ATTY_BOVIN
ID ATTY_BOVIN Reviewed; 447 AA.
AC Q58CZ9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 for phenylalanine (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 2/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; BT021798; AAX46645.1; -; mRNA.
DR RefSeq; NP_001029762.1; NM_001034590.1.
DR RefSeq; XP_005218712.1; XM_005218655.3.
DR AlphaFoldDB; Q58CZ9; -.
DR SMR; Q58CZ9; -.
DR STRING; 9913.ENSBTAP00000002866; -.
DR PaxDb; Q58CZ9; -.
DR Ensembl; ENSBTAT00000002866; ENSBTAP00000002866; ENSBTAG00000002214.
DR GeneID; 533481; -.
DR KEGG; bta:533481; -.
DR CTD; 6898; -.
DR VEuPathDB; HostDB:ENSBTAG00000002214; -.
DR VGNC; VGNC:35616; TAT.
DR eggNOG; KOG0259; Eukaryota.
DR GeneTree; ENSGT00940000156704; -.
DR InParanoid; Q58CZ9; -.
DR OrthoDB; 734452at2759; -.
DR UniPathway; UPA00139; UER00338.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000002214; Expressed in liver and 87 other tissues.
DR ExpressionAtlas; Q58CZ9; baseline.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0016597; F:amino acid binding; ISS:AgBase.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
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; ISS:AgBase.
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: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 2: Evidence at transcript level;
KW Aminotransferase; Phenylalanine catabolism; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Transferase; Tyrosine catabolism.
FT CHAIN 1..447
FT /note="Tyrosine aminotransferase"
FT /id="PRO_0000247537"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17735"
SQ SEQUENCE 447 AA; 49691 MW; A26B57A6B8CF656E CRC64;
MQDHGSLPSV LDVHVNVAGR SSVLGKVKSR KARWSVRPSD MSNKTFNPIR AIVDNMKVKP
NPNKTMIALS IGDPTVFGNL PTDPEVTQAM KDALDSGKFN GYVPSIGYLS SREEVASYYH
CPEAPLEAKD VILTSGCSQA IELCLAVLAN PGQNILVPRP GFSLYRTLAE SMGIEVKLYN
LLPEKNWEID LKQLESLIDE KTVCLIVNNP SNPCGSVFSR RHLQKILAVA ARQCVPILAD
EIYGDMVFSD SKFEPLATLS SKVPILSCGG LAKRWLVPGW RMGWILIHDR RDIFGNEIRD
GLTKLSQRIL GPCTLVQGAL KSILCRTPRV FYHNTLSFLK SNADLCYGAL AAIPGLRPIH
PSGAMYLMVG IEMEHFPEFE NDVEFTEQLV AEQSVHCLPA TCFEYPNFFR VVITVPEVMM
LEACSRIQEF CEQHYHCAEG SQEECDK