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GGGPS_SACS2
ID   GGGPS_SACS2             Reviewed;         255 AA.
AC   Q980N1;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
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, ECO:0000269|PubMed:15356000};
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=SSO0259;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=15356000; DOI=10.1074/jbc.m409207200;
RA   Hemmi H., Shibuya K., Takahashi Y., Nakayama T., Nishino T.;
RT   "(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase from the
RT   thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and
RT   characterization of a membrane-intrinsic prenyltransferase involved in the
RT   biosynthesis of archaeal ether-linked membrane lipids.";
RL   J. Biol. Chem. 279:50197-50203(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, ECO:0000269|PubMed:15356000}.
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         ECO:0000269|PubMed:15356000};
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; AE006641; AAK40599.1; -; Genomic_DNA.
DR   PIR; H90167; H90167.
DR   RefSeq; WP_010922925.1; NC_002754.1.
DR   AlphaFoldDB; Q980N1; -.
DR   SMR; Q980N1; -.
DR   STRING; 273057.SSO0259; -.
DR   EnsemblBacteria; AAK40599; AAK40599; SSO0259.
DR   GeneID; 44129232; -.
DR   KEGG; sso:SSO0259; -.
DR   PATRIC; fig|273057.12.peg.255; -.
DR   eggNOG; arCOG01085; Archaea.
DR   HOGENOM; CLU_068610_0_0_2; -.
DR   InParanoid; Q980N1; -.
DR   OMA; ADAIFFM; -.
DR   PhylomeDB; Q980N1; -.
DR   BRENDA; 1.1.1.34; 6163.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001974; 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   1: Evidence at protein level;
KW   Cytoplasm; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase.
FT   CHAIN           1..255
FT                   /note="Geranylgeranylglyceryl phosphate synthase"
FT                   /id="PRO_0000138744"
FT   BINDING         34
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         182..188
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         213..214
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         235..236
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   255 AA;  27921 MW;  AB0B8E7A187591B6 CRC64;
     MRILKKKMKL KGKVKKYLID KLNDNEKLHF SLIDPFKINS SDELKYITKN LYNAGTDAFL
     IGGTLGVSKD KLDFVISLLD DYEIPKIIFP SNINLLSEKA DALLFMSLLN SDDIYYIIGA
     QIVAAPIIKM LQMEVIPTAY VIVGHGGTAA HIGKARVIPY DNFELATAYT LAAEYLGMSF
     VYLEAGSGAP EPIRPEMISF IKNASSIPLI VGGGIRSVEV ALKLVEAGAD IIVTGNIIES
     DVNKAIKIIR GIKNK
 
 
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