ID   GLDSA_STRSD             Reviewed;         424 AA.
AC   Q2MF17; Q70IY2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=L-glutamine:2-deoxy-scyllo-inosose aminotransferase;
DE            Short=L-glutamine:DOI aminotransferase;
DE            EC=2.6.1.100 {ECO:0000250|UniProtKB:Q6L739};
DE   AltName: Full=L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase;
DE            Short=L-glutamine:amino-DOI aminotransferase;
DE            EC=2.6.1.101 {ECO:0000250|UniProtKB:Q6L739};
GN   Name=tbmB; Synonyms=tobS1;
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].
RX   PubMed=14757238; DOI=10.1016/s0378-1097(03)00881-4;
RA   Kharel M.K., Basnet D.B., Lee H.C., Liou K., Woo J.S., Kim B.-G.,
RA   Sohng J.K.;
RT   "Isolation and characterization of the tobramycin biosynthetic gene cluster
RT   from Streptomyces tenebrarius.";
RL   FEMS Microbiol. Lett. 230:185-190(2004).
RN   [2]
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.
RN   [3]
RP   FUNCTION.
RX   PubMed=15582417; DOI=10.1016/j.bmcl.2004.10.028;
RA   Kharel M.K., Subba B., Lee H.C., Liou K., Sohng J.K.;
RT   "Characterization of L-glutamine:2-deoxy-scyllo-inosose aminotransferase
RT   (tbmB) from Streptomyces tenebrarius.";
RL   Bioorg. Med. Chem. Lett. 15:89-92(2005).
CC   -!- FUNCTION: Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-
CC       inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA) using L-
CC       glutamine as the amino donor. Also catalyzes the transamination of 3-
CC       amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA) into 2-deoxystreptamine
CC       (2-DOS). {ECO:0000269|PubMed:15582417}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-L-scyllo-inosose + L-glutamine = 2-deoxy-scyllo-
CC         inosamine + 2-oxoglutaramate; Xref=Rhea:RHEA:34147,
CC         ChEBI:CHEBI:16769, ChEBI:CHEBI:58359, ChEBI:CHEBI:64796,
CC         ChEBI:CHEBI:65003; EC=2.6.1.100;
CC         Evidence={ECO:0000250|UniProtKB:Q6L739};
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         Evidence={ECO:0000250|UniProtKB:Q6L739};
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 2/4.
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; AJ579650; CAE22472.1; -; Genomic_RNA.
DR   EMBL; AJ810851; CAH18555.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF17; -.
DR   SMR; Q2MF17; -.
DR   PRIDE; Q2MF17; -.
DR   BRENDA; 2.6.1.100; 7970.
DR   UniPathway; UPA00907; UER00922.
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..424
FT                   /note="L-glutamine:2-deoxy-scyllo-inosose aminotransferase"
FT                   /id="PRO_0000233023"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  45593 MW;  62FE7F245C2AE508 CRC64;
     MPVHLAINNG TPVRTRPWPV WPQPARGALD ALERVLRSGR WAISGPYRGI ESAERRFARD
     FAAYNGVAHC VPAASGTASL MLALESCGVG VGDEVIAPGL SWVASASTIV GVNAVPVLVD
     IDPRTLCLDP AAVEAAITPA TKAVVVVHLY SAVADLDALR AVADRHGLPL IEDCAQAHGA
     EHRGRKVGSV GDVGTFSMQH SKVLTSGEGG AAITNSAELA RRMEHLRADG RCYPDTAPAP
     GRMELVETGE LMGSNRCLSE FQAAVLVEQL RELDEQNALR RRNAELLNTL LAEQGLRPQA
     TSPGTTSRTY YVYAAELPDD AFVGLPITTV TEALTAELGF PISPAYAPLH TNRLYAPASR
     RRFALGEEHE KRIDPARFHL PVCERLTRRL ITFHHAALLG DESDMHDIAA AVAKVLRHHG
     ELRA