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Q39173 (P2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADP-dependent alkenal double bond reductase P2
EC=1.3.1.74
Gene names
Name:P2
Ordered Locus Names:At5g16990
ORF Names:F2K13_140
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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) By similarity. May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)h homeostasis.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the NADP-dependent oxidoreductase L4BD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343NADP-dependent alkenal double bond reductase P2
PRO_0000218074

Regions

Nucleotide binding164 – 1674NADP By similarity
Nucleotide binding252 – 2587NADP By similarity
Nucleotide binding282 – 2843NADP By similarity

Sites

Binding site521Substrate By similarity
Binding site791Substrate By similarity
Binding site1901NADP By similarity
Binding site2061NADP By similarity
Binding site2301NADP By similarity
Binding site3321NADP By similarity

Experimental info

Sequence conflict151Missing in CAA89262. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q39173 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 491698EF58BA82DA

FASTA34337,989
        10         20         30         40         50         60 
MTTNKQVIFK DHVSGFPKES DFNFTTTTVE LRVPEGSKSV LVKNLYLSCD PYMRSRMGKP 

        70         80         90        100        110        120 
DPSSALAQAY APGKPIYGYG VSRVIESGHP DYKKGDLLWG IVGWEEYSVI TPMAHMHFKI 

       130        140        150        160        170        180 
QHTDVPLSYY TGLLGMPGMT AYAGFYEVCS PKKGETVYVS AASGAVGQLV GQFAKMMGCY 

       190        200        210        220        230        240 
VVGSAGSKEK VDLLKTKFGF DDAFNYKEES DLSAALKRCF PKGIDMYFEN VGGKMLDAVL 

       250        260        270        280        290        300 
LNMNPHGRIA VCGMISQYNL ENQEGVHNLS NIIYKRIRIQ GFVVADFYDK YPKFLELVLP 

       310        320        330        340 
RIKEGKITYV EDVADGLEKA PEALVGLFHG KNVGKQVVVI ARE

« 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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z49268 mRNA. Translation: CAA89262.1.
AL391141 Genomic DNA. Translation: CAC01712.1.
CP002688 Genomic DNA. Translation: AED92367.1.
AY091320 mRNA. Translation: AAM14259.1.
AY065253 mRNA. Translation: AAL38729.1.
IPIIPI00517835.
PIRS57612.
T51554.
RefSeqNP_197201.1. NM_121705.3.
UniGeneAt.22439.

3D structure databases

ProteinModelPortalQ39173.
SMRQ39173. Positions 3-343.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39173.

Proteomic databases

PRIDEQ39173.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G16990.1; AT5G16990.1; AT5G16990.
GeneID831562.
GenomeReviewsGene locus AT5G16990 in contig BA000015_GR.
KEGGath:AT5G16990.
NMPDRfig|3702.1.peg.23861.

Organism-specific databases

TAIRAt5g16990.

Phylogenomic databases

eggNOGKOG1196.
HOGENOMHBG753318.
InParanoidQ39173.
OMANASSEHE.
PhylomeDBQ39173.
ProtClustDBCLSN2682646.

Gene expression databases

ArrayExpressQ39173.
GenevestigatorQ39173.
GermOnlineAT5G16990. 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. 1 hit.
ProtoNetSearch...

Entry information

Entry nameP2_ARATH
AccessionPrimary (citable) accession number: Q39173
Secondary accession number(s): Q9LFK3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: December 14, 2011
This is version 87 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents