ID   CAPP_YERE8              Reviewed;         879 AA.
AC   A1JI20;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=YE0116;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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 = 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         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-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; AM286415; CAL10258.1; -; Genomic_DNA.
DR   RefSeq; WP_011815299.1; NC_008800.1.
DR   RefSeq; YP_001004510.1; NC_008800.1.
DR   AlphaFoldDB; A1JI20; -.
DR   SMR; A1JI20; -.
DR   STRING; 393305.YE0116; -.
DR   EnsemblBacteria; CAL10258; CAL10258; YE0116.
DR   KEGG; yen:YE0116; -.
DR   PATRIC; fig|393305.7.peg.207; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000000642; 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   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   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium.
FT   CHAIN           1..879
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025604"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   879 AA;  98363 MW;  5AD46BB12428921F CRC64;
     MNEQYSAMRS NVSMLGTLLG DTIKEALGEH ILEKVETIRK LSKSSRAGNE ASRQELLTTL
     QNLSNDELLP VARAFSQFLN LTNTAEQYHS ISPHGEAASN PEALAQLFTR LKDKKLSEQD
     MRSAVDELSI ELVLTAHPTE ITRRTLIHKL VEVNTCLSQL DHNDLADYER NKIMRRLRQL
     VAQSWHTDEI RKIRPSPVDE AKWGFAVVEN SLWEGVPAFL REFNEQLQNS LDYRLPVEAV
     PIRFTSWMGG DRDGNPNVTA EITRHVLLLS RWKATDLFLR DIQVLVSELS MSECTPELRE
     LAGGEEVLEP YRELMKRVRT QLTNTQAYLE ARLKGERVLP PTDLLVSNDQ LWDPLYACYQ
     SLKACGMEII ANGQLLDTLR RVRCFGVPLV RIDVRQESTR HTDAIAELTR YLGLGDYESW
     SEADKQAFLI RELNSKRPLV PLKWEPSADT QEVLETCRVI AEAPQGSIAA YVISMAKVPS
     DVLAVHLLLK EAGCPFTLPV APLFETLDDL NNADDVMTQL LNIDWYRGLI QGKQMVMIGY
     SDSAKDAGVM AASWAQYRAQ DALIKTCEKA GISLTLFHGR GGSIGRGGAP AHAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPEVTISSL ALYASAVLEA NLLPPPEPKK EWNEVMDILS
     DASCEMYRGY VRENPQFVPY FRAATPELEL GKLPLGSRPA KRRPNGGVES LRAIPWIFAW
     TQNRLMLPAW LGAGAGLQKA IDAGKKEVLA TMCRDWPFFS TRIGMLEMVF AKADLWLAEY
     YDQRLVDKSL WPLGQQLRDQ LEADIKVVLA IANDDHLMAD LPWIAESIAL RNVYTDPLNV
     LQAELLHRSR QQENAADACV EQALMVTIAG VAAGMRNTG