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dTDP-4-dehydrorhamnose reductase (EC 1.1.1.133) (dTDP-4-keto-L-rhamnose reductase) (dTDP-6-deoxy-L-lyxo-4-hexulose reductase) (dTDP-6-deoxy-L-mannose dehydrogenase) (dTDP-L-rhamnose synthase)

 RMLD_STRGR              Reviewed;         304 AA.
P29781;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
18-JUL-2018, entry version 81.
RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000250|UniProtKB:P26392};
EC=1.1.1.133 {ECO:0000250|UniProtKB:P26392};
AltName: Full=dTDP-4-keto-L-rhamnose reductase {ECO:0000250|UniProtKB:P26392};
AltName: Full=dTDP-6-deoxy-L-lyxo-4-hexulose reductase {ECO:0000250|UniProtKB:P26392};
AltName: Full=dTDP-6-deoxy-L-mannose dehydrogenase {ECO:0000250|UniProtKB:P26392};
AltName: Full=dTDP-L-rhamnose synthase {ECO:0000250|UniProtKB:P26392};
Name=strL {ECO:0000303|PubMed:1661369};
Streptomyces griseus.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1911;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BIOSYNTHESIS OF THE
STREPTOSE MOIETY OF STREPTOMYCIN, AND PATHWAY.
STRAIN=N2-3-11;
PubMed=1661369; DOI=10.1007/BF00293829;
Pissowotzki K., Mansouri K., Piepersberg W.;
"Genetics of streptomycin production in Streptomyces griseus:
molecular structure and putative function of genes strELMB2N.";
Mol. Gen. Genet. 231:113-123(1991).
-!- FUNCTION: Involved in the biosynthesis of the streptose moiety of
streptomycin (PubMed:1661369). Catalyzes the reduction of dTDP-6-
deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity).
RmlD uses NADH and NADPH nearly equally well (By similarity).
{ECO:0000250|UniProtKB:P26392, ECO:0000269|PubMed:1661369}.
-!- CATALYTIC ACTIVITY: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-
dehydro-beta-L-rhamnose + NADPH. {ECO:0000250|UniProtKB:P26392}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P26392};
Note=Binds 1 Mg(2+) ion per monomer.
{ECO:0000250|UniProtKB:P26392};
-!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
{ECO:0000305|PubMed:1661369}.
-!- PATHWAY: Antibiotic biosynthesis; streptomycin biosynthesis.
{ECO:0000305|PubMed:1661369}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26392}.
-!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase
family. {ECO:0000305}.
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EMBL; X62567; CAA44443.1; -; Genomic_DNA.
PIR; S18618; SYSMPG.
ProteinModelPortal; P29781; -.
SMR; P29781; -.
eggNOG; ENOG4105DBZ; Bacteria.
eggNOG; COG1091; LUCA.
UniPathway; UPA00066; -.
UniPathway; UPA00124; -.
GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
GO; GO:0019872; P:streptomycin biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR005913; dTDP_dehydrorham_reduct.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR029903; RmlD-like-bd.
PANTHER; PTHR10491; PTHR10491; 1.
Pfam; PF04321; RmlD_sub_bind; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01214; rmlD; 1.
1: Evidence at protein level;
Antibiotic biosynthesis; Carbohydrate metabolism; Magnesium;
Metal-binding; NAD; NADP; Oxidoreductase; Streptomycin biosynthesis.
CHAIN 1 304 dTDP-4-dehydrorhamnose reductase.
/FTId=PRO_0000207989.
NP_BIND 16 18 NAD or NADP.
{ECO:0000250|UniProtKB:P26392}.
NP_BIND 42 43 NAD or NADP.
{ECO:0000250|UniProtKB:P26392}.
NP_BIND 66 68 NAD or NADP.
{ECO:0000250|UniProtKB:P26392}.
REGION 107 108 Substrate binding.
{ECO:0000250|UniProtKB:P26392}.
ACT_SITE 131 131 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P26392}.
BINDING 135 135 NAD or NADP.
{ECO:0000250|UniProtKB:P26392}.
BINDING 157 157 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P26392}.
SITE 107 107 Could provide a fine-tuning to achieve
optimal pKa matching between active site
and substrate.
{ECO:0000250|UniProtKB:P26392}.
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


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