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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 (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
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 – 129Combined sources
Beta strandi17 – 193Combined sources
Helixi22 – 243Combined sources
Beta strandi25 – 339Combined sources
Beta strandi43 – 519Combined sources
Helixi54 – 607Combined sources
Beta strandi78 – 9013Combined sources
Beta strandi98 – 11114Combined sources
Beta strandi118 – 1203Combined sources
Helixi127 – 1315Combined sources
Turni132 – 1343Combined sources
Helixi136 – 14611Combined sources
Turni147 – 1493Combined sources
Beta strandi156 – 1616Combined sources
Helixi167 – 17711Combined sources
Beta strandi180 – 1878Combined sources
Helixi188 – 1969Combined sources
Beta strandi201 – 2055Combined sources
Helixi206 – 2083Combined sources
Helixi212 – 2198Combined sources
Beta strandi224 – 2318Combined sources
Helixi234 – 2407Combined sources
Beta strandi243 – 2519Combined sources
Helixi255 – 2573Combined sources
Helixi271 – 2744Combined sources
Beta strandi278 – 2814Combined sources
Helixi284 – 2907Combined sources
Helixi291 – 30313Combined sources
Beta strandi311 – 3166Combined sources
Helixi317 – 3193Combined sources
Helixi320 – 3267Combined sources
Helixi327 – 3293Combined sources
Beta strandi333 – 3397Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB036735 mRNA. Translation: BAA89423.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 29, 2014
This is version 55 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