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Database: UniProt/TrEMBL
Entry: M9U3G4_SULIS
LinkDB: M9U3G4_SULIS
Original site: M9U3G4_SULIS 
ID   M9U3G4_SULIS            Unreviewed;       504 AA.
AC   M9U3G4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-SEP-2017, entry version 21.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_01904};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_01904};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_01904};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_01904};
GN   Name=ppcA {ECO:0000256|HAMAP-Rule:MF_01904};
GN   ORFNames=SiL_0068 {ECO:0000313|EMBL:AGJ61549.1};
OS   Sulfolobus islandicus LAL14/1.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=1241935 {ECO:0000313|Proteomes:UP000013006};
RN   [1] {ECO:0000313|EMBL:AGJ61549.1, ECO:0000313|Proteomes:UP000013006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LAL14/1 {ECO:0000313|EMBL:AGJ61549.1,
RC   ECO:0000313|Proteomes:UP000013006};
RX   PubMed=23594878; DOI=10.1098/rsob.130010;
RA   Jaubert C., Danioux C., Oberto J., Cortez D., Bize A., Krupovic M.,
RA   She Q., Forterre P., Prangishvili D., Sezonov G.;
RT   "Genomics and genetics of Sulfolobus islandicus LAL14/1, a model
RT   hyperthermophilic archaeon.";
RL   Open Biol. 3:130010-130010(2013).
CC   -!- FUNCTION: Catalyzes the irreversible beta-carboxylation of
CC       phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-
CC       carbon dicarboxylic acid source for the tricarboxylic acid cycle.
CC       {ECO:0000256|HAMAP-Rule:MF_01904}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-
CC       Rule:MF_01904}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01904};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01904}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01904}.
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DR   EMBL; CP003928; AGJ61549.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGJ61549; AGJ61549; SiL_0068.
DR   KEGG; sic:SiL_0068; -.
DR   KO; K01595; -.
DR   OrthoDB; POG093Z01LI; -.
DR   Proteomes; UP000013006; 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_01904; PEPcase_type2; 1.
DR   InterPro; IPR007566; PEP_COase_arc-type.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF14010; PEPcase_2; 1.
DR   PIRSF; PIRSF006677; UCP006677; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR02751; PEPCase_arch; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013006};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01904}.
SQ   SEQUENCE   504 AA;  57971 MW;  0E7D1E983813E167 CRC64;
     MSTQHPDNAK VPEWAKSEVI EGEDEVKEAF LAYSMYGVHE VMWDAEGKDV DTHVVRKLLS
     NYPDYFREHI LGKDVFLTYR LPNPKVEGAD RKVFAETMES IPITYDLAEK FYGNGITVPV
     FEVILPMTTS NLEIISVARY YEKAVANEDE LELYDGVKVK DLVGEIYPKV IEVIPLVEDR
     DSLQNIDNIV EGYYKVIKPK YMRVFLARSD PAMNYGMITA VLSVKIALSE LYKLSESLNF
     EIYPIIGVGS LPFRGHLSPE NYEKVLEEYK GVYTYTIQSA FKYDYDYDKV KSAISSINNS
     RIGPAKILEK YEEDVLRKIT ILYTERYQPI IESLANAIND VSMLLPRRRA RKLHIGLFGY
     SRSAGKVSLP RAISFVGSLY SIGIPPELIG ISSLSNLDEK EWDIFKQNYV NFKHDLQTAA
     RFFNWESFEL IKDIWKISED TIAKIKEDID YAESVIGIKL GDIDYDSRKH ILMSSLFLLS
     FKEKILQESK KYLYEMALIR RSLG
//
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