ID   CAPP_CORGL              Reviewed;         919 AA.
AC   P12880;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=Cgl1585, cg1787;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RX   PubMed=2779518; DOI=10.1007/bf00331286;
RA   Eikmanns B.J., Follettie M.T., Griot M.U., Sinskey A.J.;
RT   "The phosphoenolpyruvate carboxylase gene of Corynebacterium glutamicum:
RT   molecular cloning, nucleotide sequence, and expression.";
RL   Mol. Gen. Genet. 218:330-339(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=2666264; DOI=10.1016/0378-1119(89)90072-3;
RA   O'Regan M., Thierbach G., Bachmann B., Villeval D., Lepage P., Viret J.F.,
RA   Lemoine Y.;
RT   "Cloning and nucleotide sequence of the phosphoenolpyruvate carboxylase-
RT   coding gene of Corynebacterium glutamicum ATCC13032.";
RL   Gene 77:237-251(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 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).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activity not stimulated by acetyl-CoA in the
CC       absence of any allosteric inhibitor, while the corresponding protein
CC       from E.coli is strongly stimulated.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; X14234; CAA32450.1; -; Genomic_DNA.
DR   EMBL; M25819; AAA83537.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98978.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21593.1; -; Genomic_DNA.
DR   PIR; S05512; QYFKG.
DR   RefSeq; NP_600799.1; NC_003450.3.
DR   RefSeq; WP_011014465.1; NC_006958.1.
DR   AlphaFoldDB; P12880; -.
DR   SMR; P12880; -.
DR   STRING; 196627.cg1787; -.
DR   KEGG; cgb:cg1787; -.
DR   KEGG; cgl:Cgl1585; -.
DR   PATRIC; fig|196627.13.peg.1546; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OrthoDB; 9768133at2; -.
DR   BioCyc; CORYNE:G18NG-11170-MONOMER; -.
DR   BRENDA; 4.1.1.31; 960.
DR   Proteomes; UP000000582; Chromosome.
DR   Proteomes; UP000001009; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   1: Evidence at protein level;
KW   Carbon dioxide fixation; Direct protein sequencing; Lyase; Magnesium;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2666264"
FT   CHAIN           2..919
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166591"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        579
FT                   /evidence="ECO:0000250"
FT   CONFLICT        607..608
FT                   /note="KL -> NV (in Ref. 1; CAA32450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        800..801
FT                   /note="FT -> LP (in Ref. 1; CAA32450)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        915
FT                   /note="L -> V (in Ref. 1; CAA32450)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   919 AA;  103198 MW;  676C45D0EAAF3F54 CRC64;
     MTDFLRDDIR FLGQILGEVI AEQEGQEVYE LVEQARLTSF DIAKGNAEMD SLVQVFDGIT
     PAKATPIARA FSHFALLANL AEDLYDEELR EQALDAGDTP PDSTLDATWL KLNEGNVGAE
     AVADVLRNAE VAPVLTAHPT ETRRRTVFDA QKWITTHMRE RHALQSAEPT ARTQSKLDEI
     EKNIRRRITI LWQTALIRVA RPRIEDEIEV GLRYYKLSLL EEIPRINRDV AVELRERFGE
     GVPLKPVVKP GSWIGGDHDG NPYVTAETVE YSTHRAAETV LKYYARQLHS LEHELSLSDR
     MNKVTPQLLA LADAGHNDVP SRVDEPYRRA VHGVRGRILA TTAELIGEDA VEGVWFKVFT
     PYASPEEFLN DALTIDHSLR ESKDVLIADD RLSVLISAIE SFGFNLYALD LRQNSESYED
     VLTELFERAQ VTANYRELSE AEKLEVLLKE LRSPRPLIPH GSDEYSEVTD RELGIFRTAS
     EAVKKFGPRM VPHCIISMAS SVTDVLEPMV LLKEFGLIAA NGDNPRGTVD VIPLFETIED
     LQAGAGILDE LWKIDLYRNY LLQRDNVQEV MLGYSDSNKD GGYFSANWAL YDAELQLVEL
     CRSAGVKLRL FHGRGGTVGR GGGPSYDAIL AQPRGAVQGS VRITEQGEII SAKYGNPETA
     RRNLEALVSA TLEASLLDVS ELTDHQRAYD IMSEISELSL KKYASLVHED QGFIDYFTQS
     TPLQEIGSLN IGSRPSSRKQ TSSVEDLRAI PWVLSWSQSR VMLPGWFGVG TALEQWIGEG
     EQATQRIAEL QTLNESWPFF TSVLDNMAQV MSKAELRLAK LYADLIPDTE VAERVYSVIR
     EEYFLTKKMF CVITGSDDLL DDNPLLARSV QRRYPYLLPL NVIQVEMMRR YRKGDQSEQV
     SRNIQLTMNG LSTALRNSG
//