ID A0A1I3T353_9PSEU Unreviewed; 387 AA.
AC A0A1I3T353;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=SAMN05421835_107124 {ECO:0000313|EMBL:SFJ65578.1};
OS Amycolatopsis sacchari.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=115433 {ECO:0000313|EMBL:SFJ65578.1, ECO:0000313|Proteomes:UP000199025};
RN [1] {ECO:0000313|EMBL:SFJ65578.1, ECO:0000313|Proteomes:UP000199025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44468 {ECO:0000313|EMBL:SFJ65578.1,
RC ECO:0000313|Proteomes:UP000199025};
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 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}.
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DR EMBL; FORP01000007; SFJ65578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3T353; -.
DR STRING; 115433.SAMN05421835_107124; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000199025; 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; 3.40.640.10; 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 PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
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:SFJ65578.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199025};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:SFJ65578.1}.
FT DOMAIN 30..380
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 387 AA; 41358 MW; 6C4834F445989E3C CRC64;
MRLREVTRQQ VDSPMGEAYS LLAQRGGARD LLDLAQAAPP YPPAPEVAER LARVAADPHG
AAYTPVPGLP LLRETFAAEL SRDYGAEVDA ANVVITSGCN QAFAMTISAL AGPGDEVVLV
LPFYFNHDMW LRLNEIVPVY LEPGPDLLPR AEAAEALLSS RTRAIVLVTP GNPSGATIGG
AELAAFAALA RRHGIALIVD ETYRSFREDD GPAHALFTEP GWEDTVVSLH SFSKDLAIPG
YRVGAIVGSP ALNREVLKLL DCAAICAPRA GQEAVLTGLT SAGAWRRERV AEIARRRHAF
AAVMADRPGG FTLLSAGAFF GWVRHPFRDR PTGEVVRQLI AEYDTLVIPG TAFWPGDPGT
VRVSYSNLGP EGVAELAARL ALAGKER
//
