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P37778 (RMLD_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 100. 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
Ordered Locus Names:SF2103, S2226
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length299 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 – 299299dTDP-4-dehydrorhamnose reductase
PRO_0000207987

Regions

Nucleotide binding7 – 137NADP Potential
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 binding128 – 1325NAD/NADP By similarity
Region104 – 1052Substrate binding By similarity

Sites

Binding site121NAD; via amide nitrogen By similarity
Binding site1021NADP; via carbonyl oxygen By similarity
Binding site1531Substrate; via amide nitrogen By similarity
Binding site1541NAD; via amide nitrogen By similarity
Binding site2231Substrate By similarity
Binding site2601Substrate By similarity

Experimental info

Sequence conflict891A → I in CAA50768. Ref.1
Sequence conflict1151P → A in CAA50768. Ref.1
Sequence conflict1301E → G in CAA50768. Ref.1
Sequence conflict135 – 1362GE → WG in CAA50768. Ref.1
Sequence conflict1411E → D in CAA50768. Ref.1
Sequence conflict1441A → G in CAA50768. Ref.1
Sequence conflict1721E → D in CAA50768. Ref.1
Sequence conflict1751E → T in CAA50768. Ref.1
Sequence conflict1801N → T in CAA50768. Ref.1
Sequence conflict1901E → LD in CAA50768. Ref.1
Sequence conflict1971A → R in CAA50768. Ref.1
Sequence conflict201 – 2022RV → WL in CAA50768. Ref.1
Sequence conflict2271A → P in CAA50768. Ref.1
Sequence conflict2321E → K in CAA50768. Ref.1
Sequence conflict2391I → F in CAA50768. Ref.1
Sequence conflict2421A → P in CAA50768. Ref.1
Sequence conflict2601R → G in CAA50768. Ref.1
Sequence conflict2641S → F in CAA50768. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37778 [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: F2C6EF7BA8BD54DE

FASTA29932,565
        10         20         30         40         50         60 
MNILLFGKTG QVGWELQRAL APLGNLIALD VHSTDYCGDF SNPEGVAETV KKIRPDVIVN 

        70         80         90        100        110        120 
AAAHTAVDKA ESEPNFAQLL NATCVEAIAK AANEVGAWVI HYSTDYVFPG NGDTPWLETD 

       130        140        150        160        170        180 
ATAPLNVYGE TKLAGEKALQ EHCAKHLIFR TSWVYAGKGN NFAKTMLRLA KEREELAVIN 

       190        200        210        220        230        240 
DQFGAPTGAE LLADCTAHAI RVAANKPEVA GLYHLVAGGT TTWHDYAALV FEEARRAGIN 

       250        260        270        280        290 
LALNKLNAVP TTAYPTPARR PHNSRLNTEK FQQNFALVLP DWQVGVKRML NELFTTTAI 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the dTDP-rhamnose biosynthetic genes encoded in the rfb locus of Shigella flexneri."
Macpherson D.F., Manning P.A., Morona R.
Mol. Microbiol. 11:281-292(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS.
Strain: PE577 / Serotype 2a.
[2]"Nucleotide sequence of the rhamnose biosynthetic operon of Shigella flexneri 2a and role of lipopolysaccharide in virulence."
Rajakumar K., Jost B.H., Sasakawa C., Okada N., Yoshikawa M., Adler B.
J. Bacteriol. 176:2362-2373(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: YSH6200 / Serotype 2a.
[3]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[4]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71970 Genomic DNA. Translation: CAA50768.1.
L14842 Genomic DNA. Translation: AAA53680.1.
AE005674 Genomic DNA. Translation: AAN43642.1.
AE014073 Genomic DNA. Translation: AAP17471.1.
PIRC55213.
S41535.
RefSeqNP_707935.1. NC_004337.2.
NP_837662.1. NC_004741.1.

3D structure databases

ProteinModelPortalP37778.
SMRP37778. Positions 1-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF2103.

Proteomic databases

PaxDbP37778.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN43642; AAN43642; SF2103.
AAP17471; AAP17471; S2226.
GeneID1025316.
1078509.
KEGGsfl:SF2103.
sfx:S2226.
PATRIC18705959. VBIShiFle31049_2458.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1091.
HOGENOMHOG000227712.
KOK00067.
OMAPYWRDSL.
OrthoDBEOG6HTP2V.
ProtClustDBPRK09987.

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_SHIFL
AccessionPrimary (citable) accession number: P37778
Secondary accession number(s): Q54163
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 10, 2003
Last modified: December 11, 2013
This is version 100 of the entry and version 2 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