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Entry: A0A1G7CVS2_9FLAO
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ID   A0A1G7CVS2_9FLAO        Unreviewed;       232 AA.
AC   A0A1G7CVS2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   ORFNames=SAMN05421855_101564 {ECO:0000313|EMBL:SDE42726.1};
OS   Ulvibacter litoralis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacter.
OX   NCBI_TaxID=227084 {ECO:0000313|EMBL:SDE42726.1, ECO:0000313|Proteomes:UP000199321};
RN   [1] {ECO:0000313|EMBL:SDE42726.1, ECO:0000313|Proteomes:UP000199321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16195 {ECO:0000313|EMBL:SDE42726.1,
RC   ECO:0000313|Proteomes:UP000199321};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNBA01000001; SDE42726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7CVS2; -.
DR   STRING; 227084.SAMN05421855_101564; -.
DR   OrthoDB; 9807235at2; -.
DR   Proteomes; UP000199321; Unassembled WGS sequence.
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:0002094; F:polyprenyltransferase activity; IEA:UniProt.
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; IPR039074; GGGP/HepGP_synthase_I.
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; PTHR40029; -; 1.
DR   PANTHER; PTHR40029:SF2; HEPTAPRENYLGLYCERYL PHOSPHATE SYNTHASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199321};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00112}.
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         171..177
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT   BINDING         202..203
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"
SQ   SEQUENCE   232 AA;  24989 MW;  5FC0D784B8085081 CRC64;
     MECYQALLKG ISENRKFLAI LIDPDKFFIA EADVFLKQLP KETTHLFVGG STVVEGATEA
     TVNALKRAST LPIFLFPGDY TQVTSEADVL LFLSLLSGRN AEYLIGQQVK SISKLQQTAL
     EIISTGYLLL DGGNQSAVAR VSNTEPMSQE DVGAIVHTAL AGEYMGAKLI YLEAGSGATI
     PVHPRIISEV KKAISIPLLV GGGIRTERQK QEAYTAGADL VVMGTVFEKI KK
//
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