Full text data of PDHB
PDHB
(PHE1B)
[Confidence: low (only semi-automatic identification from reviews)]
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; PDHE1-B; 1.2.4.1; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; PDHE1-B; 1.2.4.1; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P11177
ID ODPB_HUMAN Reviewed; 359 AA.
AC P11177; B2R7L0; B4DDD7; Q6FH45; Q9BQ27; Q9UFK3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-MAR-2007, sequence version 3.
DT 22-JAN-2014, entry version 165.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE Short=PDHE1-B;
DE EC=1.2.4.1;
DE Flags: Precursor;
GN Name=PDHB; Synonyms=PHE1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2323578; DOI=10.1016/0378-1119(90)90294-2;
RA Ho L., Patel M.S.;
RT "Cloning and cDNA sequence of the beta-subunit component of human
RT pyruvate dehydrogenase complex.";
RL Gene 86:297-302(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1702713; DOI=10.1111/j.1432-1033.1990.tb15656.x;
RA Chun K., MacKay N., Willard H.F., Robinson B.H.;
RT "Isolation, characterization and chromosomal localization of cDNA
RT clones for the E1 beta subunit of the pyruvate dehydrogenase
RT complex.";
RL Eur. J. Biochem. 194:587-592(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-31.
RX PubMed=2376596;
RA Huh T.L., Casazza J.P., Huh J.W., Chi Y.T., Song B.J.;
RT "Characterization of two cDNA clones for pyruvate dehydrogenase E1
RT beta subunit and its regulation in tricarboxylic acid cycle-deficient
RT fibroblast.";
RL J. Biol. Chem. 265:13320-13326(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=2377599; DOI=10.1073/pnas.87.15.5594;
RA Koike K., Urata Y., Koike M.;
RT "Molecular cloning and characterization of human pyruvate
RT dehydrogenase beta subunit gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5594-5597(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-31.
RX PubMed=3422424; DOI=10.1073/pnas.85.1.41;
RA Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.;
RT "Cloning and sequencing of cDNAs encoding alpha and beta subunits of
RT human pyruvate dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 23-69.
RX PubMed=2829898; DOI=10.1016/0006-291X(88)90714-0;
RA Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C.,
RA Mole J.E., Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S.;
RT "Identification of a cDNA clone for the beta-subunit of the pyruvate
RT dehydrogenase component of human pyruvate dehydrogenase complex.";
RL Biochem. Biophys. Res. Commun. 150:904-908(1988).
RN [13]
RP PROTEIN SEQUENCE OF 31-43.
RC TISSUE=Heart;
RX PubMed=7895732; DOI=10.1002/elps.11501501209;
RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
RT "The human myocardial two-dimensional gel protein database: update
RT 1994.";
RL Electrophoresis 15:1459-1465(1994).
RN [14]
RP PROTEIN SEQUENCE OF 31-55.
RX PubMed=2295468; DOI=10.1002/hep.1840110105;
RA Muno D., Kominami E., Ishii H., Usui K., Saifuku K., Sakakibara Y.,
RA Namihisa T.;
RT "Isolation of tryptic fragment of antigen from mitochondrial inner
RT membrane proteins reacting with antimitochondrial antibody in sera of
RT patients with primary biliary cirrhosis.";
RL Hepatology 11:16-23(1990).
RN [15]
RP SUBUNIT.
RX PubMed=14638692; DOI=10.1074/jbc.M308172200;
RA Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.;
RT "Organization of the cores of the mammalian pyruvate dehydrogenase
RT complex formed by E2 and E2 plus the E3-binding protein and their
RT capacities to bind the E1 and E3 components.";
RL J. Biol. Chem. 279:6921-6933(2004).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 32-359 IN COMPLEX WITH
RP THIAMINE PYROPHOSPHATE, AND COFACTOR.
RX PubMed=12651851; DOI=10.1074/jbc.M300339200;
RA Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.;
RT "Structural basis for flip-flop action of thiamin pyrophosphate-
RT dependent enzymes revealed by human pyruvate dehydrogenase.";
RL J. Biol. Chem. 278:21240-21246(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 32-359, SUBUNIT, AND
RP FUNCTION.
RX PubMed=17474719; DOI=10.1021/bi700083z;
RA Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M.,
RA Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.;
RT "Phosphorylation of serine 264 impedes active site accessibility in
RT the E1 component of the human pyruvate dehydrogenase multienzyme
RT complex.";
RL Biochemistry 46:6277-6287(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 31-359, CATALYTIC ACTIVITY,
RP SUBUNIT, COFACTOR, AND FUNCTION.
RX PubMed=19081061; DOI=10.1016/j.str.2008.10.010;
RA Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J.,
RA Chuang D.T.;
RT "Structural basis for inactivation of the human pyruvate dehydrogenase
RT complex by phosphorylation: role of disordered phosphorylation
RT loops.";
RL Structure 16:1849-1859(2008).
RN [20]
RP VARIANTS PDHBD CYS-132 AND SER-344.
