ID   A0A1I4WB12_9ACTN        Unreviewed;       405 AA.
AC   A0A1I4WB12;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Aspartate/methionine/tyrosine aminotransferase {ECO:0000313|EMBL:SFN10119.1};
GN   ORFNames=SAMN04487980_101192 {ECO:0000313|EMBL:SFN10119.1};
OS   Streptomyces sp. cf124.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761903 {ECO:0000313|EMBL:SFN10119.1, ECO:0000313|Proteomes:UP000198530};
RN   [1] {ECO:0000313|EMBL:SFN10119.1, ECO:0000313|Proteomes:UP000198530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF124 {ECO:0000313|EMBL:SFN10119.1,
RC   ECO:0000313|Proteomes:UP000198530};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; FOUV01000011; SFN10119.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4WB12; -.
DR   Proteomes; UP000198530; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:SFN10119.1};
KW   Transferase {ECO:0000313|EMBL:SFN10119.1}.
FT   DOMAIN          45..329
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   405 AA;  42289 MW;  EE1BBA2185811654 CRC64;
     MRRTDPEGHG PVRYGPPLPG QGLPVLPELA AVLSAAAGRP HPVPLGGDPA LLDAACGYWD
     RRGLATTRDR ALAAPGAPAL LLALTAAIGG DVLLPRPCAA WWEPQARALG RSVFHVATPA
     ECGGVPDPYA LLETVRRIRA EGGDPRLLVL CVADDPTATV APPELVHETM EAALGEGLHL
     VSDETWRDTV HDPHDTVLFS PAEMLPDRVT VVSDLAGAFL PAGWPAAVAR FPANGEGAGL
     RDRVLDVLTA LGARIATPVA AAAAHALDEP APVTERLATA VRLHARLAGA AHRAVVDAGA
     LALPPRAGRH LYADLAPLRS ALAGYGVGDA QEAEDFLTDR LGMPAPGGHR FGDDLGELRV
     RLSTDAFLGT TEEDRARALT APDPLELPQV ERALTHLGAA FEDLR
//