ID   CAPP_YERPS              Reviewed;         878 AA.
AC   Q66G74;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 97.
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};
GN   OrderedLocusNames=YPTB0108;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; 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; BX936398; CAH19348.1; -; Genomic_DNA.
DR   RefSeq; WP_011191467.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66G74; -.
DR   SMR; Q66G74; -.
DR   GeneID; 66843499; -.
DR   KEGG; ypo:BZ17_2488; -.
DR   KEGG; yps:YPTB0108; -.
DR   PATRIC; fig|273123.14.peg.2607; -.
DR   Proteomes; UP000001011; 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   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium.
FT   CHAIN           1..878
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166655"
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   878 AA;  98352 MW;  F57CEB64D37D8564 CRC64;
     MNEQYSAMRS NVSMLGTLLG DTIKEALGEH ILDRVETIRK LSKSSRAGNE ASRQELLTTL
     QNLSNDELLP VARAFSQFLN LTNTAEQYHS ISPHGEAASN PEALAQLFTR LKDKKLSDQD
     MRSAVDDLSI ELVLTAHPTE ITRRTLIHKL VEVNTCLSQL DHNDLADYER NKIMRRLRQL
     VAQSWHTDEI RKLRPSPVDE AKWGFAVVEN SLWEGVPAFL REFNEQLENS LDYRLPVEAV
     PIRFTSWMGG DRDGNPNVTA EITRHVLLLS RWKATDLFLR DIQVLVSELS MSECTPELRE
     LAGGEEVLEP YRQLMKNVRT QLTNTQAYLE ARLKGERVLP PHDLLVSNDQ LWEPLYACYQ
     SLKACGMEII ANGQLLDTLR RVRCFGVPLV RIDVRQESTR HTDAIAELTR YLGLGDYESW
     SESDKQAFLV RELNSKRPLV PLKWEPSAET QEVLETCRVI AEAPQGSIAA YVISMAKVPS
     DVLAVHLLLK EAGCPFTLPV APLFETLDDL NNADDVMTQL LGIDWYRGLI QGKQMVMIGY
     SDSAKDAGVM AASWAQYRAQ DALIKTCEKA GITLTLFHGR GGSIGRGGAP AHAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPEVTISSL ALYAGAILEA NLLPPPEPKK EWIEVMDLLS
     DASCDMYRSY VRENPEFVRY FRAATPELEL GKLPLGSRPA KRRPDGGVES LRAIPWIFAW
     TQNRLMLPAW LGAGAGLQRA IDAGKRDVLA TMCRDWPFFS TRIGMLEMVF AKADLWLAEY
     YDQRLVDKSL WPLGQQLRDQ LAADIKVVLA IANDDHLMAD LPWIAESIAL RNVYTDPLNV
     LQAELLHRSR QQEHPDACVE QALMVTIAGV AAGMRNTG
//