ZFPP_THEFY
ID ZFPP_THEFY Reviewed; 254 AA.
AC Q47SS3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=(2Z,6E)-farnesyl diphosphate synthase;
DE EC=2.5.1.68;
DE AltName: Full=Cis-prenyltransferase;
DE AltName: Full=Short-chain Z-isoprenyl diphosphate synthase;
DE AltName: Full=Z-FPP synthase;
DE Short=Z-FPPS;
DE AltName: Full=Z-Polyprenyl diphosphate synthase;
DE AltName: Full=Z-isoprenyl diphosphate synthase;
GN OrderedLocusNames=Tfu_0456;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
RN [2]
RP FUNCTION AS A FARNESYL DIPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ILE-59, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=18725204; DOI=10.1016/j.bbrc.2008.08.057;
RA Ambo T., Noike M., Kurokawa H., Koyama T.;
RT "Cloning and functional analysis of novel short-chain cis-
RT prenyltransferases.";
RL Biochem. Biophys. Res. Commun. 375:536-540(2008).
CC -!- FUNCTION: Catalyzes the condensation of only one isopentenyl
CC pyrophosphate (IPP) unit in the cis configuration to E-geranyl
CC diphosphate (E-GPP) generating the 15 carbon product (2Z,6E)-farnesyl
CC diphosphate (Z-FPP or EZ-FPP). Only geranyl diphosphate (GPP) can be
CC used as isoprenyl acceptor. {ECO:0000269|PubMed:18725204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2Z,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:23300,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:162247; EC=2.5.1.68;
CC Evidence={ECO:0000269|PubMed:18725204};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 uM for geranyl diphosphate (at 37 degrees Celsius and at pH
CC 7.5) {ECO:0000269|PubMed:18725204};
CC KM=1.2 uM for isopentenyl diphosphate (at 37 degrees Celsius and at
CC pH 7.5) {ECO:0000269|PubMed:18725204};
CC Note=kcat is 229 sec(-1) with geranyl diphosphate as substrate and
CC 282 sec(-1) with isopentenyl diphosphate as substrate.;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. Z-FPP synthase
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000088; AAZ54494.1; -; Genomic_DNA.
DR RefSeq; WP_011290903.1; NC_007333.1.
DR AlphaFoldDB; Q47SS3; -.
DR SMR; Q47SS3; -.
DR STRING; 269800.Tfu_0456; -.
DR EnsemblBacteria; AAZ54494; AAZ54494; Tfu_0456.
DR KEGG; tfu:Tfu_0456; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_2_0_11; -.
DR OMA; TKGQPDP; -.
DR OrthoDB; 1630604at2; -.
DR BRENDA; 2.5.1.68; 6298.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033850; F:Z-farnesyl diphosphate synthase activity; IDA:UniProtKB.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Transferase.
FT CHAIN 1..254
FT /note="(2Z,6E)-farnesyl diphosphate synthase"
FT /id="PRO_0000419135"
FT ACT_SITE 34
FT /evidence="ECO:0000250"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 35..38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 80..82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209..211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="May play an important role in product chain-length
FT determination or in allylic substrate recognition
FT mechanisms"
FT SITE 78
FT /note="Important for determining product length"
FT /evidence="ECO:0000250"
FT MUTAGEN 59
FT /note="I->A: Able to incorporate E-GPP, Z-FPP, and Z,E,E-
FT geranylgeranyl diphosphate (Z,E,E-GGPP) as the allylic
FT substrates. Changes in the product chain-lengths."
FT /evidence="ECO:0000269|PubMed:18725204"
FT MUTAGEN 59
FT /note="I->F: No detectable transferase activity detected."
FT /evidence="ECO:0000269|PubMed:18725204"
FT MUTAGEN 59
FT /note="I->L: Able to incorporate E-GPP, Z-FPP, and Z,E,E-
FT geranylgeranyl diphosphate (Z,E,E-GGPP) as the allylic
FT substrates. Changes in the product chain-lengths."
FT /evidence="ECO:0000269|PubMed:18725204"
FT MUTAGEN 59
FT /note="I->M: Able to incorporate E-GPP, Z-FPP, and Z,E,E-
FT geranylgeranyl diphosphate (Z,E,E-GGPP) as the allylic
FT substrates. Changes in the product chain-lengths."
FT /evidence="ECO:0000269|PubMed:18725204"
FT MUTAGEN 59
FT /note="I->V: Able to incorporate E-GPP, Z-FPP, and Z,E,E-
FT geranylgeranyl diphosphate (Z,E,E-GGPP) as the allylic
FT substrates. Changes in the product chain-lengths."
FT /evidence="ECO:0000269|PubMed:18725204"
SQ SEQUENCE 254 AA; 28884 MW; B7CC479B5B382208 CRC64;
MGLLRIPLYR LYERRLERAL SNAPKPRHVG VILDGNRRWA RLSGLSSPKE GHRAGAEKIF
ELLDWCDEVG VQVVTLWLLS TDNLARPPEE LEPLFEIIEN TVRRLCNEGR RVNPMGALDL
LPASTAQVMK EAGTTTERNP GLLVNVAVGY GGRREIADAV RSLLLEEAAK GTTLEELAER
LDLDDIAKHL YTRGQPDPDL LIRTSGEQRL SGFLLWQSAH SEFYFCEVFW PAFRKIDFLR
ALRSYSVRQR RFGC
