ID   ODPB_RICPR              Reviewed;         326 AA.
AC   Q9ZDR3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; OrderedLocusNames=RP262;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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.
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DR   EMBL; AJ235271; CAA14724.1; -; Genomic_DNA.
DR   PIR; B71681; B71681.
DR   RefSeq; NP_220647.1; NC_000963.1.
DR   RefSeq; WP_004596097.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDR3; -.
DR   SMR; Q9ZDR3; -.
DR   STRING; 272947.RP262; -.
DR   EnsemblBacteria; CAA14724; CAA14724; CAA14724.
DR   GeneID; 57569390; -.
DR   KEGG; rpr:RP262; -.
DR   PATRIC; fig|272947.5.peg.269; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_1_5; -.
DR   OMA; SRMRHHC; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..326
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta"
FT                   /id="PRO_0000162227"
FT   BINDING         59
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  35917 MW;  12A50A7ABBB28A46 CRC64;
     MQITVREALR DAMQEEMLRD EKVFVIGEEV AEYQGAYKVT QGLLEQFGSK RVIDTPITEY
     GFAGLAVGAA FAGLRPIVEF MTFNFAMQAF DHIVNSAAKT HYMSGGQVKC PIVFRGPNGA
     ASRVAAQHSQ NYTACYSHIP GLKVVAPYSA EDHKGLMLTA IRDDNPVIFL ENEILYGHSF
     DVPDIIEPIP FSKAKILKEG SNVTIVTFSI QVKLALDVVN ILQNDNIDCE LIDLRTIKPL
     DTDSIIESVK KTNRLVIVEE GWFFAGVGAS IASIVMKEAF DYLDAPIEIV SGKDVPLPYA
     VNLEKLAMPS ANDLIEAVKK VCYYSI