ID   Q31KY7_SYNE7            Unreviewed;      1017 AA.
AC   Q31KY7;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
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   OrderedLocusNames=Synpcc7942_2252 {ECO:0000313|EMBL:ABB58282.1};
OS   Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)
OS   (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1140 {ECO:0000313|EMBL:ABB58282.1, ECO:0000313|Proteomes:UP000889800};
RN   [1] {ECO:0000313|Proteomes:UP000889800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33912 / PCC 7942 / FACHB-805
RC   {ECO:0000313|Proteomes:UP000889800};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB58282.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q31KY7; -.
DR   SMR; Q31KY7; -.
DR   STRING; 1140.Synpcc7942_2252; -.
DR   PaxDb; 1140-Synpcc7942_2252; -.
DR   KEGG; syf:Synpcc7942_2252; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   BioCyc; SYNEL:SYNPCC7942_2252-MONOMER; -.
DR   Proteomes; UP000889800; 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   Reference proteome {ECO:0000313|Proteomes:UP000889800}.
FT   REGION          425..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        663
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1017 AA;  117292 MW;  856E209D3FA5D469 CRC64;
     MNYCQNARTA MSAALQSSDD AFRTVSSPLA TDLDLSSPLE FFLRHRLTVV EELWEVVLRQ
     ECGQELVDIL TQLRDLTSPE GQAPEVGGEA LVQVIETLEL SDAIRAARAF ALYFQLINIV
     EQHYEQTQYQ LAYERSRLEP LPGPDESPEG LHTIEIPQHQ LDPFAAVIPL NQDPATFQTL
     FPRLRQLNVP PQMIQELTDR LDIRLVFTAH PTEIVRHTIR DKQRRIAYLL RQLDELETGK
     NRGFRELEAQ NIRQQLTEEI RLWWRTDELH QFKPTVLDEV DYALHYFQEV LFEAIPLLYQ
     RFRLALQGTF PDLQPPRYNF CQFGSWVGSD RDGNPSVTSA VTWQTACYQR SLVLDRYITA
     VEHLRNVLSL SMHWSEVLPE LLSSLEQESM LFPETYEQLA VRYRQEPYRL KLSYILERLH
     NTRDRNTRLQ QQQEKDPTTP LPEYRDGTLY QAGTAFLEDL KLIQHNLKQT GLSCYELEKL
     ICQVEIFGFN LVHLDIRQES SRHSDAINEI CEYLQILPQP YNELSEAERT AWLVQELKTR
     RPLVPARMPF SESTREIIET LRMVKQLQEE FGEAACQTYI ISMSRELSDL LEVLLLAKEV
     GLYDPVTGKS SLQVIPLFET VEDLQNAPRV MTALFELPFY TQLNPTQSEP LQEVMLGYSD
     SNKDSGFLSS NWEIHKAQKA LGTVARDHRV KLRIFHGRGG SVGRGGGPAY EAILAQPGRT
     TDGRIKITEQ GEVLASKYAL PELALYNLET ITTAVIQSSL LGSGFDDIEP WNQIMEELAA
     RSRRHYRALV YEQPDLVDFF NQVTPIEEIS KLQISSRPAR RKTGKRDLGS LRAIPWVFSW
     TQSRFLLPSW YGVGTALQEF LQERPEQNLN LLRYFYEKWP FFRMVISKVE MTLAKVDLQI
     AHHYVHELAN PEDQERFERV FSQIAAEFQL TCHLVLTITN HGRLLDGDPE LQRSVQLRNG
     TIVPLGFLQV ALLKRLRQYR QQTETTGLMR SRYSKGELLR GALLTINGIA AGMRNTG
//