RX PubMed=15138885; DOI=10.1007/s00439-004-1124-8;
RA Brown R.M., Head R.A., Boubriak I.I., Leonard J.V., Thomas N.H.,
RA Brown G.K.;
RT "Mutations in the gene for the E1beta subunit: a novel cause of
RT pyruvate dehydrogenase deficiency.";
RL Hum. Genet. 115:123-127(2004).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2), and thereby links
CC the glycolytic pathway to the tricarboxylic cycle.
CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC -!- COFACTOR: Thiamine pyrophosphate.
CC -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The
CC heterotetramer interacts with DLAT, and is part of the multimeric
CC pyruvate dehydrogenase complex that contains multiple copies of
CC pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase
CC (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits
CC are bound to an inner core composed of about 48 DLAT and 12 PDHX
CC molecules.
CC -!- INTERACTION:
CC P10515:DLAT; NbExp=7; IntAct=EBI-1035872, EBI-2959723;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P11177-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11177-2; Sequence=VSP_012675;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P11177-3; Sequence=VSP_043364;
CC Note=No experimental confirmation available;
CC -!- DISEASE: Pyruvate dehydrogenase E1-beta deficiency (PDHBD)
CC [MIM:614111]: An enzymatic defect causing primary lactic acidosis
CC in children. It is associated with a broad clinical spectrum
CC ranging from fatal lactic acidosis in the newborn to chronic
CC neurologic dysfunction with structural abnormalities in the
CC central nervous system without systemic acidosis. Note=The disease
CC is caused by mutations affecting the gene represented in this
CC entry.
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DR EMBL; M34479; AAA36428.1; -; mRNA.
DR EMBL; M19123; AAA60052.1; ALT_SEQ; mRNA.
DR EMBL; M54788; AAA60053.1; -; mRNA.
DR EMBL; M34055; AAA60233.1; -; mRNA.
DR EMBL; M34056; AAA60054.1; -; mRNA.
DR EMBL; D90086; BAA14123.1; -; Genomic_DNA.
DR EMBL; J03576; AAA88097.1; -; mRNA.
DR EMBL; AL117618; CAB56017.1; -; mRNA.
DR EMBL; CR541911; CAG46709.1; -; mRNA.
DR EMBL; AK293153; BAG56698.1; -; mRNA.
DR EMBL; AK313022; BAG35857.1; -; mRNA.
DR EMBL; AC135507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65371.1; -; Genomic_DNA.
DR EMBL; BC000439; AAH00439.1; -; mRNA.
DR EMBL; BC001924; AAH01924.1; -; mRNA.
DR EMBL; X57778; CAA40924.1; -; mRNA.
DR PIR; JU0145; DEHUPB.
DR RefSeq; NP_000916.2; NM_000925.3.
DR RefSeq; NP_001166939.1; NM_001173468.1.
DR UniGene; Hs.161357; -.
DR PDB; 1NI4; X-ray; 1.95 A; B/D=31-359.
DR PDB; 2OZL; X-ray; 1.90 A; B/D=32-359.
DR PDB; 3EXE; X-ray; 1.98 A; B/D/F/H=31-359.
DR PDB; 3EXF; X-ray; 3.00 A; B/D/F/H=31-359.
DR 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.
DR PDB; 3EXH; X-ray; 2.44 A; B/D/F/H=31-359.
DR PDB; 3EXI; X-ray; 2.20 A; B=31-359.
DR PDBsum; 1NI4; -.
DR PDBsum; 2OZL; -.
DR PDBsum; 3EXE; -.
DR PDBsum; 3EXF; -.
DR PDBsum; 3EXG; -.
DR PDBsum; 3EXH; -.
DR PDBsum; 3EXI; -.
DR ProteinModelPortal; P11177; -.
DR SMR; P11177; 30-359.
DR DIP; DIP-37651N; -.
DR IntAct; P11177; 15.
DR MINT; MINT-3007546; -.
DR STRING; 9606.ENSP00000307241; -.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00119; Pyruvic acid.
DR PhosphoSite; P11177; -.
DR DMDM; 134044259; -.
DR REPRODUCTION-2DPAGE; IPI00549885; -.
DR SWISS-2DPAGE; P11177; -.
DR UCD-2DPAGE; P11177; -.
DR PaxDb; P11177; -.
DR PRIDE; P11177; -.
DR DNASU; 5162; -.
DR Ensembl; ENST00000302746; ENSP00000307241; ENSG00000168291.
DR Ensembl; ENST00000383714; ENSP00000373220; ENSG00000168291.
DR Ensembl; ENST00000485460; ENSP00000417267; ENSG00000168291.
DR GeneID; 5162; -.
DR KEGG; hsa:5162; -.
DR UCSC; uc003dke.4; human.
DR CTD; 5162; -.
DR GeneCards; GC03M058388; -.
DR HGNC; HGNC:8808; PDHB.
DR HPA; HPA036744; -.
DR MIM; 179060; gene.
DR MIM; 614111; phenotype.
DR neXtProt; NX_P11177; -.
DR Orphanet; 255138; Pyruvate dehydrogenase E1-beta deficiency.
