CADH1_OCIBA
ID CADH1_OCIBA Reviewed; 357 AA.
AC Q2KNL5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cinnamyl alcohol dehydrogenase 1;
DE Short=CAD 1;
DE Short=ObaCAD1;
DE EC=1.1.1.195;
GN Name=CAD1;
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 to
CC produce geranial at half the efficiency compared with its activity with
CC cinnamyl alcohol. Does not use nerol and neral as substrates.
CC {ECO:0000269|PubMed:16150417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.195;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: 60% inhibition by 5 mM Ca(+), Mg(+) or Cu(+).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=46 uM for cinnamyl alcohol {ECO:0000269|PubMed:16150417};
CC KM=72 uM for geraniol {ECO:0000269|PubMed:16150417};
CC Vmax=13 pmol/sec/ug enzyme toward cinnamyl alcohol
CC {ECO:0000269|PubMed:16150417};
CC Vmax=9.8 pmol/sec/ug enzyme toward geraniol
CC {ECO:0000269|PubMed:16150417};
CC pH dependence:
CC Optimum pH is 8.9. Active from pH 8.5 to 9.4.
CC {ECO:0000269|PubMed:16150417};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, mainly in peltate glands.
CC {ECO:0000269|PubMed:16150417}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AY879285; AAX83108.1; -; mRNA.
DR AlphaFoldDB; Q2KNL5; -.
DR SMR; Q2KNL5; -.
DR BioCyc; MetaCyc:MON-13799; -.
DR SABIO-RK; Q2KNL5; -.
DR UniPathway; UPA00711; -.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IEA:UniProtKB-UniPathway.
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..357
FT /note="Cinnamyl alcohol dehydrogenase 1"
FT /id="PRO_0000367053"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 188..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 211..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 298..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 357 AA; 38769 MW; 0A0CED8EDE0736A7 CRC64;
MGSLEVERKT VGWAARDPSG VLSPYEYTLR NTGPQDVYVE VMCCGICHTD VHQIKNDLGM
SNYPMVPGHE VVGEVVEVGS EVTKFRAGDV VGVGCIVGSC GNCRPCNSDI EQYCNKKIWS
YNDVYPDGKP TQGGFAGAMV VDQKFVVKIP DGMAPEQAAP LLCAGVTVYS PLNHFGLKQS
GLRGGILGLG GVGHMGVKIA KAMGHHVTVI SSSDKKRAEA LDHLGADDYL VSSDAARMQE
AADSLDYIID TVPVFHPLEP YLSLLKIDGK LILMGVVNTP LQFVSPMVML GRKSITGSFI
GSMKELAEML EFCKEKDLSS TIEIVKMDYI NTAFERLEKN DVRYRFVVDV AGSKLYQ
