SASY_SANAL
ID SASY_SANAL Reviewed; 569 AA.
AC E3W202;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Santalene synthase;
DE Short=SaSSy;
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 album (White sandalwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Santalales; Santalaceae; Santalum.
OX NCBI_TaxID=35974;
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 Also acts with (Z,Z)-farnesyl diphosphate isomer, producing alpha-endo-
CC bergamotene, alpha-santalene, (Z)-beta-farnesene, epi-beta-santalene,
CC and beta-santalene. {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 0.34 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; HQ343276; ADO87000.1; -; mRNA.
DR PDB; 5ZZJ; X-ray; 2.60 A; A/B/C/D=1-569.
DR PDBsum; 5ZZJ; -.
DR AlphaFoldDB; E3W202; -.
DR SMR; E3W202; -.
DR KEGG; ag:ADO87000; -.
DR BRENDA; 4.2.3.81; 5574.
DR BRENDA; 4.2.3.82; 5574.
DR BRENDA; 4.2.3.83; 5574.
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 3D-structure; Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..569
FT /note="Santalene synthase"
FT /id="PRO_0000418944"
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"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT TURN 119..123
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 244..274
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 304..325
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 353..377
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 382..404
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 411..421
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 439..445
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 450..465
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 480..488
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 492..513
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 524..538
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:5ZZJ"
FT HELIX 553..560
FT /evidence="ECO:0007829|PDB:5ZZJ"
SQ SEQUENCE 569 AA; 65163 MW; E3FB6635D46F9406 CRC64;
MDSSTATAMT APFIDPTDHV NLKTDTDASE NRRMGNYKPS IWNYDFLQSL ATHHNIVEER
HLKLAEKLKG QVKFMFGAPM EPLAKLELVD VVQRLGLNHL FETEIKEALF SIYKDGSNGW
WFGHLHATSL RFRLLRQCGL FIPQDVFKTF QNKTGEFDMK LCDNVKGLLS LYEASYLGWK
GENILDEAKA FTTKCLKSAW ENISEKWLAK RVKHALALPL HWRVPRIEAR WFIEAYEQEA
NMNPTLLKLA KLDFNMVQSI HQKEIGELAR WWVTTGLDKL AFARNNLLQS YMWSCAIASD
PKFKLARETI VEIGSVLTVV DDGYDVYGSI DELDLYTSSV ERWSCVEIDK LPNTLKLIFM
SMFNKTNEVG LRVQHERGYN SIPTFIKAWV EQCKSYQKEA RWFHGGHTPP LEEYSLNGLV
SIGFPLLLIT GYVAIAENEA ALDKVHPLPD LLHYSSLLSR LINDIGTSPD EMARGDNLKS
IHCYMNETGA SEEVAREHIK GVIEENWKIL NQCCFDQSQF QEPFITFNLN SVRGSHFFYE
FGDGFGVTDS WTKVDMKSVL IDPIPLGEE
