ID   ODPA_RHIME              Reviewed;         348 AA.
AC   Q9R9N5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; Synonyms=pdhAalpha; OrderedLocusNames=R01445;
GN   ORFNames=SMc01030;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RCR2011 / SU47;
RX   PubMed=10796014; DOI=10.1094/mpmi.2000.13.5.483;
RA   Cabanes D., Boistard P., Batut J.;
RT   "Symbiotic induction of pyruvate dehydrogenase genes from Sinorhizobium
RT   meliloti.";
RL   Mol. Plant Microbe Interact. 13:483-493(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; 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; AF190792; AAF04587.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC46024.1; -; Genomic_DNA.
DR   RefSeq; NP_385551.1; NC_003047.1.
DR   RefSeq; WP_003535472.1; NC_003047.1.
DR   AlphaFoldDB; Q9R9N5; -.
DR   SMR; Q9R9N5; -.
DR   EnsemblBacteria; CAC46024; CAC46024; SMc01030.
DR   GeneID; 61602908; -.
DR   KEGG; sme:SMc01030; -.
DR   PATRIC; fig|266834.11.peg.2865; -.
DR   eggNOG; COG1071; Bacteria.
DR   HOGENOM; CLU_029393_5_2_5; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000001976; 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   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyruvate; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..348
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000162202"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   348 AA;  38113 MW;  671DBC015C03CC78 CRC64;
     MAPRKSASVS SRKTAAKPAK KDFAGGTIAE FSKEDDLKAY REMLLIRRFE EKAGQLYGMG
     FIGGFCHLYI GQEAVVVGMQ LALKEGDQVI TGYRDHGHML ACGMSARGVM AELTGRRGGL
     SKGKGGSMHM FSKEKHFYGG HGIVGAQVSL GTGLAFANRY RGNDNVSLAY FGDGAANQGQ
     VYESFNMAAL WKLPVIYIVE NNRYAMGTSV SRASAQTDFS QRGASFGIPG YQVDGMDVRA
     VKAAADEAVE HCRSGKGPII LEMLTYRYRG HSMSDPAKYR SKDEVQKMRS EHDPIEQVKA
     RLTDKGWATE DELKQIDKEV RDIVADSADF AQSDPEPDVS ELYTDILL
//