DOIS_STRKN
ID DOIS_STRKN Reviewed; 390 AA.
AC Q6L738;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=2-deoxy-scyllo-inosose synthase;
DE Short=DOI synthase;
DE Short=DOIS;
DE EC=4.2.3.124;
GN Name=kanC; Synonyms=kanA;
OS Streptomyces kanamyceticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1967;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC Ac-837;
RX PubMed=15313224; DOI=10.1016/j.abb.2004.06.009;
RA Kharel M.K., Subba B., Basnet D.B., Woo J.S., Lee H.C., Liou K.,
RA Sohng J.K.;
RT "A gene cluster for biosynthesis of kanamycin from Streptomyces
RT kanamyceticus: comparison with gentamicin biosynthetic gene cluster.";
RL Arch. Biochem. Biophys. 429:204-214(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=21-18;
RX PubMed=15303497; DOI=10.7164/antibiotics.57.351;
RA Yanai K., Murakami T.;
RT "The kanamycin biosynthetic gene cluster from Streptomyces kanamyceticus.";
RL J. Antibiot. 57:351-354(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12853 / DSM 40500 / NBRC 13414 / NCIMB 9343 / NRRL B-2535 / VKM
RC Ac-837;
RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Cloning and sequencing of the kanamycin biosynthetic gene cluster from
RT Streptomyces kanamyceticus DSM 40500.";
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).
CC {ECO:0000269|PubMed:15313224}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius.;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 2-deoxystreptamine
CC biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 1/4.
CC -!- PATHWAY: Antibiotic biosynthesis; kanamycin biosynthesis.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI
CC synthase family. {ECO:0000305}.
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DR EMBL; AJ582817; CAE46939.1; -; Genomic_DNA.
DR EMBL; AB164642; BAD20759.1; -; Genomic_DNA.
DR EMBL; AJ628422; CAF31589.1; -; Genomic_DNA.
DR RefSeq; WP_055553819.1; NZ_LIQU01000374.1.
DR AlphaFoldDB; Q6L738; -.
DR SMR; Q6L738; -.
DR KEGG; ag:CAE46939; -.
DR OrthoDB; 1677032at2; -.
DR BioCyc; MetaCyc:MON-17187; -.
DR UniPathway; UPA00907; UER00921.
DR UniPathway; UPA00965; -.
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 1: Evidence at protein level;
KW Antibiotic biosynthesis; Cobalt; Lyase; Metal-binding; NAD.
FT CHAIN 1..390
FT /note="2-deoxy-scyllo-inosose synthase"
FT /id="PRO_0000234037"
FT REGION 371..390
FT /note="Disordered"
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 390 AA; 41477 MW; E6D9CD580CCD3494 CRC64;
MQVTTITMDD VQYPYRLGTD CLDGIVTRLG ELGASRYLIV SDPRVAELYG QGLRERLAEQ
AGPAELITHA SGEQNKGLPA LHDLAEEALR RGADRQSIVV ALGGGVTGNI AGLLAALLFR
GIRLVHVPTT VVAMLDSVLS LKQAVNAGVG KNLVGTFYQP VEVLADTAML RTLPVREVRS
GMCEVVKNSL AIRPSMIDQL SAGLRPDGRY PDDTMHWIIY ESLAAKAQVT AYDKYERGEG
LILEYGHTVG HAVEHSSQGA VPHGAAVALG MIAAAQVSHR AGWASAELVD LHRELVAKTG
VARRIPSDIP LSAVRHRLSF DNKRGYLPAS ADTYPMVLLE SPGKVLRSEG TVLTAAPRDL
VDAVVDELAE PPRPAAARTD DAATVLGGAG
