ID   DOIAD_STRSD             Reviewed;         339 AA.
AC   Q2MF22; Q70IX7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase;
DE            Short=DOIA dehydrogenase;
DE            EC=1.1.1.329;
GN   Name=tobE; Synonyms=tacD;
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.
CC   -!- FUNCTION: Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA)
CC       with NAD(+) or NADP(+), forming 3-amino-2,3-dideoxy-scyllo-inosose
CC       (amino-DOI). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-scyllo-inosamine + NADP(+) = 3-amino-2,3-dideoxy-
CC         scyllo-inosose + H(+) + NADPH; Xref=Rhea:RHEA:33879,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65002, ChEBI:CHEBI:65003; EC=1.1.1.329;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-scyllo-inosamine + NAD(+) = 3-amino-2,3-dideoxy-
CC         scyllo-inosose + H(+) + NADH; Xref=Rhea:RHEA:33883,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:65002, ChEBI:CHEBI:65003; EC=1.1.1.329;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC       biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 3/4.
CC   -!- PATHWAY: Antibiotic biosynthesis; tobramycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. DOIA dehydrogenase subfamily. {ECO:0000305}.
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DR   EMBL; AJ579650; CAE22477.1; -; Genomic_RNA.
DR   EMBL; AJ810851; CAH18550.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF22; -.
DR   SMR; Q2MF22; -.
DR   UniPathway; UPA00907; UER00923.
DR   UniPathway; UPA00971; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NAD; NADP; Oxidoreductase; Zinc.
FT   CHAIN           1..339
FT                   /note="2-deoxy-scyllo-inosamine dehydrogenase"
FT                   /id="PRO_0000234048"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  35377 MW;  0139B8EE1444928F CRC64;
     MKALSFEAPG EAVFGTREVP VPAPGEALIH LGYNSICGSD LSLYRGVWHG FSYPVVPGHE
     WSGTVVEVNG PGAELVGRDV VGDLTCACGS CAACGRGTPV LCENLQELGF TRDGACAEYM
     TIPTGNLHVL PEGLSLRAAC QVEPVAVALH AVSTVGVEPG ERVAVLGAGG IGLMLMQVAR
     QRGGVITTVG EPVAERRAVA AQLGARTVTT GRPGELAELV AKHPDLTPDV VLEASGYPVA
     VQEAIEVVRP GGRIGLVGYR VEEVGPMATH HVAVKALTIR GSLGPGGRFP EAIDLLARGE
     IEVEPLLSHE FALDDHARAL DLALRRAEGN VRSFFNLRA