ID   DOIS_STRSD              Reviewed;         386 AA.
AC   Q2MF16; Q70IY3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=2-deoxy-scyllo-inosose synthase;
DE            Short=DOI synthase;
DE            Short=DOIS;
DE            EC=4.2.3.124;
GN   Name=tbmA; Synonyms=tobC;
OS   Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 /
OS   CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1)
OS   (Streptomyces tenebrarius).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Streptoalloteichus.
OX   NCBI_TaxID=1933;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=14757238; DOI=10.1016/s0378-1097(03)00881-4;
RA   Kharel M.K., Basnet D.B., Lee H.C., Liou K., Woo J.S., Kim B.-G.,
RA   Sohng J.K.;
RT   "Isolation and characterization of the tobramycin biosynthetic gene cluster
RT   from Streptomyces tenebrarius.";
RL   FEMS Microbiol. Lett. 230:185-190(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Comparison of the gene clusters for the biosynthesis of the aminoglycoside
RT   antibiotics tobramycin-apramycin (Streptomyces tenebrarius DSM 40477), and
RT   hygromycin B (Streptomyces hygroscopicus subsp. hygroscopicus DSM 40578).";
RL   Submitted (AUG-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:14757238}.
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; tobramycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI
CC       synthase family. {ECO:0000305}.
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DR   EMBL; AJ579650; CAE22471.1; -; Genomic_RNA.
DR   EMBL; AJ810851; CAH18556.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF16; -.
DR   SMR; Q2MF16; -.
DR   BRENDA; 4.2.3.124; 7970.
DR   UniPathway; UPA00907; UER00921.
DR   UniPathway; UPA00971; -.
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..386
FT                   /note="2-deoxy-scyllo-inosose synthase"
FT                   /id="PRO_0000234041"
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   386 AA;  40662 MW;  8FEED31571C012D2 CRC64;
     MQTTTITMGD VQYPYRLGTG CVDGIVTRLG ELEASHYLVL CDATVAELYG HDLAARLRRS
     AGPASVLTHP AGEEHKGLGT LDTLADAALH AGVDRRGVVV ALGGGVTGNI AGLLAALLFR
     GIRLVHVPTT VVAMLDSVLS LKQAVNAQVG KNLVGTFYPP VEVLADTAML GTLPVREIRS
     GLCEVVKNAL AIRPSMIDFL AAELRPDGRY ADDVLRWMID ESVAAKAQVT EHDKYERREG
     LVLEYGHTVG HALEHASHGA VSHGAGVGVG MVAAAEVARR LGHVDADLVE LHRELVGKVG
     VATTLPADVP TEEITYRLGF DNKRGYQPLP ADHYAMVLLA DVGQPLYQDG LPLTPAPRAL
     VDEVVRELAD APSRIGASVG SAGGAS