ID   K9Z8H5_CYAAP            Unreviewed;      1009 AA.
AC   K9Z8H5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Cyan10605_2593 {ECO:0000313|EMBL:AFZ54668.1};
OS   Cyanobacterium aponinum (strain PCC 10605).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Cyanobacterium.
OX   NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ54668.1, ECO:0000313|Proteomes:UP000010480};
RN   [1] {ECO:0000313|Proteomes:UP000010480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003947; AFZ54668.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9Z8H5; -.
DR   STRING; 755178.Cyan10605_2593; -.
DR   KEGG; can:Cyan10605_2593; -.
DR   PATRIC; fig|755178.3.peg.2754; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   Proteomes; UP000010480; 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:AFZ54668.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010480}.
FT   ACT_SITE        186
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        656
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1009 AA;  116296 MW;  92A193E8D5375C51 CRC64;
     MTSVTTNYQE DLSIYSSSEL LLRHRLKLVE NLWESVLANE CGQELIDLLE RLKSACSPEG
     QTTETENFSV SKWIEELELD DAIKAARAFA LYFQLINIVE QHYEQRTQKL IRRTTTEAQV
     NAIQKPSVNN KTSSIDGDSY FHPKLNPSSG GTFHWLFPHL KTLNVPPQKI QKLLDELDIS
     LVFTAHPTEI VRHTIRKKQR RISYILEHLD RAEESYRAMG LTNSWEAENY RQCLLDEIRI
     WWRTDELHQF KPTVLDEVDY ALHYFQEVLF NTIPELFVRL KQALNNTFPK LQPPTHKFCY
     FGSWVGGDRD GNPFVTPEVT WSTACYQRNL VLEKYIDSVN QLGDILSLSL HWSNVLPELL
     DSLERDRIFM PEVYDKYYVR YRQEPYRLKL AYIEQKLENT KARNEALSNP ETRKSIKLAH
     KDDNVYPTTA DFLTDLNLIK ANLEHTGLNC KELEHLICQV EIFGFHLTPL DFRQDSSRHS
     EALNEIAEYL GVLDKPYNEL SEDEKTAWLT QELKTRRPLI PSEVTFSDNT KETIETFKVL
     RGLQLEFGLD ICHTYIISMT NYVSDVLEVL LLAKEAGLYD PILGVTTIRI VPLFETVEDL
     KRAPEVMTEL FELPLYRACL AGGYDNVDKS SSFLNLPELE PKNLQEIMLG YSDSNKDSGF
     MSSNWEIHKA QKNLARIGDK YGLNIKIFHG RGGSVGRGGG PAYAAILAQP TSTINGRIKI
     TEQGEVLASK YSLPELALYN LETISTAVIQ ASLLGSGFDD IEPWNEIMEE ISVASRKAYR
     QLIYEQPDFL DFFLSVTPIE EISKLQISSR PARRSSGKKD ISSLRAIPWV FSWTQSRFLL
     PAWYGVGTAL QQFLDQEPEE NLKLLRYFYL KWPFFKMVIS KVEMTLSKVD LQMASHYIEE
     LAKPEDKERF LKVFNQIAKE YYLSREMVLK INEQGRLLDN DPDLQRSVQL RNGTIVPLGF
     LQVSLLKRLR QYANQNKAGL IHFRYSKEEL LRGALLTING IAAGMRNTG
//