ID   ZERSY_ZINZE             Reviewed;         267 AA.
AC   F1SWA0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Zerumbone synthase;
DE            EC=1.1.1.326;
GN   Name=ZSD1;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   SER-142; SER-144; TYR-155 AND LYS-159.
RX   PubMed=21668645; DOI=10.1111/j.1742-4658.2011.08211.x;
RA   Okamoto S., Yu F., Harada H., Okajima T., Hattan J., Misawa N., Utsumi R.;
RT   "A short-chain dehydrogenase involved in terpene metabolism from Zingiber
RT   zerumbet.";
RL   FEBS J. 278:2892-2900(2011).
CC   -!- FUNCTION: Catalyzes 8-hydroxy-alpha-humulene into zerumbone in presence
CC       of NAD. Also converts borneol to camphor in vitro. Zerumbone is a
CC       highly promising multi-anticancer agent. {ECO:0000269|PubMed:21668645}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-hydroxy-alpha-humulene + NAD(+) = H(+) + NADH + zerumbone;
CC         Xref=Rhea:RHEA:32327, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:63892, ChEBI:CHEBI:63893;
CC         EC=1.1.1.326; Evidence={ECO:0000269|PubMed:21668645};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27.3 uM for NAD {ECO:0000269|PubMed:21668645};
CC         KM=58.5 uM for 8-hydroxy-alpha-humulene
CC         {ECO:0000269|PubMed:21668645};
CC         KM=22.8 uM for borneol {ECO:0000269|PubMed:21668645};
CC         Note=kcat is 3.8 sec(-1) with NAD as substrate. kcat is 1.3 sec(-1)
CC         with 8-hydroxy-alpha-humulene as substrate. kcat is 4.1 sec(-1) with
CC         borneol as substrate.;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems and rhizomes.
CC       {ECO:0000269|PubMed:21668645}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB480831; BAK09296.1; -; mRNA.
DR   AlphaFoldDB; F1SWA0; -.
DR   SMR; F1SWA0; -.
DR   KEGG; ag:BAK09296; -.
DR   BioCyc; MetaCyc:MON-16689; -.
DR   BRENDA; 1.1.1.326; 12510.
DR   GO; GO:0102069; F:zerumbone synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd05326; secoisolariciresinol-DH_like_SDR_c; 1.
DR   InterPro; IPR045309; ABA2-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..267
FT                   /note="Zerumbone synthase"
FT                   /id="PRO_0000418748"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
FT   BINDING         9..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         142
FT                   /note="S->A: Strong reduction in oxidoreductase activity
FT                   toward 8-hydroxy-alpha-humulene and borneol."
FT                   /evidence="ECO:0000269|PubMed:21668645"
FT   MUTAGEN         144
FT                   /note="S->A: Increased oxidoreductase activity toward 8-
FT                   hydroxy-alpha-humulene and borneol."
FT                   /evidence="ECO:0000269|PubMed:21668645"
FT   MUTAGEN         155
FT                   /note="Y->A: Strong reduction in oxidoreductase activity
FT                   toward 8-hydroxy-alpha-humulene and borneol."
FT                   /evidence="ECO:0000269|PubMed:21668645"
FT   MUTAGEN         159
FT                   /note="K->A: Abolishes all oxidoreductase activity."
FT                   /evidence="ECO:0000269|PubMed:21668645"
SQ   SEQUENCE   267 AA;  28670 MW;  0EA735846ED23C46 CRC64;
     MRLEGKVALV TGGASGIGES IARLFIEHGA KICIVDVQDE LGQQVSQRLG GDPHACYFHC
     DVTVEDDVRR AVDFTAEKYG TIDIMVNNAG ITGDKVIDIR DADFNEFKKV FDINVNGVFL
     GMKHAARIMI PKMKGSIVSL ASVSSVIAGA GPHGYTGAKH AVVGLTKSVA AELGRHGIRV
     NCVSPYAVPT RLSMPYLPES EMQEDALRGF LTFVRSNANL KGVDLMPNDV AEAVLYLATE
     ESKYVSGLNL VIDGGFSIAN HTLQVFE