ID   A0A068QQ13_9GAMM        Unreviewed;       897 AA.
AC   A0A068QQ13;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:CDG15915.1};
GN   ORFNames=XDD1_0204 {ECO:0000313|EMBL:CDG15915.1};
OS   Xenorhabdus doucetiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG15915.1, ECO:0000313|Proteomes:UP000032721};
RN   [1] {ECO:0000313|EMBL:CDG15915.1, ECO:0000313|Proteomes:UP000032721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; FO704550; CDG15915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068QQ13; -.
DR   STRING; 351671.XDD1_0204; -.
DR   KEGG; xdo:XDD1_0204; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000032721; 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 {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:CDG15915.1}.
FT   ACT_SITE        156
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        564
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   897 AA;  100454 MW;  F573621E3889DB69 CRC64;
     MRQSAGAMGD IPQHKARNPM NQQYSAMRSN VSMLGKLLGD TIKEALGEDI LDKVETIRKL
     SKSSRAGNGI HRQQLLSTLE NLSNDELLPV ARAFNQFLNL TNVAEQYHSI SPHGEAASNP
     VALAALFNRL KDKQFSNDDL INAVNALAIE LVLTAHPTEI ARRTLIHKLV EVNGCLAQLD
     HDDLADYERT NIMRRLRQLI AQSWHTDEIR KNRPTPIDEA KWGFAVVENS LWEGVPAFLR
     EFNEQLEESL GYSLLVEAVP VRFTSWMGGD RDGNPNVTAE ITRHVLLLSR WKAADLFLKD
     IQVLVSELSM SECTPELRQM AGGEQVLEPY REIAKRLRTQ LGNTLVYLEK CLKGEQALPP
     ADLLLHNEQL WQPLYACYQS LKNCGMEIIA NGQLLDTLRR IRCFGLSLVR IDIRQESTRH
     RDAIAELTQY LAMGDYASWP EAEKQAFLLR ELQSKRPLIP RDWQPSADTQ EVFATCKVIA
     ESPQDSIAAY VISMAKVPSD VLAVKLLLKE AGCPLSLPVA PLFETLDDLN NAESVIRQLL
     GIEWYRSLIK DKQMVMIGYS DSAKDAGVMA ASWAQYRAQD ALIKVCEKEG VTLTLFHGRG
     GTIGRGGAPA HSALLSQPPG SLKGGLRVTE QGEMIRFKFG LPQVTISSLA LYASAILEAN
     LLPPPEPKPE WQQIMDTLSA VSCDMYRDYV REQPEFVPYF RAATPEQELA KLPLGSRPAK
     RRPTGGVESL RAIPWIFAWT QNRLMLPAWL GAGAALQQVI DAGKLPVLTD MCRDWPFFNT
     RIAMLEMVFA KADLWLAEYY DQRLVEPKLW PLGIKLRDQL AQDIKTVLTI AQDEQLMADL
     PWIAESIALR NVYTDPLNVL QAELLQRSRQ QENPDPHLEQ ALMVTIAGVA AGMRNTG
//