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Database: UniProt/SWISS-PROT
Entry: CAPP_CORGL
LinkDB: CAPP_CORGL
Original site: CAPP_CORGL 
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   22-NOV-2017, entry version 125.
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 / JCM 1318 /
OS   LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   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
RT   glutamicum: 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 / JCM 1318 / LMG 3730 / 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.,
RA   Viret J.F., Lemoine Y.;
RT   "Cloning and nucleotide sequence of the phosphoenolpyruvate
RT   carboxylase-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 / JCM 1318 / LMG 3730 / 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 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX   PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA   Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA   Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA   McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA   Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA   Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT   and its impact on the production of L-aspartate-derived amino acids
RT   and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ENZYME REGULATION: Activity not stimulated by acetyl-CoA in the
CC       absence of any allosteric inhibitor, while the corresponding
CC       protein from E.coli is strongly stimulated.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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   ProteinModelPortal; P12880; -.
DR   SMR; P12880; -.
DR   STRING; 196627.cg1787; -.
DR   EnsemblBacteria; BAB98978; BAB98978; BAB98978.
DR   EnsemblBacteria; CAF21593; CAF21593; cg1787.
DR   GeneID; 1019553; -.
DR   KEGG; cgb:cg1787; -.
DR   KEGG; cgl:NCgl1523; -.
DR   PATRIC; fig|196627.13.peg.1546; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   BioCyc; CORYNE:G18NG-11170-MONOMER; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   1: Evidence at protein level;
KW   Carbon dioxide fixation; Complete proteome; Direct protein sequencing;
KW   Lyase; Magnesium; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:2666264}.
FT   CHAIN         2    919       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000166591.
FT   ACT_SITE    138    138       {ECO:0000250}.
FT   ACT_SITE    579    579       {ECO:0000250}.
FT   CONFLICT    607    608       KL -> NV (in Ref. 1; CAA32450).
FT                                {ECO:0000305}.
FT   CONFLICT    800    801       FT -> LP (in Ref. 1; CAA32450).
FT                                {ECO:0000305}.
FT   CONFLICT    915    915       L -> V (in Ref. 1; CAA32450).
FT                                {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
//
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