ID   CAPP_PROM0              Reviewed;         989 AA.
AC   A3PF64;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=P9301_17661;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
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; CP000576; ABO18389.1; -; Genomic_DNA.
DR   RefSeq; WP_011863677.1; NC_009091.1.
DR   AlphaFoldDB; A3PF64; -.
DR   SMR; A3PF64; -.
DR   STRING; 167546.P9301_17661; -.
DR   EnsemblBacteria; ABO18389; ABO18389; P9301_17661.
DR   KEGG; pmg:P9301_17661; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000001430; 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; Reference proteome.
FT   CHAIN           1..989
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025570"
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;  114214 MW;  14EA9E867FE45A67 CRC64;
     MESFRQIKNN NVDLISNNDP LDKNRLLIED LWESVLREEC PDDQAERLIQ LKELSYSKQI
     DGNSSKTFKN EIVDIVNSMD LAESIAAARA FSLYFQLVNI LEQRVEEDRY IQSFTNKDVQ
     KSPDNLDPFA PALARQNAPV TFRELFYRLR KLNVPPGKLE ELLQEMDIRL VFTAHPTEIV
     RHTIRHKQTR VANLLKKIQI EQFLTKDEKI SLKTQLKEEV RLWWRTDELH QFKPSVLDEV
     DYSLHYFQQV LFNAMPQLRG RITEALTENY PDVQLPPESF CNFGSWVGSD RDGNPSVTPD
     ITWRTACYQR QLMLDRYIVA TSNLRDQLSV SMQWSQVSSS LLESLETDRV KFPEIYEARA
     TRYRSEPYRL KLSYILEKLR LTQERNNLLA DSGWKFDFEG EIDNKNIDKV ENLYYKSVNE
     FTYDLELIKN SLISTDLTCD SVNNLLTQVH IFGFSLASLD IRQESTRHSD AIQELTNYLD
     LSVQYDQMSE EEKIKWLIDE LNTKRPLIPS DVNWTKTTEE TFSVFKMVKR LQQEFGSRIC
     HSYVISMSHS ASDLLEVLLL AKEMGLLDQD SQKSKLLVVP LFETVEDLQR APEVMEKLFK
     LDFYKSLLPK VGESFKPLQE LMLGYSDSNK DSGFVSSNWE IHRAQIALQN LSSRNNILLR
     LFHGRGGSVG RGGGPAYQAI LAQPSGTLKG RIKITEQGEV LASKYSLPEL ALYNLETVTT
     AVIQNSLVNS RLDATPEWNQ LMSRLAETSR SHYRKLVHEN PDLLNFFQEV TPIEEISKLQ
     ISSRPARRKK GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV GTALSAELNS DPQQIELLRV
     LHQRWPFFRM LISKVEMTLS KVDLEVARYY VDTLGSKENK DSFDNIFEVI SKEYNLTKSL
     ILEITGKNKL LESDRDLKSS VSLRNKTIIP LGFLQVSLLR RLRDQTRQPP ISEFLIDKDE
     SRRAYSRSEL LRGALLTING IAAGMRNTG