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GGGPS_PYRAE
ID   GGGPS_PYRAE             Reviewed;         239 AA.
AC   Q8ZTX5;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=PAE3045;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64634.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZTX5; -.
DR   SMR; Q8ZTX5; -.
DR   STRING; 178306.PAE3045; -.
DR   EnsemblBacteria; AAL64634; AAL64634; PAE3045.
DR   KEGG; pai:PAE3045; -.
DR   PATRIC; fig|178306.9.peg.2291; -.
DR   eggNOG; arCOG01085; Archaea.
DR   HOGENOM; CLU_068610_0_0_2; -.
DR   InParanoid; Q8ZTX5; -.
DR   OMA; ADAIFFM; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central.
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   CDD; cd02812; PcrB_like; 1.
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..239
FT                   /note="Geranylgeranylglyceryl phosphate synthase"
FT                   /id="PRO_0000138739"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         166..172
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         197..198
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         219..220
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   239 AA;  25509 MW;  801555B3C9C6FCC9 CRC64;
     MNLYEYLLEG VRHFTLIDPD KSVDYLKIAK YALEAGTDGI LIGGSLGIRE SQIAQVVKDI
     KNISNVPVVL FPGSLTQLTD LADGVLFLSV LNSLDPYFII GAQIQGAVLI AKHYPRLEVI
     STAYIIVGDG GAAGFVSMSK PIPYTRPDIA AAYALAANYI GFKAVYLEAG SGASQPVPPE
     MVRAVRRAFP RVLIVGGGIK SGEIARAIAR ERPNVIVTGT LAEESPEKLG EIVRAIKQA
 
 
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