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P37760 (RMLD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:b2040, JW2025
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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_0000207984

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 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

Sequences

Sequence LengthMass (Da)Tools
P37760 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 1D7C992FA5017AD1

FASTA29932,694
        10         20         30         40         50         60 
MNILLFGKTG QVGWELQRAL APLGNLIAFD VHSTDYCGDF SNPEGVAETV RSIRPDIIVN 

        70         80         90        100        110        120 
AAAHTAVDKA ESEPEFAQLI NATSVEAIAK AANEVGAWVI HYSTDYVFPG NGDMPWLETD 

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

       190        200        210        220        230        240 
DQFGAPTGAE LLADCTAHAI RVALNKPDVA GLYHLVASGT TTWYDYAALV FEEARKAGIP 

       250        260        270        280        290 
LALNKLNAVP TTAYPTPARR PHNSRLNTEK FQQNFALVLP DWQVGVKRML NELFTTTAI 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the O antigen of Escherichia coli K-12 and the sequence of its rfb gene cluster."
Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M., Redmond J.W., Lindquist L., Reeves P.R.
J. Bacteriol. 176:4144-4156(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / WG1.
[2]Stevenson G.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 227.
[3]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09876 Genomic DNA. Translation: AAB88399.1.
U00096 Genomic DNA. Translation: AAC75101.1.
AP009048 Genomic DNA. Translation: BAA15882.1.
PIRG64969.
RefSeqNP_416544.1. NC_000913.3.
YP_490282.1. NC_007779.1.

3D structure databases

ProteinModelPortalP37760.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP37760. 5 interactions.
STRING511145.b2040.

Proteomic databases

PRIDEP37760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75101; AAC75101; b2040.
BAA15882; BAA15882; BAA15882.
GeneID12932555.
947117.
KEGGecj:Y75_p2003.
eco:b2040.
PATRIC32119413. VBIEscCol129921_2117.

Organism-specific databases

EchoBASEEB2310.
EcoGeneEG12411. rfbD.

Phylogenomic databases

HOGENOMHOG000227712.
KOK00067.
OMAETTWHGY.
OrthoDBEOG6HTP2V.
PhylomeDBP37760.

Enzyme and pathway databases

BioCycEcoCyc:DTDPDEHYRHAMREDUCT-MONOMER.
ECOL316407:JW2025-MONOMER.
MetaCyc:DTDPDEHYRHAMREDUCT-MONOMER.
UniPathwayUPA00124.
UPA00281.

Gene expression databases

GenevestigatorP37760.

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...

Other

PROP37760.

Entry information

Entry nameRMLD_ECOLI
AccessionPrimary (citable) accession number: P37760
Secondary accession number(s): P76377
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 113 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene