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   16-JUN-2009, entry version 55.
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.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Zymomonas.
OX   NCBI_TaxID=542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29191 / DSM 3580 / IFO 13756 / NCIB 11199 / ZM6;
RX   MEDLINE=98175679; PubMed=9515924;
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.,
RA   Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M.,
RA   Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y.,
RA   Kang H.L., Lee S.Y., Lee K.J., 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
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
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; YP_163341.1; -.
DR   HSSP; P08559; 1NI4.
DR   GeneID; 3187783; -.
DR   GenomeReviews; AE008692_GR; ZMO1606.
DR   KEGG; zmo:ZMO1606; -.
DR   NMPDR; fig|264203.3.peg.80; -.
DR   HOGENOM; O66112; -.
DR   OMA; O66112; LEYETYR.
DR   BioCyc; ZMOB264203:ZMO1606-MON; -.
DR   BRENDA; 1.2.4.1; 1658.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    354       Pyruvate dehydrogenase E1 component
FT                                subunit alpha.
FT                                /FTId=PRO_0000162213.
FT   CONFLICT     69     69       C -> N (in Ref. 2; AAC70361).
FT   CONFLICT    309    309       Missing (in Ref. 2; AAC70361).
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
//