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Database: UniProt/TrEMBL
Entry: Q117S5_TRIEI
LinkDB: Q117S5_TRIEI
Original site: Q117S5_TRIEI 
ID   Q117S5_TRIEI            Unreviewed;      1038 AA.
AC   Q117S5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   20-DEC-2017, entry version 88.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Tery_0836 {ECO:0000313|EMBL:ABG50249.1};
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG50249.1, ECO:0000313|Proteomes:UP000008878};
RN   [1] {ECO:0000313|EMBL:ABG50249.1, ECO:0000313|Proteomes:UP000008878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101 {ECO:0000313|EMBL:ABG50249.1,
RC   ECO:0000313|Proteomes:UP000008878};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
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DR   EMBL; CP000393; ABG50249.1; -; Genomic_DNA.
DR   RefSeq; WP_011610641.1; NC_008312.1.
DR   ProteinModelPortal; Q117S5; -.
DR   STRING; 203124.Tery_0836; -.
DR   EnsemblBacteria; ABG50249; ABG50249; Tery_0836.
DR   KEGG; ter:Tery_0836; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000008878; 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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 2.
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:SAAS00946757}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008878};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ABG50249.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ABG50249.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008878}.
FT   COILED      205    225       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    196    196       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    685    685       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1038 AA;  120002 MW;  D26216F6D9A1E37D CRC64;
     MSSLLHSKEI TLEPGFKNPK MTASDLFLHN RIKIVENLWE SVLRQECGQE LVDILQKMRS
     GHSPEGQASD FLGSEIEQLI EKLELKDAIR AARAFALYFQ LINIVEQHYE QKIQQLAYSH
     NNSLEKLISK DDIAKDHDTR SLRVESIPVW NDNRIKHEGE GTFHYLFPLL QTLNVPSQLI
     QRLINNLDIR LVFTAHPTEI VRRTIRTKQR RIAKILQQLD QVNESLSESH VDEEQVNSLV
     SSWKIESLKE QLTEEILLWW RTDELHQFKP SVLDEVETTL HYFNEVLFDA TPELHRRFKQ
     ALHSSFPYLK PPSYNFCKFG SWVGSDRDGN PFCTPAVTWQ TACYQRQIVL EKYLNAIDRL
     KELLSLSLHW SDVLPELLDS LDRDHIQMSE VYDQWAIRYR QEPYRLKLSY IKKRLENTRD
     RNARLYNGDE VQRQKKEVLS QRQKQVLSQY QETKSIYHSS ADFLAELQLI QRNLKETGLS
     CSDLENLISQ VEIFGFNLAR LDIRQESSVH EAAIQEITEY LQILPKSYIE MSEAERTEWL
     STELPTRRPL IPTELPFSEK TCEIINTFRM LRELQLEFGE EICQTYIISM SRDVSDLLEV
     LLLAQEAGLY DPATGASSIH VVPLFETVED LRSAPRVMHD LFKLSLYRAG LAGGYDKLSK
     EPINELVNEA PYLQEVMLGY SDSNKDSGFL SSNWEIHKAQ KALYKVGEEH GIALRIFHGR
     GGSVGRGGGP AYKAILAQPG KSISGRIKIT EQGEVLASKY SLPHLAMFNL ENVTTAVIQA
     SLLHTGFDEI ETWNQIMEEL AVRSRSHYRN LIYEQEDLVE FFYQVTPMPE ISQLQISSRP
     ARRKNDKKKT ISGLRAIPWV FSWTQSRFLL PAWYGVGTAL QEFVEKEPEE HLKLLQYFYV
     KWPFFTTAIS KVEMTLAKVD LQIAHYYVRE LSKPEDRERF ETLFEEITIE YHLTRNLVLQ
     ISGHQRPLDG DPDLQRSVQL RNATIIPLGM LQVALLKRLR QHDTGTPGVI NSRYSKSELL
     RGALLTLNGI AAGMRNTG
//
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