ID   CAPP_ECOUT              Reviewed;         883 AA.
AC   Q1R3V5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPCase;
DE            Short=PEPC;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=UTI89_C4547;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + CO(2).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
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DR   EMBL; CP000243; ABE09959.1; -; Genomic_DNA.
DR   RefSeq; YP_543490.1; -.
DR   SMR; Q1R3V5; 4-883.
DR   GeneID; 3993301; -.
DR   GenomeReviews; CP000243_GR; UTI89_C4547.
DR   KEGG; eci:UTI89_C4547; -.
DR   HOGENOM; Q1R3V5; -.
DR   OMA; Q1R3V5; KITEQGE.
DR   BioCyc; ECOL364106:UTI89_C4547-MON; -.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:HAMAP.
DR   GO; GO:0015977; P:carbon utilization by fixation of carbon di...; IEA:HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00595; -; 1.
DR   InterPro; IPR001449; PEP_COase.
DR   InterPro; IPR018129; PEP_COase_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase_cat.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Complete proteome; Lyase;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    883       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_1000025558.
FT   ACT_SITE    138    138       By similarity.
FT   ACT_SITE    546    546       By similarity.
SQ   SEQUENCE   883 AA;  99090 MW;  850A8E76CF0507B7 CRC64;
     MNEQYSALRS NVSMLGKVLG ETIKDALGEH ILERVETIRK LSKSSRAGND ANRQELLTTL
     QNLSNDELLP VARAFSQFLN LANTAEQYHS ISPKGEAASN PEVIARTLRK LKNQPELSED
     TIKKAVESLS LELVLTAHPT EITRRTLIHK MVEVNACLKQ LDNKDIADYE HNQLMRRLRQ
     LIAQSWHTDE IRKLRPSPVD EAKWGFAVVE NSLWQGVPNY LRELNEQLEE NLGYKLPVEF
     VPVRFTSWMG GDRDGNPNVT ADITRHVLLL SRWKATDLFL KDIQVLVSEL SMVEATPELL
     ALVGEEGAAE PYRYLMKNLR SRLMATQAWL EARLKGEELP KPEGLLTQNE ELWEPLYACY
     QSLQACGMGI IANGDLLDTL RRVKCFGVPL VRIDIRQEST RHTEALGELT RYLGIGDYES
     WSEADKQAFL IRELNSKRPL LPRNWQPSAE TREVLDTCQV IAEAPQGSIA AYVISMAKTP
     SDVLAVHLLL KEAGIGFAMP VAPLFETLDD LNNANDVMTQ LLNIDWYRGL IQGKQMVMIG
     YSDSAKDAGV MAASWAQYQA QDALIKTCEK AGIELTLFHG RGGSIGRGGA PAHAALLSQP
     PGSLKGGLRV TEQGEMIRFK YGLPEITVSS LSLYTGAILE ANLLPPPEPK ESWRRIMDEL
     SVISCDVYRG YVRENKDFVP YFRSATPEQE LGKLPLGSRP AKRRPTGGVE SLRAIPWIFA
     WTQNRLMLPA WLGAGTALQK VVEDGKQNEL EAMCRDWPFF STRLGMLEMV FAKADLWLAE
     YYDQRLVDKA LWPLGKELRN LQEEDIKVVL AIANDSHLMA DLPWIAESIQ LRNIYTDPLN
     VLQAELLHRS RQAEKEGQEP DPRVEQALMV TIAGIAAGMR NTG
//