ID   DOIS_STRLV              Reviewed;         384 AA.
AC   Q2MF70;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=2-deoxy-scyllo-inosose synthase;
DE            Short=DOI synthase;
DE            Short=DOIS;
DE            EC=4.2.3.124;
GN   Name=livC;
OS   Streptomyces lividus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=282216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 844.73;
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). {ECO:0000250}.
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; lividomycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI
CC       synthase family. {ECO:0000305}.
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DR   EMBL; AJ748832; CAG38697.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MF70; -.
DR   SMR; Q2MF70; -.
DR   UniPathway; UPA00907; UER00921.
DR   UniPathway; UPA00968; -.
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..384
FT                   /note="2-deoxy-scyllo-inosose synthase"
FT                   /id="PRO_0000234038"
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   384 AA;  40173 MW;  44E6BAAB42E7351F CRC64;
     MHVTAITMED ANFPYRLGTD CAEELVARLG VRAASRYLVV CDTTVAALYG HDLVARLEKD
     AGPAVLLTHQ VGEVHKDVTT VGALAEQALG AGADRRSVVV ALGGGITGNI AGLLAALLFR
     GITLVHVPTT VVAMLDSVLS LKQAVNASFG KNLVGTFYQP AEVLADTAML RTLPEREVRS
     GMGEVVKNAL AVRPAMADRL AGLLRPDARY DDDALRWIIA ESVAAKADVT GADKHERGDG
     LVLEYGHTAG HAIEHAARGA VAHGAGVAVG MVIAAEVSHR LGHASASFVA RHRELISKAG
     LEDTVPACVR TDDVKNWLTY DNKRGYLDCA ADTTPMVLLA GPGRPLRTGG MPLVPVPLAV
     LNETVDALAA PGRAGTDHRT AVPV