ID   DGGGP_METM6             Reviewed;         278 AA.
AC   A9A8Y7;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=MmarC6_0995;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX01810.1; -; Genomic_DNA.
DR   RefSeq; WP_012193758.1; NC_009975.1.
DR   AlphaFoldDB; A9A8Y7; -.
DR   SMR; A9A8Y7; -.
DR   STRING; 444158.MmarC6_0995; -.
DR   EnsemblBacteria; ABX01810; ABX01810; MmarC6_0995.
DR   GeneID; 5738898; -.
DR   KEGG; mmx:MmarC6_0995; -.
DR   eggNOG; arCOG00476; Archaea.
DR   HOGENOM; CLU_073311_1_1_2; -.
DR   OMA; DYFDYEI; -.
DR   OrthoDB; 104789at2157; -.
DR   PhylomeDB; A9A8Y7; -.
DR   UniPathway; UPA00940; -.
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..278
FT                   /note="Digeranylgeranylglyceryl phosphate synthase"
FT                   /id="PRO_0000350704"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
SQ   SEQUENCE   278 AA;  31041 MW;  E1F76FF98EC881B7 CRC64;
     MDIKAYFELI RLKNCLTASF GAFIGGLIAS YFNISMIDNL ILASIVVFLV CGFGNALNDI
     YDLKIDKINK PKRPIPSKRI SLGEARIFSY LLVVMGLIIS MFNITCFLMA VLNSIVLQQY
     ASTYKKNKIV GNLIVAYLTG SVFIFGGIAV GNIDVTIMLF LCALFAMWSR EIIKDYEDIE
     GDIKEKVISI PIKCGEKSIY IAAFLLVFAV LLSPLPYLFG FFGIYYLISV IFCDLLFLIG
     IYNLVMNPSK KEAKKASRNI KIVTNLVLIA FLIGSLFK