DOIAD_MICEC
ID DOIAD_MICEC Reviewed; 340 AA.
AC Q70KF0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase;
DE Short=DOIA dehydrogenase;
DE EC=1.1.1.329;
GN Name=gacH; Synonyms=genE, gntP;
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=1877;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RX PubMed=15376556; DOI=10.7164/antibiotics.57.436;
RA Unwin J., Standage S., Alexander D., Hosted T. Jr., Horan A.C.,
RA Wellington E.M.;
RT "Gene cluster in Micromonospora echinospora ATCC15835 for the biosynthesis
RT of the gentamicin C complex.";
RL J. Antibiot. 57:436-445(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RX PubMed=15359126;
RA Kharel M.K., Basnet D.B., Lee H.C., Liou K., Moon Y.H., Kim J.-J.,
RA Woo J.S., Sohng J.K.;
RT "Molecular cloning and characterization of a 2-deoxystreptamine
RT biosynthetic gene cluster in gentamicin-producing Micromonospora
RT echinospora ATCC15835.";
RL Mol. Cells 18:71-78(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Cloning and sequencing of the gentamicin biosynthetic gene cluster from
RT Micromonospora echinospora DSM 43036.";
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; gentamicin biosynthesis.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. DOIA dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AY524043; AAR98562.1; -; Genomic_DNA.
DR EMBL; AJ575934; CAF34032.1; -; Genomic_DNA.
DR EMBL; AJ628149; CAF31445.1; -; Genomic_DNA.
DR AlphaFoldDB; Q70KF0; -.
DR SMR; Q70KF0; -.
DR UniPathway; UPA00907; UER00923.
DR UniPathway; UPA00967; -.
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; IPR029752; D-isomer_DH_CS1.
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..340
FT /note="2-deoxy-scyllo-inosamine dehydrogenase"
FT /id="PRO_0000234042"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 36023 MW; 63200F3BE27F3D09 CRC64;
MGGRMRALQF HGGHKAQIID TPRPEAPPGW AVVKVHYCCL CGSDLWLYRG KWHGNRYPIV
PGHEWAGVVD SAPEGYESWV GRPVTGDLIV GCQGCGPCRD GLPVMCENLI EIGFTVDGGC
AGYVAVPITN LYLLPEGMDL AAASQTEPLA VALHAVDRIN LRPAERVAVL GAGGIGQLIL
QSARATGATV TLATDLVAER RKIAEESGAA AAVHPSELPE LTSYADKVDV VFEASGDPES
VVRALDLVRP GGRVCLVGYQ VGAEHALETA RLPLSYASLV GVMGPGGKYR EAVDLLANGA
IDTQPILTDI VTLDDYAPAI DRAINRTDGT VRVVFDLRNE
