ID   GLADA_STRKN             Reviewed;         419 AA.
AC   Q6L733;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=kanD; Synonyms=kanS2;
OS   Streptomyces kanamyceticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC   Ac-837;
RX   PubMed=15313224; DOI=10.1016/j.abb.2004.06.009;
RA   Kharel M.K., Subba B., Basnet D.B., Woo J.S., Lee H.C., Liou K.,
RA   Sohng J.K.;
RT   "A gene cluster for biosynthesis of kanamycin from Streptomyces
RT   kanamyceticus: comparison with gentamicin biosynthetic gene cluster.";
RL   Arch. Biochem. Biophys. 429:204-214(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=21-18;
RX   PubMed=15303497; DOI=10.7164/antibiotics.57.351;
RA   Yanai K., Murakami T.;
RT   "The kanamycin biosynthetic gene cluster from Streptomyces kanamyceticus.";
RL   J. Antibiot. 57:351-354(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC   Ac-837;
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Cloning and sequencing of the kanamycin biosynthetic gene cluster from
RT   Streptomyces kanamyceticus DSM 40500.";
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; kanamycin 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; AJ582817; CAE46943.1; -; Genomic_DNA.
DR   EMBL; AB164642; BAD20764.1; -; Genomic_DNA.
DR   EMBL; AJ628422; CAF31593.1; -; Genomic_DNA.
DR   RefSeq; WP_055553810.1; NZ_LIQU01000374.1.
DR   AlphaFoldDB; Q6L733; -.
DR   SMR; Q6L733; -.
DR   PRIDE; Q6L733; -.
DR   KEGG; ag:CAE46943; -.
DR   OrthoDB; 1722208at2; -.
DR   UniPathway; UPA00907; UER00924.
DR   UniPathway; UPA00965; -.
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..419
FT                   /note="Putative L-glutamine:3-amino-2,3-dideoxy-scyllo-
FT                   inosose aminotransferase"
FT                   /id="PRO_0000234050"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   419 AA;  45162 MW;  F7589469BC5EE787 CRC64;
     MSKKLALFGG TPVRNEEFYD GPHIGPHDLD RLKSVLDSGN FGGIPFPNTH HTAFADLFTG
     KLGAPYGLMV SNGTISLSIA LRALGVRAGD EVITTGYTWM GTAAAIVHIN AVPVLVDIDP
     TTWCIDPAAV EAAITPRTKV IVPVHLGNQI ADLDALRAIA DKHGLAILED TAHGHFAEWR
     GQCVGTHGDA GSFSFESSKI MTAGEGGFLV ARDEDVYQRM MSLANCGRKE PGYDGFAGRT
     LGWNARASEL QAAFMIGQVE QHDALHAKRA ASAAKLTAGL AEIGGFTPVG NDDPRITRRQ
     YYEVIYRFDP AAWEGLHRDE VLSAILAEGI ELEGDAFYPP VHKSELFAVD AVHWPMIAER
     YGDRIGPDSV DLPVADRAAA DESVWVHHAL LTGDDKDLGD ILEAVAKVRD NLRELHDAS