DOIAD_STREY
ID DOIAD_STREY Reviewed; 339 AA.
AC Q2MFP3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase;
DE Short=DOIA dehydrogenase;
DE EC=1.1.1.329;
GN Name=parE;
OS Streptomyces paromomycinus (Streptomyces rimosus subsp. paromomycinus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=92743;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14827 / DSM 41429 / JCM 4541 / KCC S-0541 / NBRC 15454 / NRRL
RC 2455 / VKM Ac-605;
RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Analysis and comparison of the biosynthetic gene clusters for the 2-
RT deoxystreptamine-containing aminoglycoside antibiotics ribostamycin,
RT neomycin, lividomycin, paromomycin and butirosin.";
RL Submitted (FEB-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; paromomycin biosynthesis.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. DOIA dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AJ628955; CAF32372.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2MFP3; -.
DR SMR; Q2MFP3; -.
DR UniPathway; UPA00907; UER00923.
DR UniPathway; UPA00970; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
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.
DR PROSITE; PS00059; ADH_ZINC; 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_0000234047"
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; 35458 MW; 76E63F9530E1859D CRC64;
MKALMFKAPL QAVLTERDVP EPAPGEALVK LAYNSICGSD LSFYKGVWHG FTYPVVPGHE
WSGTVVEAGG GAADLVGQNV VGDLTVACGS CRHCTVGKPT LCADLQELGF TRDGACAEYM
TVPTGNLHRL PEGLSLREAT QVEPLAVALN AVDRLAVTAG EKVAITGAGG IGLLLAQAVR
LRGAEVTVLA EPVTERRQAA HALGVPHTVG GDPGELVGFV EKHPELTPDV VLEASGYPLA
VQEAVEAVRS GGRIGLIGYR IEEAATMAPH HIVVKVLSLQ ASMGPGDRFG EAIELLAAGA
VDVDALLSHE FGLADHDRAL DVALRRADGN TRSYFNLRA
