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P37760

- RMLD_ECOLI

UniProt

P37760 - RMLD_ECOLI

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Protein

dTDP-4-dehydrorhamnose reductase

Gene
rfbD, rmlD, b2040, JW2025
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 activityi

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

Cofactori

Binds 1 magnesium ion per monomer By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121NAD; via amide nitrogen By similarity
Binding sitei102 – 1021NADP; via carbonyl oxygen By similarity
Binding sitei153 – 1531Substrate; via amide nitrogen By similarity
Binding sitei154 – 1541NAD; via amide nitrogen By similarity
Binding sitei223 – 2231Substrate By similarity
Binding sitei260 – 2601Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 115NAD By similarity
Nucleotide bindingi11 – 122NADP By similarity
Nucleotide bindingi30 – 312NAD By similarity
Nucleotide bindingi39 – 402NAD/NADP By similarity
Nucleotide bindingi62 – 654NAD By similarity
Nucleotide bindingi63 – 653NADP By similarity
Nucleotide bindingi128 – 1325NAD/NADP By similarity

GO - Molecular functioni

  1. dTDP-4-dehydrorhamnose reductase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. dTDP-rhamnose biosynthetic process Source: UniProtKB-UniPathway
  2. extracellular polysaccharide biosynthetic process Source: UniProtKB
  3. lipopolysaccharide biosynthetic process Source: UniProtKB
  4. O antigen biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, NADP

Enzyme and pathway databases

BioCyciEcoCyc:DTDPDEHYRHAMREDUCT-MONOMER.
ECOL316407:JW2025-MONOMER.
MetaCyc:DTDPDEHYRHAMREDUCT-MONOMER.
UniPathwayiUPA00124.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:rfbD
Synonyms:rmlD
Ordered Locus Names:b2040, JW2025
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12411. rfbD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299dTDP-4-dehydrorhamnose reductasePRO_0000207984Add
BLAST

Proteomic databases

PRIDEiP37760.

Expressioni

Gene expression databases

GenevestigatoriP37760.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

IntActiP37760. 5 interactions.
STRINGi511145.b2040.

Structurei

3D structure databases

ProteinModelPortaliP37760.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni104 – 1052Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000227712.
KOiK00067.
OMAiETTWHGY.
OrthoDBiEOG6HTP2V.
PhylomeDBiP37760.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01214. rmlD. 1 hit.

Sequencei

Sequence statusi: Complete.

P37760-1 [UniParc]FASTAAdd to Basket

« Hide

MNILLFGKTG QVGWELQRAL APLGNLIAFD VHSTDYCGDF SNPEGVAETV    50
RSIRPDIIVN AAAHTAVDKA ESEPEFAQLI NATSVEAIAK AANEVGAWVI 100
HYSTDYVFPG NGDMPWLETD ATAPLNVYGE TKLAGEKALQ EYCAKHLIFR 150
TSWVYAGKGN NFAKTMLRLA KEREELAVIN DQFGAPTGAE LLADCTAHAI 200
RVALNKPDVA GLYHLVASGT TTWYDYAALV FEEARKAGIP LALNKLNAVP 250
TTAYPTPARR PHNSRLNTEK FQQNFALVLP DWQVGVKRML NELFTTTAI 299
Length:299
Mass (Da):32,694
Last modified:November 1, 1997 - v2
Checksum:i1D7C992FA5017AD1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09876 Genomic DNA. Translation: AAB88399.1.
U00096 Genomic DNA. Translation: AAC75101.1.
AP009048 Genomic DNA. Translation: BAA15882.1.
PIRiG64969.
RefSeqiNP_416544.1. NC_000913.3.
YP_490282.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75101; AAC75101; b2040.
BAA15882; BAA15882; BAA15882.
GeneIDi12932555.
947117.
KEGGiecj:Y75_p2003.
eco:b2040.
PATRICi32119413. VBIEscCol129921_2117.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09876 Genomic DNA. Translation: AAB88399.1 .
U00096 Genomic DNA. Translation: AAC75101.1 .
AP009048 Genomic DNA. Translation: BAA15882.1 .
PIRi G64969.
RefSeqi NP_416544.1. NC_000913.3.
YP_490282.1. NC_007779.1.

3D structure databases

ProteinModelPortali P37760.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P37760. 5 interactions.
STRINGi 511145.b2040.

Proteomic databases

PRIDEi P37760.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75101 ; AAC75101 ; b2040 .
BAA15882 ; BAA15882 ; BAA15882 .
GeneIDi 12932555.
947117.
KEGGi ecj:Y75_p2003.
eco:b2040.
PATRICi 32119413. VBIEscCol129921_2117.

Organism-specific databases

EchoBASEi EB2310.
EcoGenei EG12411. rfbD.

Phylogenomic databases

HOGENOMi HOG000227712.
KOi K00067.
OMAi ETTWHGY.
OrthoDBi EOG6HTP2V.
PhylomeDBi P37760.

Enzyme and pathway databases

UniPathwayi UPA00124 .
UPA00281 .
BioCyci EcoCyc:DTDPDEHYRHAMREDUCT-MONOMER.
ECOL316407:JW2025-MONOMER.
MetaCyc:DTDPDEHYRHAMREDUCT-MONOMER.

Miscellaneous databases

PROi P37760.

Gene expression databases

Genevestigatori P37760.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF04321. RmlD_sub_bind. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01214. rmlD. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. 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.

Entry informationi

Entry nameiRMLD_ECOLI
AccessioniPrimary (citable) accession number: P37760
Secondary accession number(s): P76377
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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