ID A0A1J6X9T5_9MICO Unreviewed; 299 AA.
AC A0A1J6X9T5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:OIU86981.1};
DE Flags: Fragment;
GN ORFNames=BFN01_10730 {ECO:0000313|EMBL:OIU86981.1};
OS Microbacterium sp. AR7-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1891970 {ECO:0000313|EMBL:OIU86981.1, ECO:0000313|Proteomes:UP000183831};
RN [1] {ECO:0000313|EMBL:OIU86981.1, ECO:0000313|Proteomes:UP000183831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR7-10 {ECO:0000313|EMBL:OIU86981.1,
RC ECO:0000313|Proteomes:UP000183831};
RA Pei D., Jiang J., Chen H., Li K., Yu W., Ma Y., Xu J.;
RT "The draft genome of Microbacterium sp. AR7-10 isolated from the wild
RT caught mosquito Anopheles.";
RL Submitted (SEP-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 ECO:0000256|RuleBase:RU003693};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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:OIU86981.1}.
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DR EMBL; MJIR01000067; OIU86981.1; -; Genomic_DNA.
DR RefSeq; WP_071643702.1; NZ_MJIR01000067.1.
DR AlphaFoldDB; A0A1J6X9T5; -.
DR STRING; 1891970.BFN01_10730; -.
DR OrthoDB; 9809616at2; -.
DR Proteomes; UP000183831; 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR PANTHER; PTHR43643:SF3; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OIU86981.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:OIU86981.1}.
FT DOMAIN 1..292
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OIU86981.1"
SQ SEQUENCE 299 AA; 31732 MW; 8C0CD28CA7209ED2 CRC64;
RYPDASAAAL RARLGEKYGV EPDAVHVAAG SVSILHQLVL GTASVGDEVV YAWRSFEAYP
SLPLVAGATG VQVPLTSGAR HDLDAMADAV TERTRVVIVC TPNNPTGPVV SSAEFAAFVA
RVPQDVLIIL DEAYAEFVTA PDAVDGLGER VFERHPNVVV LRTFSKAYGL AGLRVGYAIG
HPRVLDAART TGIPLSVTSA AERAAIASLD AEAELRERIS VIVERRTRLI GGLRTQGWQV
PDSQANFVWL PAGERTDEVA AAFDAADLIV RPFSGDGIRI SVGEEESIDR VLAVAKSLL
//
