ID   GLDSA_STRLV             Reviewed;         424 AA.
AC   Q2MF71;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
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=livS;
OS   Streptomyces lividus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=282216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 844.73;
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Piepersberg W.,
RA   Welzel K., Vente A.;
RT   "Analysis and comparison of biosynthetic gene clusters for the 2-deoxy-
RT   inosamine containing aminoglycoside antibiotics ribostamycin, neomycin,
RT   lividomycin, paromomycin and butirosin.";
RL   Submitted (JUN-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: Antibiotic biosynthesis; lividomycin 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; AJ748832; CAG38696.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF71; -.
DR   SMR; Q2MF71; -.
DR   UniPathway; UPA00907; UER00922.
DR   UniPathway; UPA00968; -.
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_0000233020"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  44995 MW;  AB92F20D00E3D7C8 CRC64;
     MAQSLAVQGG SAVRTRPWPV WPRPAAGAAE AVQQVLSSGR WSISGPYRGA ASQERRFARA
     FAEYNGVAHC VPAASGTASL MLALEACGVG AGDEVIVPGL SWVASGSTVL GVNAVPVFCD
     VDPRTLCLDP EAVEAAVTER TKAIVVVHLY SAVADMDALT ALAERHSLPL IEDCAQAHGA
     AYRGVKVGAL ATAGTFSMQH SKMLTSGEGG AVITRDADFA RRVEHLRADG RVLAGQRPGP
     GEMELVETGE LMGNNRCLSE FQAALLTEQL KDLDAQHAIR RRNAALLDGL LRESGYVPQE
     TSEGTSTRTH YTYAVRLPEG RLTHVGLATV ARALSAELGC TVAPSYAPIT RNRLYDPASR
     RRFALGVEHQ ALTDPKRFEL PVAEDAARRV LTLHHAALLG AEDDMRDIAA AFGKVLRHGA
     DLTA