SPISY_SANSP
ID SPISY_SANSP Reviewed; 569 AA.
AC E3W204;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Santalene synthase;
DE Short=SspiSSy;
DE EC=4.2.3.81;
DE EC=4.2.3.82;
DE EC=4.2.3.83;
DE AltName: Full=Alpha-santalene synthase;
DE AltName: Full=Beta-santalene synthase;
DE AltName: Full=Exo-alpha-bergamotene synthase;
OS Santalum spicatum (Australian sandalwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Santalales; Santalaceae; Santalum.
OX NCBI_TaxID=453088;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21454632; DOI=10.1074/jbc.m111.231787;
RA Jones C.G., Moniodis J., Zulak K.G., Scaffidi A., Plummer J.A.,
RA Ghisalberti E.L., Barbour E.L., Bohlmann J.;
RT "Sandalwood fragrance biosynthesis involves sesquiterpene synthases of both
RT the terpene synthase (TPS)-a and TPS-b Subfamilies, including santalene
RT synthases.";
RL J. Biol. Chem. 286:17445-17454(2011).
CC -!- FUNCTION: Catalyzes a mixture of sesquiterpenoids from (2E,6E)-farnesyl
CC diphosphate in fragrance biosynthesis. Catalyzes the formation of
CC alpha-santalene, beta-santalene, epi-beta-santalene and exo-alpha-
CC bergamotene, as well as traces of alpha-farnesene and beta-farnesene.
CC {ECO:0000269|PubMed:21454632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene +
CC diphosphate; Xref=Rhea:RHEA:31427, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62756, ChEBI:CHEBI:175763; EC=4.2.3.81;
CC Evidence={ECO:0000269|PubMed:21454632};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-alpha-santalene +
CC diphosphate; Xref=Rhea:RHEA:31435, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61677, ChEBI:CHEBI:175763; EC=4.2.3.82;
CC Evidence={ECO:0000269|PubMed:21454632};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-beta-santalene +
CC diphosphate; Xref=Rhea:RHEA:31431, ChEBI:CHEBI:10440,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.83;
CC Evidence={ECO:0000269|PubMed:21454632};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:21454632};
CC Note=kcat is 2.6 sec(-1) with (2E,6E)-farnesyl diphosphate as
CC substrate.;
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ343278; ADO87002.1; -; mRNA.
DR AlphaFoldDB; E3W204; -.
DR SMR; E3W204; -.
DR KEGG; ag:ADO87002; -.
DR BRENDA; 4.2.3.81; 12838.
DR BRENDA; 4.2.3.82; 12838.
DR BRENDA; 4.2.3.83; 12838.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..569
FT /note="Santalene synthase"
FT /id="PRO_0000418942"
FT MOTIF 321..325
FT /note="DDXXD motif"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 569 AA; 65407 MW; 868538AAD7DC62EF CRC64;
MDSSTATATT APFIDHTDHV NLKIDNDSSE SRRMGNYKPS IWNYDFLQSL AIHHNIVEEK
HLKLAEKLKG QVMSMFGAPM EPLAKLELVD VVQRLGLNHQ FETEIKEALF SVYKDGSNGW
WFGHLHATSL RFRLLRQCGL FIPQDVFKTF QSKTDEFDMK LCDNIKGLLS LYEASFLGWK
GENILDEAKA FATKYLKNAW ENISQKWLAK RVKHALALPL HWRVPRIEAR WFIEAYEQEE
NMNPTLLKLA KLDFNMVQSI HQKEIGELAR WWVTTGLDKL AFARNNLLQS YMWSCAIASD
PKFKLARETI VEIGSVLTVV DDAYDVYGSM DELDHYTYSV ERWSCVEIDK LPNTLKLIFM
SMFNKTNEVG LRVQHERGYN GIPTFIKAWV EQCKAYQKEA RWYHGGHTPP LEEYSLNGLV
SIGFPLLLIT GYIAIAENEA ALDKVHPLPD LLHYSSLLSR LINDMGTSPD EMARGDNLKS
IHCYMNETGA SEEVAREHIK GIIEENWKIL NQCCFDQSQF QEPFITFNLN SVRGSHFFYE
FGDGFGVTDS WTKVDMKSVL IDPIPLGEE
