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Database: UniProt
Entry: F4P7B9_BATDJ
LinkDB: F4P7B9_BATDJ
Original site: F4P7B9_BATDJ 
ID   F4P7B9_BATDJ            Unreviewed;       415 AA.
AC   F4P7B9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Tyrosine aminotransferase {ECO:0000256|ARBA:ARBA00015959};
DE            EC=2.6.1.5 {ECO:0000256|ARBA:ARBA00012749};
DE   AltName: Full=L-tyrosine:2-oxoglutarate aminotransferase {ECO:0000256|ARBA:ARBA00031696};
GN   ORFNames=BATDEDRAFT_20168 {ECO:0000313|EMBL:EGF79082.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF79082.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF79082.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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   -!- 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}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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   EMBL; GL882887; EGF79082.1; -; Genomic_DNA.
DR   RefSeq; XP_006680292.1; XM_006680229.1.
DR   AlphaFoldDB; F4P7B9; -.
DR   STRING; 684364.F4P7B9; -.
DR   GeneID; 18237467; -.
DR   HOGENOM; CLU_017584_4_2_1; -.
DR   InParanoid; F4P7B9; -.
DR   OMA; MDYGWIE; -.
DR   OrthoDB; 5474881at2759; -.
DR   UniPathway; UPA00139; UER00338.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006572; P:tyrosine catabolic process; IBA:GO_Central.
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   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRNR:PIRNR000517};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT   DOMAIN          36..396
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000517-1"
SQ   SEQUENCE   415 AA;  45692 MW;  81D9AE32D66CC44F CRC64;
     MTSQPIKPSI VSMRTSNPIR AIVDSLKVTP NPAKSMLSLA LGDPTTFGNY KLHQSCVDAV
     KNKLDAYSAN GYPPSIGTVA ARTSIAAKYT HPNAPLTADD IILASGCSDA LNLCIGVLCD
     EGKNILLPMP GFPLYETLAS SKGVSTRFYH LQPHNNWQVD LAHLESQIDE NTACIVVNNP
     SNPCGSVYTK EHLIAILDIA ERHHLPIIAD EIYADMAFKP HEFFSMASLT TNVPILSTGG
     IAKKYLVPGW RVGWLFIHDR HNKFSEIRKG LVNLSQLILG ANSLIQAAIP EILAAPQSFY
     DDTMKQLEES SHLSQELLKG IPGLCPVFPQ GAMYLMIELK LEEFDGIKDD VDFVEKLVEE
     ESVLLLPGKC FRCPGPFVRI VLTPPKDQLE TAYQRIRAFC ERHQSAASIE KQKAK
//
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