ID DOIAD_STRKN Reviewed; 343 AA. AC Q6L743; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 25-MAY-2022, entry version 71. DE RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase; DE Short=DOIA dehydrogenase; DE EC=1.1.1.329; GN Name=kanE; Synonyms=kanK; OS Streptomyces kanamyceticus. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1967; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM RC Ac-837; RX PubMed=15313224; DOI=10.1016/j.abb.2004.06.009; RA Kharel M.K., Subba B., Basnet D.B., Woo J.S., Lee H.C., Liou K., RA Sohng J.K.; RT "A gene cluster for biosynthesis of kanamycin from Streptomyces RT kanamyceticus: comparison with gentamicin biosynthetic gene cluster."; RL Arch. Biochem. Biophys. 429:204-214(2004). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=21-18; RX PubMed=15303497; DOI=10.7164/antibiotics.57.351; RA Yanai K., Murakami T.; RT "The kanamycin biosynthetic gene cluster from Streptomyces kanamyceticus."; RL J. Antibiot. 57:351-354(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM RC Ac-837; RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A., RA Piepersberg W.; RT "Cloning and sequencing of the kanamycin biosynthetic gene cluster from RT Streptomyces kanamyceticus DSM 40500."; 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; kanamycin biosynthesis. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. DOIA dehydrogenase subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ582817; CAF60530.1; -; Genomic_DNA. DR EMBL; AB164642; BAD20754.1; -; Genomic_DNA. DR EMBL; AJ628422; CAF31584.1; -; Genomic_DNA. DR RefSeq; WP_055545100.1; NZ_LIQU01000069.1. DR AlphaFoldDB; Q6L743; -. DR SMR; Q6L743; -. DR KEGG; ag:CAF60530; -. DR BRENDA; 1.1.1.329; 6046. DR UniPathway; UPA00907; UER00923. DR UniPathway; UPA00965; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0017000; P:antibiotic biosynthetic process; 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 Antibiotic biosynthesis; Metal-binding; NAD; NADP; Oxidoreductase; Zinc. FT CHAIN 1..343 FT /note="2-deoxy-scyllo-inosamine dehydrogenase" FT /id="PRO_0000234044" FT METAL 37 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250" FT METAL 59 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250" FT METAL 91 FT /note="Zinc 2" FT /evidence="ECO:0000250" FT METAL 94 FT /note="Zinc 2" FT /evidence="ECO:0000250" FT METAL 97 FT /note="Zinc 2" FT /evidence="ECO:0000250" FT METAL 105 FT /note="Zinc 2" FT /evidence="ECO:0000250" FT METAL 146 FT /note="Zinc 1; catalytic" FT /evidence="ECO:0000250" SQ SEQUENCE 343 AA; 35936 MW; A61AFA1521BAEFB8 CRC64; MKALVFHSPE KATFEQRDVP TPRPGEALVH IAYNSICGSD LSLYRGVWHG FGYPVVPGHE WSGTVVEING ANGHDQSLVG KNVVGDLTCA CGNCAACGRG TPVLCENLQE LGFTKDGACA EYMTIPVDNL RPLPDALSLR SACQVEPLAV ALNAVSIAGV APGDRVAVMG AGGIGLMLMQ VARHLGGEVT VVSEPVAERR AVAGQLGATE LCSAEPGQLA ELVARRPELT PDVVLEASGY PAALQEAIEV VRPGGRIGLI GYRVEETGPM SPQHIAVKAL TLRGSLGPGG RFDDAVELLA KGDDIAVEPL LSHEFGLADY ATALDLALSR TNGNVRSFFN LRD //