DR PharmGKB; PA33152; -.
DR eggNOG; COG0022; -.
DR HOGENOM; HOG000281450; -.
DR HOVERGEN; HBG000917; -.
DR InParanoid; P11177; -.
DR KO; K00162; -.
DR OMA; DIPTPYN; -.
DR OrthoDB; EOG7KSX8S; -.
DR PhylomeDB; P11177; -.
DR BioCyc; MetaCyc:HS09727-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P11177; -.
DR ChiTaRS; PDHB; human.
DR EvolutionaryTrace; P11177; -.
DR GeneWiki; Pyruvate_dehydrogenase_(lipoamide)_beta; -.
DR GenomeRNAi; 5162; -.
DR NextBio; 19970; -.
DR PRO; PR:P11177; -.
DR ArrayExpress; P11177; -.
DR Bgee; P11177; -.
DR CleanEx; HS_PDHB; -.
DR Genevestigator; P11177; -.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; TAS:ProtInc.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005476; Transketolase_C.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW Disease mutation; Glucose metabolism; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Polymorphism; Pyruvate; Reference proteome;
KW Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1 30 Mitochondrion.
FT CHAIN 31 359 Pyruvate dehydrogenase E1 component
FT subunit beta, mitochondrial.
FT /FTId=PRO_0000020457.
FT BINDING 89 89 Thiamine pyrophosphate.
FT MOD_RES 67 67 Phosphotyrosine (By similarity).
FT MOD_RES 354 354 N6-acetyllysine (By similarity).
FT VAR_SEQ 16 33 Missing (in isoform 2).
FT /FTId=VSP_012675.
FT VAR_SEQ 135 152 Missing (in isoform 3).
FT /FTId=VSP_043364.
FT VARIANT 31 31 L -> V.
FT /FTId=VAR_004967.
FT VARIANT 132 132 Y -> C (in PDHBD; dbSNP:rs28935769).
FT /FTId=VAR_030954.
FT VARIANT 344 344 P -> S (in PDHBD; dbSNP:rs28933391).
FT /FTId=VAR_021058.
FT CONFLICT 9 13 RRPLR -> AETPS (in Ref. 5).
FT CONFLICT 43 43 M -> G (in Ref. 13; AA sequence).
FT CONFLICT 160 160 Q -> G (in Ref. 5).
FT CONFLICT 213 221 PPEAQSKDF -> LRKLSQKIL (in Ref. 5).
FT CONFLICT 213 213 P -> L (in Ref. 4; AAA88097/BAA14123).
FT CONFLICT 310 312 MEG -> NGS (in Ref. 5).
FT STRAND 32 34
FT HELIX 35 49
FT STRAND 53 57
FT TURN 58 61
FT TURN 69 72
FT HELIX 73 77
FT TURN 79 81
FT STRAND 82 84
FT HELIX 89 101
FT STRAND 105 109
FT HELIX 113 119
FT HELIX 120 124
FT TURN 125 129
FT HELIX 130 133
FT TURN 134 136
FT STRAND 143 147
FT HELIX 156 158
FT HELIX 163 167
FT STRAND 173 175
FT HELIX 180 192
FT STRAND 193 195
FT STRAND 197 201
FT TURN 203 207
FT STRAND 209 211
FT HELIX 214 217
FT STRAND 229 232
FT STRAND 235 241
FT HELIX 245 257
FT TURN 258 260
FT STRAND 263 267
FT STRAND 270 272
FT HELIX 276 286
FT STRAND 289 292
FT HELIX 301 311
FT HELIX 315 317
FT STRAND 323 325
FT STRAND 329 331
FT HELIX 336 340
FT HELIX 346 357
SQ 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
//
ID ODPB_HUMAN Reviewed; 359 AA.
AC P11177; B2R7L0; B4DDD7; Q6FH45; Q9BQ27; Q9UFK3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-MAR-2007, sequence version 3.
DT 22-JAN-2014, entry version 165.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE Short=PDHE1-B;
DE EC=1.2.4.1;
DE Flags: Precursor;
GN Name=PDHB; Synonyms=PHE1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2323578; DOI=10.1016/0378-1119(90)90294-2;
RA Ho L., Patel M.S.;
RT "Cloning and cDNA sequence of the beta-subunit component of human
RT pyruvate dehydrogenase complex.";
RL Gene 86:297-302(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1702713; DOI=10.1111/j.1432-1033.1990.tb15656.x;
RA Chun K., MacKay N., Willard H.F., Robinson B.H.;
RT "Isolation, characterization and chromosomal localization of cDNA
RT clones for the E1 beta subunit of the pyruvate dehydrogenase
RT complex.";
RL Eur. J. Biochem. 194:587-592(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-31.
