TAT3_ARATH
ID TAT3_ARATH Reviewed; 445 AA.
AC Q9SK47; Q8LEN9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable aminotransferase TAT3;
DE EC=2.6.1.-;
DE AltName: Full=Tyrosine aminotransferase 3;
GN Name=TAT3; OrderedLocusNames=At2g24850; ORFNames=F27C12.23;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9342878; DOI=10.1104/pp.115.2.817;
RA Titarenko E., Rojo E., Leon J., Sanchez-Serrano J.J.;
RT "Jasmonic acid-dependent and -independent signaling pathways control wound-
RT induced gene activation in Arabidopsis thaliana.";
RL Plant Physiol. 115:817-826(1997).
RN [7]
RP INDUCTION BY WOUNDING.
RX PubMed=18247047; DOI=10.1007/s00425-008-0694-4;
RA Suza W.P., Staswick P.E.;
RT "The role of JAR1 in Jasmonoyl-L: -isoleucine production during Arabidopsis
RT wound response.";
RL Planta 227:1221-1232(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and cauline leaves.
CC {ECO:0000269|PubMed:9342878}.
CC -!- INDUCTION: By jasmonate and wounding. {ECO:0000269|PubMed:18247047,
CC ECO:0000269|PubMed:9342878}.
CC -!- MISCELLANEOUS: Induction by wounding requires COI1.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AC006585; AAD23027.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07636.1; -; Genomic_DNA.
DR EMBL; BT002475; AAO00835.1; -; mRNA.
DR EMBL; BT006593; AAP31937.1; -; mRNA.
DR EMBL; AK226395; BAE98541.1; -; mRNA.
DR EMBL; AY085324; AAM62555.1; -; mRNA.
DR PIR; C84641; C84641.
DR RefSeq; NP_180058.1; NM_128044.3.
DR AlphaFoldDB; Q9SK47; -.
DR SMR; Q9SK47; -.
DR BioGRID; 2374; 1.
DR IntAct; Q9SK47; 1.
DR STRING; 3702.AT2G24850.1; -.
DR PaxDb; Q9SK47; -.
DR PRIDE; Q9SK47; -.
DR ProteomicsDB; 234180; -.
DR EnsemblPlants; AT2G24850.1; AT2G24850.1; AT2G24850.
DR GeneID; 817022; -.
DR Gramene; AT2G24850.1; AT2G24850.1; AT2G24850.
DR KEGG; ath:AT2G24850; -.
DR Araport; AT2G24850; -.
DR TAIR; locus:2047441; AT2G24850.
DR eggNOG; KOG0259; Eukaryota.
DR HOGENOM; CLU_017584_4_2_1; -.
DR InParanoid; Q9SK47; -.
DR OMA; NDFDFCT; -.
DR OrthoDB; 734452at2759; -.
DR PhylomeDB; Q9SK47; -.
DR BioCyc; ARA:AT2G24850-MON; -.
DR PRO; PR:Q9SK47; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SK47; baseline and differential.
DR Genevisible; Q9SK47; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; ISS:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
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 Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..445
FT /note="Probable aminotransferase TAT3"
FT /id="PRO_0000412727"
FT CONFLICT 77
FT /note="A -> D (in Ref. 5; AAM62555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 48819 MW; D58AC366D558611E CRC64;
MASNGVTNCN ANANVWRFKG NGATSDAAAV TLRKLAFGMF KNCTMNSGKT ILFPTPGEPS
AHSNFRTCPE AEEAVAAAAR SGMANSYAPS PGVFKARRAV AEYLNGELPT KLKAEDVYIT
GGCNQAIEIV IDSLAGNPSA NILLPRPGYP HYDARAVYSG LEIRKYDLLP ESDWEINLDG
LEAAADENTV AMVIINPNNP CGNVYTYDHL NKVAEMARKL GIMIISDEVY DHVVYGDKPF
IPMGKFASIA PVITLGSISK GWVNPGWRVG WIAMNDPNGI FVSTGVVQAI EDFLDLTPQP
SFILQEALPD ILEKTPKEFF EKKIKAMRRN VELSCERLKD IPCLFCPKKP ESCSYLWLKL
DTSMLNNIKN DFDFCTKLVS EESLILIPGV ALGAENWVRI SIGTDESVVQ EIFDRLKGFY
DRHAISKEAI KLSGHAINQI VVSVN
