ID   DOIS_STREY              Reviewed;         386 AA.
AC   Q2MFP1;
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=parC;
OS   Streptomyces paromomycinus (Streptomyces rimosus subsp. paromomycinus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=92743;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14827 / DSM 41429 / JCM 4541 / KCC S-0541 / NBRC 15454 / NRRL
RC   2455 / VKM Ac-605;
RA   Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA   Piepersberg W.;
RT   "Analysis and comparison of the biosynthetic gene clusters for the 2-
RT   deoxystreptamine-containing aminoglycoside antibiotics ribostamycin,
RT   neomycin, lividomycin, paromomycin and butirosin.";
RL   Submitted (FEB-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; paromomycin biosynthesis.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI
CC       synthase family. {ECO:0000305}.
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DR   EMBL; AJ628955; CAF32374.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MFP1; -.
DR   SMR; Q2MFP1; -.
DR   UniPathway; UPA00907; UER00921.
DR   UniPathway; UPA00970; -.
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_0000234040"
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;  40388 MW;  F996219F0E2C89EB CRC64;
     MHVTAITMED TSFPYRLGTE CAEEIVARLG ERAASRYLVV CDTTVAALYG RDLVARLEKD
     AGPAVLLTHP AGEVHKRIGT VGDLAEQALA AGADRRSVVV ALGGGITGNI AGLLASLLFR
     GITLVHVPTT VVAMLDSVLS LKQAVNASFG KNLVGTFYQP AEVLADTAML RTLPARELRS
     GMGEVVKNAL AIRPSMIERL AAELRPDARY EDAAMRWIIE ESVAAKAQVT GADKHERRDG
     LVLEYGHTTG HAIEHAARGE VAHGAGVAIG MIVAAEVSRL LGHASGDLVG LHRELVAKAG
     LEGSVPALVD PADVKHWLTY DNKRGYMPCP PAATPMVLLS APGEVLRSGP LPLVPVPLEL
     LGRAVDALAA PAGQSAGAER LSPAPA