GGGPS_THEVO
ID GGGPS_THEVO Reviewed; 252 AA.
AC Q97AR4;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=TV0745; ORFNames=TVG0750626;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB59887.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000011; BAB59887.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_010916992.1; NC_002689.2.
DR PDB; 6NKE; X-ray; 1.72 A; A=1-252.
DR PDBsum; 6NKE; -.
DR AlphaFoldDB; Q97AR4; -.
DR SMR; Q97AR4; -.
DR STRING; 273116.14324961; -.
DR EnsemblBacteria; BAB59887; BAB59887; BAB59887.
DR GeneID; 1441840; -.
DR KEGG; tvo:TVG0750626; -.
DR eggNOG; arCOG01085; Archaea.
DR HOGENOM; CLU_068610_0_0_2; -.
DR OMA; ADAIFFM; -.
DR OrthoDB; 94629at2157; -.
DR PhylomeDB; Q97AR4; -.
DR BRENDA; 2.5.1.41; 6326.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001017; 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 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 3D-structure; Cytoplasm; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Transferase.
FT CHAIN 1..252
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000138747"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 170..176
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 201..202
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 223..224
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6NKE"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:6NKE"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6NKE"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:6NKE"
SQ SEQUENCE 252 AA; 27473 MW; CED31DDBA93DC6E3 CRC64;
MTILKQMMRK LKNEKIHMTL IDPAAKSPDE SAKIAKEAEM AGTDFIMVGG STDIDERLMD
QTVSAIKENT NLKVILFPGS SNMISRHADA IFFMSLLNSS DREFIVGHQV KASKFLSLLG
IEKIPMAYLV FSPGMTVGRV GKANLIDSFD RETALSYSLA AQYMGFKLIY FEAGSGAPRP
VSEDTISYVK SKINIPLIVG GGIRDPETAM RIALAGADMI VTGSIAEKSN NVYSVLRNII
GKIKSIEIKN SV