RX PubMed=2376596;
RA Huh T.L., Casazza J.P., Huh J.W., Chi Y.T., Song B.J.;
RT "Characterization of two cDNA clones for pyruvate dehydrogenase E1
RT beta subunit and its regulation in tricarboxylic acid cycle-deficient
RT fibroblast.";
RL J. Biol. Chem. 265:13320-13326(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=2377599; DOI=10.1073/pnas.87.15.5594;
RA Koike K., Urata Y., Koike M.;
RT "Molecular cloning and characterization of human pyruvate
RT dehydrogenase beta subunit gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5594-5597(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-31.
RX PubMed=3422424; DOI=10.1073/pnas.85.1.41;
RA Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.;
RT "Cloning and sequencing of cDNAs encoding alpha and beta subunits of
RT human pyruvate dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 23-69.
RX PubMed=2829898; DOI=10.1016/0006-291X(88)90714-0;
RA Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C.,
RA Mole J.E., Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S.;
RT "Identification of a cDNA clone for the beta-subunit of the pyruvate
RT dehydrogenase component of human pyruvate dehydrogenase complex.";
RL Biochem. Biophys. Res. Commun. 150:904-908(1988).
RN [13]
RP PROTEIN SEQUENCE OF 31-43.
RC TISSUE=Heart;
RX PubMed=7895732; DOI=10.1002/elps.11501501209;
RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
RT "The human myocardial two-dimensional gel protein database: update
RT 1994.";
RL Electrophoresis 15:1459-1465(1994).
RN [14]
RP PROTEIN SEQUENCE OF 31-55.
RX PubMed=2295468; DOI=10.1002/hep.1840110105;
RA Muno D., Kominami E., Ishii H., Usui K., Saifuku K., Sakakibara Y.,
RA Namihisa T.;
RT "Isolation of tryptic fragment of antigen from mitochondrial inner
RT membrane proteins reacting with antimitochondrial antibody in sera of
RT patients with primary biliary cirrhosis.";
RL Hepatology 11:16-23(1990).
RN [15]
RP SUBUNIT.
RX PubMed=14638692; DOI=10.1074/jbc.M308172200;
RA Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.;
RT "Organization of the cores of the mammalian pyruvate dehydrogenase
RT complex formed by E2 and E2 plus the E3-binding protein and their
RT capacities to bind the E1 and E3 components.";
RL J. Biol. Chem. 279:6921-6933(2004).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 32-359 IN COMPLEX WITH
RP THIAMINE PYROPHOSPHATE, AND COFACTOR.
RX PubMed=12651851; DOI=10.1074/jbc.M300339200;
RA Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.;
RT "Structural basis for flip-flop action of thiamin pyrophosphate-
RT dependent enzymes revealed by human pyruvate dehydrogenase.";
RL J. Biol. Chem. 278:21240-21246(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 32-359, SUBUNIT, AND
RP FUNCTION.
RX PubMed=17474719; DOI=10.1021/bi700083z;
RA Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M.,
RA Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.;
RT "Phosphorylation of serine 264 impedes active site accessibility in
RT the E1 component of the human pyruvate dehydrogenase multienzyme
RT complex.";
RL Biochemistry 46:6277-6287(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 31-359, CATALYTIC ACTIVITY,
RP SUBUNIT, COFACTOR, AND FUNCTION.
RX PubMed=19081061; DOI=10.1016/j.str.2008.10.010;
RA Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J.,
RA Chuang D.T.;
RT "Structural basis for inactivation of the human pyruvate dehydrogenase
RT complex by phosphorylation: role of disordered phosphorylation
RT loops.";
RL Structure 16:1849-1859(2008).
RN [20]
RP VARIANTS PDHBD CYS-132 AND SER-344.
RX PubMed=15138885; DOI=10.1007/s00439-004-1124-8;
RA Brown R.M., Head R.A., Boubriak I.I., Leonard J.V., Thomas N.H.,
RA Brown G.K.;
RT "Mutations in the gene for the E1beta subunit: a novel cause of
RT pyruvate dehydrogenase deficiency.";
RL Hum. Genet. 115:123-127(2004).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2), and thereby links
CC the glycolytic pathway to the tricarboxylic cycle.
CC -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC -!- COFACTOR: Thiamine pyrophosphate.
CC -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The
CC heterotetramer interacts with DLAT, and is part of the multimeric
CC pyruvate dehydrogenase complex that contains multiple copies of
CC pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase
CC (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits
CC are bound to an inner core composed of about 48 DLAT and 12 PDHX
CC molecules.
CC -!- INTERACTION:
CC P10515:DLAT; NbExp=7; IntAct=EBI-1035872, EBI-2959723;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P11177-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11177-2; Sequence=VSP_012675;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P11177-3; Sequence=VSP_043364;
CC Note=No experimental confirmation available;
CC -!- DISEASE: Pyruvate dehydrogenase E1-beta deficiency (PDHBD)
CC [MIM:614111]: An enzymatic defect causing primary lactic acidosis
CC in children. It is associated with a broad clinical spectrum
CC ranging from fatal lactic acidosis in the newborn to chronic
CC neurologic dysfunction with structural abnormalities in the
CC central nervous system without systemic acidosis. Note=The disease
CC is caused by mutations affecting the gene represented in this
CC entry.
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DR EMBL; M34479; AAA36428.1; -; mRNA.
