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Q39172 (P1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NADP-dependent alkenal double bond reductase P1

Short name=DBR1
EC=1.3.1.74
Gene names
Name:P1
Ordered Locus Names:At5g16970
ORF Names:F2K13_120
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of the 7-8 double bond of phenylpropanal substrates, such as p-coumaryl aldehyde and coniferyl aldehyde (in vitro). Has activity towards toxic substrates, such as 4-hydroxy-(2E)-nonenal (in vitro). May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)H homeostasis. Ref.4

Catalytic activity

n-alkanal + NAD(P)+ = alk-2-enal + NAD(P)H. Ref.4

Subunit structure

Homodimer. Ref.4

Sequence similarities

Belongs to the NADP-dependent oxidoreductase L4BD family.

Biophysicochemical properties

Kinetic parameters:

KM=0.53 mM for p-coumaryl aldehyde Ref.4

KM=0.41 mM for coniferyl aldehyde

KM=0.28 mM for 4-hydroxy-(2E)-nonenal

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345NADP-dependent alkenal double bond reductase P1
PRO_0000218073

Regions

Nucleotide binding166 – 1694NADP
Nucleotide binding254 – 2607NADP
Nucleotide binding284 – 2863NADP

Sites

Binding site531Substrate
Binding site811Substrate
Binding site1921NADP
Binding site2081NADP
Binding site2321NADP
Binding site3341NADP

Secondary structure

.............................................................. 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q39172 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5AFCEBB2948B2680

FASTA34538,134
        10         20         30         40         50         60 
MTATNKQVIL KDYVSGFPTE SDFDFTTTTV ELRVPEGTNS VLVKNLYLSC DPYMRIRMGK 

        70         80         90        100        110        120 
PDPSTAALAQ AYTPGQPIQG YGVSRIIESG HPDYKKGDLL WGIVAWEEYS VITPMTHAHF 

       130        140        150        160        170        180 
KIQHTDVPLS YYTGLLGMPG MTAYAGFYEV CSPKEGETVY VSAASGAVGQ LVGQLAKMMG 

       190        200        210        220        230        240 
CYVVGSAGSK EKVDLLKTKF GFDDAFNYKE ESDLTAALKR CFPNGIDIYF ENVGGKMLDA 

       250        260        270        280        290        300 
VLVNMNMHGR IAVCGMISQY NLENQEGVHN LSNIIYKRIR IQGFVVSDFY DKYSKFLEFV 

       310        320        330        340 
LPHIREGKIT YVEDVADGLE KAPEALVGLF HGKNVGKQVV VVARE 

« Hide

References

« Hide 'large scale' references
[1]"Arabidopsis thaliana NADPH oxidoreductase homologs confer tolerance of yeasts toward the thiol-oxidizing drug diamide."
Babiychuk E., Kushnir S., Belles-Boix E., van Montagu M., Inze D.
J. Biol. Chem. 270:26224-26231(1995) [PubMed: 7592828] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase At5g16970."
Youn B., Kim S.J., Moinuddin S.G., Lee C., Bedgar D.L., Harper A.R., Davin L.B., Lewis N.G., Kang C.
J. Biol. Chem. 281:40076-40088(2006) [PubMed: 17028190] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES AND NADP, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49768 mRNA. Translation: CAA89838.1.
AL391141 Genomic DNA. Translation: CAC01710.1.
CP002688 Genomic DNA. Translation: AED92364.1.
IPIIPI00542017.
PIRS57611.
RefSeqNP_197199.1. NM_121703.3.
UniGeneAt.22432.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J3HX-ray2.50A/B1-345[»]
2J3IX-ray2.80A/B1-345[»]
2J3JX-ray2.80A/B1-345[»]
2J3KX-ray2.80A/B1-345[»]
ProteinModelPortalQ39172.
SMRQ39172. Positions 1-345.
ModBaseSearch...

Protein-protein interaction databases

IntActQ39172. 1 interaction.
STRINGQ39172.

Proteomic databases

PRIDEQ39172.
ProMEXQ39172.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G16970.1; AT5G16970.1; AT5G16970.
GeneID831560.
GenomeReviewsGene locus AT5G16970 in contig BA000015_GR.
KEGGath:AT5G16970.

Organism-specific databases

TAIRAt5g16970.

Phylogenomic databases

eggNOGKOG1196.
HOGENOMHBG753318.
InParanoidQ39172.
OMAVINYRET.
PhylomeDBQ39172.
ProtClustDBCLSN2682646.

Enzyme and pathway databases

BioCycMetaCyc:AT5G16970-MONOMER.

Gene expression databases

GenevestigatorQ39172.
GermOnlineAT5G16970. Arabidopsis thaliana.

Family and domain databases

InterProIPR013149. ADH_C.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK08070.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 2 hits.
ProtoNetSearch...

Entry information

Entry nameP1_ARATH
AccessionPrimary (citable) accession number: Q39172
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: December 14, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families