ID   ODPB_STAAU              Reviewed;         325 AA.
AC   P0A0A3; Q9L6H5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12600 / DSM 20231 / IAM 12544 / NCDO 949 / NCTC 8532;
RA   Vilhelmsson O., Miller K.J.;
RT   "Synthesis of pyruvate dehydrogenase is stimulated by osmotic stress in
RT   Staphylococcus aureus.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   MASS SPECTROMETRY.
RC   STRAIN=MRSA-M2;
RX   PubMed=16714572; DOI=10.1128/iai.00392-06;
RA   Brady R.A., Leid J.G., Camper A.K., Costerton J.W., Shirtliff M.E.;
RT   "Identification of Staphylococcus aureus proteins recognized by the
RT   antibody-mediated immune response to a biofilm infection.";
RL   Infect. Immun. 74:3415-3426(2006).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3) (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- MASS SPECTROMETRY: Mass=35230; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16714572};
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DR   EMBL; AF235026; AAF36410.1; -; Genomic_DNA.
DR   RefSeq; WP_000068176.1; NZ_WYDB01000003.1.
DR   AlphaFoldDB; P0A0A3; -.
DR   SMR; P0A0A3; -.
DR   OMA; SRMRHHC; -.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.920; -; 1.
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   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   Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
FT   CHAIN           1..325
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta"
FT                   /id="PRO_0000162234"
FT   BINDING         60
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  35246 MW;  432ABDF6E4A720D5 CRC64;
     MAQMTMVQAI NDALKTELKN DQDVLIFGED VGVNGGVFRV TEGLQKEFGE DRVFDTPLAE
     SGIGGLAMGL AVEGFRPVME VQFLGFVFEV FDAIAGQIAR TRFRSGGTKT APVTIRSPFG
     GGVHTPELHA DNLEGILAQS PGLKVVIPSG PYDAKGLLIS SIRSNDPVVY LEHMKLYRSF
     REEVPEEEYT IDIGKANVKK EGNDISIITY GAMVQESMKA AEELEKDGYS VEVIDLRTVQ
     PIDVDTIVAS VEKTGRAVVV QEAQRQAGVG AAVVAELSER AILSLEAPIG RVAAADTIYP
     FTQAENVWLP NKNDIIEKAK ETLEF