ID   CAPP_PROMM              Reviewed;        1004 AA.
AC   Q7V561;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=PMT_1713;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
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; BX548175; CAE21888.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7V561; -.
DR   SMR; Q7V561; -.
DR   STRING; 74547.PMT_1713; -.
DR   EnsemblBacteria; CAE21888; CAE21888; PMT_1713.
DR   KEGG; pmt:PMT_1713; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000001423; 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..1004
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166611"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        650
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   1004 AA;  114221 MW;  6EBBCE17759851A2 CRC64;
     MIMAKPESTS ASMQQSSAQK TDCEQPRAIG EGQQAGRLLQ NRLELVEDLW QTVLRSECPP
     DQAERLLRLK QLSEPLALEG ADENSASRAI VLLIQEMDLA EAITAARAFS LYFQLVNILE
     QRIEEDSYLA SMSSGKENNR QDKPYDPFAP PLATQTDPAT FRELFERLRR LNVPPAQLET
     LLQEMDIRLV FTAHPTEIVR HTVRHKQRKV ASLLQQFQSD PTKSTSEKES LRLQLEEEIR
     LWWRTDELHQ FKPSVLDEVD YALHYFQQVL FDAMPQLRRR LITAMAESYP DVHIPQAAFC
     TFGSWVGSDR DGNPSVTPEI TWRTACYQRQ LMLERYVNAV QKLRDQLSIS MQWSQVSTPL
     LESLEMDRLR FPEVYEERAA RYRLEPYRLK LSYTLERLKL TQHRNQQLAE AGWQTPPEGL
     NPSPNLINAG EALHYKSVAE FRSDLELIRN SLVSTDLSCE PLDTLLNQVH IFAFSLASLD
     IRQESNRHSD ALDELTRYLN LPKAYGDMAE NERVQWLMEE LQTRRPLIPS AVIWSPSTAE
     TVAVFRMLHR LQEEFGSRIC RTYVISMSHT VSDLLEVLLL AKEAGLVDPA AGHAELLVVP
     LFETVEDLQR APAVMEALLS SPVYRNLLPR VSEQVQPLQE LMLGYSDSNK DSGFLSSNWE
     IHQAQIALQD LANRQGVALR LFHGRGGSVG RGGGPAYQAI LAQPSGTVRG RIKITEQGEV
     LASKYSLPEL ALYNLETFTT AVLQNSLVTN QLDATPSWNQ LMTRLAGRSR EHYRALVHNN
     PDLVAFFQQV TPIEEISKLQ ISSRPARRKS GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV
     GTALAAEVES DADQLDLLRR LHQRWPFFRM LISKVEMTLS KVDLDLAHHY MTSLGREDYR
     EAFNRIFEII ETEYSLTRRL VLNITGQPRL LAADPALQLS VDLRNRTIVP LGFLQVALLR
     KLRDQNRQPP MNDAGDGRTY SRSELLRGAL LTINGIAAGM RNTG