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 27-MAR-2024, entry version 65.
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; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; 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 GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
