ID   CAPP_PROM2              Reviewed;         989 AA.
AC   A8G779;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=P9215_18471;
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215;
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; CP000825; ABV51460.1; -; Genomic_DNA.
DR   RefSeq; WP_012008463.1; NC_009840.1.
DR   AlphaFoldDB; A8G779; -.
DR   SMR; A8G779; -.
DR   STRING; 93060.P9215_18471; -.
DR   EnsemblBacteria; ABV51460; ABV51460; P9215_18471.
DR   KEGG; pmh:P9215_18471; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000002014; 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_1000061232"
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;  114465 MW;  EB0EFECE227356B7 CRC64;
     MESFRQIKNN NVDLISNNDP LDKNRLLIED LWESVLREEC PDDQAERLIQ LKELSYSKQM
     NGDSSKTFKN EIVDIVNSMD LAESIAAARA FSLYFQLVNI LEQRVEEDRY IQSFTNKDVQ
     KSHDNLDPFA PALARQNAPV TFRELFYRLR KLNVPPGKLE ELLQEMDIRL VFTAHPTEIV
     RHTIRHKQTR VANLLKKIQI EQFLTKEEKN SLKNQLKEEV RLWWRTDELH QFKPSVLDEV
     DYALHYFQQV LFNAMPQLRG RIAEALTENY PDVQLPSQSF CNFGSWVGSD RDGNPSVTPE
     ITWRTACYQR QLMLERYIIA TSNLRDQLSV SMQWSQVSSS LLESLETDRV KFPEIYEARA
     TRYRSEPYRL KLSYILEKLR LTQERNNLLS DNGWKFDLEG EIDNKNLDKV ENLYYKSVNE
     FTYDLELIKN SLISTGLTCE SVNTLLTQVH IFGFSLASLD IRQESTRHSD AIQELTNYLD
     LTMKYDQMSE EEKIKWLIDE LNTKRPLIPS DVNWTKTTEE TFSVFKMVKR LQQEFGSRIC
     HSYVISMSHS ASDLLEVLLL AKEMGLLDQN SQKSKLLVVP LFETVEDLKR APEVMERLFK
     LDFYRSLLPK VGESFKPLQE LMLGYSDSNK DSGFVSSNWE IHRAQIALQN LSSRNNILLR
     LFHGRGGSVG RGGGPAYQAI LAQPSGTLKG RIKITEQGEV LASKYSLPEL ALYNLETVTT
     AVIQNSLVNN RLDATPEWNQ LMSRLAETSR SHYRKLVHEN PDLLNFFQEV TPIEEISKLQ
     ISSRPARRKK GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV GTALSSELNS DPRQIELLRV
     LHQRWPFFRM LISKVEMTLS KVDLEVARYY VDTLGSRENK DSFDDIFEVI SKEYNLTKSL
     ILEITGKNKL LESDRDLKLS VSLRNKTIIP LGFLQVSLLR RLRDQTRQPP ISEFIIDKDE
     SRRAYSRSEL LRGALLTING IAAGMRNTG