ID   ODPA_ZYMMO              Reviewed;         354 AA.
AC   O66112; O69011; Q5NM30;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; Synonyms=pdhAalpha; OrderedLocusNames=ZMO1606;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC   11199 / NRRL B-4490 / ZM6;
RX   PubMed=9515924; DOI=10.1128/jb.180.6.1540-1548.1998;
RA   Neveling U., Klasen R., Bringer-Meyer S., Sahm H.;
RT   "Purification of the pyruvate dehydrogenase multienzyme complex of
RT   Zymomonas mobilis and identification and sequence analysis of the
RT   corresponding genes.";
RL   J. Bacteriol. 180:1540-1548(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Lee J., Jin S., Kang H.S.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(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; Y12884; CAA73384.1; -; Genomic_DNA.
DR   EMBL; AF086791; AAC70361.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV90230.1; -; Genomic_DNA.
DR   PIR; T33722; T33722.
DR   RefSeq; WP_011241360.1; NZ_CP035711.1.
DR   AlphaFoldDB; O66112; -.
DR   SMR; O66112; -.
DR   STRING; 264203.ZMO1606; -.
DR   EnsemblBacteria; AAV90230; AAV90230; ZMO1606.
DR   GeneID; 58027325; -.
DR   KEGG; zmo:ZMO1606; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_2_5; -.
DR   OMA; FGMPGVT; -.
DR   OrthoDB; 1248201at2; -.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
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   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..354
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000162213"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        69
FT                   /note="C -> N (in Ref. 2; AAC70361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        309
FT                   /note="Missing (in Ref. 2; AAC70361)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  38654 MW;  515F5B2EDA0C1424 CRC64;
     MAKATQDSNR PHKADVGSAI PNHDLPPIPG RYHADREELL EFYRRMLMIR RFEERCGQLY
     GLGLIAGFCH LYIGQEAVAV GLQAALQPGR DSVITGYREH GHMLAYGIDP KIVMAELTGR
     ASGISHGKGG SMHMFSTEHK FFGGNGIVGA QVPLGAGLAF AHKYRNDGGC SAAYFGDGSA
     NQGQVYEAYN MAALWKLPVI FVIENNGYAM GTSIQRANAH TALSERGAGF GIPALVVDGM
     DVLEVRGAAT VAVDWVQAGK GPIILEMKTY RYRGHSMSDP ARYRSREEVN DMKENHDPLD
     NLKKDLFAAG VPEAELVKLD EDIRQQVKEA ADFAEKAPLP ADEELYTNIL VGKY