ID   DOIS_STRRI              Reviewed;         391 AA.
AC   Q4R0W3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=2-deoxy-scyllo-inosose synthase;
DE            Short=DOI synthase;
DE            Short=DOIS;
DE            EC=4.2.3.124;
GN   Name=rbmA; Synonyms=ribC;
OS   Streptomyces ribosidificus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=80859;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 21294 / JCM 4923 / NBRC 13796 / NRRL B-11466;
RX   PubMed=16258246;
RA   Subba B., Kharel M.K., Lee H.C., Liou K., Kim B.-G., Sohng J.K.;
RT   "The ribostamycin biosynthetic gene cluster in Streptomyces ribosidificus:
RT   comparison with butirosin biosynthesis.";
RL   Mol. Cells 20:90-96(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 21294 / JCM 4923 / NBRC 13796 / NRRL B-11466;
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the intramolecular carbocycle formation from D-
CC       glucose-6-phosphate to 2-deoxy-scyllo-inosose (DOI).
CC       {ECO:0000269|PubMed:16258246}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q9S5E2};
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; ribostamycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI
CC       synthase family. {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; AJ748131; CAG34718.1; -; Genomic_DNA.
DR   EMBL; AJ744850; CAG34037.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4R0W3; -.
DR   SMR; Q4R0W3; -.
DR   UniPathway; UPA00907; UER00921.
DR   UniPathway; UPA00972; -.
DR   GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR   InterPro; IPR030963; DHQ_synth_fam.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   PIRSF; PIRSF001455; DHQ_synth; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Cobalt; Lyase; Metal-binding; NAD.
FT   CHAIN           1..391
FT                   /note="2-deoxy-scyllo-inosose synthase"
FT                   /id="PRO_0000234039"
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   391 AA;  41222 MW;  7F4B20E3CFF517A3 CRC64;
     MQVTPIAMED ASFAYRLGTE CTEDVVARLA TLGASSYLVV ADTTVAGLYG HDLTARIDKE
     AGPAHLLTHE SGEVHKDLTT VSVLAEQALE RGADRRSVVV ALGGGVTGNI TGLMASLLFR
     GIRLVHVPTT VVAMLDSVLS LKQAVNATFG KNLVGTFYQP VEVLADTAFL RTLPPREIRS
     GLGEVVKNAL AIRPAMLDRL GDALRADARY DDETLRWIIA ESLTAKADVT RDDKHERRTG
     LVLEYGHTAG HAIEHASRGE VAHGAGVAVG MTIAAEVSRR LGHAGPDFVA LHRELVAAAG
     VEPAVPAHVD PALVKNWLAY DNKRGYLDSP PGHTPMVLLS APGEVLHTGP MPLVPVPLAL
     LEEAVDEAAR RGRDAAPAAA YVGPPAAGPL P