ID   ODPA_MYCGE              Reviewed;         358 AA.
AC   P47516;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; OrderedLocusNames=MG274;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
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; L43967; AAC71496.1; -; Genomic_DNA.
DR   PIR; C64230; C64230.
DR   RefSeq; WP_009885906.1; NZ_AAGX01000009.1.
DR   AlphaFoldDB; P47516; -.
DR   SMR; P47516; -.
DR   STRING; 243273.MG_274; -.
DR   EnsemblBacteria; AAC71496; AAC71496; MG_274.
DR   KEGG; mge:MG_274; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_1_0_14; -.
DR   OMA; GMFRGVN; -.
DR   OrthoDB; 1248201at2; -.
DR   BioCyc; MGEN243273:G1GJ2-332-MON; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0140032; F:glycosylation-dependent protein binding; IPI:UniProtKB.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; 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   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..358
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000162200"
SQ   SEQUENCE   358 AA;  40651 MW;  9C85D2335F80842E CRC64;
     MAILIKNKVP TTLYQVYDNE GKLIDPNHKI TLTDEQLKHA YYLMNLSRMM DKKMLVWQRA
     GKMLNFAPNL GEEALQVGMG LGLNENDWVC PTFRSGALML YRGVKPEQLL LYWNGNEKGS
     QIDAKYKTLP INITIGAQYS HAAGLGYMLH YKKQPNVAVT MIGDGGTAEG EFYEAMNIAS
     IHKWNTVFCI NNNQFAISTR TKLESAVSDL SVKAIACGIP RVRVDGNDLI ASYEAMQDAA
     NYARGGNGPV LIEFFSYRQG PHTTSDDPSI YRTKQEEEEG MKSDPVKRLR NFLFDRSILN
     QAQEEEMFSK IEQEIQAAYE KMVLDTPVSV DEVFDYNYQE LTPELVEQKQ IAKKYFKD