GGGPS_THEAC
ID GGGPS_THEAC Reviewed; 253 AA.
AC Q9HJH3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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:12801917, ECO:0000269|PubMed:24684232};
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=Ta0995;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, COFACTOR, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=12801917; DOI=10.1093/jb/mvg083;
RA Nemoto N., Oshima T., Yamagishi A.;
RT "Purification and characterization of geranylgeranylglyceryl phosphate
RT synthase from a thermoacidophilic archaeon, Thermoplasma acidophilum.";
RL J. Biochem. 133:651-657(2003).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=24684232; DOI=10.1111/mmi.12596;
RA Peterhoff D., Beer B., Rajendran C., Kumpula E.P., Kapetaniou E.,
RA Guldan H., Wierenga R.K., Sterner R., Babinger P.;
RT "A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase
RT enzyme family identifies novel members and reveals mechanisms of substrate
RT specificity and quaternary structure organization.";
RL Mol. Microbiol. 92:885-899(2014).
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. Cannot use sn-glycerol-3-phosphate (G3P) as substrate.
CC {ECO:0000269|PubMed:12801917, ECO:0000269|PubMed:24684232}.
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:12801917, ECO:0000269|PubMed:24684232};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00112,
CC ECO:0000269|PubMed:12801917};
CC Note=Cannot use Mn(2+) or Zn(2+). {ECO:0000269|PubMed:12801917};
CC -!- ACTIVITY REGULATION: Inhibited by high concentrations of magnesium (>10
CC mM) and by EDTA in vitro. {ECO:0000269|PubMed:12801917}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.2 uM for G-1,3-P (at 55 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:12801917};
CC KM=75 nM for GGPP (at 55 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:12801917};
CC Vmax=13.5 umol/min/mg enzyme (at 55 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:12801917};
CC pH dependence:
CC Optimum pH is about 7.0. Active from pH 6 to 9.
CC {ECO:0000269|PubMed:12801917};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:12801917};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00112}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12801917,
CC ECO:0000269|PubMed:24684232}.
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; AL445066; CAC12124.1; -; Genomic_DNA.
DR PDB; 6JO3; X-ray; 2.35 A; A/B=1-253.
DR PDBsum; 6JO3; -.
DR AlphaFoldDB; Q9HJH3; -.
DR SMR; Q9HJH3; -.
DR STRING; 273075.Ta0995; -.
DR EnsemblBacteria; CAC12124; CAC12124; CAC12124.
DR KEGG; tac:Ta0995; -.
DR eggNOG; arCOG01085; Archaea.
DR HOGENOM; CLU_068610_0_0_2; -.
DR OMA; ADAIFFM; -.
DR BRENDA; 2.5.1.41; 6324.
DR SABIO-RK; Q9HJH3; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001024; 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 Reference proteome; Transferase.
FT CHAIN 1..253
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000138746"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 171..177
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 202..203
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 224..225
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:6JO3"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:6JO3"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6JO3"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:6JO3"
SQ SEQUENCE 253 AA; 27252 MW; 8B61D98112103CCF CRC64;
MMTVLEDMLR KTRNGKVHMT LIDPGAKPPQ ECARIAEEAE MAGTDFIMVG GSTDIDSRAM
DEAISAIKAK TDLKVIIFPG SSLMISPKAD AIFFMSLLNS GSLEYVVGHQ VKAAIPLSAM
KIEKIPMAYL VFDPGMTVGR VGKAHLIPRD DEKTALSYAL AAQYFGFRLV YFEAGSGSPY
HVGENVVRRV KQELDIPVIV GGGIRTPEAA KALAQAGADM IVTGTIAERS VNVYEALHPI
VESIKEVGIS KIQ
