ID   K9TQ88_9CYAN            Unreviewed;      1014 AA.
AC   K9TQ88;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-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   ORFNames=Oscil6304_4786 {ECO:0000313|EMBL:AFY84296.1};
OS   Oscillatoria acuminata PCC 6304.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY84296.1, ECO:0000313|Proteomes:UP000010367};
RN   [1] {ECO:0000313|EMBL:AFY84296.1, ECO:0000313|Proteomes:UP000010367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY84296.1,
RC   ECO:0000313|Proteomes:UP000010367};
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 Oscillatoria acuminata PCC 6304.";
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; CP003607; AFY84296.1; -; Genomic_DNA.
DR   RefSeq; WP_015150914.1; NC_019693.1.
DR   AlphaFoldDB; K9TQ88; -.
DR   STRING; 56110.Oscil6304_4786; -.
DR   KEGG; oac:Oscil6304_4786; -.
DR   PATRIC; fig|56110.3.peg.5826; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   InParanoid; K9TQ88; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010367; 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:AFY84296.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010367}.
FT   ACT_SITE        181
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        661
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1014 AA;  116287 MW;  DE34246E7ED0927A CRC64;
     MTVRLEPSNS VMTVSSSDLF LRHRLKVVED LWESVLRTEC GQELVVLLAQ LRAMYSSEGQ
     AYNFSESSVL KLVEQLDLND AIRAARAFAL YFQLINIVEQ HYDQRDRLRG GAGPNTGVSE
     NQQFDVPKES PYFASSQTVT RRRELANFSA LFPKLKQLNV PPQQIQKIME SLDIRLVFTA
     HPTEIVRHTL RTKQRRLAQI LQELDTLEEG RQPDSQTTSC ETKDLIEALT EEIRLWWRTD
     ELHQFKPSVL DEVDYTLHYF KEVLFDAVPQ LHQRLKRSLQ ASFPYLQPPR YNFCKFGSWV
     GSDRDGNPYC TPSITWKTAC YQRQLILDKY MGSLDRLSQL LSLSLHWSDV LPELLESLEQ
     DRLQMPDIYE KLAIRYRQEP YRLKLAYICH RLENTRDRNQ RLYTESDWNR HLSDIKNAPM
     YHSGSEFLDE LRLIQRNLAA TGLSCRDLEQ LICQVEIYGF ILAHLDIRQE SSRHSTAITE
     IAEYLQILPR PYDDLSEAEK TEWLTTELKT RRPLIPGELP FSEQNSEIIS TFRMLRALQE
     EFGLEICQTY IISMSRDVSD LLEVLLLAKE AGLYDPATGM GTIQVVPLFE TVEDLKHAPT
     VIEDLFELPL YHALLSGGYQ NALPVTATET TGAPNISNLK SSHIQVPKLQ EVMLGYSDSN
     KDSGFLSSNW EIHKAQKALQ LIGDRFGVVL RIFHGRGGSV GRGGGPAYEA ILAQPGRSIN
     GRIKITEQGE VLASKYTLPE LALYNLETIA SAVVQSSLLG SGFDDIEAWN QIMEELADCS
     RQHYRALIYE QPDFIDFFHE VTPIDEISKL QISSRPARRS SGKRDLGSLR AIPWVFSWTQ
     TRFLLPAWYG VGTALNNFLE QEPEEHLKLL RYFYLKWPFF KMVISKVEMT LSKVDLEMAH
     HYVRELTQPE NRDRFEALFT QIASEFNQTR DLVLAITEHQ RLLDGDPDLQ RSVQLRNATI
     VPLGLLQVSL LKRLREHQSQ SVTGVIHSRY SKGELLRGAL LTINGIAAGM RNTG
//