DGGGP_THEON
ID DGGGP_THEON Reviewed; 276 AA.
AC B6YW76;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Digeranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01286};
DE Short=DGGGP synthase {ECO:0000255|HAMAP-Rule:MF_01286};
DE Short=DGGGPS {ECO:0000255|HAMAP-Rule:MF_01286};
DE EC=2.5.1.42 {ECO:0000255|HAMAP-Rule:MF_01286};
DE AltName: Full=(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01286};
DE AltName: Full=Geranylgeranylglycerol-phosphate geranylgeranyltransferase {ECO:0000255|HAMAP-Rule:MF_01286};
GN OrderedLocusNames=TON_1950;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
CC -!- FUNCTION: Prenyltransferase that catalyzes the transfer of the
CC geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2
CC hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This
CC reaction is the second ether-bond-formation step in the biosynthesis of
CC archaeal membrane lipids. {ECO:0000255|HAMAP-Rule:MF_01286}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + sn-3-O-
CC (geranylgeranyl)glycerol 1-phosphate = 2,3-bis-O-(geranylgeranyl)-sn-
CC glycerol 1-phosphate + diphosphate; Xref=Rhea:RHEA:18109,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57677, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:58837; EC=2.5.1.42; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01286};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01286};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01286}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01286};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01286}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. DGGGP
CC synthase subfamily. {ECO:0000255|HAMAP-Rule:MF_01286}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000855; ACJ17442.1; -; Genomic_DNA.
DR RefSeq; WP_012572913.1; NC_011529.1.
DR AlphaFoldDB; B6YW76; -.
DR SMR; B6YW76; -.
DR STRING; 523850.TON_1950; -.
DR EnsemblBacteria; ACJ17442; ACJ17442; TON_1950.
DR GeneID; 7017625; -.
DR KEGG; ton:TON_1950; -.
DR PATRIC; fig|523850.10.peg.1965; -.
DR eggNOG; arCOG00476; Archaea.
DR HOGENOM; CLU_073311_1_1_2; -.
DR OMA; DYFDYEI; -.
DR OrthoDB; 104789at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000002727; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047295; F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01286; DGGGP_synth; 1.
DR InterPro; IPR023547; DGGGP_synth.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF01040; UbiA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..276
FT /note="Digeranylgeranylglyceryl phosphate synthase"
FT /id="PRO_1000140371"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
SQ SEQUENCE 276 AA; 29958 MW; 281BDA43B4658FED CRC64;
MELKAFIEIT RPHNCILAGI VGLLGSIVAL GHFPDPKTAL LIFLVVTVGC AGGNTINDYF
DYEIDKINRP ERPLPRGAMG RKVALYYSML LFAVGLALAY MINIYAFILG VIAYVTMFIY
AWKLKPLPFV GNIVVAGLTG ATPLYGAVAV EHLGLAGYLA ICAFLVNVAR EVIKDIEDVE
GDMAKGAKTL PIIWGKKRAA YVGVLFALLT VIASFLPVKA SVGVGYYAMV PVDLLILYAA
YLILRNQDRE VAHKSQKLLK MSIFLAVMAF LIAAIV