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Q2KNL5 (CADH1_OCIBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cinnamyl alcohol dehydrogenase 1
Short name=CAD 1
Short name=ObaCAD1
EC=1.1.1.195
Gene names
Name:CAD1
OrganismOcimum basilicum (Sweet basil)
Taxonomic identifier39350 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Lamiaceae › Nepetoideae › Ocimeae › Ocimum

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the production of citral, a mixture of geranial and neral with a strong lemony scent. Reversibly oxidizes geraniol to produce geranial at half the efficiency compared with its activity with cinnamyl alcohol. Does not use nerol and neral as substrates. Ref.1

Catalytic activity

Cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

60% inhibition by 5 mM Ca+, Mg+ or Cu+.

Pathway

Aromatic compound metabolism; phenylpropanoid biosynthesis.

Subunit structure

Homodimer By similarity.

Tissue specificity

Expressed in leaves, mainly in peltate glands. Ref.1

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=46 µM for cinnamyl alcohol Ref.1

KM=72 µM for geraniol

Vmax=13 pmol/sec/µg enzyme toward cinnamyl alcohol

Vmax=9.8 pmol/sec/µg enzyme toward geraniol

pH dependence:

Optimum pH is 8.9. Active from pH 8.5 to 9.4.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357Cinnamyl alcohol dehydrogenase 1
PRO_0000367053

Regions

Nucleotide binding188 – 1936NADP By similarity
Nucleotide binding211 – 2166NADP By similarity
Nucleotide binding298 – 3003NADP By similarity

Sites

Metal binding471Zinc 1; catalytic By similarity
Metal binding691Zinc 1; catalytic By similarity
Metal binding701Zinc 1; catalytic By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1141Zinc 2 By similarity
Metal binding1631Zinc 1; catalytic By similarity
Binding site491NADP By similarity
Binding site1671NADP By similarity
Binding site2511NADP By similarity
Binding site2751NADP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KNL5 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 0A0CED8EDE0736A7

FASTA35738,769
        10         20         30         40         50         60 
MGSLEVERKT VGWAARDPSG VLSPYEYTLR NTGPQDVYVE VMCCGICHTD VHQIKNDLGM 

        70         80         90        100        110        120 
SNYPMVPGHE VVGEVVEVGS EVTKFRAGDV VGVGCIVGSC GNCRPCNSDI EQYCNKKIWS 

       130        140        150        160        170        180 
YNDVYPDGKP TQGGFAGAMV VDQKFVVKIP DGMAPEQAAP LLCAGVTVYS PLNHFGLKQS 

       190        200        210        220        230        240 
GLRGGILGLG GVGHMGVKIA KAMGHHVTVI SSSDKKRAEA LDHLGADDYL VSSDAARMQE 

       250        260        270        280        290        300 
AADSLDYIID TVPVFHPLEP YLSLLKIDGK LILMGVVNTP LQFVSPMVML GRKSITGSFI 

       310        320        330        340        350 
GSMKELAEML EFCKEKDLSS TIEIVKMDYI NTAFERLEKN DVRYRFVVDV AGSKLYQ

« Hide

References

[1]"Analysis of the enzymatic formation of citral in the glands of sweet basil."
Iijima Y., Wang G., Fridman E., Pichersky E.
Arch. Biochem. Biophys. 448:141-149(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: cv. SD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY879285 mRNA. Translation: AAX83108.1.

3D structure databases

ProteinModelPortalQ2KNL5.
SMRQ2KNL5. Positions 7-355.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13799.
SABIO-RKQ2KNL5.
UniPathwayUPA00711.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCADH1_OCIBA
AccessionPrimary (citable) accession number: Q2KNL5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 7, 2006
Last modified: May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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