ID   K9TW89_CHRTP            Unreviewed;      1049 AA.
AC   K9TW89;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=Chro_1139 {ECO:0000313|EMBL:AFY86668.1};
OS   Chroococcidiopsis thermalis (strain PCC 7203).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC   Chroococcidiopsidaceae; Chroococcidiopsis.
OX   NCBI_TaxID=251229 {ECO:0000313|EMBL:AFY86668.1, ECO:0000313|Proteomes:UP000010384};
RN   [1] {ECO:0000313|EMBL:AFY86668.1, ECO:0000313|Proteomes:UP000010384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7203 {ECO:0000313|EMBL:AFY86668.1,
RC   ECO:0000313|Proteomes:UP000010384};
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 Chroococcidiopsis thermalis PCC 7203.";
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; CP003597; AFY86668.1; -; Genomic_DNA.
DR   RefSeq; WP_015153217.1; NC_019695.1.
DR   AlphaFoldDB; K9TW89; -.
DR   STRING; 251229.Chro_1139; -.
DR   KEGG; cthe:Chro_1139; -.
DR   PATRIC; fig|251229.3.peg.1351; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   InParanoid; K9TW89; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010384; 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};
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:AFY86668.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010384}.
FT   REGION          647..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
FT   ACT_SITE        696
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1049 AA;  120404 MW;  CA8050FE00CAB59D CRC64;
     MTSLLHSHDE ALTISTSPFD LFLRQRLQTV EELWESVLKQ ECGQELVNLL AQLRDLCSSE
     GQAIDEQIAE VVQLISQLEL NEAIRAARAF ALYFQLINIV EQHYEQRQQL SISRALHQKA
     AKQLHQTPQP TSTINGHQTA DVNRDPGVEL LEKNWHATQQ QQKQGTFHTL FPHLRQMNVP
     PQHIQRLIDQ LDVRLVFTAH PTEIVRSTIR DKQRRLAKLL QQLDRIEEST GSIEGANPWE
     AEALREQLTE EIRLWWRTDE LHQFKPAVLD EVEYALHYFK EVLFEQIPLL NHRFKHALAS
     AFPRLRPPSN NFCKFGSWVG SDRDGNPSVT PQVTWQTACY QRQLVLEKYI HSVKRLTNLL
     SISLHWSDVL PDLLESLEQD RLQMNEVYEA LALRYRQEPY RLKLAYILKR LENTFERNAR
     LYNKNLRKQE IQEENVTTAV YKSGLDFLAE LRLIQRNLSE TGLNCRELDS LICQVEIYDF
     NLAHLDIRQE SSRHAHAFNE VLEYLQILPQ SYNELSEAER VKWLSEELQT RRPLIPAELP
     FSEKTNEAIE TLRVVRLLQQ EFGVQVCQSY IISMSRDLSD LLEVLLLAKE AGLYDPATGI
     GTIQVVPLFE TVEDLQRAPS IMQQLFDLTF YRALLAGGYE AIKRESGVGS RESVGQGDKE
     TRRQGNNSSH QPLATSHSPL TAHLQEVMLG YSDSNKDSGF LSSNWEIHKA QKALQQVAEQ
     HGVDLRIFHG RGGSVGRGGG PAYEAILAQP GHSINGRIKI TEQGEVLASK YSLPELALYN
     LETISTAVIQ ASLLRTGFDN IQPWNEILEE LAARSRQHYR ALIYEQPDFI DFFHQVTPID
     EISQLQISSR PARRQGGKKD LSGLRAIPWV FSWTQSRFLL PAWYGVGAAL QEFLNEEPEQ
     HLKLLRYFYM KWPFFKMAIS KVEMTLAKVD MQIAHHYVKE LSKPQDLERF ERLFEQILQE
     FHLTTDLVLS ITGHKRLLDG DPVLQQSVQL RSATIVPLGF LQVSLLKRLR QYSNPSTTGI
     IDSRHSKGEL LRGALLTING IAAGMRNTG
//