ID   CAPP_PROMP              Reviewed;         989 AA.
AC   Q7UZT0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=PMM1575;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(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; BX548174; CAE20034.1; -; Genomic_DNA.
DR   RefSeq; WP_011133203.1; NC_005072.1.
DR   AlphaFoldDB; Q7UZT0; -.
DR   SMR; Q7UZT0; -.
DR   STRING; 59919.PMM1575; -.
DR   EnsemblBacteria; CAE20034; CAE20034; PMM1575.
DR   KEGG; pmm:PMM1575; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000001026; 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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 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_0000166612"
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;  114381 MW;  DD384EF4726C83D7 CRC64;
     MESMKQFKNN NVDLISNNDP LDKNRALIED LWESVLREEC PDDQANRLIQ LKELSYSNKV
     EEYSPKNFKT EIVDIVNSMD LAESISAARA FSLYFQLVNI LEQRVEEDRY IQSFTNQNVK
     KSHDNLDPFA PALARQNAPV TFKELFFRLR RLNVPPGKLE ELLQEMDIRL VFTAHPTEIV
     RHTIRHKQTR VANLLQKIQV EKFLTIEDIK SLKIQLKEEI RLWWRTDELH QFKPSVIDEV
     DYALHYFQQV LFDAMPQLRG RISSALTENY PDVQMPTESF CTFGSWVGSD RDGNPSVTPE
     ITWRTACYQR QLMLERYIKA TSNLRDQLSV SMQWSQVSSS LLESLETDRV KFPEIYEARA
     TRYRSEPYRL KLSYILEKLR LTHERNNLLS EGGWKLSLER ESDNKNLELV EKLHYKSVDE
     FTYDLELIKN SLNSTDLTCE AVNKLLTQVH IFGFSLASLD IRQESTRHSD AIQELTNYLE
     LPKQYDQMSE KDRIQWLNEE LNTKRPLIPS EVNWNKSTEE TFSVFKMVKR LQEEFGSRIC
     HSYVISMSHS ASDLLEVLLL AKEMGLIDQG SQKSTLLVVP LFETVEDLQR APDVMEQLFQ
     LDFYKSLLPK VGESFKPLQE LMLGYSDSNK DSGFLSSNWE IHRAQIALQN LSSRNNILLR
     LFHGRGGSVG RGGGPAYQAI LAQPSGTLKG RIKITEQGEV LASKYSLPEL ALYNLETVTT
     AVIQNSLVNN RLDATPEWND LMTRLAETSR IQYRKLVHEN PNLLTFFQEV TPIEEISKLQ
     ISSRPARRKK GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV GTALSVELKS DPEQIELLRV
     LHQRWPFFRM LISKVEMTLS KVDLEVAKYY VDTLGSKENS KSFEEIFDVI SKEYNLTKSL
     VLEITGKNKL LESDRDLRSS VNLRNKTIIP LGFLQVSLLR RLRDQTRQPP ISEFIEDRIE
     SKRAYSRSEL LRGALLTING IAAGMRNTG