ID   CAPP_PROMS              Reviewed;         989 AA.
AC   A2BTF4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=A9601_17821;
OS   Prochlorococcus marinus (strain AS9601).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=146891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS9601;
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; CP000551; ABM71065.1; -; Genomic_DNA.
DR   RefSeq; WP_011819187.1; NC_008816.1.
DR   AlphaFoldDB; A2BTF4; -.
DR   SMR; A2BTF4; -.
DR   STRING; 146891.A9601_17821; -.
DR   EnsemblBacteria; ABM71065; ABM71065; A9601_17821.
DR   KEGG; pmb:A9601_17821; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000002590; 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_1000025573"
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;  114241 MW;  ED9923DAA5B08E37 CRC64;
     MESFRQVKNN NVDLISNNDP LDKNRLLIED LWESVLREEC PDDQAERLIQ LKELSYSKQI
     DGDSSKTFKN EIVDIVNSMD LAESIAAARA FSLYFQLVNI LEQRVEEDRY IQSFTNKDVQ
     KSPDNLDPFA PALARQNAPV TFRELFYRLR KLNVPPGKLE ELLQEMDIRL VFTAHPTEIV
     RHTIRHKQTR VANLLKKIQI EQFLTKEEKN SLKTQLKEEV RLWWRTDELH QFKPSVLDEV
     DYALHYFQQV LFNAMPQLRG RIAEALTDNY PDVQLPSESF CNFGSWVGSD RDGNPSVTPE
     ITWRTACYQR QLMLERYIIA TSNLRDQLSV SMQWSQVSSS LLESLETDRV KFPEIYEARA
     TRYRSEPYRL KLSYILEKLR LTQERNNLLA DSGWKFDLEG ETDNKNLDKV ESLYYKSVKE
     FTYDLELIKN SLISTDLNCE SVNTLLTQVH IFGFSLASLD IRQESTRHSD AIQELTNYLD
     LSVQYDQMSE EEKIKWLIDE LNTKRPLIPS DVHWTKTTEE TFSVFKMVKR LQQEFGSRIC
     HSYVISMSHS ASDLLEVLLL AKEMGLLDQN SQKSKLLVVP LFETVEDLKR APEVMEKLFK
     LDFYRSLLPK VGESFKPLQE LMLGYSDSNK DSGFVSSNWE IHRAQIALQN LSSRNNILLR
     LFHGRGGSVG RGGGPAYQAI LAQPSGTLKG RIKITEQGEV LASKYSLPEL ALYNLETVTT
     AVIQNSLVNN RLDATPEWNQ LMSRLAETSR SHYRKLVHEN PDLLNFFQEV TPIEEISKLQ
     ISSRPARRKK GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV GTALSSELNL DPQQIELLRV
     LHQRWPFFRM LISKVEMTLS KVDLEVARYY VDTLGSKENK DSFDNIFEVI SKEYNLTKSL
     ILEITGKNKL LESDRDLKSS VSLRNKTIIP LGFLQVSLLR RLRDQTRQPP ISEFFLDKDE
     STRAYSRSEL LRGALLTING IAAGMRNTG