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UniProtKB/Swiss-Prot entry Q9LMR3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TYRA2_ARATH
Primary accession number Q9LMR3
Secondary accession number Q8L7Z4
Integrated into Swiss-Prot on January 9, 2007
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 44)
Name and origin of the protein
Protein name Arogenate dehydrogenase 2, chloroplastic [Precursor]
Synonyms EC 1.3.1.78
TyrAAT2
Gene name
Name: TYRAAT2
OrderedLocusNames: At1g15710
ORFNames: F7H2.5
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1023/A:1014018926676; PubMed=11905963 [NCBI, ExPASy, EBI, Israel, Japan]
Rippert P., Matringe M.;
"Molecular and biochemical characterization of an Arabidopsis thaliana arogenate dehydrogenase with two highly similar and active protein domains.";
Plant Mol. Biol. 48:361-368(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
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.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12354106 [NCBI, ExPASy, EBI, Israel, Japan]
Rippert P., Matringe M.;
"Purification and kinetic analysis of the two recombinant arogenate dehydrogenase isoforms of Arabidopsis thaliana.";
Eur. J. Biochem. 269:4753-4761(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF434682; AAL30406.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE005172; AAF82141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK221665; BAD95346.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY123984; AAM74497.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000566; AAN18135.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C86291; C86291.
RefSeq NP_173023.1; -.
UniGene At.26593
3D structure databases
ModBase Q9LMR3.
Organism-specific databases
TAIR At1g15710; -.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0033730; Molecular function: arogenate dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004665; Molecular function: prephenate dehydrogenase (NADP+) activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006571; Biological process: tyrosine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR012070; Arogenate/prephenate_DHase_pln.
IPR004455; NADP_OxRdtase_F420.
IPR003099; Prephen_DHase.
Graphical view of domain structure.
Pfam PF03807; F420_oxidored; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036577; PDH_ADH_plant; 1.
PROSITE PS51176; PDH_ADH; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9LMR3.
Genome annotation databases
GeneID 838140; -.
GenomeReviews CT485782_GR; AT1G15710.
KEGG ath:AT1G15710; -.
NMPDR fig|3702.1.peg.1877; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast; Complete proteome; NADP; Oxidoreductase; Plastid; Transit peptide; Tyrosine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    35  35     Chloroplast (Potential). 
CHAIN   36   358  323     Arogenate dehydrogenase 2, chloroplastic. PRO_0000269678
DOMAIN   59   338  280     Prephenate/arogenate dehydrogenase. 
COMPBIAS   348   358  11     Ser-rich. 
CONFLICT   222   222        V -> F (in Ref. 3; AAM74497/BAD95346 and 4; AAN18135). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 40633 Da [This is the MW of the unprocessed precursor] CRC64: DCEFA72C62D1AF78 [This is a checksum on the sequence]
        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 

Q9LMR3 in FASTA format

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