(data stored in ACNUC10043 zone)

SWISSPROT: D1YV58_METPS

ID   D1YV58_METPS            Unreviewed;       226 AA.
AC   D1YV58;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 52.
DE   RecName: Full=Geranylgeranylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE            Short=GGGP synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE            Short=GGGPS {ECO:0000256|HAMAP-Rule:MF_00112};
DE            EC=2.5.1.41 {ECO:0000256|HAMAP-Rule:MF_00112};
DE   AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE   AltName: Full=Phosphoglycerol geranylgeranyltransferase {ECO:0000256|HAMAP-Rule:MF_00112};
GN   OrderedLocusNames=MCP_0258 {ECO:0000313|EMBL:BAI60330.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60330.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Prenyltransferase that catalyzes the transfer of the
CC       geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3
CC       hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first
CC       ether-bond-formation step in the biosynthesis of archaeal membrane
CC       lipids. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-geranylgeranyl diphosphate + sn-glycerol 1-phosphate
CC         = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate;
CC         Xref=Rhea:RHEA:23404, ChEBI:CHEBI:33019, ChEBI:CHEBI:57677,
CC         ChEBI:CHEBI:57685, ChEBI:CHEBI:58756; EC=2.5.1.41;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00112};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00112};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_00112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00112}.
CC   -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00112}.
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DR   EMBL; AP011532; BAI60330.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0258; -.
DR   EnsemblBacteria; BAI60330; BAI60330; MCP_0258.
DR   KEGG; mpd:MCP_0258; -.
DR   eggNOG; arCOG01085; Archaea.
DR   eggNOG; COG1646; LUCA.
DR   HOGENOM; HOG000015607; -.
DR   KO; K17104; -.
DR   OMA; MAKYANT; -.
DR   BioCyc; MPAL304371:GI7G-268-MONOMER; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047294; F:phosphoglycerol geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0002094; F:polyprenyltransferase activity; IEA:InterPro.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02812; PcrB_like; 1.
DR   Gene3D; 3.20.20.390; -; 1.
DR   HAMAP; MF_00112; GGGP_HepGP_synthase; 1.
DR   InterPro; IPR039074; GGGP/HepGP_synthase_I.
DR   InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR   InterPro; IPR008205; GGGP_HepGP_synthase.
DR   InterPro; IPR026438; GGGP_synthase_archaea.
DR   PANTHER; PTHR40029; PTHR40029; 1.
DR   Pfam; PF01884; PcrB; 1.
DR   TIGRFAMs; TIGR01768; GGGP-family; 1.
DR   TIGRFAMs; TIGR04146; GGGPS_Afulg; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YV58.
DR   SWISS-2DPAGE; D1YV58.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00112};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00112};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00112};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00112};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00112};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00112};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00112};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00112}.
FT   REGION          158..163
FT                   /note="Glycerol-1-phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   REGION          208..209
FT                   /note="Glycerol-1-phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   METAL           14
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   METAL           40
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         12
FT                   /note="Glycerol-1-phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         188
FT                   /note="Glycerol-1-phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   226 AA;  25175 MW;  66C3DD81CF500AE1 CRC64;
     MIDWKKWRHV TKLDPDKPIT PKAVAEIVDS GTDAIMVSGT QNITKENVAR LVDMLAQYNI
     PKVLEPAGTP GMRSDLDFAF IPSVFNTKNP KWLVGAHKDF VRDFQIDYWD KIIPEAYIVL
     NPFSAVALVT RAQTGLGPKD AAAYAEVADR FFNFPIVYVE YSGVFGNPEL VKAVKEKLHN
     SVLYYGGGID CREKAEQMAK YANTIVVGNA VYKKGGVEML KETIVK
//

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