ID   B1XMB9_PICP2            Unreviewed;       995 AA.
AC   B1XMB9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:ACA99405.1};
GN   OrderedLocusNames=SYNPCC7002_A1414 {ECO:0000313|EMBL:ACA99405.1};
OS   Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Picosynechococcus.
OX   NCBI_TaxID=32049 {ECO:0000313|EMBL:ACA99405.1, ECO:0000313|Proteomes:UP000001688};
RN   [1] {ECO:0000313|Proteomes:UP000001688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6
RC   {ECO:0000313|Proteomes:UP000001688};
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|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:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP000951; ACA99405.1; -; Genomic_DNA.
DR   RefSeq; WP_012307028.1; NZ_JAHHPU010000016.1.
DR   AlphaFoldDB; B1XMB9; -.
DR   STRING; 32049.SYNPCC7002_A1414; -.
DR   KEGG; syp:SYNPCC7002_A1414; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   Proteomes; UP000001688; 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   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:ACA99405.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001688}.
FT   ACT_SITE        173
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        642
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   995 AA;  113976 MW;  FFC4415A1D8F0BE3 CRC64;
     MNQVMHPPSA EAELLSTSQS LLRQRLTLVE DIWQAVLQKE CGQKLVERLN HLRATRTADG
     QSLNFSPSSI SELIETLDLE DAIRAARAFA LYFQLINSVE QHYEQREQQQ FRRNLASANA
     SEANGNSVHT EIAPTQAGTF DWLFPHLKHQ NMPPQTIQRL LNQLDIRLVF TAHPTEIVRH
     TIRNKQRRIA GILRQLDQTE EGLKSLGTSD SWEIENIQQQ LTEEIRLWWR TDELHQFKPQ
     VLDEVDYALH YFEEVLFDTL PELSVRLQQA LKASFPTLKV PTTNFCNFGS WVGGDRDGNP
     SVTPDVTWKT ACYQRGLVLE RYIASVESLS DVLSLSLHWS NVLPDLLDSL EQDQNIFPDI
     YETLAIRYRQ EPYRLKLAYI KRRLENTLER NRRLANMPAW ENKVEAADDK VYICGQEFLA
     DLKLIRESLV QTEINCAALD KLICQVEIFS FVLTRLDFRQ ESTRHSDAIA EIVDYLGVLP
     KSYNDLSDAE KTTWLVQELK TRRPLIPKEM HFSERTVETI QTLQVLRRLQ QEFGIGICQT
     YIISMTNEVS DVLEVLLLAQ EAGLYDPLTG MTTIRIAPLF ETVDDLRNAP EIMQALFEIP
     LYRACLAGGY EPPADGRCDE TFGDRLVPNL QEIMLGYSDS NKDSGFLSSN WEIHKAQKNL
     QQVADPYGID LRIFHGRGGS VGRGGGPAYA AILAQPPNTI NGRIKITEQG EVLASKYSLP
     DLALYHLESV STAVIQSSLL ASGFDDIQPW NRIMEDLSQR SRAAYRALIY EEPDFLDFFM
     SVTPIPEISQ LQISSRPARR KKGNKDLSSL RAIPWVFSWT QSRFLVPAWY GVGTALQGFF
     EEDPVENLKL MRYFYSKWPF FRMVISKVEM TLSKVDLQMA SHYVHELAEK EDIPRFEKLL
     EQISQEYNLT KRLILEITEN EALLDGDRPL QRSVQLRNGT IVPLGFLQVS LLKRLRQYTR
     ETQASIVHFR YSKEELLRGA LLTINGIAAG MRNTG
//