ID   ODPB_RICFE              Reviewed;         326 AA.
AC   Q4UKQ7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; OrderedLocusNames=RF_1019;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61870.1; -; Genomic_DNA.
DR   RefSeq; WP_011271335.1; NC_007109.1.
DR   AlphaFoldDB; Q4UKQ7; -.
DR   SMR; Q4UKQ7; -.
DR   STRING; 315456.RF_1019; -.
DR   EnsemblBacteria; AAY61870; AAY61870; RF_1019.
DR   KEGG; rfe:RF_1019; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_1_5; -.
DR   OMA; SRMRHHC; -.
DR   OrthoDB; 900125at2; -.
DR   Proteomes; UP000008548; 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; Thiamine pyrophosphate.
FT   CHAIN           1..326
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta"
FT                   /id="PRO_0000288761"
FT   BINDING         59
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   326 AA;  35761 MW;  4AC3ED57089C3427 CRC64;
     MQITVREALR DAMQEEMIRD DKVFVMGEEV AEYQGAYKVT QGLLEQFGPK RVIDTPITEY
     GFAGLAVGAA FAGLRPIVEF MTFNFAMQAF DHIVNSAAKT HYMSGGQAKC PIVFRGPNGA
     ASRVAAQHSQ NYTACYSHVP GLKVVAPYSA EDHKGLMLTA IRDDNPVIFL ENEILYGHSF
     DVPETIEPIP FGQAKILREG SSVTIVTFSI QVKLALDAAN VLQNDNIDCE VIDLRTIKPL
     DTDTIIESVK KTNRLVIVEE GWFFAGVGAS IASIVMKEAF DYLDAPIEIV SGKDVPLPFA
     VNLEKLALPS ESDVIEAVKK VCYYSV