CAPP_PROMA
ID CAPP_PROMA Reviewed; 1001 AA.
AC Q7V9U4;
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=Pro_1730;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00774.1; -; Genomic_DNA.
DR RefSeq; NP_876121.1; NC_005042.1.
DR RefSeq; WP_011125879.1; NC_005042.1.
DR AlphaFoldDB; Q7V9U4; -.
DR SMR; Q7V9U4; -.
DR STRING; 167539.Pro_1730; -.
DR EnsemblBacteria; AAQ00774; AAQ00774; Pro_1730.
DR GeneID; 54201057; -.
DR KEGG; pma:Pro_1730; -.
DR PATRIC; fig|167539.5.peg.1825; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_3; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 398146at2; -.
DR Proteomes; UP000001420; 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..1001
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166610"
FT ACT_SITE 189
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 642
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 1001 AA; 115162 MW; DAC040EF9398B80E CRC64;
MTELDNFSML EASKQVPDRK ESSQILADHM SGRLLQKRLE LVEDLWETVV RSECPLEQVE
RLLRLKQLSN SSGIVGEEQT NQINEIVELI KEMDLAEAIS AARAFSLYFQ LVNILEQRIE
EDSYLESISR GQEEKINTSI DPFAPPLASQ TAPATFSELF DRLRRLNVPP GQLEELLREM
DIRLVFTAHP TEIVRHTVRH KQRRVASLLQ QLQSDEVFSL SERDNLRLQL EEEIRLWWRT
DELHQFKPTV LDEVDYALHY FQQVLFDAMP QLRRRICSAL SQSYPDIDVP QEAFCTFGSW
VGSDRDGNPS VTPEITWRTA CYQRKLMLDR YMHSVQELRN QLSISMQWSQ VSTQLLESLE
MDRVRFPHIY EERAARYRLE PYRLKLSYTL ERLKFTQQRN QELSEAGWAT TIERTNVSNN
PDEDLHYCSI DEFRRDLELI RNSLVATNLS CEQLDTLLTQ VHIFAFSLAS LDIRQESTRH
SEAIDELTRY LNLPKSYIEM TEDEKVIWLM DELQTLRPLI PSAVQWSKST EETFAVFRML
DRLQKEFGSR ICRSYVISMS HTVSDLLEVL LLAKEYGLVD ISSESSDLLV IPLFETVEDL
QHAPSVMEEL FQSEIYLKLL PRVGEKSQPL QELMLGYSDS NKDSGFLSSN WEIHQAQIAL
QNLASSHGVA LRLFHGRGGS VGRGGGPAYQ AILAQPSGTL KGRIKITEQG EVLASKYSLP
ELALYNLETV TTAVLQNSLV TNQWDATPSW NELMTRLAVR SRQHYRALVH DNPDLVAFFQ
EVTPIEEISK LQISSRPARR KTGAKDLSSL RAIPWVFGWT QSRFLLPSWF GVGTALEEEL
KSDPDHIELL RMLNQRWPFF RMLISKVEMT LSKVDLEVAY HYMTSLGSHE NREAFNCIFE
IISNEYKLTR RLVLEITGKP KLLSADPALQ LSVDLRNRTI VPLGFLQVAL LCRLRDQNRQ
PPMSETLLTE GDIGRTYSRS ELLRGALLTI NGIAAGMRNT G