ID   A0A1C4BUQ6_9GAMM        Unreviewed;       881 AA.
AC   A0A1C4BUQ6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ORFNames=GA0061081_10612 {ECO:0000313|EMBL:SCC10595.1};
OS   Gilliamella bombicola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae;
OC   Gilliamella.
OX   NCBI_TaxID=1798182 {ECO:0000313|EMBL:SCC10595.1, ECO:0000313|Proteomes:UP000199670};
RN   [1] {ECO:0000313|Proteomes:UP000199670}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-53248 {ECO:0000313|Proteomes:UP000199670};
RA   Varghese N., Submissions Spin;
RL   Submitted (AUG-2016) 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; FMAQ01000006; SCC10595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4BUQ6; -.
DR   STRING; 1798182.GA0061081_10612; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000199670; Unassembled WGS sequence.
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:SCC10595.1}.
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        547
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   881 AA;  99805 MW;  4E53116FB0ED0111 CRC64;
     MNNQYSSMRS NVNMLGTLLG NAIKRATGNE TFDLVEKIRN LSKSAQQGNT QAHNELLKLI
     ENLNDDDLLH VARAFNQFLN LVNTAAEYYG ISPHGEASSS PKKMTELFST LKNLNFSNQT
     ITEAINELSI ELVLTAHPTE INRRTMINTY TAINNCLSQL DHDDLADYEI ERIMRRLKQL
     VCQAWYTDEI RKKRPTPIDE AKWGFSVIED SLWEGVPLFL RELNDQLVDA FDEQLPVDHV
     PIKFTSWMGG DRDGNPNVTA KVTEKVMLQA RLKAIELFLA DIQILVRELS MTECSDSVID
     LLDEKNKTVS EPYRAVMKQL RTRLINTHNY IEALLNNERV LPPSDILIKN EQLWMPLYTC
     YESLIDHGMS TIAHGPLLDT LRRIKSFGLQ LVRLDIRQDS SMHTEALDAL TKELNLGSYA
     KWTEQEKQAF LLTELQSNRP LLPYNWQPDQ MVQEVLDTCR VIKKAGEESI ASYVISMAKA
     PSDILAVYLL LKIVDCQKYI PVAPLFETLE DLNNAKSVMQ KLLDIPWYRD KIQGKQMVMI
     GYSDSAKDAG TLAASWAQYR SQEELVSLFE KYDTNLVLFH GRGGSIGRGG APAHAALLSQ
     PPGSLKGGLR VTEQGEMIRF KLGLPEVALS SLMLYTSAIL QANLLPPPAP KQEWRNIMDE
     MSEISCNCYR SYVRERAEFV DYFRAVTPEA ELGRLPLGSR PQKRRTGGGI ESLRAIPWIF
     AWTQNRLMVP SWLGAGSALR VAIEEGKQNL LKEMYHNWPF FNARLGMLEM VYAKAAPNIH
     EYYEQRLVDP ALWPLGEELR SLLTQDINTV LTVTDDISLM ADLPWIAQSV ALRNTYIEPL
     NLLQAELLSR SRKYSDNENI IVEQGLMITI SGIAAGMRNS G
//