ID   CAPP_EDWI9              Reviewed;         877 AA.
AC   C5BC63;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
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=NT01EI_3850;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR70969.1; -; Genomic_DNA.
DR   RefSeq; WP_015873000.1; NC_012779.2.
DR   AlphaFoldDB; C5BC63; -.
DR   SMR; C5BC63; -.
DR   STRING; 67780.B6E78_10810; -.
DR   GeneID; 69540673; -.
DR   KEGG; eic:NT01EI_3850; -.
DR   PATRIC; fig|634503.3.peg.3435; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001485; 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..877
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000212177"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   877 AA;  98769 MW;  8E9DCD5542246B5A CRC64;
     MNEQYSAMRG NVSMLGKLLG DTIKDALGEE ILDRVETIRR LSKSSRAGNE ASRQALLNTL
     QNLSNDELLP VARAFSQFLN LANVAEQYHR ISPHGEAASN PDALYHLFTR LKNKNLDEAQ
     IRQAVDNLSI ELVLTAHPTE IARRTLIHKL VEVNTCLSQL DHDDLADYER HQIMRRLRQL
     VAQSWHTDEI RKNRPTPIDE AKWGYAVVEN SLWEGVPAFL REFNEQLEKS LGYQLPVEAV
     PVRFTAWMGG DRDGNPNVTA EVTRRALLLS RWKAAELFLR DVQVLVSELS MTVCTPELRA
     LAGEHTQEPY REVLKRLRQQ LNNTLTYLDA RLRGERLPRP ADLLVSNDQL WQPLHTCYRS
     LKACGMGIIA NGQLLDTLRR VHCFGVPLVR IDIRQESTRH TEALAELTRY LGLGDYETWS
     EEDKQTFLLR ELNSKRPLVP RHWTPSPETK EVFDTCQVIA EAPAGAIAAY VISMARTPSD
     VLAVHLLLKE AGCPYNLPVV PLFETLDDLN NAEAVMTQLL SIDWYRGFIQ GKQMVMIGYS
     DSAKDAGVMA ASWAQYRAQE ALVRVCDNAG IALTLFHGRG GSIGRGGAPA HDALLSQPPG
     SLKSGLRVTE QGEMIRFKLG LPEIAVSSLT LYTSAILEAN LLPPPAPKQE WRDVMDELSQ
     TSCALYRRYI RKNPDFVPYF RSATPELELG KLPLGSRPAK RRPSGGVESL RAIPWIFAWT
     QNRLMLPAWL GAGTALEEAM TEGHRGTLEN MYRSWPFFTT RIDMLEMVFA KSDLWLAEYY
     DQRLVDPALW PLGTELRQQV QRDIQAVLTI ADTDHLMADL PWAAESIALR NVYTDPLNVL
     QAELLYRSRH QEQPDANVEQ ALMVTIAGVA AGMRNTG
//