ID   K9X7R0_9NOST            Unreviewed;      1034 AA.
AC   K9X7R0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
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   ORFNames=Cylst_5693 {ECO:0000313|EMBL:AFZ27692.1};
OS   Cylindrospermum stagnale PCC 7417.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ27692.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ27692.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ27692.1,
RC   ECO:0000313|Proteomes:UP000010475};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Cylindrospermum stagnale PCC 7417.";
RL   Submitted (JUN-2012) 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; CP003642; AFZ27692.1; -; Genomic_DNA.
DR   RefSeq; WP_015210926.1; NC_019757.1.
DR   AlphaFoldDB; K9X7R0; -.
DR   STRING; 56107.Cylst_5693; -.
DR   KEGG; csg:Cylst_5693; -.
DR   PATRIC; fig|56107.3.peg.6257; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010475; 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:AFZ27692.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010475}.
FT   ACT_SITE        199
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        681
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1034 AA;  118805 MW;  9F449DAD612FF978 CRC64;
     MGSLLYSLSQ AANIYPASEL FLRHRLQVVE ELWESVLRQE CGQKMVELLR QLRDLCSPEG
     QATHDQATSA VKLIEQLNIN EAIRAARAFA LYFQLINIIE QEYEQKQQLN RYSETEAEPA
     DQETLPNIIY STNQTEDDAP VNRGRGADLL TKSWMDKAQV KHKGTFAALF PHLFQLNVPP
     QQIQRLITQL DVRLVFTAHP TEIVRHTIRD KQRQVVNLLQ QLDVVENRSG STGGGYPWEA
     ADVREQLLEE IRLWWRTDEL HQFKPTVLDE VDYALHYFQE VLFDGIPQLY KRFKYALNQT
     FPWLEPPSKN FCSFGSWVGS DRDGNPSVTP EITWQTACYQ RKMVLERYIR SVKQLIELLS
     VSMHWSDVLP DLLESLELDQ STLSEVYDSL ALRYRQEPYR LKLAYVLKRL ENTRDRNLAL
     SKRETPKNQD SPMYSSGSEF LAELRLIERN LTETGLSCRE LENLICQVEI FDFNLTQLDI
     RQESSRHADA LNEILEYLQV LPQPYHDLTE AQRVTWLTGE LQTRRPLIPA ELPFSEKTND
     VIETFRIVRS LQQEFGVKIC QTYIISMCRD VSDVLEVLLL AKEARLFDPA IAVGSIQVVP
     LFETVEDLQR SRRVMRQLFS LPLYRALLAG GYESTEQKVL SPESTNQSQS PQIGETIQAA
     TSSVLRTDLQ EVMLGYSDSN KDSGFLSSNW EIHKAQKSLQ QIAEEYGVKL RIFHGRGGSV
     GRGGGPAYEA ILAQPGHSIN GRIKITEQGE VLASKYSLED LALYHMETIT TAVIQASLLR
     TGFDDIEPWN EIMEELAARS RQHYRALIYE QPDFTDFFHQ VTPIEEISQL QISSRPARRP
     SGKKDLSSLR AIPWVFSWTQ TRFLLPSWYG IGTALQEFVN AEPEQHLKLL RYFYVKWPFF
     KMVISKAEMT LAKVDMEMAR HYVQELSNPE DRSRFDKVFE QIASEFYLTR DLVLQITGHN
     RLLDGDPILQ RSVQLRNGTI VPLGFIQVSL LKRLRQSQNT TTSGVIHSRY SKGELLRGAL
     LTINGIAAGM RNTG
//