ID   GGGPS_METMP             Reviewed;         256 AA.
AC   Q6M1A9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE            Short=GGGP synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE            Short=GGGPS {ECO:0000255|HAMAP-Rule:MF_00112};
DE            EC=2.5.1.41 {ECO:0000255|HAMAP-Rule:MF_00112};
DE   AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE   AltName: Full=Phosphoglycerol geranylgeranyltransferase {ECO:0000255|HAMAP-Rule:MF_00112};
GN   OrderedLocusNames=MMP0007;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- FUNCTION: Prenyltransferase that catalyzes the transfer of the
CC       geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3
CC       hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first
CC       ether-bond-formation step in the biosynthesis of archaeal membrane
CC       lipids. {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + sn-glycerol 1-
CC         phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-
CC         phosphate; Xref=Rhea:RHEA:23404, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57677, ChEBI:CHEBI:57685, ChEBI:CHEBI:58756; EC=2.5.1.41;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group II
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00112}.
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DR   EMBL; BX950229; CAF29563.1; -; Genomic_DNA.
DR   RefSeq; WP_011169951.1; NC_005791.1.
DR   AlphaFoldDB; Q6M1A9; -.
DR   SMR; Q6M1A9; -.
DR   STRING; 267377.MMP0007; -.
DR   EnsemblBacteria; CAF29563; CAF29563; MMP0007.
DR   GeneID; 41278411; -.
DR   KEGG; mmp:MMP0007; -.
DR   PATRIC; fig|267377.15.peg.7; -.
DR   eggNOG; arCOG01085; Archaea.
DR   HOGENOM; CLU_068610_0_0_2; -.
DR   OMA; ADAIFFM; -.
DR   OrthoDB; 94629at2157; -.
DR   BioCyc; MMAR267377:MMP_RS00065-MON; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047294; F:phosphoglycerol geranylgeranyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.390; -; 1.
DR   HAMAP; MF_00112; GGGP_HepGP_synthase; 1.
DR   InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR   InterPro; IPR008205; GGGP_HepGP_synthase.
DR   InterPro; IPR010946; GGGP_synth.
DR   Pfam; PF01884; PcrB; 1.
DR   TIGRFAMs; TIGR01769; GGGP; 1.
DR   TIGRFAMs; TIGR01768; GGGP-family; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase.
FT   CHAIN           1..256
FT                   /note="Geranylgeranylglyceryl phosphate synthase"
FT                   /id="PRO_0000138735"
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         172..178
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         203..204
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         225..226
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   256 AA;  27801 MW;  180EFBF1B7DEEFD4 CRC64;
     MQIKIGEIES KLNKIIEEEG AAYFVLIDPD EKNYREIANH VKDYADAIII GGSIGIINLD
     EVTKDIKEIT GLPIILFPGN VDGVTKEADA VFFMSLMNSK NTYWNMTAPT LGALTIKKYG
     LETLPMAYLG IEPISKTAVG FVGEVNEIPQ KKPEIAGLYS LSASYFGMRW AYLEAGSGAE
     YPVSNEMVGI SKKLSGINII VGGGIRTPEV AYEKVMSGAD VIVTGTLTEK DPQAVVEMKK
     AIKKAGLDKL KMLSKK