Q9LMR3 (TYRA2_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 83.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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) [Reference proteome] | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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.6 |
| Catalytic activity | L-arogenate + NADP+ = L-tyrosine + NADPH + CO2. |
| Pathway | |
| Subcellular location | |
| Tissue specificity | Expressed in roots, stems, leaves, flowers, siliques and seeds. More abundant in seeds. Ref.7 |
| 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 Ref.6 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | tyrosine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | chloroplast Inferred from direct assay PubMed 18431481. Source: TAIR |
| Molecular_function | arogenate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro prephenate dehydrogenase (NADP+) activityInferred from electronic annotation. Source: InterPro prephenate dehydrogenase 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.4 | ||||||
| Sequence conflict | 222 | 1 | V → F in BAD95346. Ref.4 | ||||||
| Sequence conflict | 222 | 1 | V → F in AAN18135. Ref.5 | ||||||
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] [Europe PMC] [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] [Europe PMC] [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. Ecker J.R.Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [5] | "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. |
| [6] | "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] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. |
| [7] | "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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF434682 mRNA. Translation: AAL30406.1. AC034256 Genomic DNA. Translation: AAF82141.1. CP002684 Genomic DNA. Translation: AEE29352.1. AK221665 mRNA. Translation: BAD95346.1. AY123984 mRNA. Translation: AAM74497.1. BT000566 mRNA. Translation: AAN18135.1. |
| IPI | IPI00546018. |
| PIR | C86291. |
| RefSeq | NP_173023.1. NM_101439.4. |
| UniGene | At.26593. |
3D structure databases | |
| ProteinModelPortal | Q9LMR3. |
| SMR | Q9LMR3. Positions 59-124. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9LMR3. 4 interactions. |
Proteomic databases | |
| PaxDb | Q9LMR3. |
| PRIDE | Q9LMR3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT1G15710.1; AT1G15710.1; AT1G15710. |
| GeneID | 838140. |
| KEGG | ath:AT1G15710. |
Organism-specific databases | |
| TAIR | At1g15710. |
Phylogenomic databases | |
| eggNOG | COG0287. |
| HOGENOM | HOG000242064. |
| InParanoid | Q9LMR3. |
| KO | K15227. |
| OMA | THLIAKV. |
| PhylomeDB | Q9LMR3. |
| ProtClustDB | PLN02256. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:AT1G15710-MONOMER. |
| UniPathway | UPA00122; UER00960. |
Gene expression databases | |
| Genevestigator | Q9LMR3. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR012070. Arogenate/prephenate_DH. IPR016040. NAD(P)-bd_dom. 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 program | Plant Protein Annotation Program | ||||||||
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
