ID   ODP1_CORGL              Reviewed;         922 AA.
AC   Q8NNF6; Q6M3J1;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Pyruvate dehydrogenase E1 component;
DE            Short=E1p;
DE            Short=PDH E1 component;
DE            EC=1.2.4.1;
GN   Name=aceE; OrderedLocusNames=Cgl2248, cg2466;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [3]
RP   IDENTIFICATION IN THE ODH/PDH COMPLEX.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=16522631; DOI=10.1074/jbc.m512515200;
RA   Niebisch A., Kabus A., Schultz C., Weil B., Bott M.;
RT   "Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase
RT   activity via the phosphorylation status of the OdhI protein.";
RL   J. Biol. Chem. 281:12300-12307(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=20675489; DOI=10.1128/jb.00597-10;
RA   Hoffelder M., Raasch K., van Ooyen J., Eggeling L.;
RT   "The E2 domain of OdhA of Corynebacterium glutamicum has
RT   succinyltransferase activity dependent on lipoyl residues of the
RT   acetyltransferase AceF.";
RL   J. Bacteriol. 192:5203-5211(2010).
CC   -!- FUNCTION: Is a specific component of the pyruvate dehydrogenase (PDH)
CC       complex, that catalyzes the overall conversion of pyruvate to acetyl-
CC       CoA and CO(2). AceE has reductase activity with pyruvate but does not
CC       react with 2-oxoglutarate. {ECO:0000269|PubMed:20675489}.
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         Evidence={ECO:0000269|PubMed:20675489};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.066 mM for pyruvate {ECO:0000269|PubMed:20675489};
CC   -!- SUBUNIT: Homodimer (By similarity). Part of an unusual ODH/PDH
CC       supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together
CC       with OdhA (E1+E2). {ECO:0000250, ECO:0000269|PubMed:16522631}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene display no PDH activity.
CC       {ECO:0000269|PubMed:20675489}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000036; BAB99641.1; -; Genomic_DNA.
DR   EMBL; BX927154; CAF20589.1; -; Genomic_DNA.
DR   RefSeq; NP_601447.1; NC_003450.3.
DR   RefSeq; WP_011014985.1; NC_006958.1.
DR   AlphaFoldDB; Q8NNF6; -.
DR   SMR; Q8NNF6; -.
DR   STRING; 196627.cg2466; -.
DR   PRIDE; Q8NNF6; -.
DR   KEGG; cgb:cg2466; -.
DR   KEGG; cgl:Cgl2248; -.
DR   PATRIC; fig|196627.13.peg.2180; -.
DR   eggNOG; COG2609; Bacteria.
DR   HOGENOM; CLU_009154_2_0_11; -.
DR   OMA; PDEYRTF; -.
DR   BRENDA; 1.2.1.104; 960.
DR   BRENDA; 1.2.4.1; 960.
DR   SABIO-RK; Q8NNF6; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   1: Evidence at protein level;
KW   Glycolysis; Magnesium; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..922
FT                   /note="Pyruvate dehydrogenase E1 component"
FT                   /id="PRO_0000420522"
SQ   SEQUENCE   922 AA;  102826 MW;  5B949B2A72B855BF CRC64;
     MADQAKLGGK PSDDSNFAMI RDGVASYLND SDPEETNEWM DSLDGLLQES SPERARYLML
     RLLERASAKR VSLPPMTSTD YVNTIPTSME PEFPGDEEME KRYRRWIRWN AAIMVHRAQR
     PGIGVGGHIS TYAGAAPLYE VGFNHFFRGK DHPGGGDQIF FQGHASPGMY ARAFMEGRLS
     EDDLDGFRQE VSREQGGIPS YPHPHGMKDF WEFPTVSMGL GPMDAIYQAR FNRYLENRGI
     KDTSDQHVWA FLGDGEMDEP ESRGLIQQAA LNNLDNLTFV VNCNLQRLDG PVRGNTKIIQ
     ELESFFRGAG WSVIKVVWGR EWDELLEKDQ DGALVEIMNN TSDGDYQTFK ANDGAYVREH
     FFGRDPRTAK LVENMTDEEI WKLPRGGHDY RKVYAAYKRA LETKDRPTVI LAHTIKGYGL
     GHNFEGRNAT HQMKKLTLDD LKLFRDKQGI PITDEQLEKD PYLPPYYHPG EDAPEIKYMK
     ERRAALGGYL PERRENYDPI QVPPLDKLRS VRKGSGKQQI ATTMATVRTF KELMRDKGLA
     DRLVPIIPDE ARTFGLDSWF PTLKIYNPHG QNYVPVDHDL MLSYREAPEG QILHEGINEA
     GSVASFIAAG TSYATHGKAM IPLYIFYSMF GFQRTGDSIW AAADQMARGF LLGATAGRTT
     LTGEGLQHMD GHSPVLASTN EGVETYDPSF AYEIAHLVHR GIDRMYGPGK GEDVIYYITI
     YNEPTPQPAE PEGLDVEGLH KGIYLYSRGE GTGHEANILA SGVGMQWALK AASILEADYG
     VRANIYSATS WVNLARDGAA RNKAQLRNPG ADAGEAFVTT QLKQTSGPYV AVSDFSTDLP
     NQIREWVPGD YTVLGADGFG FSDTRPAARR FFNIDAESIV VAVLNSLARE GKIDVSVAAQ
     AAEKFKLDDP TSVSVDPNAP EE