DR EMBL; M19123; AAA60052.1; ALT_SEQ; mRNA.
DR EMBL; M54788; AAA60053.1; -; mRNA.
DR EMBL; M34055; AAA60233.1; -; mRNA.
DR EMBL; M34056; AAA60054.1; -; mRNA.
DR EMBL; D90086; BAA14123.1; -; Genomic_DNA.
DR EMBL; J03576; AAA88097.1; -; mRNA.
DR EMBL; AL117618; CAB56017.1; -; mRNA.
DR EMBL; CR541911; CAG46709.1; -; mRNA.
DR EMBL; AK293153; BAG56698.1; -; mRNA.
DR EMBL; AK313022; BAG35857.1; -; mRNA.
DR EMBL; AC135507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65371.1; -; Genomic_DNA.
DR EMBL; BC000439; AAH00439.1; -; mRNA.
DR EMBL; BC001924; AAH01924.1; -; mRNA.
DR EMBL; X57778; CAA40924.1; -; mRNA.
DR PIR; JU0145; DEHUPB.
DR RefSeq; NP_000916.2; NM_000925.3.
DR RefSeq; NP_001166939.1; NM_001173468.1.
DR UniGene; Hs.161357; -.
DR PDB; 1NI4; X-ray; 1.95 A; B/D=31-359.
DR PDB; 2OZL; X-ray; 1.90 A; B/D=32-359.
DR PDB; 3EXE; X-ray; 1.98 A; B/D/F/H=31-359.
DR PDB; 3EXF; X-ray; 3.00 A; B/D/F/H=31-359.
DR 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.
DR PDB; 3EXH; X-ray; 2.44 A; B/D/F/H=31-359.
DR PDB; 3EXI; X-ray; 2.20 A; B=31-359.
DR PDBsum; 1NI4; -.
DR PDBsum; 2OZL; -.
DR PDBsum; 3EXE; -.
DR PDBsum; 3EXF; -.
DR PDBsum; 3EXG; -.
DR PDBsum; 3EXH; -.
DR PDBsum; 3EXI; -.
DR ProteinModelPortal; P11177; -.
DR SMR; P11177; 30-359.
DR DIP; DIP-37651N; -.
DR IntAct; P11177; 15.
DR MINT; MINT-3007546; -.
DR STRING; 9606.ENSP00000307241; -.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00119; Pyruvic acid.
DR PhosphoSite; P11177; -.
DR DMDM; 134044259; -.
DR REPRODUCTION-2DPAGE; IPI00549885; -.
DR SWISS-2DPAGE; P11177; -.
DR UCD-2DPAGE; P11177; -.
DR PaxDb; P11177; -.
DR PRIDE; P11177; -.
DR DNASU; 5162; -.
DR Ensembl; ENST00000302746; ENSP00000307241; ENSG00000168291.
DR Ensembl; ENST00000383714; ENSP00000373220; ENSG00000168291.
DR Ensembl; ENST00000485460; ENSP00000417267; ENSG00000168291.
DR GeneID; 5162; -.
DR KEGG; hsa:5162; -.
DR UCSC; uc003dke.4; human.
DR CTD; 5162; -.
DR GeneCards; GC03M058388; -.
DR HGNC; HGNC:8808; PDHB.
DR HPA; HPA036744; -.
DR MIM; 179060; gene.
DR MIM; 614111; phenotype.
DR neXtProt; NX_P11177; -.
DR Orphanet; 255138; Pyruvate dehydrogenase E1-beta deficiency.
DR PharmGKB; PA33152; -.
DR eggNOG; COG0022; -.
DR HOGENOM; HOG000281450; -.
DR HOVERGEN; HBG000917; -.
DR InParanoid; P11177; -.
DR KO; K00162; -.
DR OMA; DIPTPYN; -.
DR OrthoDB; EOG7KSX8S; -.
DR PhylomeDB; P11177; -.
DR BioCyc; MetaCyc:HS09727-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P11177; -.
DR ChiTaRS; PDHB; human.
DR EvolutionaryTrace; P11177; -.
DR GeneWiki; Pyruvate_dehydrogenase_(lipoamide)_beta; -.
DR GenomeRNAi; 5162; -.
DR NextBio; 19970; -.
DR PRO; PR:P11177; -.
DR ArrayExpress; P11177; -.
DR Bgee; P11177; -.
DR CleanEx; HS_PDHB; -.
DR Genevestigator; P11177; -.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; TAS:ProtInc.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005476; Transketolase_C.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
KW Disease mutation; Glucose metabolism; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Polymorphism; Pyruvate; Reference proteome;
KW Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1 30 Mitochondrion.
FT CHAIN 31 359 Pyruvate dehydrogenase E1 component
FT subunit beta, mitochondrial.
FT /FTId=PRO_0000020457.
FT BINDING 89 89 Thiamine pyrophosphate.
FT MOD_RES 67 67 Phosphotyrosine (By similarity).
FT MOD_RES 354 354 N6-acetyllysine (By similarity).
