ID   CAPP_PROM5              Reviewed;         989 AA.
AC   A2BYV8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=P9515_17621;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000552; ABM72969.1; -; Genomic_DNA.
DR   RefSeq; WP_011821055.1; NC_008817.1.
DR   AlphaFoldDB; A2BYV8; -.
DR   SMR; A2BYV8; -.
DR   STRING; 167542.P9515_17621; -.
DR   EnsemblBacteria; ABM72969; ABM72969; P9515_17621.
DR   KEGG; pmc:P9515_17621; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000001589; 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_1000025571"
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;  114458 MW;  4542E0F7585AE1B6 CRC64;
     MESMKQLKNH NVDLISNNDP LDKNRLLIED LWESVLREEC PNDQANRLMK LKELSYCNQV
     EEDISRTFKN EIVDIVNSMD LAESISAARA FSLYFQLVNI LEQRVEEDRY IQSFTNKNNQ
     KSHDNLDPFA PALARQNAPV TFRELFYRLR KLNVPPGKLE ELLQEMDIRL VFTAHPTEIV
     RHTIRHKQTR VANLLQKIQV EKFLTVEDIK SLKIQLKEEI RLWWRTDELH QFKPSVIDEV
     DYALHYFQQV LFNAMPQLRG RISSALTENY PDVQMPTESF CTFGSWVGSD RDGNPSVTPE
     ITWRTACYQR KLMLERYISA TSNLRDQLSV SMQWSQVSSS LLESLETDRV QFPEIYEARA
     TRYRSEPYRL KLSYILEKLR LTKERNNLLA EAGWKFSLER ESDNKNIELV EKLHYRSVDE
     FTYDLELIKN SLNSTDLTCE AVSKLLTQVH IFGFSLASLD IRQESTRHSD AIQELTNYLE
     LPKKYDQMPE IERIEWLKDE LNTKRPLIPA EVSWTKSTEE TFSVFKMVKR LQEEFGSRIC
     HSYVISMSHS ASDLLEVLLL AKEMGLIDQS SQKSKLLVVP LFETVEDLKR APEVMEQLFQ
     LDFYRSLLPK VGERFKPIQE LMLGYSDSNK DSGFLSSNWE IHRAQIALQN LSSKNNILLR
     LFHGRGGSVG RGGGPAYQAI LAQPSGTLKG RIKITEQGEV LASKYSLPEL ALYNLETVTT
     AVIQNSLVIN RLDATPEWND LMTRLAETSR IQYRKLVHEN PNLLTFFQEV TPIEEISKLQ
     ISSRPARRKK GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV GTALSVELKS DPEQIELLRV
     LHQRWPFFRM LISKVEMTLS KVDLEVAKYY VDTLGSKENA KSFGDIFDVI SKEYNLTKSL
     VLEITGKNKL LESDRDLRLS VNLRNKTIIP LGFLQVSLLR RLRDQTRQPP ISEFLNERNE
     SERAYSRSEL LRGALLTING IAAGMRNTG