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Q9SLN8

- DBR_TOBAC

UniProt

Q9SLN8 - DBR_TOBAC

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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

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 (1 Publication, 1 Publication). 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 (1 Publication).2 Publications

Catalytic activityi

An n-alkanal + NADP+ = an alk-2-enal + NADPH.3 Publications
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)
  3. KM=5.8 µM for NADPH (at pH 5.4)
  4. KM=57 µM for 1-nitrocyclohexene (at pH 7.3)
  5. KM=1032 µM for 2-methylpentenal (at pH 5.4)
  6. KM=837 µM for 2-methylpentenal (at pH 7.3)
  7. KM=516 µM for methyl-trans-2-methylcinnamaldehyde (at pH 7.3)

pH dependencei

Optimum pH is 5.4 with 1-nitrocyclohexene as substrate.

Sites

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

Regions

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

GO - Molecular functioni

  1. oxidoreductase activity Source: UniProtKB-KW
  2. zinc ion binding Source: InterPro
Complete GO annotation...

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.

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: September 3, 2014
This is version 53 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 (1 Publication).

Caution

1 Publication showed an allyl-alcohol dehydrogenase activity on (2S,4S)-carveol while 1 Publication and showed an exclusive enone reductase activity.

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

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