Q9LMR3 (TYRA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Arogenate dehydrogenase 2, chloroplastic
EC=1.3.1.78

Alternative name(s):
TyrAAT2

Gene names

Name:	TYRAAT2
Ordered Locus Names:	At1g15710
ORF Names:	F7H2.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › 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	Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from L-arogenate (NADP(+) route): step 1/1.
Subcellular location	Plastid › chloroplast Ref.7.
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 binding Inferred from electronic annotation. Source: InterPro prephenate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: InterPro prephenate dehydrogenase activity Inferred 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

	Sequence		Length	Mass (Da)
	Q9LMR3 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: DCEFA72C62D1AF78	FASTA	358	40,633
	10 20 30 40 50 60 MLLHFSPAKP LISPPNLRRN SPTFLISPPR SLRIRAIDAA QIFDYETQLK SEYRKSSALK 70 80 90 100 110 120 IAVLGFGNFG QFLSKTLIRH GHDLITHSRS DYSDAANSIG ARFFDNPHDL CEQHPDVVLL 130 140 150 160 170 180 CTSILSTESV LRSFPFQRLR RSTLFVDVLS VKEFPKALFI KYLPKEFDIL CTHPMFGPES 190 200 210 220 230 240 GKHSWSGLPF VYDKVRIGDA ASRQERCEKF LRIFENEGCK MVEMSCEKHD YYAAGSQFVT 250 260 270 280 290 300 HTMGRVLEKY GVESSPINTK GYETLLDLVE NTSSDSFELF YGLFMYNPNA LEQLERLDMA 310 320 330 340 350 FESVKKELFG RLHQQYRKQM FGGEVQSPKK TEQKLLNDGG VVPMNDISSS SSSSSSSS

References

	« Hide 'large scale' referencesShow '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. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., 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. , 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] [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. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., 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

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program