GGGPS_METTH
ID GGGPS_METTH Reviewed; 245 AA.
AC O26652;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
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 Short=MtGGGPS {ECO:0000303|PubMed:24684232};
DE EC=2.5.1.41 {ECO:0000255|HAMAP-Rule:MF_00112, 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=MTH_552;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP SUBUNIT.
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 [3] {ECO:0007744|PDB:4MM1}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GLYCEROL
RP 1-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF
RP VAL-83 AND TRP-138.
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. {ECO:0000255|HAMAP-Rule:MF_00112, 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: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}.
CC -!- SUBUNIT: Homotetramer (PubMed:21761520). Homohexamer (PubMed:24684232).
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 II
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00112,
CC ECO:0000305|PubMed:24684232}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000666; AAB85058.1; ALT_INIT; Genomic_DNA.
DR PIR; A69173; A69173.
DR RefSeq; WP_048060841.1; NC_000916.1.
DR PDB; 4MM1; X-ray; 2.80 A; A/B/C/D/E/F=1-245.
DR PDB; 5NDY; X-ray; 1.95 A; A/B/C/D/E/F=1-245.
DR PDB; 5NEZ; X-ray; 2.39 A; A/B/C/D/E/F=1-245.
DR PDB; 5NF1; X-ray; 2.70 A; A/B/C/D/E/F=1-245.
DR PDBsum; 4MM1; -.
DR PDBsum; 5NDY; -.
DR PDBsum; 5NEZ; -.
DR PDBsum; 5NF1; -.
DR AlphaFoldDB; O26652; -.
DR SMR; O26652; -.
DR STRING; 187420.MTH_552; -.
DR EnsemblBacteria; AAB85058; AAB85058; MTH_552.
DR GeneID; 1470513; -.
DR KEGG; mth:MTH_552; -.
DR PATRIC; fig|187420.15.peg.532; -.
DR HOGENOM; CLU_068610_0_0_2; -.
DR OMA; ADAIFFM; -.
DR BioCyc; MetaCyc:MON-14508; -.
DR BRENDA; 2.5.1.41; 3256.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000005223; 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..245
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000138736"
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 169..175
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:24684232, ECO:0007744|PDB:4MM1"
FT BINDING 200..201
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:24684232, ECO:0007744|PDB:4MM1"
FT BINDING 222..223
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112,
FT ECO:0000269|PubMed:24684232, ECO:0007744|PDB:4MM1"
FT MUTAGEN 83
FT /note="V->G: Accepts HepPP as substrate."
FT /evidence="ECO:0000269|PubMed:24684232"
FT MUTAGEN 138
FT /note="W->A: Forms homodimers. Shows almost wild-type
FT activity."
FT /evidence="ECO:0000269|PubMed:24684232"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:5NDY"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5NDY"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:5NEZ"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:5NDY"
SQ SEQUENCE 245 AA; 26119 MW; 7CB5D1AFF72F1C53 CRC64;
MKVEDYFHDI LRERKIHLTL IDPEEQTPEE AVEIARAAIR GGTDGIMLGG STTDSSELDN
TARALRENID VPIILFPGNT TGVSRYADAI FFMSLLNSTN PYWIIGAQAL GAATVKKMGI
EALPMGYLVV EPGGTVGWVG DTKPVPRNKP DIAAAYAMAA EFLGMRLFYL EAGSGAPEHV
PEEMIALVKR CTDQILIVGG GIRSGEDAAR VAGAGADVVV TGTVVENSDN VEDKIREIVE
GMGSV
