DOIS_MICEC
ID DOIS_MICEC Reviewed; 397 AA.
AC Q70KD0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=2-deoxy-scyllo-inosose synthase;
DE Short=DOI synthase;
DE Short=DOIS;
DE EC=4.2.3.124;
GN Name=gtmA; Synonyms=genC, gntB;
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=1877;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RX PubMed=15376556; DOI=10.7164/antibiotics.57.436;
RA Unwin J., Standage S., Alexander D., Hosted T. Jr., Horan A.C.,
RA Wellington E.M.;
RT "Gene cluster in Micromonospora echinospora ATCC15835 for the biosynthesis
RT of the gentamicin C complex.";
RL J. Antibiot. 57:436-445(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RX PubMed=15359126;
RA Kharel M.K., Basnet D.B., Lee H.C., Liou K., Moon Y.H., Kim J.-J.,
RA Woo J.S., Sohng J.K.;
RT "Molecular cloning and characterization of a 2-deoxystreptamine
RT biosynthetic gene cluster in gentamicin-producing Micromonospora
RT echinospora ATCC15835.";
RL Mol. Cells 18:71-78(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15835 / DSM 43036 / BCRC 11561 / JCM 3074 / NBRC 12575 / NCIMB
RC 12882 / NRRL 2953;
RA Aboshanab K.M.A., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Cloning and sequencing of the gentamicin biosynthetic gene cluster from
RT Micromonospora echinospora DSM 43036.";
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:15359126}.
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; gentamicin biosynthesis.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DOI
CC synthase family. {ECO:0000305}.
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DR EMBL; AY524043; AAR98548.1; -; Genomic_DNA.
DR EMBL; AJ575934; CAE06511.1; -; Genomic_DNA.
DR EMBL; AJ628149; CAF31431.1; -; Genomic_DNA.
DR AlphaFoldDB; Q70KD0; -.
DR SMR; Q70KD0; -.
DR UniPathway; UPA00907; UER00921.
DR UniPathway; UPA00967; -.
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..397
FT /note="2-deoxy-scyllo-inosose synthase"
FT /id="PRO_0000234035"
FT ACT_SITE 140
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT ACT_SITE 242
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 71..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 103..107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 127..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 138..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 149..150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 182
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 245
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 261
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
SQ SEQUENCE 397 AA; 42301 MW; 6947368029536F97 CRC64;
MEVEIRLGSV RYPFRLGTDC LGAIVEDLVA MSASRLLIVC DSNTGPLFGA ELVERLSPRV
PANLLIHRAG EPYKDLQAVG TLADSALQLG ADRASVVVAV GGGVIGNIAG LMAALLFRGI
RLVHIPTSLI AMSDSVLSLK QAVNACVGKN LMGTFYAPES VLADTAMLRS LPFRETVSGL
CEVVKNSLAI RPSMVEMLRT SLRQDAVYDD ETMYEIISES ILAKASVTVD DMHECRAGLV
LEYGHTVGHA IEYTAAGGLS HGQAIGLGMV VAAEVSHRLG HLDQEAVALH RELLTRAGAM
VTIPEEVDLD EVMHRLRFDN KRGYLADPAE SSAMVLLGGL GEPLWHDGRP LVSVPMALVG
EVVNEIARPE IPNFELVAPV ETVEEGRVPD TVGAADG
