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P29781 (RMLD_STRGR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
dTDP-4-dehydrorhamnose reductase

EC=1.1.1.133
Alternative name(s):
dTDP-4-keto-L-rhamnose reductase
dTDP-6-deoxy-L-lyxo-4-hexulose reductase
dTDP-6-deoxy-L-mannose dehydrogenase
dTDP-L-rhamnose synthase
Gene names
Name:strL
OrganismStreptomyces griseus
Taxonomic identifier1911 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of the streptose moiety of streptomycin. Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well By similarity. Ref.1

Catalytic activity

dTDP-beta-L-rhamnose + NADP+ = dTDP-4-dehydro-beta-L-rhamnose + NADPH.

Cofactor

Binds 1 magnesium ion per monomer By similarity.

Pathway

Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.

Antibiotic biosynthesis; streptomycin biosynthesis.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the dTDP-4-dehydrorhamnose reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304dTDP-4-dehydrorhamnose reductase
PRO_0000207989

Regions

Nucleotide binding13 – 197NADP Potential
Nucleotide binding13 – 175NAD By similarity
Nucleotide binding17 – 182NADP By similarity
Nucleotide binding36 – 372NAD By similarity
Nucleotide binding42 – 432NAD/NADP By similarity
Nucleotide binding65 – 684NAD By similarity
Nucleotide binding66 – 683NADP By similarity
Nucleotide binding131 – 1355NAD/NADP By similarity
Region107 – 1082Substrate binding By similarity

Sites

Binding site1571Substrate; via amide nitrogen By similarity
Binding site2271Substrate By similarity
Binding site2591Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P29781 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 7594F25D3F7ED0CB

FASTA30432,215
        10         20         30         40         50         60 
MSPYPRPRWL VTGASGMLGR ELTPLLDRRG AAVTALGRGH LDITDGAAVR SAVAEHRPAV 

        70         80         90        100        110        120 
VVNCAAWTAV DEAESEPALA MAVNGEGPRH LAQACRAVGA VLLQLSTDYV FPGSGGRPYR 

       130        140        150        160        170        180 
EDHPTGPRTV YGCTKRAGER AVLEVLPDTG YIVRTAWLYG AGGPNFVAKM IRLEADEDTV 

       190        200        210        220        230        240 
LVVDDQHGQP TWTADLADRL AALGAAALAG TAPAGIYHAT NTGGTTWNAL APETFRLLGA 

       250        260        270        280        290        300 
DPARVRPTTS LALARPAVRP RYSVLDQSRW KAAGLEPLRH WRAALTESFP ALCGRAGRPV 


PGPR 

« Hide

References

[1]"Genetics of streptomycin production in Streptomyces griseus: molecular structure and putative function of genes strELMB2N."
Pissowotzki K., Mansouri K., Piepersberg W.
Mol. Gen. Genet. 231:113-123(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BIOSYNTHESIS OF THE STREPTOSE MOIETY OF STREPTOMYCIN.
Strain: N2-3-11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62567 Genomic DNA. Translation: CAA44443.1.
PIRSYSMPG. S18618.

3D structure databases

ProteinModelPortalP29781.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00066.
UPA00124.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
TIGRFAMsTIGR01214. rmlD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRMLD_STRGR
AccessionPrimary (citable) accession number: P29781
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 11, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways