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Database: UniProt
Entry: A0A0T2L1T8_9MICO
LinkDB: A0A0T2L1T8_9MICO
Original site: A0A0T2L1T8_9MICO 
ID   A0A0T2L1T8_9MICO        Unreviewed;       399 AA.
AC   A0A0T2L1T8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:KRA25893.1};
GN   ORFNames=ASD65_04405 {ECO:0000313|EMBL:KRA25893.1};
OS   Microbacterium sp. Root61.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA25893.1, ECO:0000313|Proteomes:UP000051216};
RN   [1] {ECO:0000313|EMBL:KRA25893.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA25893.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA25893.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA25893.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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   -!- 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:KRA25893.1}.
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DR   EMBL; LMGU01000001; KRA25893.1; -; Genomic_DNA.
DR   RefSeq; WP_056224454.1; NZ_LMGU01000001.1.
DR   AlphaFoldDB; A0A0T2L1T8; -.
DR   STRING; 1736570.ASD65_04405; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000051216; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43807; FI04487P; 1.
DR   PANTHER; PTHR43807:SF20; FI04487P; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:KRA25893.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051216};
KW   Transferase {ECO:0000313|EMBL:KRA25893.1}.
FT   DOMAIN          41..370
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   399 AA;  42495 MW;  F0D220605653B5F9 CRC64;
     MREIPGAWRR TLAGAGLMAD DGTTRPTIFA EMSALAAETG AINLGQGFPD EDGPAAVLEA
     AREAISAGAN QYPPGRGLPD LREAISEHQT RFYGLHPDPD TEVLVTAGAT EGLAAALLAL
     IDGPDDEVVV FEPYYDSYAA CVALAGGRLV TVPLQWPDFQ PDLDELRGAV NDRTRVILVN
     DPHNPTGAVF SAEVRAEVVR LAEEHDAIIV TDEVYEHLAF DGPHVPIATL PGAWERTLTL
     SSGGKTFSTT GWKIGWATGP APLVDAVLAV KQFLTYVNGA PFQPATAVGL RLPDEFFRGI
     ADTLRAKRDL LGDGLLRAGF EVSTPAGTYF TVADAAALGA EDADAFCREL PVRAGVVAIP
     LTAFVTPEHR ARYRTLVRFA ACKRVDVIED AASRLSALR
//
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