TAT1_ARATH
ID TAT1_ARATH Reviewed; 449 AA.
AC Q67Y55; O49451;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable aminotransferase TAT1;
DE EC=2.6.1.-;
DE AltName: Full=Tyrosine aminotransferase 1;
GN OrderedLocusNames=At4g28420; ORFNames=F20O9.100;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q67Y55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q67Y55-2; Sequence=VSP_041762, VSP_041763;
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AL021749; CAA16881.1; -; Genomic_DNA.
DR EMBL; AL161572; CAB79644.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85484.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85485.1; -; Genomic_DNA.
DR EMBL; AY142527; AAN13070.1; -; mRNA.
DR EMBL; AK176613; BAD44376.1; -; mRNA.
DR PIR; T04612; T04612.
DR RefSeq; NP_001031739.1; NM_001036662.2. [Q67Y55-1]
DR RefSeq; NP_194571.1; NM_118984.3. [Q67Y55-2]
DR AlphaFoldDB; Q67Y55; -.
DR SMR; Q67Y55; -.
DR STRING; 3702.AT4G28420.2; -.
DR PaxDb; Q67Y55; -.
DR PRIDE; Q67Y55; -.
DR ProteomicsDB; 234189; -. [Q67Y55-1]
DR EnsemblPlants; AT4G28420.1; AT4G28420.1; AT4G28420. [Q67Y55-2]
DR EnsemblPlants; AT4G28420.2; AT4G28420.2; AT4G28420. [Q67Y55-1]
DR GeneID; 828959; -.
DR Gramene; AT4G28420.1; AT4G28420.1; AT4G28420. [Q67Y55-2]
DR Gramene; AT4G28420.2; AT4G28420.2; AT4G28420. [Q67Y55-1]
DR KEGG; ath:AT4G28420; -.
DR Araport; AT4G28420; -.
DR TAIR; locus:2121407; AT4G28420.
DR eggNOG; KOG0259; Eukaryota.
DR HOGENOM; CLU_017584_4_2_1; -.
DR InParanoid; Q67Y55; -.
DR OMA; FETEHDE; -.
DR OrthoDB; 734452at2759; -.
DR PhylomeDB; Q67Y55; -.
DR BioCyc; ARA:AT4G28420-MON; -.
DR BRENDA; 2.6.1.5; 399.
DR PRO; PR:Q67Y55; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q67Y55; baseline and differential.
DR Genevisible; Q67Y55; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006572; P:tyrosine catabolic process; IBA:GO_Central.
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 Alternative splicing; Aminotransferase; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..449
FT /note="Probable aminotransferase TAT1"
FT /id="PRO_0000412725"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 368..389
FT /note="TKLKLPLLEDIEDDMDFCMKLA -> VPPPTSLILFHDSRSIWMILIS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_041762"
FT VAR_SEQ 390..449
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_041763"
SQ SEQUENCE 449 AA; 49782 MW; 07DEE210466AE55A CRC64;
MNHNSNLVLP SHQTETQTQD ETDISVWRFR GSDNAAKASS VTMRVIVYKL FDECSLDVKK
PLLPLAHGDP SVYPCYRTSI LVENAVVDVL RSGKGNSYGP AAGILPARQA VADYVNRDLT
NKVKPNDVFI TVGCNQGIEV VLQSLARPNA NILLPRPSYP HYEARAVYSG LEVRKFDLLP
EKEWEIDLPG IEAMADENTV AMVIINPNNP CGNVYSYDHL KKVAETAKKL GIMVITDEVY
CQTIFGDKPF VPMGEFSSIT PVITLGGISK GWIVPGWRIG WIALNDPRGI LKSTGMVQSI
QQNLDITPDA TTIVQAALPE ILGKANKELF AKKNSMLKQN VELVCDRLKE IPCLVCNKKP
ESCTYLLTKL KLPLLEDIED DMDFCMKLAK EENLVLLPGV ALGLKNWIRI TIGVEAQMLE
DALERLNGFC KRHLKKTESS FQALSNGKI
