ID   K9YQH2_CYASC            Unreviewed;      1020 AA.
AC   K9YQH2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=Cyast_2422 {ECO:0000313|EMBL:AFZ48368.1};
OS   Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Cyanobacterium.
OX   NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ48368.1, ECO:0000313|Proteomes:UP000010483};
RN   [1] {ECO:0000313|Proteomes:UP000010483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
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; CP003940; AFZ48368.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9YQH2; -.
DR   STRING; 292563.Cyast_2422; -.
DR   KEGG; csn:Cyast_2422; -.
DR   PATRIC; fig|292563.3.peg.2527; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   Proteomes; UP000010483; 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:UP000010483}.
FT   ACT_SITE        197
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        667
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1020 AA;  117301 MW;  1F929481884F1AE2 CRC64;
     MTFTKTSHKE ELSIYSNSEL LLRHRLKLVE NLWELVLRNE CGQHLVDLLE QLKSACSPEG
     QTSETPKQSV SKWIEQLELD DAIKAVRALA LYFQLINIVE QHYEQRNQKI IRSTTTEDQV
     NGSQVDSIID KLIEGETQKV VVDSGDKDYS YFEQKPNPAS GGTFHWLFPH LQQLNMPPQK
     IQDLLDELDI RLVFTAHPTE IVRHTIRKKQ RRISQILERL DVAEESCRAM GLTNSYEAEH
     FRNRLMDEIQ LWWRTDELHQ FKPTVLDEVD YALHYFQEVL FDSLPHLSKR LQQALHNTFP
     KLKPPSHKFC YFGSWVGGDR DGNPFVTPEV TWSTACYQRN LVIEKYLESV AKLNDVLSLS
     LHWCNVLPEL LDSLEKDRIK MPEVYDKLYV RYRQEPYRLK LAFIEKKLEN TKARNEALSN
     PETRKSIKLA TKDDNLYPSA SDFLEDLNLL KLNLEQTGLN CQELDHLIFQ VDIYGFHLAE
     LDFRQDSSRH SDALNEIAEY LGVLDKPYNE LSEEEKTAWL VRELKTRRPL VPNPIPFSET
     TAETIETFKV LRALQVEFGI EICNTYIISM TNYVSDVLEV LLLAKEAGLY DPVIGASSIR
     IVPLFETVED LKRSHSVMKE LFDLPLYRAC LAGGYDSSGD SQSNVTMPKL TPHNLQEIML
     GYSDSNKDSG FMSSNWEIHK AQKVLAKLGN AYGVKIKIFH GRGGSVGRGG GPAYAAILAQ
     PTSTINGRIK ITEQGEVLAS KYSLPELALY NLETISTAVI QASLLGSGFD DIEPWNEIME
     EIAIASRKAY RSLIYEEPDF IDFFLSVTPI EEISKLQISS RPARRKKGKK DISSLRAIPW
     VFSWTQSRFL LPAWYGVGTA LQEFLAKEPE ENLKLLRYFY LKWPFFKMVI SKVEMTLSKV
     DLQMASHYVE ELAEDEDKER FHKLFSQIAK EYYLSREMVL KINQQERLLD TDPELQRSVQ
     LRNGSIVPLG FLQVSLLKRL REYANQDKAG LIHFRYSKDE LLRGALLTIN GIAAGMRNTG
//