr; 1.
Pfam; PF02780; Transketolase_C; 1.
SMART; SM00861; Transket_pyr; 1.
SUPFAM; SSF52518; SSF52518; 1.
SUPFAM; SSF52922; SSF52922; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
Disease mutation; Glucose metabolism; Mitochondrion; Oxidoreductase;
Phosphoprotein; Polymorphism; Pyruvate; Reference proteome;
Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle.
TRANSIT 1 30 Mitochondrion.
{ECO:0000269|PubMed:2295468,
ECO:0000269|PubMed:7895732}.
CHAIN 31 359 Pyruvate dehydrogenase E1 component
subunit beta, mitochondrial.
/FTId=PRO_0000020457.
BINDING 89 89 Thiamine pyrophosphate.
{ECO:0000269|PubMed:12651851}.
SITE 319 319 Important for interaction with DLAT.
{ECO:0000269|PubMed:20160912}.
MOD_RES 67 67 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9D051}.
MOD_RES 354 354 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D051}.
VAR_SEQ 16 33 Missing (in isoform 2).
{ECO:0000303|PubMed:11230166}.
/FTId=VSP_012675.
VAR_SEQ 135 152 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043364.
VARIANT 31 31 L -> V. {ECO:0000269|PubMed:2376596,
ECO:0000269|PubMed:3422424}.
/FTId=VAR_004967.
VARIANT 132 132 Y -> C (in PDHBD; dbSNP:rs28935769).
{ECO:0000269|PubMed:15138885}.
/FTId=VAR_030954.
VARIANT 344 344 P -> S (in PDHBD; dbSNP:rs28933391).
{ECO:0000269|PubMed:15138885}.
/FTId=VAR_021058.
MUTAGEN 259 259 E->A,Q: Does not affect interaction with
DLAT. {ECO:0000269|PubMed:20160912}.
MUTAGEN 262 262 E->A,Q: Does not affect interaction with
DLAT. {ECO:0000269|PubMed:20160912}.
MUTAGEN 264 264 E->A,Q: Does not affect interaction with
DLAT. {ECO:0000269|PubMed:20160912}.
MUTAGEN 319 319 D->A: Inhibits interaction with DLAT.
Does not affect pyruvate decarboxylase
activity. Loss of multienzyme pyruvate
dehydrogenase complex activity.
{ECO:0000269|PubMed:20160912}.
MUTAGEN 319 319 D->N: Reduces interaction with DLAT.
Reduces multienzyme pyruvate
dehydrogenase complex activity. Does not
affect pyruvate decarboxylase activity.
{ECO:0000269|PubMed:20160912}.
MUTAGEN 359 359 I->A: Reduces pyruvate decarboxylase and
multienzyme pyruvate dehydrogenase
complex activity. Does not affect
interaction with DLAT.
{ECO:0000269|PubMed:20160912}.
MUTAGEN 359 359 Missing: Reduces pyruvate decarboxylase
and multienzyme pyruvate dehydrogenase
complex activity. Does not affect
interaction with DLAT.
{ECO:0000269|PubMed:20160912}.
CONFLICT 9 13 RRPLR -> AETPS (in Ref. 5).
{ECO:0000305}.
CONFLICT 43 43 M -> G (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 160 160 Q -> G (in Ref. 5). {ECO:0000305}.
CONFLICT 213 221 PPEAQSKDF -> LRKLSQKIL (in Ref. 5).
{ECO:0000305}.
CONFLICT 213 213 P -> L (in Ref. 4; AAA88097/BAA14123).
{ECO:0000305}.
CONFLICT 310 312 MEG -> NGS (in Ref. 5). {ECO:0000305}.
STRAND 32 34 {ECO:0000244|PDB:2OZL}.
HELIX 35 49 {ECO:0000244|PDB:2OZL}.
STRAND 53 57 {ECO:0000244|PDB:2OZL}.
TURN 58 61 {ECO:0000244|PDB:3EXI}.
TURN 69 72 {ECO:0000244|PDB:2OZL}.
HELIX 73 77 {ECO:0000244|PDB:2OZL}.
TURN 79 81 {ECO:0000244|PDB:2OZL}.
STRAND 82 84 {ECO:0000244|PDB:2OZL}.
HELIX 89 101 {ECO:0000244|PDB:2OZL}.
STRAND 105 109 {ECO:0000244|PDB:2OZL}.
HELIX 113 119 {ECO:0000244|PDB:2OZL}.
HELIX 120 124 {ECO:0000244|PDB:2OZL}.
TURN 125 129 {ECO:0000244|PDB:2OZL}.
HELIX 130 133 {ECO:0000244|PDB:2OZL}.
TURN 134 136 {ECO:0000244|PDB:3EXI}.
STRAND 143 147 {ECO:0000244|PDB:2OZL}.
HELIX 156 158 {ECO:0000244|PDB:2OZL}.
HELIX 163 167 {ECO:0000244|PDB:2OZL}.
STRAND 173 175 {ECO:0000244|PDB:2OZL}.
HELIX 180 192 {ECO:0000244|PDB:2OZL}.
STRAND 193 195 {ECO:0000244|PDB:2OZL}.
STRAND 197 201 {ECO:0000244|PDB:2OZL}.
TURN 203 207 {ECO:0000244|PDB:2OZL}.
STRAND 209 211 {ECO:0000244|PDB:2OZL}.
HELIX 214 217 {ECO:0000244|PDB:2OZL}.
STRAND 229 232 {ECO:0000244|PDB:2OZL}.
STRAND 235 241 {ECO:0000244|PDB:2OZL}.
HELIX 245 257 {ECO:0000244|PDB:2OZL}.
TURN 258 260 {ECO:0000244|PDB:2OZL}.
STRAND 263 267 {ECO:0000244|PDB:2OZL}.
STRAND 270 272 {ECO:0000244|PDB:2OZL}.
HELIX 276 286 {ECO:0000244|PDB:2OZL}.
STRAND 289 292 {ECO:0000244|PDB:2OZL}.
HELIX 301 311 {ECO:0000244|PDB:2OZL}.
HELIX 315 317 {ECO:0000244|PDB:2OZL}.
STRAND 323 325 {ECO:0000244|PDB:2OZL}.
STRAND 329 331 {ECO:0000244|PDB:3EXE}.
HELIX 336 340 {ECO:0000244|PDB:2OZL}.
HELIX 346 357 {ECO:0000244|PDB:2OZL}.
SEQUENCE 359 AA; 39233 MW; AB459B1259FBDBD3 CRC64;
MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD EKVFLLGEEV
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI
DQVINSAAKT YYMSGGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS
EDAKGLIKSA IRDNNPVVVL ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV
SHSRPVGHCL EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI


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