ID   STPS1_SANAL             Reviewed;         559 AA.
AC   B5A435;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Sesquiterpene synthase;
DE            Short=SaSesquiTPS1;
DE            EC=4.2.3.-;
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, COFACTOR, AND CATALYTIC ACTIVITY.
RX   PubMed=18541135; DOI=10.1016/j.abb.2008.05.008;
RA   Jones C.G., Keeling C.I., Ghisalberti E.L., Barbour E.L., Plummer J.A.,
RA   Bohlmann J.;
RT   "Isolation of cDNAs and functional characterisation of two multi-product
RT   terpene synthase enzymes from sandalwood, Santalum album L.";
RL   Arch. Biochem. Biophys. 477:121-130(2008).
CC   -!- FUNCTION: Sesquiterpene synthase producing the monocyclic sesquiterpene
CC       alcohol germacrene D-4-ol and helminthogermacrene and minor amounts of
CC       bicyclic compounds such as alpha-bulnesene, gamma-muurolene, alpha- and
CC       beta-selinenes, when incubated with farnesyl diphosphate.
CC       {ECO:0000269|PubMed:18541135}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:18541135};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000305|PubMed:18541135};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC       {ECO:0000305|PubMed:18541135};
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; EU798693; ACF24768.1; -; mRNA.
DR   AlphaFoldDB; B5A435; -.
DR   SMR; B5A435; -.
DR   BRENDA; 4.2.3.126; 5574.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0033383; P:geranyl diphosphate metabolic process; IDA:UniProtKB.
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; 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   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Lyase; Magnesium; Manganese; Metal-binding.
FT   CHAIN           1..559
FT                   /note="Sesquiterpene synthase"
FT                   /id="PRO_0000419324"
FT   MOTIF           312..316
FT                   /note="DDXXD motif"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   559 AA;  65791 MW;  323AE6C6C9E7BD59 CRC64;
     MENQKVPISS VPNLKELSRP IANFPPSIWG DRFINYACED ENEQAQKERQ VEELKEQVRR
     ELAATVDKPL QQLNIIDATQ RLGIAYHFEN EIEESLEHIY LHTYVENNCF QGSHDLYSVA
     LWFRLLRQDG YKVSCDVFDK FRDYEDNFKN SLMEDAKGLL ELYEATHLSV HGEEMLDDAL
     EFAKTRLESI VNHLNYPLAE QVRHALYRPL RKGLPRLEAV YFFRIYEAYD SHNKALLKLA
     KLDFNLLQSL HKKELSDMAR WWKSLDFAAK FPFARDRLVE GYFWVLGVYF EPQYSLARKI
     IIKVFTMIST IDDIYDAYGT LDELELFTKA MQRWDVGSLD QLPEYMKPCY KSILDVYNEI
     EEEMDNQGSL FRMHYAKEVM KKLVEGYMDE AKWCHEKYVP TFEEYMPVAL VTSGYTFLTT
     ISYLGMGEIA SKEAFDWLFS HPPVIEASES VCRLMDDMRS HKFEQERGHV ASGIECYMKQ
     YGVTEEEAHD EFRKQLVKAW KDINEECLRP YRVPKPLLMR ILNLTRVIDV IYKNEDGYTH
     VKKAMKDNIA SLLIDPMIV