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Database: UniProt
Entry: T1KD99_TETUR
LinkDB: T1KD99_TETUR
Original site: T1KD99_TETUR 
ID   T1KD99_TETUR            Unreviewed;       441 AA.
AC   T1KD99;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=107363316 {ECO:0000313|EnsemblMetazoa:tetur09g02170.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur09g02170.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur09g02170.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
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|PIRNR:PIRNR000517}.
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DR   EMBL; CAEY01002011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015786020.1; XM_015930534.1.
DR   AlphaFoldDB; T1KD99; -.
DR   STRING; 32264.T1KD99; -.
DR   EnsemblMetazoa; tetur09g02170.1; tetur09g02170.1; tetur09g02170.
DR   GeneID; 107363316; -.
DR   KEGG; tut:107363316; -.
DR   eggNOG; KOG0259; Eukaryota.
DR   HOGENOM; CLU_017584_4_2_1; -.
DR   OMA; CALDLCI; -.
DR   OrthoDB; 5474881at2759; -.
DR   UniPathway; UPA00139; UER00338.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
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   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   InterPro; IPR005957; Tyrosine_aminoTrfase.
DR   NCBIfam; TIGR01264; tyr_amTase_E; 1.
DR   NCBIfam; TIGR01265; tyr_nico_aTase; 1.
DR   PANTHER; PTHR45744; TYROSINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR45744:SF2; TYROSINE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRNR:PIRNR000517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT   DOMAIN          38..400
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          414..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         246
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000517-1"
SQ   SEQUENCE   441 AA;  49083 MW;  1E2EB9C144000AB6 CRC64;
     MKSERQWDIK VSHYAQNTIN PIRQVLENLN ASPNPNKKLI PLSIGDPTVF GNLEPNNVII
     EAMVESIQSN KFNGYLPSNG IESARKAIAE YSSTNNVQVD PKDVIITSGC SHALEMAINV
     LAEPGKNILL PRPGFPLYQT LCGGLGIGMK YYNLDAEKNW EIDLDHLEAQ IDPSTVAIVY
     NNPSNPCGSV YSASHIRSFL EICEKHKVPV IADEIYEHLV FPGHKFTPIA SLTQEVPILS
     CRGTTKRFMV PGYRCGWIII HDKQERFGNP IRKGLNNLTH RIVGANSIVQ GALPKILKEI
     PDEYFQDCIS LIHANAKICY SITKRIPGLT PIMPTGAMYI MVGIDTSYFP ELSSDLHFVE
     RLMSEESIFV LPGKMFGVNG YIRIVLTVPS ELLIEACNRL ENFCLRNVIL PSNQQQNGQP
     PTTPAKPLPL PLNLRESVKV D
//
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