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Database: UniProt
Entry: A0A0Q9NTL8_9MICC
LinkDB: A0A0Q9NTL8_9MICC
Original site: A0A0Q9NTL8_9MICC 
ID   A0A0Q9NTL8_9MICC        Unreviewed;       434 AA.
AC   A0A0Q9NTL8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:KRE78907.1};
GN   ORFNames=ASG77_17770 {ECO:0000313|EMBL:KRE78907.1};
OS   Arthrobacter sp. Soil762.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE78907.1, ECO:0000313|Proteomes:UP000051715};
RN   [1] {ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|Proteomes:UP000051715};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE78907.1, ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|EMBL:KRE78907.1,
RC   ECO:0000313|Proteomes:UP000051715};
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:KRE78907.1}.
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DR   EMBL; LMSG01000002; KRE78907.1; -; Genomic_DNA.
DR   RefSeq; WP_056341894.1; NZ_LMSG01000002.1.
DR   AlphaFoldDB; A0A0Q9NTL8; -.
DR   OrthoDB; 199743at2; -.
DR   Proteomes; UP000051715; 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; PTHR42790; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42790:SF19; AROMATIC AMINO ACID AMINOTRANSFERASE DDB_G0272014; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:KRE78907.1};
KW   Transferase {ECO:0000313|EMBL:KRE78907.1}.
FT   DOMAIN          72..423
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   434 AA;  46623 MW;  648102CCAEBEABEA CRC64;
     MSHETLDAGA VQLPAEAIDA IERAATSAHR AAHPHEALFS ERAANIKQSA VRDVFDISMR
     PGLVSLAGGS PYLQSLPLER LAATAASIIA NEGLTALQYG GGQGTEELRT QICEVMAAEG
     ILDAVPQNVV ITAGSQSAQD VATKVFCNPG DVVLVENPTY VGALNTFEAY QVEVATVEMD
     DDGLVPELLE ARIAALQTAG KNIKFLYTIP NFNNPSGITL AGERRQRIVD ICRNANILVL
     EDNPYGLLRY NGTPLEPLRA ANPADVIYMG SFSKIFAPGL RIGWALVPEH LQRRYYLASE
     SVTLCPPTLN QMLVSAYLSD YDWKGQIETY RGLYAERCTA MLAALDEHMP AGTSWTSPEG
     GFFVWVTLPA GVDTYPLLQK AIDAGVVFIP GAAFTPSDSP SNKLRLAFSA VPPNAIKEGV
     RRLAPVLREA LAAL
//
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