ID   CAPP_CORDI              Reviewed;         902 AA.
AC   P61448;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   04-NOV-2026, entry version 102.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=DIP1122;
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA   Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA   Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = phosphoenolpyruvate +
CC         hydrogencarbonate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; BX248357; CAE49642.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61448; -.
DR   SMR; P61448; -.
DR   STRING; 257309.DIP1122; -.
DR   KEGG; cdi:DIP1122; -.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   OMA; AAAIPQC; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   NCBIfam; NF000584; ppc; 1.
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   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..902
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166589"
FT   REGION          327..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        561
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   902 AA;  101058 MW;  8B92C1E171D798FC CRC64;
     MTAAISDRVR EDIRLLGRVL GRVIAQQEGE EVYELVEATR RMAFDVSHGD ADPEDLMVIF
     RDLDITKTNL VARAFSYFAL LANLVEDLDD ESVEADVSLR KTFAKLKREG VSAADAASVI
     RSAEVAPVLT AHPTETRRRT VFDTQTRIKQ LLKDAHHGGD MQVIEQEMYL RMTLLWQTAL
     IRIARPTLED EIDVGLRYYK KSLLEQVPAL NRSIRHSMRE TFGLQLPDIA VMRPGSWIGG
     DHDGNPYVNA RTLTYATRQA AKTVARYYVE QLGELERELS LSDRYSSCSK ELLALAEASG
     NNWESRVDEP YRRAVYGMRA RMKSNVDALE RPEKTAGKKS SKRTPYATPE EFLRDLDVID
     RSLRAHNDDV IADDRLARIR SAVTTFGFHL YTLDIRQNSE SFEAVIEEVF AAARRVPGGK
     RYSELAEAEK VELLIQELQT PRPLLFPGAL EVEDAFSADT TKELGIFLAA AQAVRDFGSR
     SIAHCIISMT ATVSDILEPM VLLKEVGLRD VDVVPLFETI DDLRCGAAIL RELWSHPFYR
     EHLRARGDIQ EVMLGYSDSN KDGGYLQANW ALYDAELGLV ELCREHNIEL RLAHGRGGAV
     GRGGGPTYDA ILAQPKGAVS GSVRITEQGE VISAKYGAPE TARRHLEAFV SGALEASLLD
     TEPIADPDRA YAIMRDLAGF SGQRYQELVG DPGFIEYFTQ STPLHEIGEL NLGSRPAARK
     QTTAISDLRA IPWVLSWSQS RTNIPGWFGV GSAVSRFVSA VPEKDRESRW QELRDLYATW
     PFFRSVMSNM AQVMAKAEIS LARLYADLVD DPEVADRIYA LIAEEFELTR RAYLAITGNE
     ALVSENQRQA RSLKRRYPYL LPLNAIQLEL LRRYRGGDDQ FLVSKTIQVT MNGLATALRN
     AG
//