ID   ODPB_YEAST              Reviewed;         366 AA.
AC   P32473; D6VQL7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   02-SEP-2026, entry version 207.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            EC=1.2.4.1 {ECO:0000305|PubMed:8433986};
DE   AltName: Full=Pyruvate dehydrogenase complex component E1 beta;
DE            Short=PDHE1-B;
DE   Flags: Precursor;
GN   Name=PDB1; OrderedLocusNames=YBR221C; ORFNames=YBR1511;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-54 AND 206-219,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8433986; DOI=10.1073/pnas.90.4.1252;
RA   Miran S.G., Lawson J.E., Reed L.J.;
RT   "Characterization of PDH beta 1, the structural gene for the pyruvate
RT   dehydrogenase beta subunit from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1252-1256(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000305|PubMed:8433986}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H(+) = N(6)-
CC         [(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000305|PubMed:8433986};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19190;
CC         Evidence={ECO:0000305|PubMed:8433986};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P11177};
CC   -!- SUBUNIT: Pyruvate dehydrogenase (E1) is a tetramer of 2 alpha and 2
CC       beta subunits. Eukaryotic pyruvate dehydrogenase (PDH) complexes are
CC       organized as a core consisting of the oligomeric dihydrolipoamide
CC       acetyl-transferase (E2), around which are arranged multiple copies of
CC       pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and
CC       protein X (E3BP) bound by non-covalent bonds.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: Present with 9970 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; M98476; AAA34583.1; -; Genomic_DNA.
DR   EMBL; Z36090; CAA85184.1; -; Genomic_DNA.
DR   EMBL; AY692982; AAT93001.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07337.1; -; Genomic_DNA.
DR   PIR; S46097; S46097.
DR   RefSeq; NP_009780.1; NM_001178569.1.
DR   AlphaFoldDB; P32473; -.
DR   SMR; P32473; -.
DR   BioGRID; 32918; 416.
DR   ComplexPortal; CPX-3207; Mitochondrial pyruvate dehydrogenase complex.
DR   DIP; DIP-1499N; -.
DR   FunCoup; P32473; 1013.
DR   IntAct; P32473; 65.
DR   MINT; P32473; -.
DR   STRING; 4932.YBR221C; -.
DR   iPTMnet; P32473; -.
DR   PaxDb; 4932-YBR221C; -.
DR   PeptideAtlas; P32473; -.
DR   EnsemblFungi; YBR221C_mRNA; YBR221C; YBR221C.
DR   GeneID; 852522; -.
DR   KEGG; sce:YBR221C; -.
DR   AGR; SGD:S000000425; -.
DR   SGD; S000000425; PDB1.
DR   VEuPathDB; FungiDB:YBR221C; -.
DR   eggNOG; KOG0524; Eukaryota.
DR   HOGENOM; CLU_012907_1_1_1; -.
DR   InParanoid; P32473; -.
DR   OMA; WYANCPG; -.
DR   OrthoDB; 10266385at2759; -.
DR   BioCyc; YEAST:YBR221C-MONOMER; -.
DR   Reactome; R-SCE-9837999; Mitochondrial protein degradation.
DR   Reactome; R-SCE-9861559; PDH complex synthesizes acetyl-CoA from PYR.
DR   BioGRID-ORCS; 852522; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P32473; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P32473; protein.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:SGD.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IMP:SGD.
DR   GO; GO:0006086; P:pyruvate decarboxylation to acetyl-CoA; IDA:SGD.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   FunFam; 3.40.50.920:FF:000001; Pyruvate dehydrogenase E1 beta subunit; 1.
DR   FunFam; 3.40.50.970:FF:000006; Pyruvate dehydrogenase E1 component subunit beta; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR027110; PDHB_mito-type.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   NCBIfam; NF006667; PRK09212.1; 1.
DR   NCBIfam; NF008854; PRK11892.1; 1.
DR   PANTHER; PTHR11624; DEHYDROGENASE RELATED; 1.
DR   PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Potassium; Pyruvate; Reference proteome; Thiamine pyrophosphate;
KW   Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:8433986"
FT   CHAIN           34..366
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000020461"
FT   BINDING         95
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /ligand_note="ligand shared with alpha subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         196
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         197
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         199
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         201
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   CONFLICT        160
FT                   /note="V -> L (in Ref. 1; AAA34583)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  40054 MW;  547FD49ED2CB8A97 CRC64;
     MFSRLPTSLA RNVARRAPTS FVRPSAAAAA LRFSSTKTMT VREALNSAMA EELDRDDDVF
     LIGEEVAQYN GAYKVSKGLL DRFGERRVVD TPITEYGFTG LAVGAALKGL KPIVEFMSFN
     FSMQAIDHVV NSAAKTHYMS GGTQKCQMVF RGPNGAAVGV GAQHSQDFSP WYGSIPGLKV
     LVPYSAEDAR GLLKAAIRDP NPVVFLENEL LYGESFEISE EALSPEFTLP YKAKIEREGT
     DISIVTYTRN VQFSLEAAEI LQKKYGVSAE VINLRSIRPL DTEAIIKTVK KTNHLITVES
     TFPSFGVGAE IVAQVMESEA FDYLDAPIQR VTGADVPTPY AKELEDFAFP DTPTIVKAVK
     EVLSIE
//