ID   A0A1K1SQF0_9PSEU        Unreviewed;       388 AA.
AC   A0A1K1SQF0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=SAMN04489730_6413 {ECO:0000313|EMBL:SFW86545.1};
OS   Amycolatopsis australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW86545.1, ECO:0000313|Proteomes:UP000182740};
RN   [1] {ECO:0000313|EMBL:SFW86545.1, ECO:0000313|Proteomes:UP000182740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW86545.1,
RC   ECO:0000313|Proteomes:UP000182740};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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|RuleBase:RU000481}.
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DR   EMBL; FPJG01000006; SFW86545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1SQF0; -.
DR   STRING; 546364.SAMN04489730_6413; -.
DR   Proteomes; UP000182740; 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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE 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:SFW86545.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          68..370
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   388 AA;  41089 MW;  1B5815F3A212EA96 CRC64;
     MSPVRPTAAD PVTAGGSASA ETDPPTPAGW TRERAIEIAV AAGHAPLDLS LGVPGEPPPT
     WCRAPVSRVA AAYPASRGTL PLRVAAAGYL ARRYGITISA DAVAASTGSK EFISTAPLFL
     REVLGPTTRD TVLIPALGYP PYEVGARLAG LRVHRIPTDE QFRMRLDRLP DTVAERALCL
     WVNSPANPTG VVTELGRIVR WARERGVLVL SDEAYAETTW CDVPRTALEH GCDGVLAVQS
     MSKRSNAPGL RVGFYAGDPA VVAGLVTHRR AAGFMASSDS QAQAAMLLDD DAHAQALREM
     NKYRIRYLVS ALAVHGLPCS VPDGGMFAWL AVPDGDGVAF ARYAAERAGL IVAAGQQYGP
     AGHGHVRIAA TREVTAVRPR LELLRRDG
//