GGGPS_FLAJ1
ID GGGPS_FLAJ1 Reviewed; 243 AA.
AC A5FJK8;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Fjoh_1584 {ECO:0000312|EMBL:ABQ04616.1};
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=19717629; DOI=10.1128/aem.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
RN [2] {ECO:0007744|PDB:4JEJ}
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) IN COMPLEX WITH GLYCEROL
RP 1-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF
RP ILE-90.
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; CP000685; ABQ04616.1; -; Genomic_DNA.
DR RefSeq; WP_012023660.1; NZ_MUGZ01000017.1.
DR PDB; 4JEJ; X-ray; 1.52 A; A=1-243.
DR PDBsum; 4JEJ; -.
DR AlphaFoldDB; A5FJK8; -.
DR SMR; A5FJK8; -.
DR STRING; 376686.Fjoh_1584; -.
DR EnsemblBacteria; ABQ04616; ABQ04616; Fjoh_1584.
DR KEGG; fjo:Fjoh_1584; -.
DR eggNOG; COG1646; Bacteria.
DR HOGENOM; CLU_068610_0_0_10; -.
DR OMA; ADAIFFM; -.
DR OrthoDB; 1560657at2; -.
DR Proteomes; UP000006694; 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 3D-structure; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Transferase.
FT CHAIN 1..243
FT /note="Geranylgeranylglyceryl phosphate synthase"
FT /id="PRO_0000436908"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT BINDING 178..184
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:4JEJ"
FT BINDING 209..210
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:4JEJ"
FT BINDING 231..232
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:4JEJ"
FT MUTAGEN 90
FT /note="I->A: Accepts HepPP as substrate."
FT /evidence="ECO:0000269|PubMed:24684232"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:4JEJ"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:4JEJ"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:4JEJ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4JEJ"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:4JEJ"
FT TURN 108..112
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:4JEJ"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:4JEJ"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:4JEJ"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:4JEJ"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4JEJ"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:4JEJ"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:4JEJ"
SQ SEQUENCE 243 AA; 26385 MW; 0F36B2131DA6B7E9 CRC64;
MEQKILTTIH QQILEAKKNG QKLLAILLDP DKIVWENLDH LLLKINQSPA THIFVGGSIV
ESTIIEDLIA QLKQKTRLPV VIFPGDPSQI SPKADAILFL SLLSGRNPDY LIEYQVQAAP
ILKKTNLEVI STGYILIESG NETAVARVSK TEPLNRENFD LALATAQAGE MLGSKLIYLE
AGSGAKKPVP LEMISVISQN VEIPIIVGGG IVDLHGIKKA YNAGADLVVI GTAFENDSHF
FDS
