OLEL_STRAT
ID OLEL_STRAT Reviewed; 204 AA.
AC Q9RR30;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Probable dTDP-4-oxo-2,6-dideoxy-D-glucose 3,5-epimerase {ECO:0000305|PubMed:10770761};
DE EC=5.1.3.-;
GN Name=oleL {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:AAD55452.1};
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 conversion of dTDP-4-keto-
CC 2,6-dideoxy-alpha-D-glucose to dTDP-4-keto-2,6-dideoxy-beta-L-
CC galactose. {ECO:0000269|PubMed:10770761}.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:10770761}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, lacks the
CC conserved His active site in position 60, which is replaced by an Thr
CC residue, suggesting a different reaction mechanism. {ECO:0000305}.
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DR EMBL; AF055579; AAD55452.1; -; Genomic_DNA.
DR PIR; T51104; T51104.
DR AlphaFoldDB; Q9RR30; -.
DR SMR; Q9RR30; -.
DR KEGG; ag:AAD55452; -.
DR BioCyc; MetaCyc:MON-17066; -.
DR GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR000888; dTDP_sugar_isom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR21047; PTHR21047; 1.
DR Pfam; PF00908; dTDP_sugar_isom; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Isomerase.
FT CHAIN 1..204
FT /note="Probable dTDP-4-oxo-2,6-dideoxy-D-glucose 3,5-
FT epimerase"
FT /id="PRO_0000444446"
FT REGION 164..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SFD1"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SFD1"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SFD1"
FT BINDING 45..47
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SFD1"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SFD1"
FT SITE 136
FT /note="Participates in a stacking interaction with the
FT thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT /evidence="ECO:0000250|UniProtKB:Q5SFD1"
SQ SEQUENCE 204 AA; 22248 MW; DA2AC0153CE00778 CRC64;
MELLDVDGAW LYTPEIMRDE RGEFLEWFRG RTFQEKIGHP LSLAQANCSV SRKAFCAAST
SPTPPPGQAK YVTCASGTVL DVVVDVRRGS PTFGRWAAVR LDAARHQGLY LAEGLGHAFM
ALTDDATVVY LCSQPYVAEA ERAVDPLDPA IGIEWPTDID IVPVGEGTPT HRPWRRPRRP
GILPDYEGVP GALHRGGGRR GTGP
