ID F4B1B3_DOKS4 Unreviewed; 257 AA.
AC F4B1B3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Geranylgeranylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE Short=GGGP synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE Short=GGGPS {ECO:0000256|HAMAP-Rule:MF_00112};
DE EC=2.5.1.41 {ECO:0000256|HAMAP-Rule:MF_00112};
DE AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE AltName: Full=Phosphoglycerol geranylgeranyltransferase {ECO:0000256|HAMAP-Rule:MF_00112};
GN OrderedLocusNames=Krodi_1368 {ECO:0000313|EMBL:AEE19351.1};
OS Dokdonia sp. (strain 4H-3-7-5) (Krokinobacter sp. (strain 4H-3-7-5)).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Dokdonia.
OX NCBI_TaxID=983548 {ECO:0000313|EMBL:AEE19351.1, ECO:0000313|Proteomes:UP000008290};
RN [1] {ECO:0000313|EMBL:AEE19351.1, ECO:0000313|Proteomes:UP000008290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4H-3-7-5 {ECO:0000313|EMBL:AEE19351.1,
RC ECO:0000313|Proteomes:UP000008290};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
RN [2] {ECO:0000313|Proteomes:UP000008290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4H-3-7-5 {ECO:0000313|Proteomes:UP000008290};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Piela B., Lochner A.,
RA Antranikian F.I., Woyke T.;
RT "Complete sequence of Krokinobacter diaphorus 4H-3-7-5.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4H-3-7-5;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Piela B., Lochner A.,
RA Antranikian F.I., Woyke T.;
RT "Complete sequence of Krokinobacter sp. 4H-3-7-5.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00000742, ECO:0000256|HAMAP-
CC Rule:MF_00112};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00112};
CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group II
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00112}.
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DR EMBL; CP002528; AEE19351.1; -; Genomic_DNA.
DR AlphaFoldDB; F4B1B3; -.
DR STRING; 983548.Krodi_1368; -.
DR KEGG; kdi:Krodi_1368; -.
DR eggNOG; COG1646; Bacteria.
DR HOGENOM; CLU_068610_0_0_10; -.
DR Proteomes; UP000008290; 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; FMN-linked oxidoreductases; 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 NCBIfam; TIGR01769; GGGP; 1.
DR NCBIfam; TIGR01768; GGGP-family; 1.
DR PANTHER; PTHR21235:SF22; GERANYLGERANYLGLYCERYL PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 1.
DR Pfam; PF01884; PcrB; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00112};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00112};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00112}.
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 193..199
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 224..225
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 246..247
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
SQ SEQUENCE 257 AA; 27722 MW; 75BC7CA93CDF4225 CRC64;
MFTVINNEEH SLYCNSYLRV VTIYSQIIHK KEEGGKLLAI LIDPDKFELD SAFAKAYLKK
IPTATTHIFI GGSTDPARKT ATVVQLLKAE TALPIILFPG NYNQVTPDAD AILFLSLLSG
DNAEFLIGQQ TKAARAVQQS ELEVIPTGYL LIDGGSITAV QRVSQTSPMS QDDKERIVDT
ALAGQYLGKK CIYLEAGSGA KKAVQPSIIK AVCDTLTIPV IVGGGIRNST QMELAHEAGA
TMVVIGTAFE ENSWNDC
//
