ID   GLDSA_STREY             Reviewed;         424 AA.
AC   Q2MFP2;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-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=parS;
OS   Streptomyces paromomycinus (Streptomyces rimosus subsp. paromomycinus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=92743;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14827 / DSM 41429 / JCM 4541 / KCC S-0541 / NBRC 15454 / NRRL
RC   2455 / VKM Ac-605;
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Analysis and comparison of the biosynthetic gene clusters for the 2-
RT   deoxystreptamine-containing aminoglycoside antibiotics ribostamycin,
RT   neomycin, lividomycin, paromomycin and butirosin.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q6L739}.
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: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC       biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 4/4.
CC   -!- PATHWAY: Antibiotic biosynthesis; paromomycin 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; AJ628955; CAF32373.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MFP2; -.
DR   SMR; Q2MFP2; -.
DR   UniPathway; UPA00907; UER00922.
DR   UniPathway; UPA00907; UER00924.
DR   UniPathway; UPA00970; -.
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_0000233022"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  45105 MW;  6D7C86696A5496DF CRC64;
     MTRSLAVQGG SPVRTRPWPL WPQPAPGAVR ALDGVLTSGR WSISGPYRGA ASQERRFAQA
     FAAYNGVEHC VPAASGTASL MLAMEACGIG AGDEVIVPGL SWVASGSTVL GVNAVPVFCD
     VDPDTLCLDP AAVESALTER TKAIVVVHLY SAVAAMDALR ALADRHGLPL LEDCAQAHGA
     EYRGVKVGAL ATAGTFSMQH SKVLTSGEGG AVITRDAEFA RRVEHLRADG RCLAGQPVGD
     GQMELVETGE LMGSNRCVSE FQAALLVEQL GVLDEQNERR RRNAALLDKL LADEGYRPQT
     TSEGTSTRTY YTYAARLPEG ELTHVDAAAV GEALTAELGF PVAPCYAPIT RNRLYDPRSR
     GRFALGVQHE SRIDPKRFEL PVCEEAARRT VTVHHAALLG DESDMHDIAT AFGKVVRHGA
     LLTG