ID GGGPS_STAMF Reviewed; 245 AA.
AC A3DN81;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=Smar_0993;
OS Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=399550;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=19341479; DOI=10.1186/1471-2164-10-145;
RA Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I.,
RA Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A.,
RA Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B.,
RA Woese C., Bristow J., Kyrpides N.;
RT "The complete genome sequence of Staphylothermus marinus reveals
RT differences in sulfur metabolism among heterotrophic Crenarchaeota.";
RL BMC Genomics 10:145-145(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43588 / DSM 3639 / JCM 9404 / F1;
RX PubMed=21304655; DOI=10.4056/sigs.30527;
RA Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986
RT type strain F1.";
RL Stand. Genomic Sci. 1:183-188(2009).
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; CP000575; ABN70091.1; -; Genomic_DNA.
DR RefSeq; WP_011839282.1; NC_009033.1.
DR AlphaFoldDB; A3DN81; -.
DR SMR; A3DN81; -.
DR STRING; 399550.Smar_0993; -.
DR GeneID; 4908007; -.
DR KEGG; smr:Smar_0993; -.
DR eggNOG; arCOG01085; Archaea.
DR HOGENOM; CLU_068610_0_0_2; -.
DR OrthoDB; 7409at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000254; 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:0002094; F:polyprenyltransferase activity; IEA:UniProt.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02812; PcrB_like; 1.
DR Gene3D; 3.20.20.390; FMN-linked oxidoreductases; 1.
DR HAMAP; MF_00112; GGGP_HepGP_synthase; 1.
DR InterPro; IPR039074; GGGP/HepGP_synthase_I.
DR InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR InterPro; IPR008205; GGGP_HepGP_synthase.
DR InterPro; IPR010946; GGGP_synth.
DR NCBIfam; TIGR01769; GGGP; 1.
DR NCBIfam; TIGR01768; GGGP-family; 1.
DR PANTHER; PTHR40029; -; 1.
DR PANTHER; PTHR40029:SF2; HEPTAPRENYLGLYCERYL PHOSPHATE SYNTHASE; 1.
DR Pfam; PF01884; PcrB; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 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..245
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000350687"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 54
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 245 AA; 26533 MW; 9B0AC265C0CDA4E3 CRC64;
MGKVNKYIVE KINNGEKLHF TLIDPDRVND LGKLEETAIK MAEFGTDAFL IGGSLGVTPE
EAGETAKILK KTGLPVIIFP GNINCLTPYA DAVLFMILMN SMEQYYLMHA QIAAAPIIKK
YKLETLPTGY IVIYGETAVA HVGRTYPIPV SKPEILLSYT WAAEMIGIKY IYLEAGSGSP
KPVPPSFPAI VKKYTNLITI VGGGIRSPFI AKELASSGAD IIVTGTIVEE DPDKASKIIS
AIKKN
//
