ID   ODP1_AZOVI              Reviewed;          45 AA.
AC   P10801;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            EC=1.2.4.1;
DE   Flags: Fragment;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / NBRC
RC   102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16;
RX   PubMed=3292237; DOI=10.1111/j.1432-1033.1988.tb14140.x;
RA   Hanemaaijer R., Janssen A., de Kok A., Veeger C.;
RT   "The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase
RT   complex from Azotobacter vinelandii. Molecular cloning and sequence
RT   analysis.";
RL   Eur. J. Biochem. 174:593-599(1988).
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   -!- 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: Homodimer.
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DR   EMBL; X12455; CAA30986.1; -; Genomic_DNA.
DR   PIR; S12208; S12208.
DR   AlphaFoldDB; P10801; -.
DR   SMR; P10801; -.
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; IPR009014; Transketo_C/PFOR_II.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   4: Predicted;
KW   Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
FT   CHAIN           <1..45
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000162239"
FT   NON_TER         1
SQ   SEQUENCE   45 AA;  4957 MW;  C2929BB637D1B032 CRC64;
     EVDRYWVVLA ALEALADRGD IEAKVVAEAI AKFGIDPDKR NPLDC