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Protein

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

Gene

DBR

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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, Ref. 3). 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.3 Publications

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)DescriptionActionsGraphical viewLength
    Binding sitei55SubstrateBy similarity1
    Binding sitei80SubstrateBy similarity1
    Binding sitei186NADP; via amide nitrogen1 Publication1
    Binding sitei190NADP1 Publication1
    Binding sitei206NADP1 Publication1
    Binding sitei230NADP1 Publication1
    Binding sitei252NADP1 Publication1
    Binding sitei258NADP1 Publication1
    Binding sitei332NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi165 – 166NADP1 Publication2
    Nucleotide bindingi282 – 284NADP1 Publication3

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.54. 3645.
    1.3.1.102. 3645.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-alkenal reductase (NADP(+)-dependent) (EC:1.3.1.1023 Publications)
    Alternative name(s):
    Alkenal double bound reductase
    Allylic alcohol dehydrogenase 11 Publication
    Short name:
    allyl-ADH11 Publication
    Flavin-free double bond reductase1 Publication
    Short name:
    NtDBR
    Pulegone reductase1 Publication
    Short name:
    NtRed-1
    Gene namesi
    Name:DBR
    OrganismiNicotiana tabacum (Common tobacco)
    Taxonomic identifieri4097 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004230241 – 3432-alkenal reductase (NADP(+)-dependent)Add BLAST343

    Proteomic databases

    PRIDEiQ9SLN8.

    PTM databases

    iPTMnetiQ9SLN8.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Structurei

    Secondary structure

    1343
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 12Combined sources9
    Beta strandi17 – 19Combined sources3
    Helixi22 – 24Combined sources3
    Beta strandi25 – 33Combined sources9
    Beta strandi43 – 51Combined sources9
    Helixi54 – 60Combined sources7
    Beta strandi78 – 90Combined sources13
    Beta strandi98 – 111Combined sources14
    Beta strandi118 – 120Combined sources3
    Helixi127 – 131Combined sources5
    Turni132 – 134Combined sources3
    Helixi136 – 146Combined sources11
    Turni147 – 149Combined sources3
    Beta strandi156 – 161Combined sources6
    Helixi167 – 177Combined sources11
    Beta strandi180 – 187Combined sources8
    Helixi188 – 196Combined sources9
    Beta strandi201 – 205Combined sources5
    Helixi206 – 208Combined sources3
    Helixi212 – 219Combined sources8
    Beta strandi224 – 231Combined sources8
    Helixi234 – 240Combined sources7
    Beta strandi243 – 251Combined sources9
    Helixi255 – 257Combined sources3
    Helixi271 – 274Combined sources4
    Beta strandi278 – 281Combined sources4
    Helixi284 – 290Combined sources7
    Helixi291 – 303Combined sources13
    Beta strandi311 – 316Combined sources6
    Helixi317 – 319Combined sources3
    Helixi320 – 326Combined sources7
    Helixi327 – 329Combined sources3
    Beta strandi333 – 339Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4HFJX-ray2.00A/B1-343[»]
    4HFMX-ray1.90A/B1-343[»]
    4HFNX-ray2.10A/B1-343[»]
    ProteinModelPortaliQ9SLN8.
    SMRiQ9SLN8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK19825.

    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.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 2 hits.
    SSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9SLN8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAEEVSNKQV ILKNYVTGYP KESDMEIKNV TIKLKVPEGS NDVVVKNLYL
    60 70 80 90 100
    SCDPYMRSRM RKIEGSYVES FAPGSPITGY GVAKVLESGD PKFQKGDLVW
    110 120 130 140 150
    GMTGWEEYSI ITPTQTLFKI HDKDVPLSYY TGILGMPGMT AYAGFHEVCS
    160 170 180 190 200
    PKKGETVFVS AASGAVGQLV GQFAKMLGCY VVGSAGSKEK VDLLKSKFGF
    210 220 230 240 250
    DEAFNYKEEQ DLSAALKRYF PDGIDIYFEN VGGKMLDAVL VNMKLYGRIA
    260 270 280 290 300
    VCGMISQYNL EQTEGVHNLF CLITKRIRME GFLVFDYYHL YPKYLEMVIP
    310 320 330 340
    QIKAGKVVYV EDVAHGLESA PTALVGLFSG RNIGKQVVMV SRE
    Length:343
    Mass (Da):38,088
    Last modified:May 1, 2000 - v1
    Checksum:i235A567096F42637
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB036735 mRNA. Translation: BAA89423.1.
    RefSeqiNP_001313179.1. NM_001326250.1.
    XP_016514079.1. XM_016658593.1.
    UniGeneiNta.1970.

    Genome annotation databases

    GeneIDi107830910.
    KEGGiag:BAA89423.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB036735 mRNA. Translation: BAA89423.1.
    RefSeqiNP_001313179.1. NM_001326250.1.
    XP_016514079.1. XM_016658593.1.
    UniGeneiNta.1970.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4HFJX-ray2.00A/B1-343[»]
    4HFMX-ray1.90A/B1-343[»]
    4HFNX-ray2.10A/B1-343[»]
    ProteinModelPortaliQ9SLN8.
    SMRiQ9SLN8.
    ModBaseiSearch...
    MobiDBiSearch...

    PTM databases

    iPTMnetiQ9SLN8.

    Proteomic databases

    PRIDEiQ9SLN8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi107830910.
    KEGGiag:BAA89423.

    Phylogenomic databases

    KOiK19825.

    Enzyme and pathway databases

    BRENDAi1.1.1.54. 3645.
    1.3.1.102. 3645.

    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.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 2 hits.
    SSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 67 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 (Ref. 4). 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 (Ref. 3).

    Caution

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.