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Database: UniProt
Entry: A0A1J4P4P7_9ACTN
LinkDB: A0A1J4P4P7_9ACTN
Original site: A0A1J4P4P7_9ACTN 
ID   A0A1J4P4P7_9ACTN        Unreviewed;       472 AA.
AC   A0A1J4P4P7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OIJ68445.1};
GN   ORFNames=WN71_008490 {ECO:0000313|EMBL:OIJ68445.1};
OS   Streptomyces mangrovisoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1428628 {ECO:0000313|EMBL:OIJ68445.1, ECO:0000313|Proteomes:UP000034196};
RN   [1] {ECO:0000313|EMBL:OIJ68445.1, ECO:0000313|Proteomes:UP000034196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC149T {ECO:0000313|Proteomes:UP000034196};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Streptomyces mangrovisoli MUSC 149.";
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   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:OIJ68445.1}.
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DR   EMBL; LAVA02000016; OIJ68445.1; -; Genomic_DNA.
DR   RefSeq; WP_046582072.1; NZ_LAVA02000016.1.
DR   AlphaFoldDB; A0A1J4P4P7; -.
DR   STRING; 1428628.WN71_008490; -.
DR   Proteomes; UP000034196; 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:UniProt.
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; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:OIJ68445.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034196};
KW   Transferase {ECO:0000313|EMBL:OIJ68445.1}.
SQ   SEQUENCE   472 AA;  51560 MW;  EB2C6D56D94DFAC0 CRC64;
     MNSLISTEEC ERMPIARMHE LYRRHVSSGQ VTLLSAFGFG RDAVDSASGC WITLRDGRRV
     LDFTGGIGVL NHGHNHPRIL AARRRFQELQ RMEVHKNYFS PYVAALGHNL SQLLPADLDV
     SYFPNSGAEA VEGALKMAYK YHRGHRGTVL HSDIAFHGKL LGAGSLTTSP EVHFSFPKIP
     GTDSFAFDDL PSLRLALERH TTPEGGSDVY ALVLEPFSAS SLRECSPEFL REARRLCTEH
     DIVLIFDEVY TSWGRTGSLF HFMRHPGLVP DVVTTSKSFG GGKASISGYV AREPVFRRAY
     DSLPDATLHS TTYYGFGEET VTALEAVAIT VEDDYPARAR RLGARLHRGL TTLAAGHPHL
     VAEVRGTGAL HGVVLRHGPA ALDHALRLLP SSFARDPQAR AKLATAAVVA DLYRSHGVLT
     YYGSNHDLPL IAAPPLVAED SDVDLFLEAL DATLAKGMPR LLAGLVREKV AA
//
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