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   27-MAR-2024, entry version 113.
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=Csal_1640;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; CP000285; ABE58993.1; -; Genomic_DNA.
DR   RefSeq; WP_011506939.1; NC_007963.1.
DR   AlphaFoldDB; Q1QX15; -.
DR   SMR; Q1QX15; -.
DR   STRING; 290398.Csal_1640; -.
DR   KEGG; csa:Csal_1640; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000000239; 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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..883
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000072622"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        547
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
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
//