ID CAPP_SALNS Reviewed; 883 AA.
AC B4T0W7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 22-NOV-2017, entry version 57.
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=SNSL254_A4450;
OS Salmonella newport (strain SL254).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=423368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL254;
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
CC source for the tricarboxylic acid cycle. {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
CC -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC phosphoenolpyruvate + HCO(3)(-). {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_00595}.
DR EMBL; CP001113; ACF61945.1; -; Genomic_DNA.
DR RefSeq; WP_001005548.1; NZ_CCMR01000001.1.
DR ProteinModelPortal; B4T0W7; -.
DR SMR; B4T0W7; -.
DR EnsemblBacteria; ACF61945; ACF61945; SNSL254_A4450.
DR KEGG; see:SNSL254_A4450; -.
DR HOGENOM; HOG000238648; -.
DR KO; K01595; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000008824; Chromosome.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
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 Carbon dioxide fixation; Complete proteome; Lyase; Magnesium.
FT CHAIN 1 883 Phosphoenolpyruvate carboxylase.
FT /FTId=PRO_1000129842.
FT ACT_SITE 138 138 {ECO:0000255|HAMAP-Rule:MF_00595}.
FT ACT_SITE 546 546 {ECO:0000255|HAMAP-Rule:MF_00595}.
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
//
