ID   K9XJ82_9CHRO            Unreviewed;      1025 AA.
AC   K9XJ82;
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=Glo7428_3645 {ECO:0000313|EMBL:AFZ32111.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ32111.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ32111.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ32111.1,
RC   ECO:0000313|Proteomes:UP000010476};
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., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
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; CP003646; AFZ32111.1; -; Genomic_DNA.
DR   RefSeq; WP_015189980.1; NC_019745.1.
DR   AlphaFoldDB; K9XJ82; -.
DR   STRING; 1173026.Glo7428_3645; -.
DR   KEGG; glp:Glo7428_3645; -.
DR   PATRIC; fig|1173026.3.peg.3850; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010476; 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; 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; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595}; Coiled coil {ECO:0000256|SAM:Coils};
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:AFZ32111.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010476}.
FT   COILED          205..232
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        673
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1025 AA;  117501 MW;  FD1CB921F833DE50 CRC64;
     MSSLINLSSD EALTVPSPLD LFLRQRLELV EDLWESVLKQ DCGQELVNLL GQLRDLCSPE
     GQATNDQAAE VTKLIAQLDL NEAIRAARAF ALYFQLINIV EQHYEQRLQL ARSSQHTALS
     KQVTSANGQL LDSETALNGQ PGAEMLEKSW QAIQSDNQKY STFHALFPHL KEQNVPPQQI
     QRLIDQLDVR MVFTAHPTEI VRPTIREKQR RMAKLLQRLD QLEEKQGFLN KTTSWEAAQL
     REQLTEEIRL WWRTDELHQF KPTVLDEVEY ALHYFQEVLF NEIPQLHQRF KHALSSSFPR
     LNAPKHDFCK FGSWVGADRD GNPSVTSQVT WQTACYQRQM VLEKYIQSVK HLITLLSLSL
     HWSDVLPELL ESLEQDQSQM NDVYDALALR YRQEPYRLKL SYLLKRLENT RDRNSRLSNR
     DLRQREIIET ESDFREIYRS SADFLAELRL IQRNLEATGL SCRELENLIC QVEIYDFNLA
     HLDIRQESSR HADVLEEILQ YLQIVPRSYK ELSEAERVAW LVSELQTRRP LIPAELPFSP
     QTTEVIETFR VVRSLQQEFG SSICQTYIIS MSHEVSDLLE VLLLAKEAGL YDPATGTSTL
     QVVPLFETVE DLLRAPRVMQ QLFELPLYRA LLAGGYHAHS AENSSTNTTP PPPPSTLTPN
     LQEVMLGYSD SNKDSGFLSS NWEIHKAQKA LQQIAEQFGL QLRIFHGRGG SVGRGGGPAY
     EAILAQPGHS INGRIKITEQ GEVLASKYSL PELAVYNLET ITTAVVQASL LRTGFDNIQP
     WNEIIEEIAA RSRSHYRALI YEQPDFIDFF HQVTPIDEIS QLQISSRPAR RQGGKKDLSS
     LRAIPWVFSW TQSRFLLPAW YGVGTALQEF VNEEPEEHLK LLRYFYLKWP FFKMAISKVE
     MTLAKVDLQM AKHYVQELSQ PEDLARFEKL FEQIANEFYL TRDLVLTITG HKRLLDGDPV
     LQKSVQLRNG TIVPLGFLQV SLLKRLRQCN NTTSGVIHSR YSKGELLRGA LLTINGIAAG
     MRNTG
//