SAUSY_SANAS
ID SAUSY_SANAS Reviewed; 569 AA.
AC E3W203;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Santalene synthase;
DE Short=SauSSy;
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 austrocaledonicum (Sandalwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Santalales; Santalaceae; Santalum.
OX NCBI_TaxID=293154;
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 0.91 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; HQ343277; ADO87001.1; -; mRNA.
DR AlphaFoldDB; E3W203; -.
DR SMR; E3W203; -.
DR KEGG; ag:ADO87001; -.
DR BRENDA; 4.2.3.81; 12837.
DR BRENDA; 4.2.3.82; 12837.
DR BRENDA; 4.2.3.83; 12837.
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_0000418943"
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; 65268 MW; 4853A03055CF355E CRC64;
MDSSTATAMT APFIDPTDHV NLKTDTDASE NRRMGNYKPS IWNYDFLQSL ATHHNIVEER
HLKLAEKLKG QVKFMFGAPM EPLAKLELVD VVQRLGLNHR FETEIKEALF SIYKDESNGW
WFGHLHATSL RFRLLRQCGL FIPQDVFKTF QNKTGEFDMK LCDNVKGLLS LYEASYLGWK
GENILDEAKA FATKYLKSAW ENISEKWLAK RVKHALALPL HWRVPRIEAR WFIEAYEQEA
NMNPTLLKLA KLDFNMVQSI HQKEIGELAR WWVTTGLDKL AFARNNLLQS YMWSCAIASD
PKFKLARETI VEIGSVLTVV DDAYDVYGSM DELDLYTSSV ERWSCVEIDK LPNTLKLIFM
SMFNKTNEVG LRVQHERGYN SIPTFIKAWV QQCKSYQKEA RWFHGGHTPP LEEYSLNGLV
SIGFPLLLIT GYVAIAENEA ALDKVHPLPD LLHYSSLLSR LINDIGTSPD EMARGDNLKS
IHCYMNGTGA SEEVAREHIK GVIEENWKIL NQCCFDQSQF QEPFITFNLN SVRGSHFFYE
FGDGFGVTDS WTKVDMKSVL IDPIPLGEE
