ID   OLEU_STRAT              Reviewed;         295 AA.
AC   Q9RR27;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Probable dTDP-4,6-dihydroxy-2-methyloxan-3-one 4-ketoreductase {ECO:0000305|PubMed:10770761};
DE            EC=1.1.1.- {ECO:0000305};
GN   Name=oleU {ECO:0000303|PubMed:10770761};
OS   Streptomyces antibioticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205
RC   {ECO:0000312|EMBL:AAD55455.1};
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).
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
CC       (PubMed:10770761). Probably catalyzes the reduction of dTDP-4-keto-2,6-
CC       dideoxy-beta-L-galactose to yield dTDP-L-olivose.
CC       {ECO:0000269|PubMed:10770761}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P26392};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P26392};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:10770761}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AF055579; AAD55455.1; -; Genomic_DNA.
DR   PIR; T51107; T51107.
DR   AlphaFoldDB; Q9RR27; -.
DR   SMR; Q9RR27; -.
DR   KEGG; ag:AAD55455; -.
DR   BioCyc; MetaCyc:MON-17067; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR10491; PTHR10491; 1.
DR   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01214; rmlD; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Magnesium; Metal-binding; NAD; NADP;
KW   Oxidoreductase.
FT   CHAIN           1..295
FT                   /note="Probable dTDP-4,6-dihydroxy-2-methyloxan-3-one 4-
FT                   ketoreductase"
FT                   /id="PRO_0000444445"
FT   ACT_SITE        126
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         10..12
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         11..12
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         36..37
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         36..37
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         60..62
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         60..62
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         126
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         126
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         130
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         130
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   SITE            102
FT                   /note="Could provide a fine-tuning to achieve optimal pKa
FT                   matching between active site and substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
SQ   SEQUENCE   295 AA;  32099 MW;  2D5E4490EB85023F CRC64;
     MRWLITGAAG MLGRELVRRL AENEEDVAAL GHDHLDVTRP SAVRAALAEH RPGIVVNCAA
     YTAVDDAETD EAAAALLNAE APRLLAEGLR PHRRHGLVHL STDYVFPGDA RTPYAEDHPT
     APRSAYGRTK RDGEQAVLTA LPTATVLRTA WLYGRTGRSF VRTMIEREAR GGAIDVVADQ
     RGQPTWTGDL ADRIIAVGRH PGVHGILHAT NAGSATWYDL AQEVFRLLDA DPGRVRPTTG
     AAFRRPAPRP AYSVLGHDRW RGTGLAPLRD WRSALREAFP DILAAEHPPT RRGAA