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Entry version 162 (13 Nov 2019)
Sequence version 2 (01 Nov 1997)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei84Substrate; via carbonyl oxygenBy similarity1
Binding sitei99NADBy similarity1
Binding sitei133SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi11 – 12NADBy similarity2
Nucleotide bindingi32 – 35NADBy similarity4
Nucleotide bindingi58 – 59NADBy similarity2
Nucleotide bindingi80 – 84NADBy similarity5
Nucleotide bindingi167 – 171NADBy similarity5

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processLipopolysaccharide biosynthesis
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:DTDPGLUCDEHYDRAT-MONOMER
ECOL316407:JW2026-MONOMER
MetaCyc:DTDPGLUCDEHYDRAT-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P37759

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00124
UPA00281

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
dTDP-glucose 4,6-dehydratase 1By similarity (EC:4.2.1.46By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:rfbB
Synonyms:rmlB
Ordered Locus Names:b2041, JW2026
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001832381 – 361dTDP-glucose 4,6-dehydratase 1Add BLAST361

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P37759

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P37759

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P37759

PRoteomics IDEntifications database

More...
PRIDEi
P37759

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259679, 184 interactors
849655, 4 interactors

Database of interacting proteins

More...
DIPi
DIP-10680N

Protein interaction database and analysis system

More...
IntActi
P37759, 7 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2041

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P37759

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni206 – 207Substrate bindingBy similarity2
Regioni222 – 224Substrate bindingBy similarity3
Regioni296 – 300Substrate bindingBy similarity5

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily.By similarity

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C1B Bacteria
COG1088 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000168006

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P37759

KEGG Orthology (KO)

More...
KOi
K01710

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P37759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05246 dTDP_GD_SDR_e, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005888 dTDP_Gluc_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01181 dTDP_gluc_dehyt, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC3F64643271C14C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti123K → E in AAB88398 (PubMed:7517391).Curated1
Sequence conflicti250G → V in AAB88398 (PubMed:7517391).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U09876 Genomic DNA Translation: AAB88398.1
U00096 Genomic DNA Translation: AAC75102.1
AP009048 Genomic DNA Translation: BAA15883.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H64969

NCBI Reference Sequences

More...
RefSeqi
NP_416545.1, NC_000913.3
WP_000699460.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75102; AAC75102; b2041
BAA15883; BAA15883; BAA15883

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945276

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2026
eco:b2041

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.210

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

SMRiP37759
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4259679, 184 interactors
849655, 4 interactors
DIPiDIP-10680N
IntActiP37759, 7 interactors
STRINGi511145.b2041

Proteomic databases

EPDiP37759
jPOSTiP37759
PaxDbiP37759
PRIDEiP37759

Genome annotation databases

EnsemblBacteriaiAAC75102; AAC75102; b2041
BAA15883; BAA15883; BAA15883
GeneIDi945276
KEGGiecj:JW2026
eco:b2041
PATRICifig|1411691.4.peg.210

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2311

Phylogenomic databases

eggNOGiENOG4105C1B Bacteria
COG1088 LUCA
HOGENOMiHOG000168006
InParanoidiP37759
KOiK01710
PhylomeDBiP37759

Enzyme and pathway databases

UniPathwayiUPA00124
UPA00281
BioCyciEcoCyc:DTDPGLUCDEHYDRAT-MONOMER
ECOL316407:JW2026-MONOMER
MetaCyc:DTDPGLUCDEHYDRAT-MONOMER
SABIO-RKiP37759

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P37759

Family and domain databases

CDDicd05246 dTDP_GD_SDR_e, 1 hit
InterProiView protein in InterPro
IPR005888 dTDP_Gluc_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01181 dTDP_gluc_dehyt, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRMLB1_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P37759
Secondary accession number(s): P78082
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: November 13, 2019
This is version 162 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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