ID A0A059T9L9_MORME Unreviewed; 454 AA. AC A0A059T9L9; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 25-MAY-2022, entry version 26. DE RecName: Full=Tyrosine aminotransferase {ECO:0000256|ARBA:ARBA00015959, ECO:0000256|PIRNR:PIRNR000517}; DE Short=TAT {ECO:0000256|PIRNR:PIRNR000517}; DE EC=2.6.1.5 {ECO:0000256|ARBA:ARBA00012749, ECO:0000256|PIRNR:PIRNR000517}; GN Name=Tat {ECO:0000313|EMBL:AHM92288.1}; OS Mormoops megalophylla (Ghost-faced bat) (Peter's ghost-faced bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Mormoopidae; OC Mormoops. OX NCBI_TaxID=59460 {ECO:0000313|EMBL:AHM92288.1}; RN [1] {ECO:0000313|EMBL:AHM92288.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24824435; RA Shen B., Fang T., Yang T., Jones G., Irwin D.M., Zhang S.; RT "Relaxed evolution in the tyrosine aminotransferase gene tat in old world RT fruit bats (chiroptera: pteropodidae)."; RL PLoS ONE 9:E97483-E97483(2014). CC -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts CC tyrosine to p-hydroxyphenylpyruvate. {ECO:0000256|PIRNR:PIRNR000517}. 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:0000256|ARBA:ARBA00001125, CC ECO:0000256|PIRNR:PIRNR000517}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|PIRNR:PIRNR000517, ECO:0000256|PIRSR:PIRSR000517-1}; CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation; CC acetoacetate and fumarate from L-phenylalanine: step 2/6. CC {ECO:0000256|ARBA:ARBA00005203, ECO:0000256|PIRNR:PIRNR000517}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, CC ECO:0000256|PIRNR:PIRNR000517}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441, CC ECO:0000256|PIRNR:PIRNR000517}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KJ161843; AHM92288.1; -; mRNA. DR UniPathway; UPA00139; UER00338. DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW. 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 {ECO:0000313|EMBL:AHM92288.1}; KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, KW ECO:0000256|PIRNR:PIRNR000517}; Transferase {ECO:0000313|EMBL:AHM92288.1}; KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}. FT DOMAIN 1..40 FT /note="TAT_ubiq" FT /evidence="ECO:0000259|Pfam:PF07706" FT DOMAIN 72..434 FT /note="Aminotran_1_2" FT /evidence="ECO:0000259|Pfam:PF00155" FT MOD_RES 280 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR000517-1" SQ SEQUENCE 454 AA; 50610 MW; B905BB043A806EC8 CRC64; MDLYVIQMNG KGSLPPVLDV HVNIGGKNSL PGKGKGRKAR WSVKPSDMSN NTFNPIRAIV DSMKVKPNPD KPMISLSIGD PTVFGNLPTD PEVTQAMKDA LDSGKYNGYA PSIGYLSSRE EIASYYHCPE APLEAKDVIL TSGCSQAIEL CLAVLANPGQ NILVPRPGFS LYRTLAESLG VEVRFYNLLP EKSWEIDLKQ LESLIDEKTA CLIINNPSNP CGSVFRRSHL QKILAVAARQ CVPILADEIY ADMVFSDSKF EPLANLSSDV PILSCGGLAK RWLVPGWRLG WILIHDRRDI FGNEIRDGLV KLSQRILGPC TIVQGALKSI LRRTPREFYH NTLSFLKSSA DLCYGALAAI PGLRPIRPLG AMYLMVEIEM EHFPEFENDE EFTERLIAEQ SVQLLPAKCF EYPNFFRVVI TVPEVMMLEA CSRIQEFCEQ HYHCAEGSQE ECDK //