TAT2_ARATH
ID TAT2_ARATH Reviewed; 414 AA.
AC Q9FN30; Q8H146;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable aminotransferase TAT2;
DE EC=2.6.1.-;
DE AltName: Full=Tyrosine aminotransferase 2;
GN OrderedLocusNames=At5g53970; ORFNames=K19P17.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INDUCTION BY CORONATINE.
RX PubMed=16008101; DOI=10.1016/j.jplph.2005.04.019;
RA Hollaender-Czytko H., Grabowski J., Sandorf I., Weckermann K., Weiler E.W.;
RT "Tocopherol content and activities of tyrosine aminotransferase and cystine
RT lyase in Arabidopsis under stress conditions.";
RL J. Plant Physiol. 162:767-770(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- INDUCTION: By coronatine. {ECO:0000269|PubMed:16008101}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AB007644; BAB10727.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96434.1; -; Genomic_DNA.
DR EMBL; BT000782; AAN31921.1; -; mRNA.
DR EMBL; BT001912; AAN71911.1; -; mRNA.
DR RefSeq; NP_200208.1; NM_124776.5.
DR AlphaFoldDB; Q9FN30; -.
DR SMR; Q9FN30; -.
DR STRING; 3702.AT5G53970.1; -.
DR PaxDb; Q9FN30; -.
DR PRIDE; Q9FN30; -.
DR ProteomicsDB; 234260; -.
DR EnsemblPlants; AT5G53970.1; AT5G53970.1; AT5G53970.
DR GeneID; 835480; -.
DR Gramene; AT5G53970.1; AT5G53970.1; AT5G53970.
DR KEGG; ath:AT5G53970; -.
DR Araport; AT5G53970; -.
DR TAIR; locus:2154714; AT5G53970.
DR eggNOG; KOG0259; Eukaryota.
DR HOGENOM; CLU_017584_4_2_1; -.
DR InParanoid; Q9FN30; -.
DR OMA; RIKCFYL; -.
DR OrthoDB; 734452at2759; -.
DR PhylomeDB; Q9FN30; -.
DR BioCyc; ARA:AT5G53970-MON; -.
DR BRENDA; 2.6.1.5; 399.
DR PRO; PR:Q9FN30; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN30; baseline and differential.
DR Genevisible; Q9FN30; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006572; P:tyrosine catabolic process; IDA:TAIR.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR005958; TyrNic_aminoTrfase.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01265; tyr_nico_aTase; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..414
FT /note="Probable aminotransferase TAT2"
FT /id="PRO_0000412726"
FT CONFLICT 73
FT /note="P -> H (in Ref. 3; AAN31921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45902 MW; D8FE4EFB0F6B71FA CRC64;
MENGATTTST ITIKGILSLL MESITTEEDE GGKRVISLGM GDPTLYSCFR TTQVSLQAVS
DSLLSNKFHG YSPTVGLPQA RRAIAEYLSR DLPYKLSQDD VFITSGCTQA IDVALSMLAR
PRANILLPRP GFPIYELCAK FRHLEVRYVD LLPENGWEID LDAVEALADE NTVALVVINP
GNPCGNVYSY QHLMKIAESA KKLGFLVIAD EVYGHLAFGS KPFVPMGVFG SIVPVLTLGS
LSKRWIVPGW RLGWFVTTDP SGSFKDPKII ERFKKYFDIL GGPATFIQAA VPTILEQTDE
SFFKKTLNSL KNSSDICCDW IKEIPCIDSS HRPEGSMAMM VKLNLSLLED VSDDIDFCFK
LAREESVILL PGTAVGLKNW LRITFAADAT SIEEAFKRIK CFYLRHAKTQ YPTI