ID   ODPA_BACSU              Reviewed;         371 AA.
AC   P21881; Q59227;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
DE   AltName: Full=S complex, 42 kDa subunit;
DE   AltName: Full=Vegetative protein 220;
DE            Short=VEG220;
GN   Name=pdhA; Synonyms=aceA; OrderedLocusNames=BSU14580;
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).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(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; AAA62681.1; -; Genomic_DNA.
DR   EMBL; AF012285; AAC24932.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13331.1; -; Genomic_DNA.
DR   PIR; B36718; DEBSPA.
DR   RefSeq; NP_389341.1; NC_000964.3.
DR   RefSeq; WP_003222294.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P21881; -.
DR   SMR; P21881; -.
DR   IntAct; P21881; 1.
DR   MINT; P21881; -.
DR   STRING; 224308.BSU14580; -.
DR   jPOST; P21881; -.
DR   PaxDb; P21881; -.
DR   PRIDE; P21881; -.
DR   EnsemblBacteria; CAB13331; CAB13331; BSU_14580.
DR   GeneID; 64303347; -.
DR   GeneID; 936005; -.
DR   KEGG; bsu:BSU14580; -.
DR   PATRIC; fig|224308.179.peg.1590; -.
DR   eggNOG; COG1071; Bacteria.
DR   InParanoid; P21881; -.
DR   OMA; GMFRGVN; -.
DR   PhylomeDB; P21881; -.
DR   BioCyc; BSUB:BSU14580-MON; -.
DR   PRO; PR:P21881; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF41; PTHR11516:SF41; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03181; PDH_E1_alph_x; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Oxidoreductase; Pyruvate;
KW   Reference proteome; Thiamine pyrophosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298659"
FT   CHAIN           2..371
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000162199"
FT   CONFLICT        179
FT                   /note="A -> R (in Ref. 1; AAA62681)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   371 AA;  41548 MW;  984AE665278C1462 CRC64;
     MAAKTKKAIV DSKKQFDAIK KQFETFQILN EKGEVVNEAA MPDLTDDQLK ELMRRMVFTR
     VLDQRSISLN RQGRLGFYAP TAGQEASQIA THFALEKEDF VLPGYRDVPQ LIWHGLPLYQ
     AFLFSRGHFR GNQMPDDVNA LSPQIIIGAQ YIQTAGVALG LKKRGKKAVA ITYTGDGGAS
     QGDFYEGINF AGAYKAPAIF VVQNNRYAIS TPVEKQSAAE TIAQKAVAAG IVGVQVDGMD
     PLAVYAATAE ARERAINGEG PTLIETLTFR YGPHTMAGDD PTKYRTKEIE NEWEQKDPLV
     RFRAFLENKG LWSEEEEAKV IEDAKEEIKQ AIKKADAEPK QKVTDLMKIM YEKMPHNLEE
     QFEIYTQKES K