ID   B5F0U5_SALA4            Unreviewed;       912 AA.
AC   B5F0U5;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
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:ACH50907.1};
GN   OrderedLocusNames=SeAg_B4360 {ECO:0000313|EMBL:ACH50907.1};
OS   Salmonella agona (strain SL483).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH50907.1, ECO:0000313|Proteomes:UP000008819};
RN   [1] {ECO:0000313|EMBL:ACH50907.1, ECO:0000313|Proteomes:UP000008819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483 {ECO:0000313|EMBL:ACH50907.1,
RC   ECO:0000313|Proteomes:UP000008819};
RX   PubMed=21602358; DOI=10.1128/JB.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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, ECO:0000256|HAMAP-
CC         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; CP001138; ACH50907.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5F0U5; -.
DR   KEGG; sea:SeAg_B4360; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000008819; 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:ACH50907.1}.
FT   ACT_SITE        167
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        575
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   912 AA;  102539 MW;  5BB626D5DE8C851E CRC64;
     MTWVGERSQR RRSVKDAGQL QQRWGVWDHM NEQYSALRSN VSMLGKVLGE TIKDALGEHI
     LDRVETIRKL SKSSRAGNEA NRQELLTTLQ NLSNDELLPV ARAFSQFLNL ANTAEQYHSI
     SPKGEAASNP EVIARTLRKL KNQPDLNDAT IKKAVESLSL ELVLTAHPTE ITRRTLIHKM
     GEINNCLKQL DNTDIADYER HQVMRRLRQL IAQSWHTDEI RKQRPSPVDE AKWGFAVVEN
     SLWQGVPNYL RELNEQLEEN LGYKLPVDFV PVRFTSWMGG DRDGNPNVTA DITRHVLLLS
     RWKATDLFLK DIHVLVSELS MVDATPELLA LVGEEGASEP YRYLMKKLRA RLMATQSWLE
     ARLKGEKLPK PAGLLTQNEQ LWEPLYACYQ SLQACGMGII ANGELLDTLR RVKCFGVPLV
     RIDIRQESTR HTEALGEITR YLGIGDYESW SEADKQAFLI RELNSKRPLL PRNWEPSNDT
     REVLETCKVI AEAPKGSIAA YVISMAKTPS DVLAVHLLLK EAGIGFAMPV APLFETLDDL
     NNADDVMTQL LNIDWYRGLI QGKQMVMIGY SDSAKDAGVM AASWAQYQAQ DALIKTCEKA
     GIELTLFHGR GGSIGRGGAP AHAALLSQPP GSLKGGLRVT EQGEMIRFKY GLPEVTVSSL
     SLYTSAILEA NLLPPPEPKD SWRHIMDELS VISCETYRGY VRENKDFVPY FRSATPEQEL
     GKLPLGSRPA KRRPTGGVES LRAIPWIFAW TQNRLMLPAW LGAGTALQKV VEDGKQSELE
     AMCRDWPFFS TRLGMLEMVF SKADLWLADY YDQRLVAKTL WPLGKELRDL LEEDIKVVLA
     IANDSHLMAD LPWIAESIQL RNVYTDPLNV LQAELLYRSR LTEEQGKSPD PRVEQALMVT
     IAGVAAGMRN TG
//