ODPB_YEAST
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 03-AUG-2022, entry version 190.
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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, 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 -!- 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; 379.
DR ComplexPortal; CPX-3207; Mitochondrial pyruvate dehydrogenase complex.
DR DIP; DIP-1499N; -.
DR IntAct; P32473; 34.
DR MINT; P32473; -.
DR STRING; 4932.YBR221C; -.
DR iPTMnet; P32473; -.
DR SWISS-2DPAGE; P32473; -.
DR MaxQB; P32473; -.
DR PaxDb; P32473; -.
DR PRIDE; P32473; -.
DR EnsemblFungi; YBR221C_mRNA; YBR221C; YBR221C.
DR GeneID; 852522; -.
DR KEGG; sce:YBR221C; -.
DR SGD; S000000425; PDB1.
DR VEuPathDB; FungiDB:YBR221C; -.
DR eggNOG; KOG0524; Eukaryota.
DR GeneTree; ENSGT00940000155146; -.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; P32473; -.
DR OMA; SRMRHHC; -.
DR BioCyc; YEAST:YBR221C-MON; -.
DR Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SCE-70268; Pyruvate metabolism.
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:0005967; C:mitochondrial pyruvate dehydrogenase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IMP:SGD.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:SGD.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR027110; PDHB.
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 PANTHER; PTHR11624; PTHR11624; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase;
KW Pyruvate; Reference proteome; Thiamine pyrophosphate; 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 /evidence="ECO:0000250"
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
