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Database: UniProt
Entry: A0A3M2MB70_9ACTN
LinkDB: A0A3M2MB70_9ACTN
Original site: A0A3M2MB70_9ACTN 
ID   A0A3M2MB70_9ACTN        Unreviewed;       370 AA.
AC   A0A3M2MB70;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:RMI46716.1};
GN   ORFNames=EBN88_00325 {ECO:0000313|EMBL:RMI46716.1};
OS   Streptomyces triticirhizae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2483353 {ECO:0000313|EMBL:RMI46716.1, ECO:0000313|Proteomes:UP000278673};
RN   [1] {ECO:0000313|EMBL:RMI46716.1, ECO:0000313|Proteomes:UP000278673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY642 {ECO:0000313|EMBL:RMI46716.1,
RC   ECO:0000313|Proteomes:UP000278673};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of actinobacteria from
RT   wheat.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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:RMI46716.1}.
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DR   EMBL; RFFJ01000001; RMI46716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2MB70; -.
DR   Proteomes; UP000278673; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:RMI46716.1};
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:RMI46716.1}.
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         181
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   370 AA;  39122 MW;  269B842A91641111 CRC64;
     MTGLPPLRAT EELSQSTLAA LAGMPDPAGA ECTTRFEHDL TEAFASRHAV SVSSGTMALH
     AALSAIGVGP GDEVLVPALT VIMTAAPVVQ LGARPVFVDS DPATLDLDYA DAAAKITART
     MAIVPVHLWG RMGDPAALRA FAAAKGLIIV EDAAQALGTS RAGVRAGTVG ATGCFSMKDG
     KLLWSGEGGF VLTDDFALAA HVRAFRSHWL TPPPGSLPQE QLAVNARLAE PLAALARANL
     RKFSALLGRR RAQTVHLLRA LREARGLTPL RPATDETWNH YAPLLHIGLP NPRAFAEHLA
     ERGVPNSTGS FRLVPCDTRP MFTSADRAPC RGAAQILDHT LALIITERDD EAVLDRYAAI
     IAREAAAWRA
//
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