ID   K9SCF4_9CYAN            Unreviewed;      1003 AA.
AC   K9SCF4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=GEI7407_3411 {ECO:0000313|EMBL:AFY67878.1};
OS   Geitlerinema sp. PCC 7407.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC   Geitlerinemataceae; Geitlerinema.
OX   NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY67878.1, ECO:0000313|Proteomes:UP000010383};
RN   [1] {ECO:0000313|EMBL:AFY67878.1, ECO:0000313|Proteomes:UP000010383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY67878.1,
RC   ECO:0000313|Proteomes:UP000010383};
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 genome of Geitlerinema sp. PCC 7407.";
RL   Submitted (MAY-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; CP003591; AFY67878.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9SCF4; -.
DR   STRING; 1173025.GEI7407_3411; -.
DR   KEGG; gei:GEI7407_3411; -.
DR   PATRIC; fig|1173025.3.peg.3798; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   Proteomes; UP000010383; 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:AFY67878.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010383}.
FT   ACT_SITE        191
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        651
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1003 AA;  115929 MW;  A28AD2A357FBBA99 CRC64;
     MLASENAAVP LSSNLFLRHR LKVVEDLWEF VLQQECGQEL VDLLQQLRDL CSPEGQAPNF
     QETEVLKLVE KLDLNDAIRA ARAFALYFQL INIVEQHYEQ RGQQQQYRAA YDSPQAEASD
     RKPPVIEETA DDLGHLKADF LAKSLEESTA ARRELTTFHG LFPKLRKLNV PPQHIQNLLD
     QLDVRLVFTA HPTEIVRHTI RDKQRRIAHI LRQLDQAEES NQALGVTSSW EVESLRDQLT
     EEIRLWWRTD ELHQFKPTVL DEVDYTLHYF QEVLFDVIPQ LYHRCKRAVE TAFPSLNPPS
     YDFCKFGSWV GSDRDGNPSV TPKITWQTAC YQRNLVLEKY IQSVRRLINL LSLSLHWSDV
     LPDLLESLEQ DQVQMPEVYD QLAIRYRQEP YRLKLSYILK RLENTRDRNW RLYNFDEKDQ
     AVREELNPAT FYRSGEEFQN ELRLIHHNLQ ETGLSCRDLE DLLCQVEIYG FNLAYLDIRQ
     ESSRHSDTIN EIVGYLQILP QPYNDLSEAE RTAWLASELQ TRRPLIPAEL PFSEKTCEII
     ETFRMVRRLQ QEFGPAICQT YVISMSHEVS DLLEVLLLAK EAGLYDPATG SGTLQVVPLF
     ETVEDLQRAP SVMRELFELS LYRSYLAGGY QAQEGSPSPQ EVMLGYSDSN KDSGFLSSNW
     EIHKAQKALQ QLAEEFSVRL RIFHGRGGSV GRGGGPAYEA ILAQPGHSIN GRIKITEQGE
     VLASKYSLPE LALYNLETVA TAVIQASLLR NGFDDIQPWN EIMEELAQRS RRHYRALIHE
     QPDFLDFFHQ VTPIEEISQL QISSRPSRRG GKRDFSSLRA IPWVFSWTQS RFLLPSWYGV
     GTALRDFLQE EPEENLKLLR YFYYKWPFFR MAVSKVEMTL SKVDLQIANH YVQELSQSED
     IERFEKVFSQ ISSEYHLTRE MVLTITGNQR LLDGDPDLQR SVQLRNGTIV PLGFLQVSLL
     KRLRQHKAQS ASGFIRSRYS RGELLRGALL TINGIAAGMR NTG
//