DOIAD_STRFR
ID DOIAD_STRFR Reviewed; 340 AA.
AC Q53U21;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=2-deoxy-scyllo-inosamine dehydrogenase;
DE Short=DOIA dehydrogenase;
DE EC=1.1.1.329;
GN Name=neoA; Synonyms=nemC, neoE;
OS Streptomyces fradiae (Streptomyces roseoflavus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1906;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Piepersberg W.,
RA Welzel K., Vente A.;
RT "Analysis and comparison of biosynthetic gene clusters for the 2-deoxy-
RT inosamine containing aminoglycoside antibiotics ribostamycin, neomycin,
RT lividomycin, paromomycin and butirosin.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RA Subba B., Kharel M.K., Sthapit B., Liou K., Lee H.C., Woo J.S., Sohng J.K.;
RT "Cloning and characterization of a neomycin biosynthetic gene cluster from
RT Streptomyces fradiae, ATCC 10745.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RX PubMed=16506694; DOI=10.1038/ja.2005.104;
RA Kudo F., Yamamoto Y., Yokoyama K., Eguchi T., Kakinuma K.;
RT "Biosynthesis of 2-deoxystreptamine by three crucial enzymes in
RT Streptomyces fradiae NBRC 12773.";
RL J. Antibiot. 58:766-774(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC 8233 / NRRL B-1195 / VKM Ac-150;
RX PubMed=15827636; DOI=10.1039/b501199j;
RA Huang F., Haydock S.F., Mironenko T., Spiteller D., Li Y., Spencer J.B.;
RT "The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233:
RT characterisation of an aminotransferase involved in the formation of 2-
RT deoxystreptamine.";
RL Org. Biomol. Chem. 3:1410-1418(2005).
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:0000269|PubMed:16506694}.
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 Evidence={ECO:0000269|PubMed:16506694};
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 Evidence={ECO:0000269|PubMed:16506694};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000305};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 3/4.
CC -!- PATHWAY: Antibiotic biosynthesis; neomycin biosynthesis.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. DOIA dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; AJ629247; CAF33310.1; -; Genomic_DNA.
DR EMBL; AJ786317; CAH05103.1; -; Genomic_DNA.
DR EMBL; AB211959; BAD95818.1; -; Genomic_DNA.
DR EMBL; AJ843080; CAH58688.1; -; Genomic_DNA.
DR RefSeq; WP_031129625.1; NZ_MUNC01000914.1.
DR AlphaFoldDB; Q53U21; -.
DR SMR; Q53U21; -.
DR KEGG; ag:BAD95818; -.
DR BioCyc; MetaCyc:MON-17231; -.
DR BRENDA; 1.1.1.329; 5932.
DR UniPathway; UPA00907; UER00923.
DR UniPathway; UPA00969; -.
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; 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 1: Evidence at protein level;
KW Metal-binding; NAD; NADP; Oxidoreductase; Zinc.
FT CHAIN 1..340
FT /note="2-deoxy-scyllo-inosamine dehydrogenase"
FT /id="PRO_0000234043"
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 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 144
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; 35228 MW; C86A5BADED1976CE CRC64;
MKALVFEAPE RAVLTHRDIP APAPGEALVR VAYNSVCGSD LSFYKGVWHG FTYPVVPGHE
WSGSVVDVNG PRGADLVGRN VVGDLTCSCG TCAHCAAGTP TLCEDLGELG FTRDGACAEY
MTVPVANLRP LPDTLPLRTA CQVEPLAVAL NAVDRLGVTP GEKVAVMGAG GIGLLLVQAV
RLRGGTVTAV AEPVPERRAA ALALGVPAAV GGDPGALVEL TRSDPAAVPD VVLEASGYPT
AVQEAVEAVR PGGRVGLVGY RIEEAAVMAP HHIVLKVLTV RASMGPGTRF EEAVDVLASG
AVDVDALLSH EFALDDYAKA LDVALRRADG NTRSYFNLRA
