ID A0A177WRE4_BATDL Unreviewed; 427 AA.
AC A0A177WRE4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BDEG_25710 {ECO:0000313|EMBL:OAJ42225.1};
OS Batrachochytrium dendrobatidis (strain JEL423).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=403673 {ECO:0000313|EMBL:OAJ42225.1, ECO:0000313|Proteomes:UP000077115};
RN [1] {ECO:0000313|EMBL:OAJ42225.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ42225.1,
RC ECO:0000313|Proteomes:UP000077115};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Cuomo C., Devon K., Jaffe D., Butler J.,
RA Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA O'Leary S., Kodira C., Zeng Q., Yandava C., Alvarado L., Longcore J.,
RA James T.;
RT "The Genome Sequence of Batrachochytrium dendrobatidis JEL423.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAJ42225.1, ECO:0000313|Proteomes:UP000077115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL423 {ECO:0000313|EMBL:OAJ42225.1,
RC ECO:0000313|Proteomes:UP000077115};
RA Cuomo C.A., Farrer R.A., James T., Longcore J., Birren B.;
RT "Lineage-specific infection strategies underlie the spectrum of fungal
RT disease in amphibians.";
RL Submitted (MAY-2016) 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; DS022307; OAJ42225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177WRE4; -.
DR STRING; 403673.A0A177WRE4; -.
DR VEuPathDB; FungiDB:BDEG_25710; -.
DR eggNOG; KOG0259; Eukaryota.
DR UniPathway; UPA00139; UER00338.
DR Proteomes; UP000077115; Unassembled WGS sequence.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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-UniPathway.
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 PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OAJ42225.1};
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:UP000077115};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAJ42225.1};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT DOMAIN 70..408
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000517-1"
SQ SEQUENCE 427 AA; 47207 MW; AEDC04A9FD16D95C CRC64;
MTSQPIKPSI VSMRTSNPIR AIVDSLKVTP NPAKSMLSLA LGDPTTFGNY KLHQRYCRMC
PTNLLSYCVD AVKNKLDAYS ANGYPPSIGT VAARTSIAAK YTHPNAPLTA DDIILASGCS
DALNLCIGVL CDEGKNILLP MPGFPLYETL ASSKGVSTRF YHLQPHNNWQ VDLAHLESQI
DENTACIVVN NPSNPCGSVY TKEHLIAILD IAERHHLPII ADEIYADMAF KPHEFFSMAS
LTTNVPILST GGIAKKYLVP GWRVGWLFIH DRHNKFSEIR KGLVNLSQLI LGANSLIQAA
IPEILAAPQS FYDDTMKQLE ESSHLSQELL KGIPGLCPVF PQGAMYLMIE LKLEEFDGIK
DDVDFVEKLV EEESVLLLPG KCFRCPGPFV RIVLTPPKDQ LETAYQRIRA FCERHQSAAS
IEKQKAK
//
