ID   A0A0N0ATA7_9ACTN        Unreviewed;       423 AA.
AC   A0A0N0ATA7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Aminotransferase DegT {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ADL06_22025 {ECO:0000313|EMBL:KOX23563.1};
OS   Streptomyces sp. NRRL F-6491.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX23563.1, ECO:0000313|Proteomes:UP000037743};
RN   [1] {ECO:0000313|EMBL:KOX23563.1, ECO:0000313|Proteomes:UP000037743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX23563.1,
RC   ECO:0000313|Proteomes:UP000037743};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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 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:KOX23563.1}.
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DR   EMBL; LGEE01000227; KOX23563.1; -; Genomic_DNA.
DR   RefSeq; WP_053645753.1; NZ_LGEE01000227.1.
DR   AlphaFoldDB; A0A0N0ATA7; -.
DR   PATRIC; fig|1519495.3.peg.4703; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000037743; Unassembled WGS sequence.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}.
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   423 AA;  46259 MW;  28D25BA4AE2A2A7F CRC64;
     MESAPSAVVP LGSPTRPARG SILGDDELAV IEELLRSGSP LSGGIWRERF EEAFRAHLGV
     AHALSVTSGT TALRLALHLL DLRPGDEVIA TPQTYMATVQ PLLDYGVRVR FCDVEPDSLN
     IDASRIEELI TERTRAVVMV HYGGRAADMP RIMALAERYG LTVVEDAAHA IGGSLNGRPL
     GSFGDFGIFS FHSSKNITTL GEGGMLVVRD DEHAARATAL RDNSVDAVYV PSRHTFASTS
     RPPAGAMFPA DSYTADCLML RGTGINGTLA EPAAAVGFVQ LGKLPRLQAR RRELAHRYTE
     RLAAVPGLRV PPVPEGVDHP YHLFTAFVDP ELIDRDALLD AMDAAGDPLP LRYFPLHLMP
     EWRAHGHREG ECPVAERRWF REMINIPCQP GIDDDQADQL MDRLEHALDR SWRHGRAPLG
     RTA
//