ID   GEDH1_OCIBA             Reviewed;         360 AA.
AC   Q2KNL6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Geraniol dehydrogenase 1;
DE            Short=ObaGEDH1;
DE            EC=1.1.1.183;
GN   Name=GEDH1;
OS   Ocimum basilicum (Sweet basil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC   Ocimum.
OX   NCBI_TaxID=39350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. SD;
RX   PubMed=16150417; DOI=10.1016/j.abb.2005.07.026;
RA   Iijima Y., Wang G., Fridman E., Pichersky E.;
RT   "Analysis of the enzymatic formation of citral in the glands of sweet
RT   basil.";
RL   Arch. Biochem. Biophys. 448:141-149(2006).
CC   -!- FUNCTION: Involved in the production of citral, a mixture of geranial
CC       and neral with a strong lemony scent. Reversibly oxidizes geraniol and
CC       nerol in equal efficiency. Also active, although at a lower efficiency,
CC       with cinnamyl alcohol. {ECO:0000269|PubMed:16150417}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geraniol + NADP(+) = (2E)-geranial + H(+) + NADPH;
CC         Xref=Rhea:RHEA:14521, ChEBI:CHEBI:15378, ChEBI:CHEBI:16980,
CC         ChEBI:CHEBI:17447, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.183;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: 66% inhibition by 5 mM Zn(2+).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=655 uM for cinnamyl alcohol {ECO:0000269|PubMed:16150417};
CC         KM=30 uM for geraniol {ECO:0000269|PubMed:16150417};
CC         KM=37 uM for nerol {ECO:0000269|PubMed:16150417};
CC         Vmax=23 pmol/sec/ug enzyme toward cinnamyl alcohol
CC         {ECO:0000269|PubMed:16150417};
CC         Vmax=13 pmol/sec/ug enzyme toward geraniol
CC         {ECO:0000269|PubMed:16150417};
CC         Vmax=19 pmol/sec/ug enzyme toward nerol
CC         {ECO:0000269|PubMed:16150417};
CC       pH dependence:
CC         Optimum pH is 9.5. Active from pH 8.5 to 10.0.
CC         {ECO:0000269|PubMed:16150417};
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, with a very low expression in
CC       peltate glands. {ECO:0000269|PubMed:16150417}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AY879284; AAX83107.1; -; mRNA.
DR   AlphaFoldDB; Q2KNL6; -.
DR   SMR; Q2KNL6; -.
DR   BioCyc; MetaCyc:MON-13798; -.
DR   BRENDA; 1.1.1.183; 4385.
DR   SABIO-RK; Q2KNL6; -.
DR   GO; GO:0047924; F:geraniol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; NADP; Oxidoreductase; Zinc.
FT   CHAIN           1..360
FT                   /note="Geraniol dehydrogenase 1"
FT                   /id="PRO_0000367052"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  39044 MW;  0D53B63806C33253 CRC64;
     MAKSPETEHP VKALGWAATD NSGTFSPFNF SRRATGERDV QFRVLYCGVC HSDLHMVKNE
     WGVTHYPIVP GHEIVGIVTE VGSKVEKVKI GDKVGVGVLV GSCRQCDQCS NDLENYCYKQ
     ILTYGAPYLD GTIARGGYSD IMVADEHFII RWPENFPLDA GAPLLCAGIT TYSPLKYFGL
     DKPGLRVGVN GLGGLGHVAV KFAKAFGTKV TVISTSLSKK EEAMQHLGVD EFVVSTDPQQ
     MQAAVGTLDG IIDTVSAPHP IVPLLSLLKP HGKLIVVGLP DKPLQLPVFP LIQGRRTIAG
     SGIGGLKETQ EMIDFAAKNN IVADVEVIPI DYINTAMDRL LKSDVKYRFV IDVEKSLKPQ