GFPS_AERPX
ID GFPS_AERPX Reviewed; 318 AA.
AC Q9UWR6;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Geranylfarnesyl diphosphate synthase;
DE Short=GFPS;
DE EC=2.5.1.81;
DE AltName: Full=Farnesylgeranyl diphosphate synthase;
DE Short=FGPP synthase;
GN Name=fgs;
OS Aeropyrum pernix.
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=56636;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A GERANYLFARNESYL
RP DIPHOSPHATE, AND SUBSTRATE SPECIFICITY.
RX PubMed=10632701; DOI=10.1046/j.1432-1327.2000.00967.x;
RA Tachibana A., Yano Y., Otani S., Nomura N., Sako Y., Taniguchi M.;
RT "Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase
RT from a hyperthermophilic archaeon, Aeropyrum pernix. Molecularevolution
RT with alteration in product specificity.";
RL Eur. J. Biochem. 267:321-328(2000).
RN [2]
RP FUNCTION AS A GERANYLFARNESYL DIPHOSPHATE SYNTHASE, MUTAGENESIS OF ALA-64;
RP VAL-84; HIS-88; ILE-177 AND MET-191, AND CHAIN ELONGATION SPECIFICITY.
RX PubMed=15548566; DOI=10.1093/protein/gzh089;
RA Lee P.C., Mijts B.N., Petri R., Watts K.T., Schmidt-Dannert C.;
RT "Alteration of product specificity of Aeropyrum pernix farnesylgeranyl
RT diphosphate synthase (Fgs) by directed evolution.";
RL Protein Eng. Des. Sel. 17:771-777(2004).
CC -!- FUNCTION: Probably involved in biosynthesis of the precursor for C25
CC (sesterterpanyl chain) moiety of C25-C25 diether (2,3-di-O-
CC sesterterpanyl-sn-glycero) membrane lipid. Catalyzes the condensation
CC of isopentenyl pyrophosphate with the allylic pyrophosphates to yield
CC all-trans geranylfarnesyl diphosphate (GFPP). Geranylgeranyl
CC diphosphate (GGPP) is the preferred substrate, however methylallyl
CC diphosphate (DMAPP), farnesyl diphosphate (FPP) and geranyl diphosphate
CC (GPP) can also be used as allylic substrate.
CC {ECO:0000269|PubMed:10632701, ECO:0000269|PubMed:15548566}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl
CC diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate +
CC diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769;
CC EC=2.5.1.81;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AB025791; BAA88983.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UWR6; -.
DR SMR; Q9UWR6; -.
DR KEGG; ag:BAA88983; -.
DR BioCyc; MetaCyc:MON-15678; -.
DR BRENDA; 2.5.1.81; 171.
DR GO; GO:0044687; F:geranylfarnesyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Transferase.
FT CHAIN 1..318
FT /note="Geranylfarnesyl diphosphate synthase"
FT /id="PRO_0000419206"
FT BINDING 31
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 34
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 65
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 81
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 166
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT SITE 64
FT /note="The 8th amino acid upstream of the first aspartate-
FT rich motif (FARM) is an important determinant in
FT controlling the chain elongation of C25 FGPP synthase"
FT MUTAGEN 64
FT /note="A->T: Produces only C20 (GGPP) as a final product.
FT It seems to block further chain elongation of GGPP to
FT GFPP."
FT /evidence="ECO:0000269|PubMed:15548566"
FT MUTAGEN 64
FT /note="A->V: Produces only C20 (GGPP) as a final product.
FT It seems to block further chain elongation of GGPP to
FT GFPP."
FT /evidence="ECO:0000269|PubMed:15548566"
FT MUTAGEN 84
FT /note="V->I: Produces a mixed population of C15 (FPP) and
FT C20 (GGPP); when associated with R-88; M-177 and V-191."
FT /evidence="ECO:0000269|PubMed:15548566"
FT MUTAGEN 88
FT /note="H->R: Produces a mixed population of C15 (FPP) and
FT C20 (GGPP); when associated with I-84; M-177 and V-191."
FT /evidence="ECO:0000269|PubMed:15548566"
FT MUTAGEN 177
FT /note="I->M: Produces a mixed population of C15 (FPP) and
FT C20 (GGPP); when associated with I-84; R-88 and V-191."
FT /evidence="ECO:0000269|PubMed:15548566"
FT MUTAGEN 191
FT /note="M->V: Produces a mixed population of C15 (FPP) and
FT C20 (GGPP); when associated with I-84; R-88 and M-177."
FT /evidence="ECO:0000269|PubMed:15548566"
SQ SEQUENCE 318 AA; 34982 MW; EA9599E16D9CEF94 CRC64;
MLIDHYIMDF MSITPDRLSG ASLHLIKAGG KRLRPLITLL TARMLGGLEA EARAIPLAAS
IETAHTFSLI HDDIMDRDEV RRGVPTTHVV YGDDWAILAG DTLHAAAFKM IADSREWGMS
HEQAYRAFKV LSEAAIQISR GQAYDMLFEE TWDVDVADYL NMVRLKTGAL IEAAARIGAV
AAGAGSEIEK MMGEVGMNAG IAFQIRDDIL GVIGDPKVTG KPVYNDLRRG KKTLLVIYAV
KKAGRREIVD LIGPKASEDD LKRAASIIVD SGALDYAESR ARFYVERARD ILSRVPAVDA
ESKELLNLLL DYIVERVK
