Reviewed,
UniProtKB/Swiss-Prot Q9LTV6 (DECR2_ARATH)
Last modified
June 16, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peroxisomal 2,4-dienoyl-CoA reductase EC=1.3.1.34 | ||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||
| Taxonomic identifier | 3702 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 298 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 component | Peroxisome |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | peroxisome Inferred from direct assay. Source: TAIR plasma membraneInferred from direct assay. Source: TAIR |
| Molecular function | 2,4-dienoyl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 298 | 298 | Peroxisomal 2,4-dienoyl-CoA reductase | PRO_0000054564 | |||||
Regions | |||||||||
| Nucleotide binding | 17 – 41 | 25 | NADP By similarity | ||||||
| Motif | 296 – 298 | 3 | Microbody targeting signal Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 127 | 1 | M → L in BAD44394. Ref.3 | ||||||
| Sequence conflict | 238 – 239 | 2 | MA → IT in BAD43663. Ref.3 | ||||||
Sequences
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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. 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. 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. | |
| IPI | IPI00548046. |
| RefSeq | NP_187886.2. |
| UniGene | At.47252 |
3D structure databases | |
| HSSP | HSSP built from PDB template 2HSD based on UniProtKB P19992. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9LTV6. |
Genome annotation databases | |
| GeneID | 820462. |
| GenomeReviews | Gene locus AT3G12800 in contig BA000014_GR. |
| KEGG | ath:AT3G12800. |
| NMPDR | fig|3702.1.peg.13360. |
Organism-specific databases | |
| TAIR | At3g12800. |
Phylogenomic databases | |
| OMA | Q9LTV6. NKTEIAH. |
Enzyme and pathway databases | |
| BRENDA | 1.3.1.34. 302. |
Gene expression databases | |
| GermOnline | AT3G12800. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| PANTHER | PTHR19410. ADH_short_C2. 1 hit. |
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] |
| PRINTS | PR00081. GDHRDH. PR00080. SDRFAMILY. |
| PROSITE | PS00061. ADH_SHORT. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DECR2_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9LTV6 Secondary accession number(s): Q67Y37, Q680G7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


