GFPS_NATPD
ID GFPS_NATPD Reviewed; 341 AA.
AC Q3IPL1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=idsA3; OrderedLocusNames=NP_3696A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
RN [2]
RP FUNCTION AS A GERANYLFARNESYL DIPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RX PubMed=8137956; DOI=10.1016/0014-5793(94)80475-3;
RA Tachibana A.;
RT "A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the
RT haloalkaliphilic archaeon, Natronobacterium pharaonis.";
RL FEBS Lett. 341:291-294(1994).
CC -!- FUNCTION: Probably involved in biosynthesis of the precursor for C25
CC (sesterterpanyl chain) moiety of C20-C25 diether (2-O-sesterterpanyl-3-
CC O-phytanyl-sn-glycer) membrane lipid. Catalyzes the condensation of
CC isopentenyl pyrophosphate with the allylic pyrophosphates to yield
CC geranylfarnesyl diphosphate (GFPP). Geranylgeranyl diphosphate (GGPP)
CC is the preferred substrate, but dimethylallyl diphosphate (DMAPP) and
CC farnesyl diphosphate (FPP) can also be used as allylic substrate.
CC {ECO:0000269|PubMed:8137956}.
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; Evidence={ECO:0000269|PubMed:8137956};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; CR936257; CAI49939.1; -; Genomic_DNA.
DR RefSeq; WP_011323557.1; NC_007426.1.
DR AlphaFoldDB; Q3IPL1; -.
DR SMR; Q3IPL1; -.
DR STRING; 348780.NP_3696A; -.
DR EnsemblBacteria; CAI49939; CAI49939; NP_3696A.
DR GeneID; 3702862; -.
DR KEGG; nph:NP_3696A; -.
DR eggNOG; arCOG01726; Archaea.
DR HOGENOM; CLU_014015_2_1_2; -.
DR OMA; CEGQALD; -.
DR OrthoDB; 55053at2157; -.
DR Proteomes; UP000002698; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..341
FT /note="Geranylfarnesyl diphosphate synthase"
FT /id="PRO_0000419207"
FT BINDING 47
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 50
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 95
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 111
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 193
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 37411 MW; F29F336AB8F96852 CRC64;
MTSADHVESA IAERREIVNE AVSEQLPVQK PERLYSASRY LLDAGGKRLR PTILLLAAES
LADVEPLSAD YRQFPSLPGD EVDVLSAAVS IEVIQSFTLI HDDIMDDDDL RRGVPAVHRE
YDLETAILAG DTLYSKAFEY MLDTGAPAER SVEALDELAT TCTEICEGQA LDVDFENRSD
VTTEEYLEMV EFKTAVLYAA AASIPAILLG SDDETVEALH GYGLDIGRAF QIQDDLLDLT
APSDELGKQR GSDLVENKRT VITLHARDQG IDVEGLVSDD PSDAEIEAAV QTLEDAGSID
FAREMALDLV TSGKERLDVL PENEARQLLE DIADFLVERS Y
