ID   CAPP_PROMH              Reviewed;         878 AA.
AC   B4F183;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
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=PMI3227;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR46321.1; -; Genomic_DNA.
DR   RefSeq; WP_004246402.1; NC_010554.1.
DR   AlphaFoldDB; B4F183; -.
DR   SMR; B4F183; -.
DR   EnsemblBacteria; CAR46321; CAR46321; PMI3227.
DR   GeneID; 6801836; -.
DR   KEGG; pmr:PMI3227; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000008319; 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_1000129836"
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;  98678 MW;  208C42D3EA1C9AA3 CRC64;
     MNQQYSAMRS NVSMLGKLLG DTIKEALGEE ILDKVESIRK LSKSSRAGNE VQRQKLLLTL
     QNLSNDELLP VARAFNQFLN LTNVAEQYHS ISPHGEAASN PVALAKLIER LKDKNFTNQQ
     LKQAVEQISI ELVLTAHPTE IARRTLIHKL VEVNTCLSQL DHDDLADYER TNIMRRLRQL
     VAQSWHTDEI RKIRPTPIDE AKWGFAVVEN SLWEGVPAFL REFNEQLEES IDYNLPVEAS
     PIRFTSWMGG DRDGNPNVTA EITRHALLLS RWKAADLFLN DIQVLVSELS MTESTPELRE
     LAGGADVAEP YREIAKQLRT RLQVTRDYLE QRIKGQQSLP PEGLLIDNSA LWEPLYACYQ
     SLHQCGMRII ANGQLLDTLR RIRCFGLQLV RLDIRQESTN HTEALSELTQ YLELGDYASW
     SEEQKQTFLL TELNSKRPLI PTHWQPSEAT KEVFETCRVI AESPKDSIAS YVISMAKVPS
     DVLAVKLLLK EAGADIRLPV APLFETLEDL NNAESVMTRL FDIPWYRDLI DNKQMVMIGY
     SDSAKDAGVM AASWAQYRAQ DALIKLCEKS GVTLTLFHGR GGTIGRGGAP AHAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPQVTISSL AHYAGAILEA NLLPPPEPKT AWIEVMDALS
     DVSCEMYRGY VRGEKDFVPY FRAATPEGEL GKLPLGSRPA KRRPTGGVET LRAIPWIFAW
     TQNRLMLPAW LGAGAALQHE IDNGKQAVLD DMCENWPFFN TRIAMLEMVY AKADLWLAEY
     YDQRLVEENL WPLGAKLRQQ LSDDIKSVLA ISKDEHLMAD LPWVAESIAL RNVYTDPLNV
     LQAELLQRSR THSESDPRIE QALMVTIAGI AAGMRNTG
//