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DGGGP_META3
ID   DGGGP_META3             Reviewed;         279 AA.
AC   A6UVU6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Maeo_1040;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL   Submitted (JUN-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; CP000743; ABR56618.1; -; Genomic_DNA.
DR   RefSeq; WP_011973750.1; NC_009635.1.
DR   AlphaFoldDB; A6UVU6; -.
DR   SMR; A6UVU6; -.
DR   STRING; 419665.Maeo_1040; -.
DR   EnsemblBacteria; ABR56618; ABR56618; Maeo_1040.
DR   GeneID; 5326667; -.
DR   KEGG; mae:Maeo_1040; -.
DR   eggNOG; arCOG00476; Archaea.
DR   HOGENOM; CLU_073311_1_1_2; -.
DR   OMA; DYFDYEI; -.
DR   OrthoDB; 104789at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001106; 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; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..279
FT                   /note="Digeranylgeranylglyceryl phosphate synthase"
FT                   /id="PRO_0000350701"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        131..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        157..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        201..221
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        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
SQ   SEQUENCE   279 AA;  30702 MW;  38775A707EDD0782 CRC64;
     MNLKIKYYLE LIRVKNCLTA SFGTIIGGLI ASNFNFGLIG YILLASLIVF LVCGFGNALN
     DIQDIEIDKI NKPNRPLPSN KISLKSATIF SYLLMISGII ISLFNMICFA IALINSIVLY
     LYAKKYKRNK IIGNLIVAYL TGSIFIFGGA SVGNVEITLI LFLCALFATW SREIIKDYED
     LDGDKSEGVI SLPIKYGKNS IFVAIGFLLC SILLSPLPYI LGMFGAPYLM AIMICNVLFI
     LAVLKLLKNP SKEIAGSSSK YIKIIMNLVL LSFVIGSLM
 
 
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