OLEW_STRAT
ID OLEW_STRAT Reviewed; 328 AA.
AC Q9RR32;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase {ECO:0000303|Ref.1};
DE EC=1.1.1.384 {ECO:0000269|Ref.1};
DE AltName: Full=dTDP-3,4-diketo-2,6-dideoxyglucose 3-ketoreductase {ECO:0000305};
GN Name=oleW {ECO:0000303|PubMed:10770761};
GN Synonyms=orf11 {ECO:0000303|Ref.1};
OS Streptomyces antibioticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1890;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND SUBSTRATE SPECIFICITY.
RC STRAIN=Tu99 {ECO:0000312|EMBL:AAF59931.1};
RA Draeger G., Park S.-H.H., Floss H.G.;
RT "Mechanism of the 2-deoxygenation step in the biosynthesis of the
RT deoxyhexose moieties of the antibiotics granaticin and oleandomycin.";
RL J. Am. Chem. Soc. 121:2611-2612(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205
RC {ECO:0000312|EMBL:AAD55450.1};
RX PubMed=10770761; DOI=10.1128/aac.44.5.1266-1275.2000;
RA Aguirrezabalaga I., Olano C., Allende N., Rodriguez L., Brana A.F.,
RA Mendez C., Salas J.A.;
RT "Identification and expression of genes involved in biosynthesis of L-
RT oleandrose and its intermediate L-olivose in the oleandomycin producer
RT Streptomyces antibioticus.";
RL Antimicrob. Agents Chemother. 44:1266-1275(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tu99 {ECO:0000312|EMBL:AAF59931.1};
RA Park S.H., Sohng J.K., August P.R., Niggemann J., Floss H.G.;
RT "A cluster of genes from Streptomyces antibioticus involved in the
RT biosynthesis of the deoxysugar moieties of oleandomycin.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of one of the two 2,6-
CC deoxysugars, dTDP-L-oleandrose, attached to the macrolactone ring
CC oleandolide to produce the aglycone antibiotic oleandomycin (Ref.1,
CC PubMed:10770761). Catalyzes the reduction of the C-3 keto moiety of
CC dTDP-3,4-diketo-2,6-dideoxy-alpha-D-glucose to yield dTDP-4-keto-2,6-
CC dideoxy-alpha-D-glucose (Ref.1). NADPH is the better reductant, however
CC NADH can also be used (Ref.1). {ECO:0000269|PubMed:10770761,
CC ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-
CC 3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H(+) + NADPH;
CC Xref=Rhea:RHEA:44624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84537, ChEBI:CHEBI:84540;
CC EC=1.1.1.384; Evidence={ECO:0000269|Ref.1};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:10770761,
CC ECO:0000305|Ref.1}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF055579; AAD55450.1; -; Genomic_DNA.
DR EMBL; AH009200; AAF59931.1; -; Genomic_DNA.
DR PIR; T51102; T51102.
DR AlphaFoldDB; Q9RR32; -.
DR SMR; Q9RR32; -.
DR KEGG; ag:AAD55450; -.
DR BioCyc; MetaCyc:MON-17065; -.
DR BRENDA; 1.1.1.384; 5974.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; NADP; Oxidoreductase.
FT CHAIN 1..328
FT /note="dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-
FT reductase"
FT /id="PRO_0000444244"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 38..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 75
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
SQ SEQUENCE 328 AA; 35835 MW; 271B218F26C11A31 CRC64;
MPSPRLRFGV LGAADIALRR TVPALLAHPD VTVVAVSSRD TARAARFAAA FGCEAVPGHQ
ALLDRDDIDA LYVPLPVMVH TPWVEAALLR GRHVLVEKPL TATRSGAEDL IALARSRGLV
LMENFTSLHH AQHGTVTDLL RDGTIGELRS LSAAFTIPPK PEGDIRYQPD VGGGALLDIG
IYPLRAALHF LGPDLHAAGA VLRRERRRNV VVSGHVLLTT PHGVVAELAF GMEHAYRSEY
TLFGTAGRLR LDRAFTPPET HRPRVEIHRQ DALDIVDLPP DAQFANLVRD FVLAVREGPG
RLTQHHADAV RQADLVERVM AVARVRWC
