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Reviewed, UniProtKB/Swiss-Prot Q9LTV6 (DECR2_ARATH)

Last modified June 16, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxisomal 2,4-dienoyl-CoA reductase
    EC=1.3.1.34
Gene names
Ordered Locus Names: At3g12800
ORF Names: MBK21.23
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA By similarity.

Catalytic activity

Trans-2,3-didehydroacyl-CoA + NADP+ = trans,trans-2,3,4,5-tetradehydroacyl-CoA + NADPH.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily.

Caution

Was originally assigned as At3g12790.

Ontologies

Keywords
   Cellular componentPeroxisome
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from direct assay. Source: TAIR

plasma membrane

Inferred from direct assay. Source: TAIR

   Molecular function2,4-dienoyl-CoA reductase (NADPH) activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Peroxisomal 2,4-dienoyl-CoA reductase
PRO_0000054564

Regions

Nucleotide binding17 – 4125NADP By similarity
Motif296 – 2983Microbody targeting signal Potential

Experimental info

Sequence conflict1271M → L in BAD44394. Ref.3
Sequence conflict238 – 2392MA → IT in BAD43663. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9LTV6-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5606E22FC53D4F0A

FASTA29831,796
        10         20         30         40         50         60 
MDSPFKPDVV RGQVALITGG GSGIGFEISS QFGKHGASIA IMGRRKQVLD DAVSALRSLG 

        70         80         90        100        110        120 
IQAIGLEGDV RKQEDARRVV EATFQHFGKL DILVNAAAGN FLAAAEDLSP NGFRTVLDID 

       130        140        150        160        170        180 
AVGTFNMCHA ALKYLKKGAP GRDSSSGGGS IINISATLHY TASWYQIHVS AAKAAVDATT 

       190        200        210        220        230        240 
RNLALEWGTD YDIRVNGIAP GPIGGTPGMS KLVPEEIENK TREYMPLYKV GEKWDIAMAA 

       250        260        270        280        290 
LYLSCDSGKY VSGLTMVVDG GLWLSKPRHL PKEAVKQLSR AVEKRSRAKP VGLPTSKL 

« Hide

References

[1]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed: 10819329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[3]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.

Cross-references

Sequence databases

AB024033 Genomic DNA. Translation: BAB02424.1.
AY072396 mRNA. Translation: AAL62388.1.
AY114700 mRNA. Translation: AAM48019.1.
AK175259 mRNA. Translation: BAD43022.1.
AK175900 mRNA. Translation: BAD43663.1.
AK176181 mRNA. Translation: BAD43944.1.
AK176305 mRNA. Translation: BAD44068.1.
AK176508 mRNA. Translation: BAD44271.1.
AK176631 mRNA. Translation: BAD44394.1.
AK176892 mRNA. Translation: BAD44655.1.
AK176909 mRNA. Translation: BAD44672.1.
AK176776 mRNA. Translation: BAD44539.1.
AK221326 mRNA. Translation: BAD94126.1.
IPIIPI00548046.
RefSeqNP_187886.2.
UniGeneAt.47252

3D structure databases

HSSPHSSP built from PDB template 2HSD based on UniProtKB P19992.
ModBaseSearch...

Proteomic databases

PRIDEQ9LTV6.

Genome annotation databases

GeneID820462.
GenomeReviewsGene locus AT3G12800 in contig BA000014_GR.
KEGGath:AT3G12800.
NMPDRfig|3702.1.peg.13360.

Organism-specific databases

TAIRAt3g12800.

Phylogenomic databases

OMAQ9LTV6. NKTEIAH.

Enzyme and pathway databases

BRENDA1.3.1.34. 302.

Gene expression databases

GermOnlineAT3G12800. Arabidopsis thaliana.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDECR2_ARATH
AccessionPrimary (citable) accession number: Q9LTV6
Secondary accession number(s): Q67Y37, Q680G7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents