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Protein

dTDP-glucose 4,6-dehydratase 1

Gene

rfbB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction.By similarity

Catalytic activityi

dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.By similarity

Cofactori

NAD+By similarityNote: Binds 1 NAD+ per subunit.By similarity

Pathwayi: dTDP-L-rhamnose biosynthesis

This protein is involved in the pathway dTDP-L-rhamnose biosynthesis, which is part of Carbohydrate biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway dTDP-L-rhamnose biosynthesis and in Carbohydrate biosynthesis.

Pathwayi: LPS O-antigen biosynthesis

This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei80NAD; via carbonyl oxygenBy similarity1
Binding sitei84Substrate; via carbonyl oxygenBy similarity1
Binding sitei99NADBy similarity1
Active sitei134Proton donorBy similarity1
Active sitei135Proton acceptorBy similarity1
Active sitei167Proton acceptorBy similarity1
Binding sitei196SubstrateBy similarity1
Binding sitei197NAD; via amide nitrogenBy similarity1
Binding sitei231SubstrateBy similarity1
Binding sitei266SubstrateBy similarity1
Binding sitei357SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 13NADBy similarity7
Nucleotide bindingi32 – 35NADBy similarity4
Nucleotide bindingi58 – 59NADBy similarity2
Nucleotide bindingi167 – 171NADBy similarity5

GO - Molecular functioni

  • coenzyme binding Source: EcoCyc
  • dTDP-glucose 4,6-dehydratase activity Source: UniProtKB
  • identical protein binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:DTDPGLUCDEHYDRAT-MONOMER.
ECOL316407:JW2026-MONOMER.
MetaCyc:DTDPGLUCDEHYDRAT-MONOMER.
UniPathwayiUPA00124.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase 1By similarity (EC:4.2.1.46By similarity)
Gene namesi
Name:rfbB
Synonyms:rmlB
Ordered Locus Names:b2041, JW2026
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12412. rfbB.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001832381 – 361dTDP-glucose 4,6-dehydratase 1Add BLAST361

Proteomic databases

EPDiP37759.
PaxDbiP37759.
PRIDEiP37759.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259679. 173 interactors.
DIPiDIP-10680N.
IntActiP37759. 7 interactors.
MINTiMINT-1302103.
STRINGi511145.b2041.

Structurei

3D structure databases

ProteinModelPortaliP37759.
SMRiP37759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni133 – 135Substrate bindingBy similarity3
Regioni206 – 207Substrate bindingBy similarity2
Regioni222 – 224Substrate bindingBy similarity3
Regioni297 – 300Substrate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
HOGENOMiHOG000168006.
InParanoidiP37759.
KOiK01710.
OMAiGGWNEMT.
PhylomeDBiP37759.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.

Sequencei

Sequence statusi: Complete.

P37759-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKILVTGGAG FIGSAVVRHI INNTQDSVVN VDKLTYAGNR ESLADVSDSE
60 70 80 90 100
RYVFEHADIC DAPAMARIFA QHQPDAVMHL AAESHVDRSI TGPAAFIETN
110 120 130 140 150
IVGTYVLLEA ARNYWSALDS DKKNSFRFHH ISTDEVYGDL PHPDEVNNTE
160 170 180 190 200
ELPLFTETTA YAPSSPYSAS KASSDHLVRA WKRTYGLPTI VTNCSNNYGP
210 220 230 240 250
YHFPEKLIPL VILNALEGKA LPIYGKGDQI RDWLYVEDHA RALYTVVTEG
260 270 280 290 300
KAGETYNIGG HNEKKNIDVV LTICDLLDEI VPKEKSYREQ ITYVADRPGH
310 320 330 340 350
DRRYAIDAEK IGRALGWKPQ ETFESGIRKT VEWYLSNTKW VDNVKSGAYQ
360
SWIEQNYEGR Q
Length:361
Mass (Da):40,558
Last modified:November 1, 1997 - v2
Checksum:iC3F64643271C14C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti123K → E in AAB88398 (PubMed:7517391).Curated1
Sequence conflicti250G → V in AAB88398 (PubMed:7517391).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09876 Genomic DNA. Translation: AAB88398.1.
U00096 Genomic DNA. Translation: AAC75102.1.
AP009048 Genomic DNA. Translation: BAA15883.1.
PIRiH64969.
RefSeqiNP_416545.1. NC_000913.3.
WP_000699460.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75102; AAC75102; b2041.
BAA15883; BAA15883; BAA15883.
GeneIDi945276.
KEGGiecj:JW2026.
eco:b2041.
PATRICi32119415. VBIEscCol129921_2118.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09876 Genomic DNA. Translation: AAB88398.1.
U00096 Genomic DNA. Translation: AAC75102.1.
AP009048 Genomic DNA. Translation: BAA15883.1.
PIRiH64969.
RefSeqiNP_416545.1. NC_000913.3.
WP_000699460.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP37759.
SMRiP37759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259679. 173 interactors.
DIPiDIP-10680N.
IntActiP37759. 7 interactors.
MINTiMINT-1302103.
STRINGi511145.b2041.

Proteomic databases

EPDiP37759.
PaxDbiP37759.
PRIDEiP37759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75102; AAC75102; b2041.
BAA15883; BAA15883; BAA15883.
GeneIDi945276.
KEGGiecj:JW2026.
eco:b2041.
PATRICi32119415. VBIEscCol129921_2118.

Organism-specific databases

EchoBASEiEB2311.
EcoGeneiEG12412. rfbB.

Phylogenomic databases

eggNOGiENOG4105C1B. Bacteria.
COG1088. LUCA.
HOGENOMiHOG000168006.
InParanoidiP37759.
KOiK01710.
OMAiGGWNEMT.
PhylomeDBiP37759.

Enzyme and pathway databases

UniPathwayiUPA00124.
UPA00281.
BioCyciEcoCyc:DTDPGLUCDEHYDRAT-MONOMER.
ECOL316407:JW2026-MONOMER.
MetaCyc:DTDPGLUCDEHYDRAT-MONOMER.

Miscellaneous databases

PROiP37759.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005888. dTDP_Gluc_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR10366:SF41. PTHR10366:SF41. 1 hit.
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01181. dTDP_gluc_dehyt. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRMLB1_ECOLI
AccessioniPrimary (citable) accession number: P37759
Secondary accession number(s): P78082
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 138 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

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 one 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.