Reviewed,
UniProtKB/Swiss-Prot Q9LMR3 (TYRA2_ARATH)
Last modified
June 16, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Arogenate dehydrogenase 2, chloroplastic EC=1.3.1.78 Alternative name(s): TyrAAT2 | ||||||
| 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 | 358 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Involved in the biosynthesis of tyrosine. Has a weak prephenate dehydrogenase activity. Ref.5 |
| Catalytic activity | L-arogenate + NADP+ = L-tyrosine + NADPH + CO2. |
| Pathway | Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from L-arogenate: step 1/1. |
| Subcellular location | |
| Tissue specificity | Expressed in roots, stems, leaves, flowers, siliques and seeds. More abundant in seeds. |
| Induction | Strongly inhibited by tyrosine. |
| Miscellaneous | Unlike TYRAAT1, TYRAAT2 is composed of a single catalytically active domain. |
| Sequence similarities | Contains 1 prephenate/arogenate dehydrogenase domain. |
| biophysicochemical properties | Kinetic parameters: NADP increases the apparent affinity for arogenate. KM=14.3 µM for NADP KM=84.2 µM for arogenate KM=17000 µM for prephenate Vmax=73 µmol/min/mg enzyme |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Aromatic amino acid biosynthesis Tyrosine biosynthesis |
| Cellular component | Chloroplast Plastid |
| Domain | Transit peptide |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tyrosine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | chloroplast Inferred from direct assay. Source: TAIR |
| Molecular function | arogenate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro prephenate dehydrogenase (NADP+) activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 35 | 35 | Chloroplast Potential | ||||||
| Chain | 36 – 358 | 323 | Arogenate dehydrogenase 2, chloroplastic | PRO_0000269678 | |||||
Regions | |||||||||
| Domain | 59 – 338 | 280 | Prephenate/arogenate dehydrogenase | ||||||
| Compositional bias | 348 – 358 | 11 | Ser-rich | ||||||
Experimental info | |||||||||
| Sequence conflict | 222 | 1 | V → F in AAM74497. Ref.3 | ||||||
| Sequence conflict | 222 | 1 | V → F in BAD95346. Ref.3 | ||||||
| Sequence conflict | 222 | 1 | V → F in AAN18135. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase with two highly similar and active protein domains." Rippert P., Matringe M. Plant Mol. Biol. 48:361-368(2002) [PubMed: 11905963] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia. |
| [2] | "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. Davis R.W.Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | "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. |
| [4] | "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 (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [5] | "Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana." Rippert P., Matringe M. Eur. J. Biochem. 269:4753-4761(2002) [PubMed: 12354106] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. |
| [6] | "Tyrosine and phenylalanine are synthesized within the plastids in Arabidopsis." Rippert P., Puyaubert J., Grisollet D., Derrier L., Matringe M. Plant Physiol. 149:1251-1260(2009) [PubMed: 19136569] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
Cross-references
Sequence databases | |
|---|---|
| AF434682 mRNA. Translation: AAL30406.1. AE005172 Genomic DNA. Translation: AAF82141.1. AK221665 mRNA. Translation: BAD95346.1. AY123984 mRNA. Translation: AAM74497.1. BT000566 mRNA. Translation: AAN18135.1. | |
| IPI | IPI00546018. |
| PIR | C86291. |
| RefSeq | NP_173023.1. |
| UniGene | At.26593 |
3D structure databases | |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9LMR3. |
Genome annotation databases | |
| GeneID | 838140. |
| GenomeReviews | Gene locus AT1G15710 in contig CT485782_GR. |
| KEGG | ath:AT1G15710. |
| NMPDR | fig|3702.1.peg.1877. |
Organism-specific databases | |
| TAIR | At1g15710. |
Phylogenomic databases | |
| OMA | Q9LMR3. MVEMSCE. |
Enzyme and pathway databases | |
| BRENDA | 1.3.1.78. 302. |
Family and domain databases | |
| InterPro | IPR012070. Arogenate/prephenate_DH_pln. IPR003099. Prephen_DH. [Graphical view] |
| Pfam | PF02153. PDH. 1 hit. [Graphical view] |
| PIRSF | PIRSF036577. PDH_ADH_plant. 1 hit. |
| PROSITE | PS51176. PDH_ADH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TYRA2_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9LMR3 Secondary accession number(s): Q8L7Z4 | ||||||||
| 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 |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


