ID   ATTY_DICDI              Reviewed;         417 AA.
AC   Q54K95;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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; ORFNames=DDB_G0287515;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Transaminase involved in tyrosine breakdown. Converts
CC       tyrosine to p-hydroxyphenylpyruvate. Has much lower affinity and
CC       transaminase activity towards phenylalanine (By similarity).
CC       {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; AAFI02000102; EAL63657.1; -; Genomic_DNA.
DR   RefSeq; XP_637160.1; XM_632068.1.
DR   AlphaFoldDB; Q54K95; -.
DR   SMR; Q54K95; -.
DR   STRING; 44689.DDB0230996; -.
DR   PaxDb; Q54K95; -.
DR   EnsemblProtists; EAL63657; EAL63657; DDB_G0287515.
DR   GeneID; 8626161; -.
DR   KEGG; ddi:DDB_G0287515; -.
DR   dictyBase; DDB_G0287515; tat.
DR   eggNOG; KOG0259; Eukaryota.
DR   HOGENOM; CLU_017584_4_2_1; -.
DR   InParanoid; Q54K95; -.
DR   OMA; WRMGWII; -.
DR   PhylomeDB; Q54K95; -.
DR   Reactome; R-DDI-8963684; Tyrosine catabolism.
DR   UniPathway; UPA00139; UER00338.
DR   PRO; PR:Q54K95; -.
DR   Proteomes; UP000002195; Chromosome 5.
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: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; IPR005958; TyrNic_aminoTrfase.
DR   InterPro; IPR005957; Tyrosine_aminoTrfase.
DR   Pfam; PF00155; Aminotran_1_2; 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   3: Inferred from homology;
KW   Aminotransferase; Phenylalanine catabolism; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Tyrosine catabolism.
FT   CHAIN           1..417
FT                   /note="Tyrosine aminotransferase"
FT                   /id="PRO_0000327651"
FT   MOD_RES         249
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   417 AA;  46485 MW;  4B59356CCB02E941 CRC64;
     MQDNVSQRKW NVESSKSANN AFNPIRRIVD KGGFKPNPNK STISLSIGDP CVFGNLNILD
     YANDLLIENI KSSKFNGYPP STGYEIAREA VAKYVETPTS KLTSKDIIVA SGASGAIELA
     IGVLLNEGDN ILVPKPGFPL YECTSKTKFI NVKHYNLLEK QGFNVDLEHL RSLIDDKTKA
     ILVNNPSNPC GIVYSKQHLL DIIQVAREYC LPIIADEIYS DLTFGEHKFY PMASLTDKVP
     ILSIGGIAKR FLVPGWRLGW VAIHDRDNIF SNGRIIEGLI SLSQVILGPN SLVQSILPKL
     LDPQNTQVKE WCSTITKTLE SHSKLTVDML SKANGLKPVC SSGTMYQMIE IDCSKYEDIA
     DDNEFVGKLL EEQSVFLLQG TVFSLPNFFR IVFCAPIDKL TEAYERIIEF CETHKKK