TAT_ARATH
ID TAT_ARATH Reviewed; 420 AA.
AC Q9LVY1; Q8W462;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Tyrosine aminotransferase;
DE Short=TAT;
DE EC=2.6.1.5 {ECO:0000269|PubMed:21188077};
DE AltName: Full=L-tyrosine:2-oxoglutarate aminotransferase;
GN Name=TAT; OrderedLocusNames=At5g36160; ORFNames=MAB16.11;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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] OF 168-420 AND 235-420.
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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21188077; DOI=10.1155/2010/549572;
RA Prabhu P.R., Hudson A.O.;
RT "Identification and partial characterization of an L-tyrosine
RT aminotransferase (TAT) from Arabidopsis thaliana.";
RL Biochem. Res. Int. 2010:549572-549572(2010).
CC -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts
CC tyrosine to 3-(4-hydroxyphenyl)pyruvate. Can catalyze the reverse
CC reaction, using L-glutamate in vitro. Can convert phenylalanine to
CC phenylpyruvate and catalyze the reverse reaction in vitro.
CC {ECO:0000269|PubMed:21188077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tyrosine = 3-(4-hydroxyphenyl)pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:15093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; EC=2.6.1.5;
CC Evidence={ECO:0000269|PubMed:21188077};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15094;
CC Evidence={ECO:0000305|PubMed:21188077};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15095;
CC Evidence={ECO:0000305|PubMed:21188077};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.84 mM for L-phenylalanine {ECO:0000269|PubMed:21188077};
CC KM=1.4 mM for L-glutamate {ECO:0000269|PubMed:21188077};
CC KM=0.22 mM for 3-(4-hydroxyphenyl)pyruvate
CC {ECO:0000269|PubMed:21188077};
CC KM=1.2 mM for 2-ketoglutarate {ECO:0000269|PubMed:21188077};
CC KM=0.13 mM for phenylpyruvate {ECO:0000269|PubMed:21188077};
CC KM=0.19 mM for L-tyrosine {ECO:0000269|PubMed:21188077};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 2/6.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL32903.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018112; BAA96891.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94050.1; -; Genomic_DNA.
DR EMBL; AY062825; AAL32903.1; ALT_INIT; mRNA.
DR EMBL; AY081649; AAM10211.1; -; mRNA.
DR RefSeq; NP_198465.3; NM_123007.6.
DR AlphaFoldDB; Q9LVY1; -.
DR SMR; Q9LVY1; -.
DR STRING; 3702.AT5G36160.1; -.
DR PaxDb; Q9LVY1; -.
DR PRIDE; Q9LVY1; -.
DR ProteomicsDB; 234220; -.
DR EnsemblPlants; AT5G36160.1; AT5G36160.1; AT5G36160.
DR GeneID; 833613; -.
DR Gramene; AT5G36160.1; AT5G36160.1; AT5G36160.
DR KEGG; ath:AT5G36160; -.
DR Araport; AT5G36160; -.
DR TAIR; locus:2158926; AT5G36160.
DR eggNOG; KOG0259; Eukaryota.
DR HOGENOM; CLU_017584_4_2_1; -.
DR InParanoid; Q9LVY1; -.
DR OMA; CITCPCK; -.
DR OrthoDB; 734452at2759; -.
DR PhylomeDB; Q9LVY1; -.
DR BioCyc; ARA:AT5G36160-MON; -.
DR BRENDA; 2.6.1.5; 399.
DR UniPathway; UPA00139; UER00338.
DR PRO; PR:Q9LVY1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVY1; baseline and differential.
DR Genevisible; Q9LVY1; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA: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:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:TAIR.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006572; P:tyrosine catabolic process; IDA: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 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..420
FT /note="Tyrosine aminotransferase"
FT /id="PRO_0000412724"
SQ SEQUENCE 420 AA; 46450 MW; 8B70892ADB369069 CRC64;
MGENGAKRWN FGANEVVERS NSLTIRDYLN TLINCLDGGD VRPVIPLGHG DPSPFPSFRT
DQAAVEAICD AVRSTKFNNY SSSSGVPVAR KAVAEYLSSD LSYQISPNDV HITAGCVQAI
EILISALAIP GANILLPRPT YPMYDSRAAF CQLEVRYFDL LPENGWDVDL DGVEALADDK
TVAILVINPC NPCGNVFSRQ HLQKIAETAC KLGILVIADE VYDHFAFGDK PFVSMAEFAE
LVPVIVLGAI SKRWFVPGWR LGWMVTLDPH GIMKDSGFVQ TLINVVNMST DPATFIQGAM
PDIIGNTKEE FFSSKLEMVK KCAEICYEEL MKIPCITCPC KPEGSMFTMV KLNFSLLEDI
SDDLDFCSKL AKEESMIILP GQAVGLKNWL RITFAVELEL LIEGFSRLKN FTERHSKNQP
