ID   DOIAD_STRRI             Reviewed;         340 AA.
AC   Q4R0W1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase;
DE            Short=DOIA dehydrogenase;
DE            EC=1.1.1.329;
GN   Name=rbmC; Synonyms=ribE;
OS   Streptomyces ribosidificus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=80859;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21294 / JCM 4923 / NBRC 13796 / NRRL B-11466;
RX   PubMed=16258246;
RA   Subba B., Kharel M.K., Lee H.C., Liou K., Kim B.-G., Sohng J.K.;
RT   "The ribostamycin biosynthetic gene cluster in Streptomyces ribosidificus:
RT   comparison with butirosin biosynthesis.";
RL   Mol. Cells 20:90-96(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21294 / JCM 4923 / NBRC 13796 / NRRL B-11466;
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 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; ribostamycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. DOIA dehydrogenase subfamily. {ECO:0000305}.
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DR   EMBL; AJ748131; CAG34720.1; -; Genomic_DNA.
DR   EMBL; AJ744850; CAG34039.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4R0W1; -.
DR   SMR; Q4R0W1; -.
DR   UniPathway; UPA00907; UER00923.
DR   UniPathway; UPA00972; -.
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   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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..340
FT                   /note="2-deoxy-scyllo-inosamine dehydrogenase"
FT                   /id="PRO_0000234046"
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         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  35413 MW;  F73E7DE1F7216481 CRC64;
     MKALVFEAPE RALLTHRDIP DPAPGEALVR IAYNSVCGSD LSFYKGVWHG STYPVVPGHE
     WSGTVVDVNG PLGAELIGTN VVGDLTVSCG TCAHCTARTP TLCEDLGELG FTRDGACAEY
     MTIPVGNLRR LPDTLPLRAA CQVEPLAVAL NAVDRLGVTA GEKVAVMGAG GIGLLLAQAV
     RLRGGSVTAV AEPVPERRAA ALALGVPAAV SGEPGALVEL TRTHPDAVPD VVLEASGYPT
     AVQESLEAVR PGGRVGLVGY RIGETAVMAP HHIVLKVLTI RASMGPGTRF EEAIEVLASG
     AVTVDALLSH EFALDDYAKA LDVALRRADS NTRSYFNLQA