DOIS_STRFR
ID DOIS_STRFR Reviewed; 430 AA.
AC Q53U19;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=2-deoxy-scyllo-inosose synthase;
DE Short=DOI synthase;
DE Short=DOIS;
DE EC=4.2.3.124;
GN Name=neoC; Synonyms=nemA;
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], AND FUNCTION.
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).
RN [5]
RP FUNCTION, REACTION MECHANISM, AND COFACTOR.
RC STRAIN=ATCC 21096 / DSM 40943 / NBRC 13147 / MA-2898 / NRRL B-3357;
RA Yamauchi N., Kakinuma K.;
RT "Enzymatic carbocycle formation in microbial secondary metabolism. The
RT mechanism of the 2-deoxy-scyllo-inosose synthase reaction as a crucial step
RT in the 2-deoxystreptamine biosynthesis in Streptomyces fradiae.";
RL J. Org. Chem. 60:5614-5619(1995).
CC -!- FUNCTION: Catalyzes the intramolecular carbocycle formation from D-
CC glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI).
CC {ECO:0000269|PubMed:16506694, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate = 2-deoxy-L-scyllo-inosose + phosphate;
CC Xref=Rhea:RHEA:33071, ChEBI:CHEBI:43474, ChEBI:CHEBI:61548,
CC ChEBI:CHEBI:64796; EC=4.2.3.124;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|Ref.5};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q9S5E2};
CC Note=Binds 1 Co(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9S5E2};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 1/4.
CC -!- PATHWAY: Antibiotic biosynthesis; neomycin biosynthesis.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI
CC synthase family. {ECO:0000305}.
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DR EMBL; AJ629247; CAF33312.1; -; Genomic_DNA.
DR EMBL; AJ786317; CAH05101.1; -; Genomic_DNA.
DR EMBL; AB211959; BAD95820.1; -; Genomic_DNA.
DR EMBL; AJ843080; CAH58690.1; -; Genomic_DNA.
DR AlphaFoldDB; Q53U19; -.
DR SMR; Q53U19; -.
DR KEGG; ag:BAD95820; -.
DR BioCyc; MetaCyc:MON-17230; -.
DR UniPathway; UPA00907; UER00921.
DR UniPathway; UPA00969; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR030960; DHQS/DOIS.
DR Pfam; PF01761; DHQ_synthase; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Cobalt; Lyase; Metal-binding; NAD.
FT CHAIN 1..430
FT /note="2-deoxy-scyllo-inosose synthase"
FT /id="PRO_0000234036"
FT REGION 371..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT ACT_SITE 244
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 73..76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 105..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 129..130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 140..142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 151..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 184
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 247
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 263
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
SQ SEQUENCE 430 AA; 43960 MW; 5C6AF02D3F3E0B70 CRC64;
MQTTRIAMED ASFPYRLGTD CAEDVVARLA ALEASSYLVV ADTTVAELYG AALTAHIDKE
AGPSHLLTHE VGEVHKTLAT VSALAEQALG RGADRRSVVV ALGGGVTGNI AGLMASLLFR
GIRLVHVPTT VVAMLDSVLS LKQAVNTTFG KNLAGTFYQP VEVLADTAAL RTLPPREIRS
GMGEVVKNAL AIRPAMLDRL AGALRPDTRY DDETMRWIIA ESLAAKADVT SGDKHERRSG
LVLEYGHTAG HAIEHASRGA VAHGAGVAVG MTLAAEVSRR LGHADAGLVA LHRELVAAAG
VEPAVPDHVD TALVKNWLAY DNKRGYLDSP PGHTPMVLLS APGEVLHTGT MPLVPVPLAL
LEEVVDESAA RGGAGGGAAE PAAARTGPVP DGPEAAVPAT PGPVPAGPAA AAPLPSGPAP
TAPAAAGPVP