FT VAR_SEQ 16 33 Missing (in isoform 2).
FT /FTId=VSP_012675.
FT VAR_SEQ 135 152 Missing (in isoform 3).
FT /FTId=VSP_043364.
FT VARIANT 31 31 L -> V.
FT /FTId=VAR_004967.
FT VARIANT 132 132 Y -> C (in PDHBD; dbSNP:rs28935769).
FT /FTId=VAR_030954.
FT VARIANT 344 344 P -> S (in PDHBD; dbSNP:rs28933391).
FT /FTId=VAR_021058.
FT CONFLICT 9 13 RRPLR -> AETPS (in Ref. 5).
FT CONFLICT 43 43 M -> G (in Ref. 13; AA sequence).
FT CONFLICT 160 160 Q -> G (in Ref. 5).
FT CONFLICT 213 221 PPEAQSKDF -> LRKLSQKIL (in Ref. 5).
FT CONFLICT 213 213 P -> L (in Ref. 4; AAA88097/BAA14123).
FT CONFLICT 310 312 MEG -> NGS (in Ref. 5).
FT STRAND 32 34
FT HELIX 35 49
FT STRAND 53 57
FT TURN 58 61
FT TURN 69 72
FT HELIX 73 77
FT TURN 79 81
FT STRAND 82 84
FT HELIX 89 101
FT STRAND 105 109
FT HELIX 113 119
FT HELIX 120 124
FT TURN 125 129
FT HELIX 130 133
FT TURN 134 136
FT STRAND 143 147
FT HELIX 156 158
FT HELIX 163 167
FT STRAND 173 175
FT HELIX 180 192
FT STRAND 193 195
FT STRAND 197 201
FT TURN 203 207
FT STRAND 209 211
FT HELIX 214 217
FT STRAND 229 232
FT STRAND 235 241
FT HELIX 245 257
FT TURN 258 260
FT STRAND 263 267
FT STRAND 270 272
FT HELIX 276 286
FT STRAND 289 292
FT HELIX 301 311
FT HELIX 315 317
FT STRAND 323 325
FT STRAND 329 331
FT HELIX 336 340
FT HELIX 346 357
SQ 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
//
MIM
179060
*RECORD*
*FIELD* NO
179060
*FIELD* TI
*179060 PYRUVATE DEHYDROGENASE, BETA POLYPEPTIDE; PDHB
;;PYRUVATE DEHYDROGENASE COMPLEX, E1 BETA POLYPEPTIDE; PHE1B
read more*FIELD* TX
DESCRIPTION
Pyruvate decarboxylase is a tetramer consisting of 2 alpha subunits
(PDHA1; 300502) and 2 beta subunits. The enzyme, which is found in
mitochondria, is one of the component enzymes of the pyruvate
dehydrogenase multienzyme complex (PDH). It catalyzes the first reaction
of an oxidative decarboxylation sequence converting pyruvate to
acetyl-CoA and CO(2) (summary by Koike et al., 1988).
CLONING
Koike et al. (1988) cloned and sequenced cDNAs encoding the alpha and
the beta subunits.
Ho et al. (1988) isolated a 1.5-kb cDNA clone for the beta subunit of E1
from a human liver gamma-gt11 cDNA library using anti-E1 serum.
MAPPING
Using a cDNA probe, Olson et al. (1990) demonstrated that the PHE1B gene
is located on 3p13-q23.
GENE STRUCTURE
Koike et al. (1990) described the molecular cloning of the entire human
PHE1B gene, its characterization by restriction enzyme analysis, and its
complete nucleotide sequence. The PHE1B gene contains 10 exons. All
intron-exon splice junctions follow the GT/AG rule. The Alu family was
found in introns 2 and 8.
MOLECULAR GENETICS
In 2 unrelated patients with pyruvate dehydrogenase deficiency (PDHBD;
614111), Brown et al. (2004) identified homozygous mutations in the PDHB
gene (179060.0001-179060.0002). The patients presented with lactic
acidosis and neurologic dysfunction and had little residual PDH activity
in cultured fibroblasts. The consequences of the mutations could be
analyzed by comparison with the normal structure of the human PDH E1
enzyme.
*FIELD* AV
.0001
PYRUVATE DEHYDROGENASE E1-BETA DEFICIENCY
PDHB, TYR132CYS
In an infant with pyruvate dehydrogenase deficiency (614111), the son of
first-cousin parents, Brown et al. (2004) identified a homozygous 395A-G
transition in exon 6 of the PDHB gene, resulting in a tyr132-to-cys
(Y132C) substitution.
.0002
PYRUVATE DEHYDROGENASE E1-BETA DEFICIENCY
PDHB, PRO344SER
In an infant with pyruvate dehydrogenase deficiency (614111), the son of
consanguineous parents, Brown et al. (2004) identified a 1030C-T
transition in exon 10 of the PDHB gene, resulting in a pro344-to-ser
(P344S) substitution.
