ID   ODPA_ACHLA              Reviewed;         345 AA.
AC   P35485;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
DE   Flags: Fragment;
GN   Name=pdhA;
OS   Acholeplasma laidlawii.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=2148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1735725; DOI=10.1128/jb.174.4.1388-1396.1992;
RA   Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.;
RT   "Identification and analysis of the genes coding for the putative pyruvate
RT   dehydrogenase enzyme complex in Acholeplasma laidlawii.";
RL   J. Bacteriol. 174:1388-1396(1992).
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: Heterodimer of an alpha and a beta chain.
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DR   EMBL; M81753; AAA21907.1; -; Genomic_DNA.
DR   PIR; A42653; A42653.
DR   AlphaFoldDB; P35485; -.
DR   SMR; P35485; -.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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   4: Predicted;
KW   Glycolysis; Oxidoreductase; Pyruvate; Thiamine pyrophosphate.
FT   CHAIN           <1..345
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000162197"
FT   NON_TER         1
SQ   SEQUENCE   345 AA;  38962 MW;  797F9F67DE0C2995 CRC64;
     DQNGKVVNEK MEPKLPKETL LKMYKTAVLG RNADIKALQY QRQGRMLTYA PNMGQEAAQI
     GMAAAMEPQD WNSPMYRELN TLLYRGDKLE NVFLYWYGNE RGSIKPEGVK ILPTNIIIGS
     QSNIAAGLAM ASKIRKTNEV TAFTIGDGGT AHGEFYEGLN FAASFKAPVV AVIQNNQWAI
     STPVRKASNS ETLAQKGVAF GIPYIQVDGN DMLAMYVASK EAMDRARKGD GPTLIEAFTY
     RMGPHTTSDD PCSIYRTKEE ENEWAKKDQI ARFKTYLINK GYWSEEEDKK LEEEVLAEIN
     DTFKKVESYG ANVELIEIFE HTYAEMTPQL KEQYEEHKKY LEGVK