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Q46769 (RMLD_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 68. 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:rfbD
Synonyms:rmlD
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well. 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.

Bacterial outer membrane biogenesis; LPS O-antigen 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 – 301301dTDP-4-dehydrorhamnose reductase
PRO_0000207985

Regions

Nucleotide binding7 – 115NAD By similarity
Nucleotide binding11 – 122NADP By similarity
Nucleotide binding30 – 312NAD By similarity
Nucleotide binding39 – 402NAD/NADP By similarity
Nucleotide binding62 – 654NAD By similarity
Nucleotide binding63 – 653NADP By similarity
Nucleotide binding129 – 1335NAD/NADP By similarity
Region104 – 1052Substrate binding By similarity

Sites

Binding site121NAD; via amide nitrogen By similarity
Binding site1021NADP; via carbonyl oxygen By similarity
Binding site1551Substrate; via amide nitrogen By similarity
Binding site1561NAD; via amide nitrogen By similarity
Binding site2251Substrate By similarity
Binding site2621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46769 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A1C4271C20AB4A13

FASTA30132,866
        10         20         30         40         50         60 
MNILLFGKTG QVGWELQRAL APLGNLIALD VHSTDYCGDF SNPEGVAETV KKIRPDVIVN 

        70         80         90        100        110        120 
AAAHTDVDKA ESEPEFAQLL NATSVEAIAK AANEVGAWVI HYSTDYVFPG TGEIPWQGGT 

       130        140        150        160        170        180 
DATAPLNVYG ETKLSSEKKA LQKHCGKHII FRTSWVYAGK GNNFAKTMLR LAKEREELAV 

       190        200        210        220        230        240 
INDQFGRPTG AELLADCTAH AIRVAVDKPE VAGLYHLVAG GTTTWHDYAA LVFEEARKAG 

       250        260        270        280        290        300 
INLALNKLNA VPTTAYPTPA RRPHNSRLNT EKFQQNFALV LPDWQVGVKR MLNELFTTTA 


I 

« Hide

References

[1]"Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene."
Marolda C.L., Valvano M.A.
J. Bacteriol. 177:5539-5546(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS.
Strain: O7:K1 / VW187.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF125322 Genomic DNA. Translation: AAC63613.1.
PIRS78543.

3D structure databases

ProteinModelPortalQ46769.
SMRQ46769. Positions 1-299.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ46769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1091.

Enzyme and pathway databases

UniPathwayUPA00124.
UPA00281.

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_ECOLX
AccessionPrimary (citable) accession number: Q46769
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 68 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