ID   ODPB_BACSU              Reviewed;         325 AA.
AC   P21882;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
DE   AltName: Full=S complex, 36 kDa subunit;
GN   Name=pdhB; Synonyms=aceB; OrderedLocusNames=BSU14590;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1697575; DOI=10.1128/jb.172.9.5052-5063.1990;
RA   Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.;
RT   "Secretory S complex of Bacillus subtilis: sequence analysis and identity
RT   to pyruvate dehydrogenase.";
RL   J. Bacteriol. 172:5052-5063(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA   Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT   "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT   168 chromosome: sequencing of a 27 kb segment and identification of several
RT   genes in the area.";
RL   Microbiology 142:3033-3037(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Caldwell R.M., Ferrari E.;
RT   "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT   chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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).
CC   -!- FUNCTION: The B.subtilis PDH complex possesses also branched-chain 2-
CC       oxoacid dehydrogenase (BCDH) activity.
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   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
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DR   EMBL; M57435; AAA62682.1; -; Genomic_DNA.
DR   EMBL; AF012285; AAC24933.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13332.1; -; Genomic_DNA.
DR   PIR; C36718; C36718.
DR   RefSeq; NP_389342.1; NC_000964.3.
DR   RefSeq; WP_003232313.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P21882; -.
DR   SMR; P21882; -.
DR   IntAct; P21882; 1.
DR   MINT; P21882; -.
DR   STRING; 224308.BSU14590; -.
DR   jPOST; P21882; -.
DR   PaxDb; P21882; -.
DR   PRIDE; P21882; -.
DR   EnsemblBacteria; CAB13332; CAB13332; BSU_14590.
DR   GeneID; 939496; -.
DR   KEGG; bsu:BSU14590; -.
DR   PATRIC; fig|224308.179.peg.1591; -.
DR   eggNOG; COG0022; Bacteria.
DR   InParanoid; P21882; -.
DR   OMA; SRMRHHC; -.
DR   PhylomeDB; P21882; -.
DR   BioCyc; BSUB:BSU14590-MON; -.
DR   Proteomes; UP000001570; Chromosome.
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   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..325
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta"
FT                   /id="PRO_0000162222"
FT   BINDING         60
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  35474 MW;  887EECA29C0C4E25 CRC64;
     MAQMTMIQAI TDALRTELKN DENVLVFGED VGVNGGVFRA TEGLQKEFGE DRVFDTPLAE
     SGIGGLALGL GLNGFRPVME IQFFGFVYEV MDSVSGQMAR MRYRSGGRWT SPVTIRSPFG
     GGVHTPELHA DSLEGLVAQQ PGIKVVIPST PYDAKGLLIS AIRDNDPVVF LEHMKLYRSF
     RQEVPEEEYT IELGKADVKR EGTDLSIITY GAMVHESLKA ADELEKDGIS AEVVDLRTVS
     PLDIDTIIAS VEKTGRAIVV QEAQKQAGIA ANVVAEINDR AILSLEAPVL RVAAPDTVFP
     FSQAESVWLP NHKDVLETAR KVLEF