ID A0A182W564_9DIPT Unreviewed; 447 AA.
AC A0A182W564;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN005477-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN005477-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN005477-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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|ARBA:ARBA00007441,
CC ECO:0000256|PIRNR:PIRNR000517}.
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DR AlphaFoldDB; A0A182W564; -.
DR STRING; 112268.A0A182W564; -.
DR EnsemblMetazoa; AMIN005477-RA; AMIN005477-PA; AMIN005477.
DR VEuPathDB; VectorBase:AMIN005477; -.
DR OrthoDB; 5474881at2759; -.
DR UniPathway; UPA00139; UER00338.
DR Proteomes; UP000075920; 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; 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 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.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR000517};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT DOMAIN 58..418
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000517-1"
SQ SEQUENCE 447 AA; 49917 MW; 3CDB633EAB1491E2 CRC64;
MKDLVDLPTT LHQLNAQRPI KSKRNRWNVA ISDFARLTHN PIRAIVEGLN IQPNPNKPLI
ALSIGDPTTF GNLKPSPETV DAIRQAIDDG TSNGYAPANG HLDAREAVAR YVQHQGPVTP
NDVILCSGCS SSLDICISVL GSPGKNILIP KPGFSIYRTL AEGFGIECRT YDLLPERNWE
ADLIQLEQLI DEQTCALIVT NPGNPCGSVF PRTHLEAIVD IAERHFVPII ADEIYEHFVF
PGHEFHAVSS LSNRVPVLSC GGLTKRFLVP GWRMGWIIVH DRDGVFGEVR RGLANLSVRI
LGSNTLVQRA LPAILDNTPN DFFDDLVATL HRHAELAYKA IKQIRGLNPI MPGGAMYMMV
GIDVEHFPEF ETDLSFVEAL VHEQSVFCLP GQCFEYPNYF RLVLTVPEEM IVEAVKRLEE
FCEQHYKFDN DILLQQQNGL LNQMTQL
//