ID   GLADA_STRSD             Reviewed;         416 AA.
AC   Q2MF12;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Putative L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase;
DE            Short=Putative L-glutamine:amino-DOI aminotransferase;
DE            EC=2.6.1.101;
GN   Name=tobS2;
OS   Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 /
OS   CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1)
OS   (Streptomyces tenebrarius).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Streptoalloteichus.
OX   NCBI_TaxID=1933;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Comparison of the gene clusters for the biosynthesis of the aminoglycoside
RT   antibiotics tobramycin-apramycin (Streptomyces tenebrarius DSM 40477), and
RT   hygromycin B (Streptomyces hygroscopicus subsp. hygroscopicus DSM 40578).";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transamination of 3-amino-2,3-dideoxy-scyllo-
CC       inosose (amino-DOI) into 2-deoxystreptamine (DOS). {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-amino-2,3-dideoxy-scyllo-inosose + L-glutamine = 2-
CC         deoxystreptamine + 2-oxoglutaramate; Xref=Rhea:RHEA:34151,
CC         ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:65002,
CC         ChEBI:CHEBI:65069; EC=2.6.1.101;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC       biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 4/4.
CC   -!- PATHWAY: Antibiotic biosynthesis; tobramycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. L-glutamine:2-deoxy-
CC       scyllo-inosose/scyllo-inosose aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ810851; CAH18560.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF12; -.
DR   SMR; Q2MF12; -.
DR   UniPathway; UPA00907; UER00924.
DR   UniPathway; UPA00971; -.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; PTHR30244; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..416
FT                   /note="Putative L-glutamine:3-amino-2,3-dideoxy-scyllo-
FT                   inosose aminotransferase"
FT                   /id="PRO_0000234051"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  46095 MW;  1F5AD15F82E42665 CRC64;
     MTSELALFGG TPVRTEPFPD GPRFRERDLE RIREVLESGS LGGIPFPNRT HRAFAEQFCG
     RLGARHGVLV ANGTVSLSVA LRALGVHAGD EVITTGYTWM GTAASIVHIN AVPVLVDIDP
     NTWCIDPAAV EAAITPRTRA IVPVHLANQI ADLDALLEIA RKHDLVVLED CAHAHFAEWR
     GRCVGTHGDA GSFSFESSKI MTSGEGGFLV SGDETTHHRA MSLVNCGRKE EGYDSFEGRM
     LGWNNRATEL QAAFLIGQVE QHDELHAQRK SNVELLTKGL TEIGGFTPVG DDDPRVTRRQ
     YYEVLYRFDP EQWAGVHRDR VLEALLAEGV EFEGITFYPP LHRDSLFTVS AEDWPMIRDR
     YGDRMGPEDF HLPVSERAAY DESVWVHHSL LTGPATDVDQ ILEAVAKVRR NVDALR