ZFPS_SOLHA
ID ZFPS_SOLHA Reviewed; 303 AA.
AC B8XA40;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=(2Z,6Z)-farnesyl diphosphate synthase, chloroplastic;
DE EC=2.5.1.92;
DE AltName: Full=Z,Z-FPP synthase;
DE AltName: Full=Z,Z-farnesyl pyrophosphate synthase;
DE Flags: Precursor;
GN Name=ZFPS;
OS Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=62890;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=19155349; DOI=10.1105/tpc.107.057885;
RA Sallaud C., Rontein D., Onillon S., Jabes F., Duffe P., Giacalone C.,
RA Thoraval S., Escoffier C., Herbette G., Leonhardt N., Causse M.,
RA Tissier A.;
RT "A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl
RT pyrophosphate in the wild tomato Solanum habrochaites.";
RL Plant Cell 21:301-317(2009).
CC -!- FUNCTION: Specifically forms (2Z,6Z)-farnesyl diphosphate (Z,Z-FPP)
CC from dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate
CC (IPP). Also able to use nerylpyrophosphate (NPP) as substrate. Involved
CC in the biosynthesis of several sesquiterpenes.
CC {ECO:0000269|PubMed:19155349}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + 2 isopentenyl diphosphate =
CC (2Z,6Z)-farnesyl diphosphate + 2 diphosphate; Xref=Rhea:RHEA:27810,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:60374,
CC ChEBI:CHEBI:128769; EC=2.5.1.92;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for dimethylallyl diphosphate in the presence of 35 uM
CC isopentenyl diphosphate {ECO:0000269|PubMed:19155349};
CC KM=35 uM for dimethylallyl diphosphate in the presence of 210 uM
CC isopentenyl diphosphate {ECO:0000269|PubMed:19155349};
CC KM=10 uM for nerylpyrophosphate in the presence of 180 uM isopentenyl
CC diphosphate {ECO:0000269|PubMed:19155349};
CC Note=isopentenyl diphosphate acts as activator of its own catalysis.;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19155349}.
CC -!- SIMILARITY: Belongs to the UPP synthetase family. {ECO:0000305}.
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DR EMBL; FJ194969; ACJ38408.1; -; mRNA.
DR PDB; 5HXN; X-ray; 2.05 A; A=72-303.
DR PDB; 5HXO; X-ray; 2.05 A; A=72-303.
DR PDB; 5HXP; X-ray; 1.95 A; A/C=72-303.
DR PDB; 5HXQ; X-ray; 1.95 A; A/C=72-303.
DR PDB; 5HXT; X-ray; 2.15 A; A/B=72-303.
DR PDBsum; 5HXN; -.
DR PDBsum; 5HXO; -.
DR PDBsum; 5HXP; -.
DR PDBsum; 5HXQ; -.
DR PDBsum; 5HXT; -.
DR AlphaFoldDB; B8XA40; -.
DR SMR; B8XA40; -.
DR KEGG; ag:ACJ38408; -.
DR BioCyc; MetaCyc:MON-14834; -.
DR BRENDA; 2.5.1.92; 3102.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102059; F:2-cis,6-cis-farnesyl pyrophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
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 3D-structure; Chloroplast; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..303
FT /note="(2Z,6Z)-farnesyl diphosphate synthase,
FT chloroplastic"
FT /id="PRO_0000405119"
FT ACT_SITE 86
FT /evidence="ECO:0000250"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5HXP"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:5HXP"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5HXQ"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:5HXP"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:5HXP"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 203..219
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:5HXP"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5HXP"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5HXP"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:5HXP"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:5HXP"
SQ SEQUENCE 303 AA; 34430 MW; C9289E0BC89193BE CRC64;
MSSLVLQCWK LSSPSLILQQ NTSISMGAFK GIHKLQIPNS PLTVSARGLN KISCSLSLQT
EKLCYEDNDN DLDEELMPKH IALIMDGNRR WAKDKGLDVS EGHKHLFPKL KEICDISSKL
GIQVITAFAF STENWKRAKG EVDFLMQMFE ELYDEFSRSG VRVSIIGCKT DLPMTLQKCI
ALTEETTKGN KGLHLVIALN YGGYYDILQA TKSIVNKAMN GLLDVEDINK NLFDQELESK
CPNPDLLIRT GGDQRVSNFL LWQLAYTEFY FTKTLFPDFG EEDLKEAIIN FQQRHRRFGG
HTY
