ID   CAPP_PROMA              Reviewed;        1001 AA.
AC   Q7V9U4;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 103.
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}; OrderedLocusNames=Pro_1730;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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;
CC         Evidence={ECO:0000255|HAMAP-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; AE017126; AAQ00774.1; -; Genomic_DNA.
DR   RefSeq; NP_876121.1; NC_005042.1.
DR   RefSeq; WP_011125879.1; NC_005042.1.
DR   AlphaFoldDB; Q7V9U4; -.
DR   SMR; Q7V9U4; -.
DR   STRING; 167539.Pro_1730; -.
DR   EnsemblBacteria; AAQ00774; AAQ00774; Pro_1730.
DR   KEGG; pma:Pro_1730; -.
DR   PATRIC; fig|167539.5.peg.1825; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001420; 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..1001
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166610"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        642
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   1001 AA;  115162 MW;  DAC040EF9398B80E CRC64;
     MTELDNFSML EASKQVPDRK ESSQILADHM SGRLLQKRLE LVEDLWETVV RSECPLEQVE
     RLLRLKQLSN SSGIVGEEQT NQINEIVELI KEMDLAEAIS AARAFSLYFQ LVNILEQRIE
     EDSYLESISR GQEEKINTSI DPFAPPLASQ TAPATFSELF DRLRRLNVPP GQLEELLREM
     DIRLVFTAHP TEIVRHTVRH KQRRVASLLQ QLQSDEVFSL SERDNLRLQL EEEIRLWWRT
     DELHQFKPTV LDEVDYALHY FQQVLFDAMP QLRRRICSAL SQSYPDIDVP QEAFCTFGSW
     VGSDRDGNPS VTPEITWRTA CYQRKLMLDR YMHSVQELRN QLSISMQWSQ VSTQLLESLE
     MDRVRFPHIY EERAARYRLE PYRLKLSYTL ERLKFTQQRN QELSEAGWAT TIERTNVSNN
     PDEDLHYCSI DEFRRDLELI RNSLVATNLS CEQLDTLLTQ VHIFAFSLAS LDIRQESTRH
     SEAIDELTRY LNLPKSYIEM TEDEKVIWLM DELQTLRPLI PSAVQWSKST EETFAVFRML
     DRLQKEFGSR ICRSYVISMS HTVSDLLEVL LLAKEYGLVD ISSESSDLLV IPLFETVEDL
     QHAPSVMEEL FQSEIYLKLL PRVGEKSQPL QELMLGYSDS NKDSGFLSSN WEIHQAQIAL
     QNLASSHGVA LRLFHGRGGS VGRGGGPAYQ AILAQPSGTL KGRIKITEQG EVLASKYSLP
     ELALYNLETV TTAVLQNSLV TNQWDATPSW NELMTRLAVR SRQHYRALVH DNPDLVAFFQ
     EVTPIEEISK LQISSRPARR KTGAKDLSSL RAIPWVFGWT QSRFLLPSWF GVGTALEEEL
     KSDPDHIELL RMLNQRWPFF RMLISKVEMT LSKVDLEVAY HYMTSLGSHE NREAFNCIFE
     IISNEYKLTR RLVLEITGKP KLLSADPALQ LSVDLRNRTI VPLGFLQVAL LCRLRDQNRQ
     PPMSETLLTE GDIGRTYSRS ELLRGALLTI NGIAAGMRNT G
//