ID   CAPP_SALTY              Reviewed;         883 AA.
AC   Q8ZKM0;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=STM4119;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: The enzyme has distinct binding sites for each of
CC       the allosteric effectors such as acetyl-CoA, fructose 1,6-bisphosphate,
CC       guanosine 3'-diphosphate 5'-diphosphate, long chain fatty acids, and L-
CC       aspartate. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; AE006468; AAL22958.1; -; Genomic_DNA.
DR   RefSeq; NP_462999.1; NC_003197.2.
DR   RefSeq; WP_001005548.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZKM0; -.
DR   SMR; Q8ZKM0; -.
DR   STRING; 99287.STM4119; -.
DR   PaxDb; Q8ZKM0; -.
DR   EnsemblBacteria; AAL22958; AAL22958; STM4119.
DR   GeneID; 1255646; -.
DR   KEGG; stm:STM4119; -.
DR   PATRIC; fig|99287.12.peg.4341; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   PhylomeDB; Q8ZKM0; -.
DR   BioCyc; SENT99287:STM4119-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Carbon dioxide fixation; Lyase; Magnesium;
KW   Reference proteome.
FT   CHAIN           1..883
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166622"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        546
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   883 AA;  99003 MW;  2F28CE22308A003E CRC64;
     MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILDRVETIRK LSKSSRAGNE ANRQELLTTL
     QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKNQPDLNDA
     TIKKAVESLS LELVLTAHPT EITRRTLIHK MGEINNCLKQ LDNTDIADYE RHQVMRRLRQ
     LIAQSWHTDE IRKQRPSPVD EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVDF
     VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIHVLVSEL SMVDATPELL
     ALVGEEGASE PYRYLMKKLR ARLMATQSWL EARLKGEKLP KPAGLLTQNE QLWEPLYACY
     QSLQACGMGI IANGELLDTL RRVKCFGVPL VRIDIRQEST RHTEALGEIT RYLGIGDYES
     WSEADKQAFL IRELNSKRPL LPRNWEPSND TREVLETCKV IAEAPKGSIA AYVISMAKTP
     SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNADDVMTQ LLNIDWYRGL IQGKQMVMIG
     YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK YGLPEVTVSS LSLYTSAILE ANLLPPPEPK DSWRHIMDEL
     SVISCETYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGTALQK VVEDGKQSEL EAMCRDWPFF STRLGMLEMV FSKADLWLAD
     YYDQRLVAKT LWPLGKELRD LLEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNVYTDPLN
     VLQAELLYRS RLTEEQGKSP DPRVEQALMV TIAGVAAGMR NTG