DOIAD_STRKN
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 03-AUG-2022, entry version 72.
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}.
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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 BioCyc; MetaCyc:MON-17186; -.
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 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 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 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="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
