ID   GLADA_MICEC             Reviewed;         418 AA.
AC   Q70KD4; Q6QVT9;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 54.
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;
DE   AltName: Full=Putative gentamicin aminotransferase II;
GN   Name=gtmD; Synonyms=genS2, gntF;
OS   Micromonospora echinospora (Micromonospora purpurea).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=1877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC   12882 / NRRL 2953;
RX   PubMed=15376556; DOI=10.7164/antibiotics.57.436;
RA   Unwin J., Standage S., Alexander D., Hosted T. Jr., Horan A.C.,
RA   Wellington E.M.;
RT   "Gene cluster in Micromonospora echinospora ATCC15835 for the biosynthesis
RT   of the gentamicin C complex.";
RL   J. Antibiot. 57:436-445(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC   12882 / NRRL 2953;
RX   PubMed=15359126;
RA   Kharel M.K., Basnet D.B., Lee H.C., Liou K., Moon Y.H., Kim J.-J.,
RA   Woo J.S., Sohng J.K.;
RT   "Molecular cloning and characterization of a 2-deoxystreptamine
RT   biosynthetic gene cluster in gentamicin-producing Micromonospora
RT   echinospora ATCC15835.";
RL   Mol. Cells 18:71-78(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC   12882 / NRRL 2953;
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Cloning and sequencing of the gentamicin biosynthetic gene cluster from
RT   Micromonospora echinospora DSM 43036.";
RL   Submitted (FEB-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; gentamicin biosynthesis.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. L-glutamine:2-deoxy-
CC       scyllo-inosose/scyllo-inosose aminotransferase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR98552.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY524043; AAR98552.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AJ575934; CAE06507.1; -; Genomic_DNA.
DR   EMBL; AJ628149; CAF31435.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q70KD4; -.
DR   SMR; Q70KD4; -.
DR   PRIDE; Q70KD4; -.
DR   KEGG; ag:CAF31435; -.
DR   UniPathway; UPA00907; UER00924.
DR   UniPathway; UPA00967; -.
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..418
FT                   /note="Putative L-glutamine:3-amino-2,3-dideoxy-scyllo-
FT                   inosose aminotransferase"
FT                   /id="PRO_0000234049"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   418 AA;  46794 MW;  3C1F5EC0293FBFE4 CRC64;
     MTQKLAILGG DPVRTRPWPE WPHVGPEDVD RLRTVIESRN LGGIPFPNTM HQQFAERFTA
     KLGAKYGLLA TNGTVTLSMA LRALGIHAGD EVITTAFTWV GTVAGIVHVN AVPVLADISD
     DNWCIDPVKV EEAITDRTRA IMVVHLGNQV ADMDALLDIC RRHNLLLIED CAHAHFAEWR
     GRCVGTIGDA GSYSFETSKI MTSGEGGFLV TATEEAFHRA MSLAHVGRKE APYDRFPGRV
     FGWNHRATEM QAAVLLGQLD RYDALDKQRT AMAEMLTQGL VEIGGFKPLA EDPRVTRRQR
     YELLFRFDTE AWDGLHRDKV LEAILAEGVE FEGNTFYPPM HRDELFHITA DDWPAIRERY
     GEKIEPDAFH LPVAERVAFD EAVWIHHSLL SVEPEDVQDM LDAVVKVRDN LGALKKSL