ATTY_RAT
ID ATTY_RAT Reviewed; 454 AA.
AC P04694; Q5EBB6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Tyrosine aminotransferase;
DE Short=TAT;
DE EC=2.6.1.5;
DE AltName: Full=L-tyrosine:2-oxoglutarate aminotransferase;
GN Name=Tat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT MET-1.
RX PubMed=2863382; DOI=10.1016/0022-2836(85)90386-9;
RA Grange T., Guenet C., Dietrich J.-B., Chasserot S., Fromont M., Befort N.,
RA Jami J., Beck G., Pictet R.;
RT "Complete complementary DNA of rat tyrosine aminotransferase messenger RNA.
RT Deduction of the primary structure of the enzyme.";
RL J. Mol. Biol. 184:347-350(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, COFACTOR, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=2562840; DOI=10.1016/s0021-9258(17)31222-x;
RA Hargrove J.L., Scoble H.A., Mathews W.R., Baumstark B.R., Biemann K.;
RT "The structure of tyrosine aminotransferase. Evidence for domains involved
RT in catalysis and enzyme turnover.";
RL J. Biol. Chem. 264:45-53(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 190-386.
RC TISSUE=Liver;
RX PubMed=1983704; DOI=10.3109/10425179009016044;
RA Morozov I.V.;
RT "Nucleotide sequence of rat liver tyrosine aminotransferase gene
RT fragment.";
RL DNA Seq. 1:151-155(1990).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=1682164; DOI=10.1016/0014-5793(91)81317-2;
RA Lorber B., Dietrich J.-B., Kern D.;
RT "Isolation and characterization of active N-terminal truncated apo- and
RT holoenzyme of mammalian liver tyrosine aminotransferase.";
RL FEBS Lett. 291:345-349(1991).
RN [6]
RP STRUCTURAL PROPERTIES.
RX PubMed=2901862; DOI=10.1016/0300-9084(88)90252-0;
RA Dietrich J.-B., Genot G., Beck G.;
RT "Structural and immunochemical properties of rat liver tyrosine
RT aminotransferase.";
RL Biochimie 70:673-679(1988).
CC -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts
CC tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction,
CC using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has
CC much lower affinity and transaminase activity towards phenylalanine.
CC {ECO:0000269|PubMed:1682164}.
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:1682164};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:1682164, ECO:0000269|PubMed:2562840};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for tyrosine {ECO:0000269|PubMed:1682164};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 2/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1682164}.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X02741; CAA26519.1; -; mRNA.
DR EMBL; M18340; AAA42203.1; -; mRNA.
DR EMBL; BC089813; AAH89813.1; -; mRNA.
DR EMBL; X15690; CAA33725.1; -; Genomic_DNA.
DR PIR; A23310; XNRTY.
DR RefSeq; NP_036800.1; NM_012668.2.
DR AlphaFoldDB; P04694; -.
DR SMR; P04694; -.
DR STRING; 10116.ENSRNOP00000022721; -.
DR BindingDB; P04694; -.
DR ChEMBL; CHEMBL5947; -.
DR iPTMnet; P04694; -.
DR PhosphoSitePlus; P04694; -.
DR PaxDb; P04694; -.
DR PRIDE; P04694; -.
DR Ensembl; ENSRNOT00000022721; ENSRNOP00000022721; ENSRNOG00000016348.
DR GeneID; 24813; -.
DR KEGG; rno:24813; -.
DR UCSC; RGD:3820; rat.
DR CTD; 6898; -.
DR RGD; 3820; Tat.
DR eggNOG; KOG0259; Eukaryota.
DR GeneTree; ENSGT00940000156704; -.
DR HOGENOM; CLU_017584_4_2_1; -.
DR InParanoid; P04694; -.
DR OMA; WRMGWII; -.
DR OrthoDB; 734452at2759; -.
DR PhylomeDB; P04694; -.
DR TreeFam; TF105999; -.
DR BioCyc; MetaCyc:MON-15101; -.
DR BRENDA; 2.6.1.5; 5301.
DR Reactome; R-RNO-8963684; Tyrosine catabolism.
DR SABIO-RK; P04694; -.
DR UniPathway; UPA00139; UER00338.
DR PRO; PR:P04694; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000016348; Expressed in liver and 6 other tissues.
DR Genevisible; P04694; RN.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0016597; F:amino acid binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IDA:RGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISO:RGD.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:RGD.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
DR GO; GO:0046689; P:response to mercury ion; IDA:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR GO; GO:0006572; P:tyrosine catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR011715; Tyr_aminoTrfase_ubiquitination.
DR InterPro; IPR005958; TyrNic_aminoTrfase.
DR InterPro; IPR005957; Tyrosine_aminoTrfase.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF07706; TAT_ubiq; 1.
DR PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01264; tyr_amTase_E; 1.
DR TIGRFAMs; TIGR01265; tyr_nico_aTase; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Direct protein sequencing;
KW Phenylalanine catabolism; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase; Tyrosine catabolism.
FT CHAIN 1..454
FT /note="Tyrosine aminotransferase"
FT /id="PRO_0000123889"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:2863382"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:2562840"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17735"
FT CONFLICT 59..60
FT /note="IV -> KT (in Ref. 2; AAA42203)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..210
FT /note="TA -> LE (in Ref. 2; AAA42203)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="P -> L (in Ref. 4; CAA33725)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="Missing (in Ref. 4; CAA33725)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..360
FT /note="AI -> DL (in Ref. 2; AAA42203)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="A -> D (in Ref. 2; AAA42203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 50635 MW; 835EBE0D2476AF71 CRC64;
MDSYVIQTDV DDSLSSVLDV HVNIGGRNSV QGRKKGRKAR WDVRPSDMSN KTFNPIRAIV
DNMKVQPNPN KTVISLSIGD PTVFGNLPTD PEVTQAMKDA LDSGKYNGYA PSIGYLSSRE
EVASYYHCHE APLEAKDVIL TSGCSQAIEL CLAVLANPGQ NILIPRPGFS LYRTLAESMG
IEVKLYNLLP EKSWEIDLKQ LESLIDEKTA CLVVNNPSNP CGSVFSKRHL QKILAVAERQ
CVPILADEIY GDMVFSDCKY EPLANLSTNV PILSCGGLAK RWLVPGWRLG WILIHDRRDI
FGNEIRDGLV KLSQRILGPC TIVQGALKSI LQRTPQEFYH DTLSFLKSNA DLCYGALAAI
PGLQPVRPSG AMYLMVGIEM EHFPEFENDV EFTERLIAEQ AVHCLPATCF EYPNFFRVVI
TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE ECDK
