ID   CAPP_CHRSD              Reviewed;         883 AA.
AC   Q1QX15;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPCase;
DE            Short=PEPC;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=Csal_1640;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000285; ABE58993.1; -; Genomic_DNA.
DR   RefSeq; YP_573692.1; -.
DR   GeneID; 4025908; -.
DR   GenomeReviews; CP000285_GR; Csal_1640.
DR   KEGG; csa:Csal_1640; -.
DR   NMPDR; fig|290398.4.peg.1635; -.
DR   HOGENOM; Q1QX15; -.
DR   OMA; Q1QX15; KITEQGE.
DR   BioCyc; CSAL290398:CSAL_1640-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_1000072622.
FT   ACT_SITE    141    141       By similarity.
FT   ACT_SITE    547    547       By similarity.
SQ   SEQUENCE   883 AA;  99159 MW;  BDF0D9B6E7C765DE CRC64;
     MSHDLHESLR DNVRILGDSL GRTIADDLGD GFVDKIETIR GLAKRGRQDD SESRRELIEY
     LRALPEKDLL PVTRAFNQFL NFSNIAEQHY RARFRRVEDY KPGTQPDLGE LLERIRGAGH
     APRKLVETLA AMRVELVLTA HPTEVIRRTL IRKYDAIDEC LTTMEGATER EEIAARARGR
     LEELISQAWH TDEIRHERPT PVDEAKWGFA VIENSLWQAV PDFHRELDDL LLASAGERLP
     LDAAPLRFAS WMGGDRDGNP NVTARVTEEV LLLGRWMAAD LYARDLLRLK SELSMWKANG
     ALRAEVGSDP EPYRALLKRL LARVEATRDW AKARLDGRPF DSNVAIIETR DQLYAPLLSC
     YRSLCDVGLD TIANGALLDT LRRVAVFGVS LTKLDIRQEA GRHAQVFDEL SDCLGLGHYR
     DWDEAQRQDF LLEELESPRP LIPRRWDCSA ETREVIDTFR VIAREHREAL GTYVISMAGQ
     PSDVLAVALL MKEVGGDLQL PIAPLFETLD DLNRAGDVIE RLLSLPGYRR MAGDGQEVMI
     GYSDSAKDAG QLAAAWAQYR AQEQLVGICR QHDVALTLFH GRGGTVGRGG GPAHAAILSQ
     PPGSVNGSLR VTEQGEMIRF KFGQPDIALR SMEIYACAVL EATLLPPPDP EPVWREEMDR
     LSDIAHRAYV GVVREDPDFV PYFRSVTPES ALGRLPLGSR PAKRRQEGGV ESLRAIPWIF
     AWTQTRLMLP AWLGSGEAFA TRLDEPGGRE RLRDMRARWP FFGTYLDMLE MLLAKADPDI
     AAYYERRLVD EPALQALGKS LRERLSRLET VLLDILDQDT LLEHTPLIRQ AIEVRNPYID
     PLHGLQAELL QRNRDADGAI SPELSRALMV TMAGIAAGLR NTG
//