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
//