ID   B0JPY0_MICAN            Unreviewed;      1018 AA.
AC   B0JPY0;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
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:BAG03704.1};
GN   OrderedLocusNames=MAE_38820 {ECO:0000313|EMBL:BAG03704.1};
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447 {ECO:0000313|EMBL:BAG03704.1, ECO:0000313|Proteomes:UP000001510};
RN   [1] {ECO:0000313|EMBL:BAG03704.1, ECO:0000313|Proteomes:UP000001510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 {ECO:0000313|EMBL:BAG03704.1,
RC   ECO:0000313|Proteomes:UP000001510};
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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; AP009552; BAG03704.1; -; Genomic_DNA.
DR   RefSeq; WP_012266643.1; NC_010296.1.
DR   AlphaFoldDB; B0JPY0; -.
DR   STRING; 449447.MAE_38820; -.
DR   PaxDb; 449447-MAE_38820; -.
DR   EnsemblBacteria; BAG03704; BAG03704; MAE_38820.
DR   KEGG; mar:MAE_38820; -.
DR   PATRIC; fig|449447.4.peg.3516; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   BioCyc; MAER449447:MAE_RS16775-MONOMER; -.
DR   Proteomes; UP000001510; 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:BAG03704.1}.
FT   ACT_SITE        193
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        665
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1018 AA;  117011 MW;  0FCBEA99DAA3F925 CRC64;
     MSVLVSSTET EQDIFSTSNL FLQQRLKLIE DLWKEVLVSE CGQELVDLLE LLRHLCSEEG
     QVTDDSPEAT IAKMIEDLEL GEAIKVTRAF ALYFQLINII EQHYEQRDQQ LLRRTVIGEE
     NESPKADPTQ KSLLATIVGA DWLEKTLNES DHSGPKSGLF HWLFPYLKQV NVPPQEIQRL
     LDQLDIRLVF TAHPTEIVRH TIRIKQRRIS GILEKLDQAE EIFRSMGLTN SREAQTVTKQ
     LKEEIRFWWR TDELHQFKPT VVDEVDYALH YFDEVLFDSL PQLTLRLQQS LQSSFPRLQA
     PKNNFCRFGS WVGGDRDGNP SVTPEVTWKT CCYQRNLVIK KYLDAIRDLT SILSASLHWC
     HVLPELLDSL DRDKQQMPEI YSQLAIRYRQ EPYRLKLAFI QKRLENTRDR NDRLNDPEER
     QLLTKLNETN IYRSGSEFLA ELQLLKRSLF QTGLSCQELD RLIAQVEIFG FVLTQLDFRQ
     ESTRHAECIE EIAQYLGVLP KPYGKLTESE KIAWLVAELK TRRPLIPREM PFSERTCETI
     ETLRVLRSLQ GEFGLEICQT YIISMTNEAS DVLEVLLLAQ EAGLYDPATS RSSLRIVPLF
     ETVDDLKHAP GIMQTLFELP LYRATLAGGY DHLAALNGED VTPEPAILEP SNLQEIMVGY
     SDSNKDSGFL SSNWEIHKAQ KALQKTAKQY GVNLRLFHGR GGSVGRGGGP AYAAILAQPR
     GTINGRIKIT EQGEVLASKY SLPELALYNL ETAVTAVIQA SLLGSGFDDL EPWNRIMEEL
     ATRSRQTYRS LIYEEPDFLD FFLSVTPIPE ISLLQISSRP ARRKSGQQDL STLRAIPWVF
     SWTQTRFLLP AWYGLGTALQ MFLDDSPSRN LELLRHFYHK WPFFQMVISK ADMTLSKVDL
     QMAYHYVSEL SKQEDRERFQ RLFERIKEEY NRTSEIVLQI TGEKHLLDND PNLQRSVQLR
     NGSIVPLGFL QVSLLKRLRQ YNSQAQSGVI HFRYSKEELL RGALMTINGI AAGMRNTG
//