*FIELD* RF
1. Brown, R. M.; Head, R. A.; Boubriak, I. I.; Leonard, J. V.; Thomas,
N. H.; Brown, G. K.: Mutations in the gene for the E1-beta subunit:
a novel cause of pyruvate dehydrogenase deficiency. Hum. Genet. 115:
123-127, 2004.
2. 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.
3. 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. Nat. Acad. Sci. 85: 41-45, 1988.
4. Koike, K.; Urata, Y.; Koike, M.: Molecular cloning and characterization
of human pyruvate dehydrogenase beta subunit gene. Proc. Nat. Acad.
Sci. 87: 5594-5597, 1990.
5. Olson, S.; Song, B. J.; Huh, T.-L.; Chi, Y.-T.; Veech, R. L.; McBride,
O. W.: Three genes for enzymes of the pyruvate dehydrogenase complex
map to human chromosomes 3, 7, and X. Am. J. Hum. Genet. 46: 340-349,
1990. Note: Erratum: Am. J. Hum. Genet. 46: 1235 only, 1990.
*FIELD* CN
Victor A. McKusick - updated: 7/14/2004
*FIELD* CD
Victor A. McKusick: 2/12/1988
*FIELD* ED
terry: 03/28/2013
carol: 7/22/2011
carol: 8/17/2004
tkritzer: 7/23/2004
tkritzer: 7/19/2004
terry: 7/14/2004
supermim: 3/16/1992
carol: 9/7/1990
carol: 8/23/1990
carol: 6/13/1990
supermim: 3/20/1990
supermim: 2/27/1990
*RECORD*
*FIELD* NO
179060
*FIELD* TI
*179060 PYRUVATE DEHYDROGENASE, BETA POLYPEPTIDE; PDHB
;;PYRUVATE DEHYDROGENASE COMPLEX, E1 BETA POLYPEPTIDE; PHE1B
read more*FIELD* TX
DESCRIPTION
Pyruvate decarboxylase is a tetramer consisting of 2 alpha subunits
(PDHA1; 300502) and 2 beta subunits. The enzyme, which is found in
mitochondria, is one of the component enzymes of the pyruvate
dehydrogenase multienzyme complex (PDH). It catalyzes the first reaction
of an oxidative decarboxylation sequence converting pyruvate to
acetyl-CoA and CO(2) (summary by Koike et al., 1988).
CLONING
Koike et al. (1988) cloned and sequenced cDNAs encoding the alpha and
the beta subunits.
Ho et al. (1988) isolated a 1.5-kb cDNA clone for the beta subunit of E1
from a human liver gamma-gt11 cDNA library using anti-E1 serum.
MAPPING
Using a cDNA probe, Olson et al. (1990) demonstrated that the PHE1B gene
is located on 3p13-q23.
GENE STRUCTURE
Koike et al. (1990) described the molecular cloning of the entire human
PHE1B gene, its characterization by restriction enzyme analysis, and its
complete nucleotide sequence. The PHE1B gene contains 10 exons. All
intron-exon splice junctions follow the GT/AG rule. The Alu family was
found in introns 2 and 8.
MOLECULAR GENETICS
In 2 unrelated patients with pyruvate dehydrogenase deficiency (PDHBD;
614111), Brown et al. (2004) identified homozygous mutations in the PDHB
gene (179060.0001-179060.0002). The patients presented with lactic
acidosis and neurologic dysfunction and had little residual PDH activity
in cultured fibroblasts. The consequences of the mutations could be
analyzed by comparison with the normal structure of the human PDH E1
enzyme.
*FIELD* AV
.0001
PYRUVATE DEHYDROGENASE E1-BETA DEFICIENCY
PDHB, TYR132CYS
In an infant with pyruvate dehydrogenase deficiency (614111), the son of
first-cousin parents, Brown et al. (2004) identified a homozygous 395A-G
transition in exon 6 of the PDHB gene, resulting in a tyr132-to-cys
(Y132C) substitution.
.0002
PYRUVATE DEHYDROGENASE E1-BETA DEFICIENCY
PDHB, PRO344SER
In an infant with pyruvate dehydrogenase deficiency (614111), the son of
consanguineous parents, Brown et al. (2004) identified a 1030C-T
transition in exon 10 of the PDHB gene, resulting in a pro344-to-ser
(P344S) substitution.
*FIELD* RF
1. Brown, R. M.; Head, R. A.; Boubriak, I. I.; Leonard, J. V.; Thomas,
N. H.; Brown, G. K.: Mutations in the gene for the E1-beta subunit:
a novel cause of pyruvate dehydrogenase deficiency. Hum. Genet. 115:
123-127, 2004.
2. 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.
3. 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. Nat. Acad. Sci. 85: 41-45, 1988.
4. Koike, K.; Urata, Y.; Koike, M.: Molecular cloning and characterization
of human pyruvate dehydrogenase beta subunit gene. Proc. Nat. Acad.
Sci. 87: 5594-5597, 1990.
