ID   DOIAD_STRLV             Reviewed;         339 AA.
AC   Q2MF72;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase;
DE            Short=DOIA dehydrogenase;
DE            EC=1.1.1.329;
GN   Name=livE;
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 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; lividomycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. DOIA dehydrogenase subfamily. {ECO:0000305}.
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DR   EMBL; AJ748832; CAG38695.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF72; -.
DR   SMR; Q2MF72; -.
DR   UniPathway; UPA00907; UER00923.
DR   UniPathway; UPA00968; -.
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..339
FT                   /note="2-deoxy-scyllo-inosamine dehydrogenase"
FT                   /id="PRO_0000234045"
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;  35290 MW;  D67BD6C6602DF7B2 CRC64;
     MKALMFEAPE RAVLIQRDLP EPAPGEALVR LAYNSVCGSD LSFYKGVWHG STYPVVPGHE
     WSGTVVDVNG ADSGLVGVDV VGDLTCSCGT CRHCAEGKPT LCGDLQELGF TRDGACAEYM
     TIPAANLHRL PPGTSLRAAC QVEPLAVALN AVDRLAVVPG EKVAITGAGG IGLLLALAVR
     QRGGEVTAFA EPVAERREAA AALGVSATVG GAPGDLVALV EKHPELRPDV VLEASGYPSA
     VQEAIEAVRS GGRVGLIGYR VEEVGPMAPQ HIVIKMLTLQ ASMGPGTRFG EAIGLLSSGA
     VDVDALLSHE FALEDHARAL DVALRRADGN TRSFFNLRT