AC   MF_00112;
DC   Protein; auto
TR   HAMAP; MF_00112; -; 1; level=0
XX
Names: GGGP_HepGP_synthase
XX
case <OC:Archaea> or <OC:Bacteroidota>
ID   GGGPS
DE   RecName: Full=Geranylgeranylglyceryl phosphate synthase;
DE            Short=GGGP synthase;
DE            Short=GGGPS;
DE            EC=2.5.1.41;
DE   AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase;
DE   AltName: Full=Phosphoglycerol geranylgeranyltransferase;
else case <OC:Bacillales>
ID   PCRB
DE   RecName: Full=Heptaprenylglyceryl phosphate synthase;
DE            Short=HepGP synthase;
DE            EC=2.5.1.n9;
DE   AltName: Full=Glycerol-1-phosphate heptaprenyltransferase;
GN   Name=pcrB;
end case
XX
case <OC:Archaea>
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.
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   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
else case <OC:Bacteroidota>
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).
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;
else case <OC:Bacillales>
CC   -!- FUNCTION: Prenyltransferase that catalyzes in vivo the transfer of the
CC       heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon
CC       atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing
CC       heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-
CC       formation step in the biosynthesis of archaea-type G1P-based membrane
CC       lipids found in Bacillales.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate =
CC         3-heptaprenyl-sn-glycero-1-phosphate + diphosphate;
CC         Xref=Rhea:RHEA:33495, ChEBI:CHEBI:33019, ChEBI:CHEBI:57685,
CC         ChEBI:CHEBI:58206, ChEBI:CHEBI:64781; EC=2.5.1.n9;
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
case <FTGroup:1>
CC   -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I
CC       subfamily.
else case <FTGroup:2>
CC   -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group II
CC       subfamily.
else
CC   -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family.
end case
XX
DR   Pfam; PF01884; PcrB; 1; trigger=no
DR   NCBIfam; TIGR01768; GGGP-family; 1; trigger=no
DR   NCBIfam; TIGR01769; GGGP; 0-1; trigger=no
DR   NCBIfam; TIGR04146; GGGPS_Afulg; 0-1; trigger=no
DR   NCBIfam; TIGR04147; GGGPS_Halobact; 0-1; trigger=no
XX
case <OC:Archaea>
KW   Cytoplasm
end case
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Magnesium
KW   Metal-binding
KW   Phospholipid biosynthesis
KW   Phospholipid metabolism
KW   Transferase
XX
case <OC:Archaea> or <OC:Bacteroidota>
GO   GO:0047294; F:phosphoglycerol geranylgeranyltransferase activity
else case <OC:Bacillales>
GO   GO:0002094; F:polyprenyltransferase activity
end case
GO   GO:0000287; F:magnesium ion binding
GO   GO:0046474; P:glycerophospholipid biosynthetic process
case <OC:Archaea>
GO   GO:0005737; C:cytoplasm
end case
XX
FT   From: GGGPS_ARCFU (O29844)
FT   BINDING         165..170
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT   Optional; Group: 1; Condition: Y-[IVLM]-E-Y-S-G
FT   BINDING         215..216
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT   Optional; Group: 1; Condition: G-[ND]
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: [ST]
FT   BINDING         11
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT   Optional; Group: 1; Condition: K
FT   BINDING         195
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT   Optional; Group: 1; Condition: G
FT   From: GGGPS_METTH (O26652)
FT   BINDING         169..175
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT   Optional; Group: 2; Condition: [YF]-[LMFI]-[ED]-[AGS]-G-S-G
FT   BINDING         200..201
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT   Optional; Group: 2; Condition: G-G
FT   BINDING         222..223
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT   Optional; Group: 2; Condition: G-[TNS]
XX
Size: 210-304;
Related: None;
Template: O29844; B0R2Z3; Q9YEF5; O26652; P0C882; A6VHZ5; Q980N1; Q5JDY1; Q9HJH3; O34790; Q5L3C1; Q8Y6C8; Q53726; A5FJK8;
Scope:
 Bacteria; Bacillales
 Bacteria; Bacteroidota
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Bacteroidota have GGGPS activity like the archaeal enzyme, but the physiological function is
 unknown (PubMed=24684232).
 Two phylogenetic subgroups (I and II) exist within the family. They use alternative amino acid residues
 to bind G1P (PubMed=24684232).
 Many Halobacteria possess two paralogs of GGGPS.
XX
# Revision 1.33 2023/06/01
//