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Database: UniProt/TrEMBL
Entry: K9XZZ9_STAC7
LinkDB: K9XZZ9_STAC7
Original site: K9XZZ9_STAC7 
ID   K9XZZ9_STAC7            Unreviewed;      1041 AA.
AC   K9XZZ9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 34.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Sta7437_3775 {ECO:0000313|EMBL:AFZ37267.1};
OS   Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC   Bacteria; Cyanobacteria; Pleurocapsales; Dermocarpellaceae; Stanieria.
OX   NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ37267.1, ECO:0000313|Proteomes:UP000010473};
RN   [1] {ECO:0000313|Proteomes:UP000010473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E.,
RA   Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M.,
RA   Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M.,
RA   Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M.,
RA   Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-
RT   driven genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP003653; AFZ37267.1; -; Genomic_DNA.
DR   RefSeq; WP_015194928.1; NC_019748.1.
DR   EnsemblBacteria; AFZ37267; AFZ37267; Sta7437_3775.
DR   KEGG; scs:Sta7437_3775; -.
DR   PATRIC; fig|111780.3.peg.3913; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000010473; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 3.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010473};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AFZ37267.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AFZ37267.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010473}.
FT   ACT_SITE    207    207       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    680    680       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1041 AA;  119442 MW;  78DA8F86F1AC713F CRC64;
     MSSLLQSSSS EVTNISAAHL LLHGRLKLVE DLWESVLRSE CGQEMVELLK KMRGLSSPEG
     QATELPESSV LELVEKLNLN DAIQASRALA LYFQLINIVE QHYEQKGQKV ARRVTIEQLK
     QNQNGNGESK ANGNGNGNGN GTLSQVTASP IPGVNLLEDS WSQPEHHSNK AGTFHWLFPY
     LQKLNMPPRV IQRLLDQLDI RLVFTAHPTE IVRHTIRKKQ RRISRILEKL DLAEEALREI
     SLTNSWEAEE ATNQLMEEIR LWWRTDELHQ FKPKVIDEVD YALHYFQEVL FDVVPQLSVR
     LKQALRSTFP WLSPPRNNFC YFGSWVGADR DGNPFVTPQV TWETACYQRS LVLDRYIHSV
     EQLRELLSLS LHWSNVLPDL LDSLEKDRLQ IPEIYEQLAI RYRQEPYRLK LTYIEQRLKN
     TRDRNLALSR ADVTQNITEL ANNIYRSGEE FLAELQLIQK SLAETKLHCR ELDNLICQVE
     VYGFYLAQLD FRQESSRHAE AIEEIAEYLN ILPKPYSQLS ETEKTTWLIE ELKTRRPLIP
     AEMPFSETTC ETIKTLRMLR QLQQEFGVGI CQTYIISMTN HVSDVLEVML LAQEAGLYDP
     ATSQITLRIV PLFETVDDLK RAPEVMRALF ELPLYRAALA GGYHCLTNSE GKLVEAKLCR
     PTLEPTNLQE VMLGYSDSNK DSGFLSSNWE IHKAQKSLQK VASEYGVSLR LFHGRGGSVG
     RGGGPAYAAI LAQPTDTIKG RIKITEQGEV LASKYSLPEL ALYNLETITT AVIQSSLLGS
     GFDRVEPWNE IMEELATRSR SAYRSLVYEQ PDFVDFFMSV TPIEVISQLQ IGSRPSKRPP
     GNLKTDNQEQ AKKRNISSLR AIPWVFSWTQ SRFLLPAWYG VGTALQEFLE QEPEKNLNLL
     RYFYFKWPFF KMVISKVEMT LAKVDLQIAE HYVRELSKPE DLDRFERLFE QIAQEYYLTK
     QLVLTVNGQT KLLDNDPELQ RSVQLRNGTI VPLGFLQVSL IKRLRQYEES NVVHFRFSKE
     ELLRGAMLTI NGIAAGMRNT G
//
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