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Q9SLN8

- DBR_TOBAC

UniProt

Q9SLN8 - DBR_TOBAC

Protein

2-alkenal reductase (NADP(+)-dependent)

Gene

DBR

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Reduces the C=C double bonds of alpha, beta unsaturated enones, but has no activity on enones with an endocyclic C=C double-bond. Shows a high specificity for NADPH as the hybrid donor. Substrates are 1-nitrocyclohexene, 2-methylpentenal, trans-cinnamaldehyde, methyl-trans-2-methylcinnamaldehyde, trans-2-nonenal and 1-octen-3-one. Reduced activity with aplha-methyl transcinnamaldehyde, 1-cyclohexene-1-carboxaldehyde, methyl crotonate, (R)-pulegone, and dimethyl itaconate and no activity with maleimides, citral, (5R)- or (5S)-carvone, (S)-perillyl alcohol, and substituted cyclohexenones and cyclopentenones (PubMed:17945329, PubMed:24826896). May also act as a allyl-alcohol dehydrogenase by catalyzing the dehydrogenation of secondary allylic alcohols rather than saturated secondary alcohols. Allyl-alcohol dehydrogenase is specific for the S-stereoisomer of the alcohols (PubMed:11117876).3 Publications

    Catalytic activityi

    An n-alkanal + NADP+ = an alk-2-enal + NADPH.
    Allyl alcohol + NADP+ = acrolein + NADPH.

    Kineticsi

    kcat is 3.3 sec(-1) for (R)-pulegone at pH 7.0. kcat is 2.8 sec(-1) for (S)-pulegone at pH 7.0. kcat is 1.3 sec(-1) for NADPH at pH 7.3. kcat is 1.46 sec(-1) for 1-nitrocyclohexene at pH 7.3. kcat is 9.2 sec(-1) for 2-methylpentenal at pH 5.4. kcat is 0.66 sec(-1) for 2-methylpentenal at pH 7.3. kcat is 1.1 sec(-1) for methyl-trans-2-methylcinnamaldehyde at pH 7.3.

    1. KM=1.4 mM for (R)-pulegone (at pH 7.0)2 Publications
    2. KM=8.3 mM for (S)-pulegone (at pH 7.0)2 Publications
    3. KM=5.8 µM for NADPH (at pH 5.4)2 Publications
    4. KM=57 µM for 1-nitrocyclohexene (at pH 7.3)2 Publications
    5. KM=1032 µM for 2-methylpentenal (at pH 5.4)2 Publications
    6. KM=837 µM for 2-methylpentenal (at pH 7.3)2 Publications
    7. KM=516 µM for methyl-trans-2-methylcinnamaldehyde (at pH 7.3)2 Publications

    pH dependencei

    Optimum pH is 5.4 with 1-nitrocyclohexene as substrate.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei55 – 551SubstrateBy similarity
    Binding sitei80 – 801SubstrateBy similarity
    Binding sitei186 – 1861NADP; via amide nitrogen1 Publication
    Binding sitei190 – 1901NADP1 Publication
    Binding sitei206 – 2061NADP1 Publication
    Binding sitei230 – 2301NADP1 Publication
    Binding sitei252 – 2521NADP1 Publication
    Binding sitei258 – 2581NADP1 Publication
    Binding sitei332 – 3321NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi165 – 1662NADP1 Publication
    Nucleotide bindingi282 – 2843NADP1 Publication

    GO - Molecular functioni

    1. allyl-alcohol dehydrogenase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-alkenal reductase (NADP(+)-dependent) (EC:1.3.1.102)
    Alternative name(s):
    Alkenal double bound reductase
    Allyl-alcohol dehydrogenase (EC:1.1.1.54)
    Allylic alcohol dehydrogenase 1
    Short name:
    allyl-ADH1
    Flavin-free double bond reductase
    Short name:
    NtDBR
    Pulegone reductase
    Short name:
    NtRed-1
    Gene namesi
    Name:DBR
    OrganismiNicotiana tabacum (Common tobacco)
    Taxonomic identifieri4097 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3433432-alkenal reductase (NADP(+)-dependent)PRO_0000423024Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Structurei

