ID   RMLC_STRGR              Reviewed;         200 AA.
AC   P29783;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=dTDP-4-dehydrorhamnose 3,5-epimerase {ECO:0000250|UniProtKB:P9WH11};
DE            EC=5.1.3.13 {ECO:0000250|UniProtKB:P9WH11};
DE   AltName: Full=Thymidine diphospho-4-keto-rhamnose 3,5-epimerase {ECO:0000250|UniProtKB:P9WH11};
DE   AltName: Full=dTDP-4-keto-6-deoxyglucose 3,5-epimerase {ECO:0000303|PubMed:1661369};
DE   AltName: Full=dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase {ECO:0000250|UniProtKB:P9WH11};
DE   AltName: Full=dTDP-L-rhamnose synthase {ECO:0000250|UniProtKB:P9WH11};
GN   Name=strM {ECO:0000303|PubMed:1661369};
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BIOSYNTHESIS OF THE
RP   STREPTOSE MOIETY OF STREPTOMYCIN, AND PATHWAY.
RC   STRAIN=N2-3-11;
RX   PubMed=1661369; DOI=10.1007/bf00293829;
RA   Pissowotzki K., Mansouri K., Piepersberg W.;
RT   "Genetics of streptomycin production in Streptomyces griseus: molecular
RT   structure and putative function of genes strELMB2N.";
RL   Mol. Gen. Genet. 231:113-123(1991).
CC   -!- FUNCTION: Involved in the biosynthesis of the dihydrostreptose moiety
CC       of streptomycin (PubMed:1661369). Catalyzes the epimerization of the
CC       C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-
CC       deoxy-L-lyxo-4-hexulose (By similarity). {ECO:0000250|UniProtKB:P9WH11,
CC       ECO:0000269|PubMed:1661369}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-
CC         L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649,
CC         ChEBI:CHEBI:62830; EC=5.1.3.13;
CC         Evidence={ECO:0000250|UniProtKB:P9WH11};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000250|UniProtKB:P26394}.
CC   -!- PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis.
CC       {ECO:0000305|PubMed:1661369}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; X62567; CAA44442.1; -; Genomic_DNA.
DR   PIR; S18619; XUSMEG.
DR   RefSeq; WP_003970234.1; NZ_UAVD01000010.1.
DR   AlphaFoldDB; P29783; -.
DR   SMR; P29783; -.
DR   GeneID; 6214583; -.
DR   OMA; RGVFLEW; -.
DR   UniPathway; UPA00066; -.
DR   UniPathway; UPA00124; -.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Carbohydrate metabolism; Isomerase;
KW   Streptomycin biosynthesis.
FT   CHAIN           1..200
FT                   /note="dTDP-4-dehydrorhamnose 3,5-epimerase"
FT                   /id="PRO_0000207983"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         45..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   SITE            135
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   200 AA;  21956 MW;  DB63F5BFC218932E CRC64;
     MRPLSVQGAW LSETRAFADD RGEFQELYSA RSLRGALGYD PGVAQVNRSV SRRGVLRGVH
     FAQLPPSQAK YVTCLSGAVL DVVVDIRTGS PTYRAWEAVR LDDPHRSLYV EAGLGHSFMA
     LTDDAVVVYL TSQGYAAGRE HGVHPLDPDL GIAWPDGIEP VLSEKDRQAP GIAEMERRGL
     LPDYEECLAF RRSLCERGTG