GGGPS_ARCFU
ID GGGPS_ARCFU Reviewed; 231 AA.
AC O29844;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000305};
DE Short=AfGGGPS {ECO:0000303|PubMed:21761520};
DE Short=GGGP synthase {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000303|PubMed:19558961};
DE Short=GGGPS {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000305};
DE EC=2.5.1.41 {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000269|PubMed:16377641, ECO:0000269|PubMed:19558961, ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232};
DE AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000305};
DE AltName: Full=Phosphoglycerol geranylgeranyltransferase {ECO:0000255|HAMAP-Rule:MF_00112, ECO:0000305};
GN OrderedLocusNames=AF_0403;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=19558961; DOI=10.1016/j.ymben.2009.01.008;
RA Lai D., Lluncor B., Schroeder I., Gunsalus R.P., Liao J.C.,
RA Monbouquette H.G.;
RT "Reconstruction of the archaeal isoprenoid ether lipid biosynthesis pathway
RT in Escherichia coli through digeranylgeranylglyceryl phosphate.";
RL Metab. Eng. 11:184-191(2009).
RN [3]
RP FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, SUBUNIT, AND
RP MUTAGENESIS OF TRP-99.
RX PubMed=21761520; DOI=10.1002/anie.201101832;
RA Guldan H., Matysik F.M., Bocola M., Sterner R., Babinger P.;
RT "Functional assignment of an enzyme that catalyzes the synthesis of an
RT archaea-type ether lipid in bacteria.";
RL Angew. Chem. Int. Ed. Engl. 50:8188-8191(2011).
RN [4]
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).
RN [5] {ECO:0007744|PDB:2F6U, ECO:0007744|PDB:2F6X}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH GLYCEROL
RP 1-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=16377641; DOI=10.1074/jbc.m509377200;
RA Payandeh J., Fujihashi M., Gillon W., Pai E.F.;
RT "The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase
RT reveals an ancient fold for an ancient enzyme.";
RL J. Biol. Chem. 281:6070-6078(2006).
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. To a much lesser extent, is also able to use heptaprenyl
CC pyrophosphate (HepPP; 35 carbon atoms) as the prenyl donor.
CC {ECO:0000269|PubMed:16377641, ECO:0000269|PubMed:19558961,
CC ECO:0000269|PubMed:21761520, 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:16377641, ECO:0000269|PubMed:19558961,
CC ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232};
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, ECO:0000269|PubMed:19558961}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16377641,
CC ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00112}.
CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00112,
CC ECO:0000305|PubMed:24684232}.
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DR EMBL; AE000782; AAB90827.1; -; Genomic_DNA.
DR PIR; C69300; C69300.
DR RefSeq; WP_010877910.1; NC_000917.1.
DR PDB; 2F6U; X-ray; 1.55 A; A/B=1-231.
DR PDB; 2F6X; X-ray; 2.00 A; A/B=1-231.
DR PDBsum; 2F6U; -.
DR PDBsum; 2F6X; -.
DR AlphaFoldDB; O29844; -.
DR SMR; O29844; -.
DR STRING; 224325.AF_0403; -.
DR EnsemblBacteria; AAB90827; AAB90827; AF_0403.
DR GeneID; 24793941; -.
DR KEGG; afu:AF_0403; -.
DR eggNOG; arCOG01085; Archaea.
DR HOGENOM; CLU_095211_0_0_2; -.
DR OMA; TGAHKEW; -.
DR OrthoDB; 74340at2157; -.
DR PhylomeDB; O29844; -.
DR UniPathway; UPA00940; -.
DR EvolutionaryTrace; O29844; -.
DR Proteomes; UP000002199; 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:InterPro.
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; IPR039074; GGGP/HepGP_synthase_I.
DR InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR InterPro; IPR008205; GGGP_HepGP_synthase.
DR InterPro; IPR026438; GGGP_synthase_archaea.
DR PANTHER; PTHR40029; PTHR40029; 1.
DR Pfam; PF01884; PcrB; 1.
DR TIGRFAMs; TIGR01768; GGGP-family; 1.
DR TIGRFAMs; TIGR04146; GGGPS_Afulg; 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..231
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000138728"
FT BINDING 11
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:16377641, ECO:0007744|PDB:2F6X"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 165..170
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:16377641, ECO:0007744|PDB:2F6X"
FT BINDING 195
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:16377641, ECO:0007744|PDB:2F6X"
FT BINDING 215..216
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:16377641, ECO:0007744|PDB:2F6X"
FT MUTAGEN 99
FT /note="W->A: Increased efficiency with HepPP as substrate,
FT wich becomes similar to that of B.subtilis PcrB."
FT /evidence="ECO:0000269|PubMed:21761520"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:2F6U"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2F6U"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:2F6U"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:2F6U"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:2F6U"
SQ SEQUENCE 231 AA; 26144 MW; 935D2D657550ABDD CRC64;
MRWRKWRHIT KLDPDRTNTD EIIKAVADSG TDAVMISGTQ NVTYEKARTL IEKVSQYGLP
IVVEPSDPSN VVYDVDYLFV PTVLNSADGD WITGKHAQWV RMHYENLQKF TEIIESEFIQ
IEGYIVLNPD SAVARVTKAL CNIDKELAAS YALVGEKLFN LPIIYIEYSG TYGNPELVAE
VKKVLDKARL FYGGGIDSRE KAREMLRYAD TIIVGNVIYE KGIDAFLETL P