5. Olson, S.; Song, B. J.; Huh, T.-L.; Chi, Y.-T.; Veech, R. L.; McBride,
O. W.: Three genes for enzymes of the pyruvate dehydrogenase complex
map to human chromosomes 3, 7, and X. Am. J. Hum. Genet. 46: 340-349,
1990. Note: Erratum: Am. J. Hum. Genet. 46: 1235 only, 1990.
*FIELD* CN
Victor A. McKusick - updated: 7/14/2004
*FIELD* CD
Victor A. McKusick: 2/12/1988
*FIELD* ED
terry: 03/28/2013
carol: 7/22/2011
carol: 8/17/2004
tkritzer: 7/23/2004
tkritzer: 7/19/2004
terry: 7/14/2004
supermim: 3/16/1992
carol: 9/7/1990
carol: 8/23/1990
carol: 6/13/1990
supermim: 3/20/1990
supermim: 2/27/1990
MIM
614111
*RECORD*
*FIELD* NO
614111
*FIELD* TI
#614111 PYRUVATE DEHYDROGENASE E1-BETA DEFICIENCY; PDHBD
*FIELD* TX
A number sign (#) is used with this entry because pyruvate dehydrogenase
read moreE1-beta deficiency is caused by homozygous mutation in the PDHB gene
(179060) on chromosome 3p.
For a general phenotypic description and a discussion of genetic
heterogeneity of pyruvate dehydrogenase deficiency, see 312170.
CLINICAL FEATURES
Brown et al. (2004) reported 2 unrelated patients with pyruvate
dehydrogenase deficiency. The first patient, the son of first-cousin
parents, was investigated at age 3 months because of lactic acidosis and
hypotonia. Two previous sibs had died early, one with lactic acidosis.
The patient developed metabolic acidosis on day 1. He required
ventilation from day 3 to day 22. MRI demonstrated agenesis of the
corpus callosum. At age 3 months, he showed global hypotonia and reduced
reflexes. He developed severe lactic acidosis following general
anesthesia for muscle biopsy and lumbar puncture. He suffered
respiratory arrest but was successfully treated with ventilation and
bicarbonate. The second patient, also the son of consanguineous parents,
was hypotonic at birth with poor respiratory effort. He was investigated
at 9 weeks of age because of continuing hypotonia, lack of visual
attention, and respiratory stridor. MRI of the brain was normal. He made
little developmental progress and died at 12 months of age.
MOLECULAR GENETICS
In 2 unrelated patients with pyruvate dehydrogenase deficiency, Brown et
al. (2004) identified homozygous mutations in the PDHB gene
(179060.0001-179060.0002).
*FIELD* RF
1. Brown, R. M.; Head, R. A.; Boubriak, I. I.; Leonard, J. V.; Thomas,
N. H.; Brown, G. K.: Mutations in the gene for the E1-beta subunit:
a novel cause of pyruvate dehydrogenase deficiency. Hum. Genet. 115:
123-127, 2004.
*FIELD* CD
Carol A. Bocchini: 7/22/2011
*FIELD* ED
carol: 07/22/2011
*RECORD*
*FIELD* NO
614111
*FIELD* TI
#614111 PYRUVATE DEHYDROGENASE E1-BETA DEFICIENCY; PDHBD
*FIELD* TX
A number sign (#) is used with this entry because pyruvate dehydrogenase
read moreE1-beta deficiency is caused by homozygous mutation in the PDHB gene
(179060) on chromosome 3p.
For a general phenotypic description and a discussion of genetic
heterogeneity of pyruvate dehydrogenase deficiency, see 312170.
CLINICAL FEATURES
Brown et al. (2004) reported 2 unrelated patients with pyruvate
dehydrogenase deficiency. The first patient, the son of first-cousin
parents, was investigated at age 3 months because of lactic acidosis and
hypotonia. Two previous sibs had died early, one with lactic acidosis.
The patient developed metabolic acidosis on day 1. He required
ventilation from day 3 to day 22. MRI demonstrated agenesis of the
corpus callosum. At age 3 months, he showed global hypotonia and reduced
reflexes. He developed severe lactic acidosis following general
anesthesia for muscle biopsy and lumbar puncture. He suffered
respiratory arrest but was successfully treated with ventilation and
bicarbonate. The second patient, also the son of consanguineous parents,
was hypotonic at birth with poor respiratory effort. He was investigated
at 9 weeks of age because of continuing hypotonia, lack of visual
attention, and respiratory stridor. MRI of the brain was normal. He made
little developmental progress and died at 12 months of age.
MOLECULAR GENETICS
In 2 unrelated patients with pyruvate dehydrogenase deficiency, Brown et
al. (2004) identified homozygous mutations in the PDHB gene
(179060.0001-179060.0002).
*FIELD* RF
1. Brown, R. M.; Head, R. A.; Boubriak, I. I.; Leonard, J. V.; Thomas,
N. H.; Brown, G. K.: Mutations in the gene for the E1-beta subunit:
a novel cause of pyruvate dehydrogenase deficiency. Hum. Genet. 115:
123-127, 2004.
*FIELD* CD
Carol A. Bocchini: 7/22/2011
*FIELD* ED
carol: 07/22/2011