ID   ZSS1_ZINZE              Reviewed;         548 AA.
AC   B1B1U3;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Alpha-humulene synthase;
DE            EC=4.2.3.104;
GN   Name=ZSS1;
OS   Zingiber zerumbet (Shampoo ginger) (Amomum zerumbet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Zingiber.
OX   NCBI_TaxID=311405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=18273640; DOI=10.1007/s00425-008-0700-x;
RA   Yu F.N., Okamoto S., Nakasone K., Adachi K., Matsuda S., Harada H.,
RA   Misawa N., Utsumi R.;
RT   "Molecular cloning and functional characterization of alpha-humulene
RT   synthase, a possible key enzyme of zerumbone biosynthesis in shampoo ginger
RT   (Zingiber zerumbet Smith).";
RL   Planta 227:1291-1299(2008).
CC   -!- FUNCTION: Catalyzes the formation of alpha-humulene in the first step
CC       of zerumbone biosynthesis, a highly promising multi-anticancer agent.
CC       Also mediates formation of beta-caryophyllene at a much lower level.
CC       {ECO:0000269|PubMed:18273640}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC         Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:175763; EC=4.2.3.104;
CC         Evidence={ECO:0000269|PubMed:18273640};
CC   -!- TISSUE SPECIFICITY: Mostly expressed in rhizomes.
CC       {ECO:0000269|PubMed:18273640}.
CC   -!- INDUCTION: Up-regulated in leaves and rhizomes following treatment with
CC       methyl jasmonate (meJA). {ECO:0000269|PubMed:18273640}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AB247331; BAG12020.1; -; mRNA.
DR   EMBL; AB263736; BAG12315.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1B1U3; -.
DR   SMR; B1B1U3; -.
DR   PRIDE; B1B1U3; -.
DR   KEGG; ag:BAG12020; -.
DR   BioCyc; MetaCyc:MON-14875; -.
DR   BRENDA; 4.2.3.104; 12510.
DR   GO; GO:0080017; F:alpha-humulene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; 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; Metal-binding.
FT   CHAIN           1..548
FT                   /note="Alpha-humulene synthase"
FT                   /id="PRO_0000418755"
FT   MOTIF           302..306
FT                   /note="DDXXD motif"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         453
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  64518 MW;  D21A6983B9AC2C5A CRC64;
     MERQSMALVG DKEEIIRKSF EYHPTVWGDY FIRNYSCLPL EKECMIKRVE ELKDRVRNLF
     EETHDVLQIM ILVDSIQLLG LDYHFEKEIT AALRLIYEAD VENYGLYEVS LRFRLLRQHG
     YNLSPDVFNK FKDDKGRFLP TLNGDAKGLL NLYNAAYLGT HEETILDEAI SFTKCQLESL
     LGELEQPLAI EVSLFLETPL YRRTRRLLVR KYIPIYQEKV MRNDTILELA KLDFNLLQSL
     HQEEVKKITI WWNDLALTKS LKFARDRVVE CYYWIVAVYF EPQYSRARVI TSKAISLMSI
     MDDIYDNYST LEESRLLTEA IERWEPQAVD CVPEYLKDFY LKLLKTYKDF EDELEPNEKY
     RIPYLQEEIK VLSRAYFQEA KWGVERYVPA LEEHLLVSLI TAGYFAVACA SYVGLGEDAT
     KETFEWVASS PKILKSCSIH CRLMDDITSH QREQERDHFA STVESYMKEH GTSAKVACEK
     LQVMVEQKWK DLNEECLRPT QVARPLIEII LNLSRAMEDI YKHKDTYTNS NTRMKDNVSL
     IFVESFLI