ID   A0A0F0KT45_9MICO        Unreviewed;       400 AA.
AC   A0A0F0KT45;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=RL72_02057 {ECO:0000313|EMBL:KJL23270.1};
OS   Microbacterium azadirachtae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL23270.1, ECO:0000313|Proteomes:UP000033448};
RN   [1] {ECO:0000313|EMBL:KJL23270.1, ECO:0000313|Proteomes:UP000033448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL23270.1,
RC   ECO:0000313|Proteomes:UP000033448};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC       ECO:0000256|RuleBase:RU000481}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJL23270.1}.
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DR   EMBL; JYIT01000077; KJL23270.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0KT45; -.
DR   PATRIC; fig|582680.7.peg.2105; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000033448; 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   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   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.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:KJL23270.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033448};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KJL23270.1}.
FT   DOMAIN          36..389
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   400 AA;  42748 MW;  A119971BDA828EDF CRC64;
     MTERAPLSRK LSAIAESATL KVDAKAKALK AEGKPVVSYA AGEPDFATPQ FIVDAAAEAL
     ANPANYRYTP AAGLPELREA IAAKTLRDSG LEVSPSQVIV TNGGKQSVYQ AFQAVVNPGD
     EVLLPAPYWT TYPEAIRLAD GVPVEVFAGA DQDYKVTVDQ LEAARTERTT VLVFVSPSNP
     TGSVYSAEET KAIAAWALEH GIWIVSDEIY QNLTYEGVKA TSVVEALPEV AGQTILVNGV
     AKTYAMTGWR VGWMVGPADA IKIAGNLQSH LTSNVNNVAQ RAAIAALNGP QTEAEQMREA
     FDRRRRLIVS ELSKIEGLVV PNPTGAFYVY PDVQGLLGRT WGGVTPTTSL ELADLILDQA
     EVAVVPGEAF GPSGYIRMSY ALGDDQLLEG VQRLQRLFAS
//