GGGPS_ZUNPS
ID GGGPS_ZUNPS Reviewed; 234 AA.
AC D5BCE4;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
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: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=ZPR_4469 {ECO:0000312|EMBL:ADF54770.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87;
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
RN [2]
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). {ECO:0000255|HAMAP-
CC 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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24684232}.
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; CP001650; ADF54770.1; -; Genomic_DNA.
DR RefSeq; WP_013073830.1; NC_014041.1.
DR AlphaFoldDB; D5BCE4; -.
DR SMR; D5BCE4; -.
DR STRING; 655815.ZPR_4469; -.
DR EnsemblBacteria; ADF54770; ADF54770; ZPR_4469.
DR KEGG; zpr:ZPR_4469; -.
DR eggNOG; COG1646; Bacteria.
DR HOGENOM; CLU_068610_0_0_10; -.
DR OMA; ADAIFFM; -.
DR OrthoDB; 1560657at2; -.
DR Proteomes; UP000001654; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 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 Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT CHAIN 1..234
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000436910"
FT BINDING 24
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 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 234 AA; 25221 MW; A6B48F949BDA5B2F CRC64;
MPKILDAIIK ASKINKKLLA VLIDPEKFAT ENYSYFIEKL PEAVTHIFVG GSTATTAQSE
VCVDFIKTKT NLPVILFPGD KEQITEKADG ILLLSLISGR NPEYLIEQHI KAVPKLLNAG
LEIIPTGYLL LDGGNQSAVA RVSKTKPIQQ DEIELIRNTA LAGAMLGKQL VYLEAGSGAL
IPVSEKVIAE VKRDLNIPLI VGGGIRNATQ LKKAYKAGAD LVVIGTAFEN GEFK
