DGGGP_THEGJ
ID DGGGP_THEGJ Reviewed; 276 AA.
AC C5A1J7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=TGAM_1764;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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}.
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DR EMBL; CP001398; ACS34266.1; -; Genomic_DNA.
DR RefSeq; WP_015859375.1; NC_012804.1.
DR AlphaFoldDB; C5A1J7; -.
DR SMR; C5A1J7; -.
DR STRING; 593117.TGAM_1764; -.
DR PaxDb; C5A1J7; -.
DR EnsemblBacteria; ACS34266; ACS34266; TGAM_1764.
DR GeneID; 7987483; -.
DR KEGG; tga:TGAM_1764; -.
DR PATRIC; fig|593117.10.peg.1772; -.
DR eggNOG; arCOG00476; Archaea.
DR HOGENOM; CLU_073311_1_1_2; -.
DR OMA; DYFDYEI; -.
DR OrthoDB; 104789at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001488; 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_1000214210"
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT TRANSMEM 107..127
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; 29711 MW; 24F8298249E390BE CRC64;
MELRAFVEIT RPHNCALAGL VGVLGSMVAL GSVPEGKILI LVFLVVSLGC AGGNTINDYF
DYEIDRINRP ERPLPRGAMD RRTALWYSLF LFAVGLALAL LISLKAFAFA LLAYITMFLY
AWKLKPLPFI GNIAVAALTG VTPLYGAIAV GKIGLAGTLA VCAFLVNVAR EIVKDIEDVE
GDLKKGAKTL PIILGRRKAA YVAAFFGVAT VIASFLPVKA GVGVGYYAMV PVDLIILYAV
YLILRNQDEK TAHRSQLLLK ASIFLAVFAF LIAALM
