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Protein

dTDP-4-dehydrorhamnose reductase

Gene

rfbD

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per monomer.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121NAD; via amide nitrogenBy similarity
Binding sitei102 – 1021NADP; via carbonyl oxygenBy similarity
Binding sitei155 – 1551Substrate; via amide nitrogenBy similarity
Binding sitei156 – 1561NAD; via amide nitrogenBy similarity
Binding sitei225 – 2251SubstrateBy similarity
Binding sitei262 – 2621SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 115NADBy similarity
Nucleotide bindingi11 – 122NADPBy similarity
Nucleotide bindingi30 – 312NADBy similarity
Nucleotide bindingi39 – 402NAD/NADPBy similarity
Nucleotide bindingi62 – 654NADBy similarity
Nucleotide bindingi63 – 653NADPBy similarity
Nucleotide bindingi129 – 1335NAD/NADPBy 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

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
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301dTDP-4-dehydrorhamnose reductasePRO_0000207985Add
BLAST

Proteomic databases

PaxDbiQ46769.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ46769.
SMRiQ46769. Positions 1-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1091.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
IPR029900. RmlD.
IPR029903. RmlD-like-bd.
[Graphical view]
PANTHERiPTHR10491. PTHR10491. 1 hit.
PTHR10491:SF5. PTHR10491:SF5. 1 hit.
PfamiPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01214. rmlD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q46769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNILLFGKTG QVGWELQRAL APLGNLIALD VHSTDYCGDF SNPEGVAETV
60 70 80 90 100
KKIRPDVIVN AAAHTDVDKA ESEPEFAQLL NATSVEAIAK AANEVGAWVI
110 120 130 140 150
HYSTDYVFPG TGEIPWQGGT DATAPLNVYG ETKLSSEKKA LQKHCGKHII
160 170 180 190 200
FRTSWVYAGK GNNFAKTMLR LAKEREELAV INDQFGRPTG AELLADCTAH
210 220 230 240 250
AIRVAVDKPE VAGLYHLVAG GTTTWHDYAA LVFEEARKAG INLALNKLNA
260 270 280 290 300
VPTTAYPTPA RRPHNSRLNT EKFQQNFALV LPDWQVGVKR MLNELFTTTA

I
Length:301
Mass (Da):32,866
Last modified:October 31, 1996 - v1
Checksum:iA1C4271C20AB4A13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125322 Genomic DNA. Translation: AAC63613.1.
PIRiS78543.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125322 Genomic DNA. Translation: AAC63613.1.
PIRiS78543.

3D structure databases

ProteinModelPortaliQ46769.
SMRiQ46769. Positions 1-299.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ46769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1091.

Enzyme and pathway databases

UniPathwayiUPA00124.
UPA00281.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005913. dTDP_dehydrorham_reduct.
IPR016040. NAD(P)-bd_dom.
IPR029900. RmlD.
IPR029903. RmlD-like-bd.
[Graphical view]
PANTHERiPTHR10491. PTHR10491. 1 hit.
PTHR10491:SF5. PTHR10491:SF5. 1 hit.
PfamiPF04321. RmlD_sub_bind. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01214. rmlD. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS.
    Strain: O7:K1 / VW187.

Entry informationi

Entry nameiRMLD_ECOLX
AccessioniPrimary (citable) accession number: Q46769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: October 31, 1996
Last modified: March 31, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.