RMLD_STRGR
ID RMLD_STRGR Reviewed; 304 AA.
AC P29781;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000250|UniProtKB:P26392};
DE EC=1.1.1.133 {ECO:0000250|UniProtKB:P26392};
DE AltName: Full=dTDP-4-keto-L-rhamnose reductase {ECO:0000250|UniProtKB:P26392};
DE AltName: Full=dTDP-6-deoxy-L-lyxo-4-hexulose reductase {ECO:0000250|UniProtKB:P26392};
DE AltName: Full=dTDP-6-deoxy-L-mannose dehydrogenase {ECO:0000250|UniProtKB:P26392};
DE AltName: Full=dTDP-L-rhamnose synthase {ECO:0000250|UniProtKB:P26392};
GN Name=strL {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 streptose moiety of
CC streptomycin (PubMed:1661369). Catalyzes the reduction of dTDP-6-deoxy-
CC L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity). RmlD uses
CC NADH and NADPH nearly equally well (By similarity).
CC {ECO:0000250|UniProtKB:P26392, ECO:0000269|PubMed:1661369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-
CC rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:62830; EC=1.1.1.133;
CC Evidence={ECO:0000250|UniProtKB:P26392};
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: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000305|PubMed:1661369}.
CC -!- PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis.
CC {ECO:0000305|PubMed:1661369}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26392}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC {ECO:0000305}.
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DR EMBL; X62567; CAA44443.1; -; Genomic_DNA.
DR PIR; S18618; SYSMPG.
DR AlphaFoldDB; P29781; -.
DR SMR; P29781; -.
DR UniPathway; UPA00066; -.
DR UniPathway; UPA00124; -.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Antibiotic biosynthesis; Carbohydrate metabolism; Magnesium; Metal-binding;
KW NAD; NADP; Oxidoreductase; Streptomycin biosynthesis.
FT CHAIN 1..304
FT /note="dTDP-4-dehydrorhamnose reductase"
FT /id="PRO_0000207989"
FT ACT_SITE 131
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 16..18
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 17..18
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 42..43
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 42..43
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 66..68
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 66..68
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 107..108
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 131
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 131
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 135
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 135
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 157
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT SITE 107
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 304 AA; 32215 MW; 7594F25D3F7ED0CB CRC64;
MSPYPRPRWL VTGASGMLGR ELTPLLDRRG AAVTALGRGH LDITDGAAVR SAVAEHRPAV
VVNCAAWTAV DEAESEPALA MAVNGEGPRH LAQACRAVGA VLLQLSTDYV FPGSGGRPYR
EDHPTGPRTV YGCTKRAGER AVLEVLPDTG YIVRTAWLYG AGGPNFVAKM IRLEADEDTV
LVVDDQHGQP TWTADLADRL AALGAAALAG TAPAGIYHAT NTGGTTWNAL APETFRLLGA
DPARVRPTTS LALARPAVRP RYSVLDQSRW KAAGLEPLRH WRAALTESFP ALCGRAGRPV
PGPR
