ID   K9VUS5_9CYAN            Unreviewed;      1044 AA.
AC   K9VUS5;
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=Cri9333_0948 {ECO:0000313|EMBL:AFZ11863.1};
OS   Crinalium epipsammum PCC 9333.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC   Crinalium.
OX   NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ11863.1, ECO:0000313|Proteomes:UP000010472};
RN   [1] {ECO:0000313|EMBL:AFZ11863.1, ECO:0000313|Proteomes:UP000010472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ11863.1,
RC   ECO:0000313|Proteomes:UP000010472};
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 Crinalium epipsammum PCC 9333.";
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; CP003620; AFZ11863.1; -; Genomic_DNA.
DR   RefSeq; WP_015201985.1; NC_019753.1.
DR   AlphaFoldDB; K9VUS5; -.
DR   STRING; 1173022.Cri9333_0948; -.
DR   KEGG; cep:Cri9333_0948; -.
DR   PATRIC; fig|1173022.3.peg.1029; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010472; 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:AFZ11863.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010472}.
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        692
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1044 AA;  119725 MW;  E15D73791FC887DA CRC64;
     MSSLLHTHDQ ELTVTSASDL FLRHRLKVVE DLWESVLRQE CGQELVDLLK QLRSLCSPEG
     QTPELPETSV PKLIEKLDLN SAIRASRAFA LYFQLINIVE QHYEQREQQL SLRANHHLPA
     TNKAVLPPTS ATISPAPNIG DLEELQPNSP NNNLGADLLE KTLQDNGVPP RDQGTFHWLF
     PYLRSMNVPP QHIQRLLNNL EIRLVFTAHP TEIVRHTIRG KQRRIAHLLQ QLDQAEEGMN
     SLGLNYSLEA ETFEEQLTEE IRLWWRTDEL HQFKPTVIDE VDYTLHYFEQ VLFEAIPQLS
     RRLKQALKDS FPWLTPPNHK FCQFGSWVGS DRDGNPSVTP EVTWQTACYQ RGVVLEKYIQ
     SLRQLTDLLS LSLHWSDVLP ELLESLEQDR GRMPEVYDRL AIRYRQEPYR LKLAYILARL
     ENSRDRNSQL AYGDHQKWQN SDTYAKSFYR TGEEFLAELQ LIQHNLKETG LSCRDLENLI
     CQVEIYGFNL AYLDIRQESS RHSDTINEIV EYLQVLHKPY NELTETERSL WLATELQTKR
     PLIPSELPFS QKTSETVESF RMLRQLHQEF GSPICQTYVI SMSHDVSDLL EVLLLAKEAG
     LYDPRTGITS LQVVPLFETV EDLKRAPAVM EALFELPFYR ALLAGGYEVA QANSEQTQPQ
     IINSQSQTPI KSSSAITPHL QEVMLGYSDS NKDSGFLSSN WEIHKAQKAL QKIAEKYNLN
     LRIFHGRGGS VGRGGGPAYE AILAQPGHTI KGRIKITEQG EVLASKYSLP ELALYNLETV
     TTAVIKASLL GTSFDDIQPW NEIMEELSVR SRAHYRSLIY EQTDLVDFFH QVTPIEEISQ
     LQISSRPARR GGKKDLASLR AIPWVFSWTQ SRFLLPSWYG VGTALQEFLN EEPDENLNLL
     RYFYFKWPFF KMAISRVEMT LAKVDLQMAH HYVRELSKPE DIERFEALFD QIAKEYNLVC
     ELVLTITGHK RLLDGDPELQ RSVQLRNGSI VPLGFLQVSL LKRLREHGKL TTTGVVHSRY
     SKGELLRGAL LTINGIAAGM RNTG
//