    Secondary structure

    1
    343
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 129
    Beta strandi17 – 193
    Helixi22 – 243
    Beta strandi25 – 339
    Beta strandi43 – 519
    Helixi54 – 607
    Beta strandi78 – 9013
    Beta strandi98 – 11114
    Beta strandi118 – 1203
    Helixi127 – 1315
    Turni132 – 1343
    Helixi136 – 14611
    Turni147 – 1493
    Beta strandi156 – 1616
    Helixi167 – 17711
    Beta strandi180 – 1878
    Helixi188 – 1969
    Beta strandi201 – 2055
    Helixi206 – 2083
    Helixi212 – 2198
    Beta strandi224 – 2318
    Helixi234 – 2407
    Beta strandi243 – 2519
    Helixi255 – 2573
    Helixi271 – 2744
    Beta strandi278 – 2814
    Helixi284 – 2907
    Helixi291 – 30313
    Beta strandi311 – 3166
    Helixi317 – 3193
    Helixi320 – 3267
    Helixi327 – 3293
    Beta strandi333 – 3397

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HFJX-ray2.00A/B1-343[»]
    4HFMX-ray1.90A/B1-343[»]
    4HFNX-ray2.10A/B1-343[»]
    ProteinModelPortaliQ9SLN8.
    SMRiQ9SLN8. Positions 6-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9SLN8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEEVSNKQV ILKNYVTGYP KESDMEIKNV TIKLKVPEGS NDVVVKNLYL    50
    SCDPYMRSRM RKIEGSYVES FAPGSPITGY GVAKVLESGD PKFQKGDLVW 100
    GMTGWEEYSI ITPTQTLFKI HDKDVPLSYY TGILGMPGMT AYAGFHEVCS 150
    PKKGETVFVS AASGAVGQLV GQFAKMLGCY VVGSAGSKEK VDLLKSKFGF 200
    DEAFNYKEEQ DLSAALKRYF PDGIDIYFEN VGGKMLDAVL VNMKLYGRIA 250
    VCGMISQYNL EQTEGVHNLF CLITKRIRME GFLVFDYYHL YPKYLEMVIP 300
    QIKAGKVVYV EDVAHGLESA PTALVGLFSG RNIGKQVVMV SRE 343
    Length:343
    Mass (Da):38,088
    Last modified:May 1, 2000 - v1
    Checksum:i235A567096F42637
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB036735 mRNA. Translation: BAA89423.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB036735 mRNA. Translation: BAA89423.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HFJ X-ray 2.00 A/B 1-343 [» ]
    4HFM X-ray 1.90 A/B 1-343 [» ]
    4HFN X-ray 2.10 A/B 1-343 [» ]
    ProteinModelPortali Q9SLN8.
    SMRi Q9SLN8. Positions 6-343.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR013149. ADH_C.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    Pfami PF00107. ADH_zinc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "A 38 kDa allylic alcohol dehydrogenase from the cultured cells of Nicotiana tabacum."
      Hirata T., Tamura Y., Yokobatake N., Shimoda K., Ashida Y.
      Phytochemistry 55:297-303(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 85-101 AND 153-178, FUNCTION, SUBUNIT.
    2. "An enone reductase from Nicotiana tabacum: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant proteins."
      Matsushima A., Sato Y., Otsuka M., Watanabe T., Yamamoto H., Hirata T.
      Bioorg. Chem. 36:23-28(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 62-74, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    3. "Stereospecific hydrogenation of the C C double bond of enones by Escherichia coli overexpressing an enone reductase of Nicotiana tabacum."
      Hirataa T., Matsushimab A., Satoa Y., Iwasakia T., Nomuraa H., Watanabea T., Toyodaa S., Izumia S.
      J. Mol. Catal., B Enzym. 59:158-162(2009)
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    4. "Finding Sequences for over 270 Orphan Enzymes."
      Shearer A.G., Altman T., Rhee C.D.
      PLoS ONE 9:E97250-E97250(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    5. "Biocatalytic asymmetric alkene reduction: crystal structure and characterization of a double bond reductase from Nicotiana tabacum."
      Mansell D.J., Toogood H.S., Waller J., Hughes J.M.X., Levy C.W., Gardiner J.M., Scrutton N.S.
      ACS Catal. 3:370-379(2013)
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADPH AND SUBSTRATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiDBR_TOBAC
    AccessioniPrimary (citable) accession number: Q9SLN8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2013
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are no hydrogen bonds between the substrate tested and the crystalized protein (). The reduction of pulegone shows no sterospecificity and only the pro-4R hydrogen of NADPH is incorporated into the C=C double bond of pulegone (PubMed:24826896).

    Caution

    PubMed:11117876 showed an allyl-alcohol dehydrogenase activity on (2S,4S)-carveol while PubMed:17945329 and showed an exclusive enone reductase activity.Curated

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3