ID   CAPP_PROM9              Reviewed;         989 AA.
AC   Q318G7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=PMT9312_1667;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RX   PubMed=16556843; DOI=10.1126/science.1122050;
RA   Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
RA   Delong E.F., Chisholm S.W.;
RT   "Genomic islands and the ecology and evolution of Prochlorococcus.";
RL   Science 311:1768-1770(2006).
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; CP000111; ABB50728.1; -; Genomic_DNA.
DR   RefSeq; WP_011377209.1; NC_007577.1.
DR   AlphaFoldDB; Q318G7; -.
DR   SMR; Q318G7; -.
DR   STRING; 74546.PMT9312_1667; -.
DR   KEGG; pmi:PMT9312_1667; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002715; 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.
FT   CHAIN           1..989
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025572"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        630
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   989 AA;  114117 MW;  D497EEFF87656186 CRC64;
     MESFQQIKNN KVDLISTNDP LDKNRLLIED LWESVLREEC PDDQAERLIQ LKELSYSKQI
     EGDSSKTFKK EIVDIVNSMD LAESIAAARA FSLYFQLVNI LEQRVEEDRY IQSFTNKNVQ
     KSPDNLDPFA PALARQNAPV TFRELFYRLR KLNVPPGKLE ELLQEMDIRL VFTAHPTEIV
     RHTIRHKQTR VANLLKKIQV EQFLTKEEKN FLKIQLKEEV RLWWRTDELH QFKPSVLDEV
     DYALHYFQQV LFNAMPQLRG RIAEALTENY PDVQLPSQSF CNFGSWVGSD RDGNPSVTPE
     ITWRTACYQR QLMLERYITA TSHLRDQLSV SMQWSQVSSS LLESLETDRV KFPAIYEARA
     TRYRSEPYRL KLSYILEKLR LTQERNNLLA DNGWKFDLEG ELNTKNIDKV ENLYYKSVNE
     FTYDLELIKN SLISTDLTCE AVNTLLTQVH IFGFSLASLD IRQESTRHSD AIQELTKYLD
     LSVQYDQMSE DEKIKWLVDE LNTKRPLIPS DVKWTNTTEE TFSVFKMVKR LQQEFGSRIC
     HAYVISMSHS ASDLLEVLLL AKEMGLLDQN SKNSNLLVVP LFETVEDLKR APEVMEKLFK
     LDFYKSLLPK VGESFKPLQE LMLGYSDSNK DSGFVSSNWE IHRAQIALQN LASRNNILLR
     LFHGRGGSVG RGGGPAYQAI LAQPSGTLKG RIKITEQGEV LASKYSLPEL ALYNLETVTT
     AVIQNSLVNN RLDATPEWNQ LMSRLAETSR SHYRKLVYEN PDLLNFFQEV TPIEEISKLQ
     ISSRPARRKK GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV GTALSSELNS DPQQIELLRV
     LHQRWPFFRM LISKVEMTLS KVDLEVAKYY VDTLGSEENK DSFDDIFEVI SKEYSLTKSL
     VLEITGKNKL LESDRDLKSS VSLRNKTIIP LGFLQVSLLR RLRDQTRQPP ISEFLIDKDE
     SRRAYSRSEL LRGALLTING IAAGMRNTG
//