ID   DGGGP_METLZ             Reviewed;         282 AA.
AC   A2SRL0;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=Mlab_0795;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL   Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN06966.1; -; Genomic_DNA.
DR   RefSeq; WP_011833167.1; NC_008942.1.
DR   AlphaFoldDB; A2SRL0; -.
DR   SMR; A2SRL0; -.
DR   STRING; 410358.Mlab_0795; -.
DR   EnsemblBacteria; ABN06966; ABN06966; Mlab_0795.
DR   GeneID; 4794459; -.
DR   KEGG; mla:Mlab_0795; -.
DR   eggNOG; arCOG00476; Archaea.
DR   HOGENOM; CLU_073311_1_1_2; -.
DR   OMA; DYFDYEI; -.
DR   OrthoDB; 104789at2157; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000365; 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..282
FT                   /note="Digeranylgeranylglyceryl phosphate synthase"
FT                   /id="PRO_0000350706"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        127..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        154..173
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        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01286"
SQ   SEQUENCE   282 AA;  30269 MW;  43E6E451B109F1A9 CRC64;
     MSLAGYGKII RPMNAGVSGV TAGIAYFIAG GTQPLFSVLL FFIVLVICGA GNVLNDYFDL
     EIDKVNRPDR PIPSGKVSPK GAVVWAGILF AAGVAAACFT NIWCLAIALV NVVLLIIYAA
     KFKGIPFLGN LSVAYLSGSI FLFGGFLVGP ESFLVMLPLF AITFFGTLAR ELLKDAEDIE
     GDRLGGARTL PMQIGVRKTS VLAVIFVLFA VLCSFVPFLT WGVVYLVLIG VVDAFILLVT
     LRALKFETST ELTASNCTTY LKYGMFAALF VFLLMEILAV FL