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Protein

dTDP-glucose 4,6-dehydratase 2

Gene

rffG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 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>
-Experimental evidence at protein leveli <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.3 Publications

Caution

Was originally thought to be rffE, the UDP-N-acetylglucosamine epimerase.1 Publication

<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+1 PublicationNote: Binds 1 NAD+ per subunit.1 Publication

<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-4-acetamido-4,6-dideoxygalactose biosynthesis

This protein is involved in the pathway dTDP-4-acetamido-4,6-dideoxygalactose biosynthesis, which is part of Nucleotide-sugar biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway dTDP-4-acetamido-4,6-dideoxygalactose biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: enterobacterial common antigen biosynthesis

This protein is involved in the pathway enterobacterial common 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 enterobacterial common antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei85Substrate; via carbonyl oxygenBy similarity1
Binding sitei100NADCombined sources1 Publication1
Binding sitei134SubstrateBy similarity1
<p>This subsection of the ‘Function’ 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 sitei135Proton donor2 Publications1
Active sitei136Proton acceptor2 Publications1
Active sitei160Proton acceptor2 Publications1
Binding sitei189SubstrateBy similarity1
Binding sitei190NAD; via amide nitrogenCombined sources1 Publication1
Binding sitei224SubstrateBy similarity1
Binding sitei259SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi12 – 13NADCombined sources1 Publication2
Nucleotide bindingi33 – 36NADCombined sources1 Publication4
Nucleotide bindingi59 – 60NADCombined sources1 Publication2
Nucleotide bindingi81 – 85NADCombined sources1 Publication5
Nucleotide bindingi160 – 164NADCombined sources1 Publication5

<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

  • dTDP-glucose 4,6-dehydratase activity Source: UniProtKB

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
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:DTDPGLUCDEHYDRAT2-MONOMER
MetaCyc:DTDPGLUCDEHYDRAT2-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.46 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P27830

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

More...
UniPathwayi
UPA00566

UPA00817

<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 21 Publication (EC:4.2.1.463 Publications)
<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:rffG
Ordered Locus Names:b3788, JW5598
<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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG11453 rffG

<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_00001832361 – 355dTDP-glucose 4,6-dehydratase 2Add BLAST355

Proteomic databases

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

More...
PaxDbi
P27830

PRoteomics IDEntifications database

More...
PRIDEi
P27830

<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.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262077, 235 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_3977

<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

Secondary structure

1355
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P27830

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

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SMRi
P27830

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P27830

<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>Regioni199 – 200Substrate bindingBy similarity2
Regioni215 – 217Substrate bindingBy similarity3
Regioni293 – 297Substrate 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

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
P27830

KEGG Orthology (KO)

More...
KOi
K01710

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P27830

Family and domain databases

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>.<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.

P27830-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRKILITGGA GFIGSALVRY IINETSDAVV VVDKLTYAGN LMSLAPVAQS
60 70 80 90 100
ERFAFEKVDI CDRAELARVF TEHQPDCVMH LAAESHVDRS IDGPAAFIET
110 120 130 140 150
NIVGTYTLLE AARAYWNALT EDKKSAFRFH HISTDEVYGD LHSTDDFFTE
160 170 180 190 200
TTPYAPSSPY SASKASSDHL VRAWLRTYGL PTLITNCSNN YGPYHFPEKL
210 220 230 240 250
IPLMILNALA GKSLPVYGNG QQIRDWLYVE DHARALYCVA TTGKVGETYN
260 270 280 290 300
IGGHNERKNL DVVETICELL EELAPNKPHG VAHYRDLITF VADRPGHDLR
310 320 330 340 350
YAIDASKIAR ELGWLPQETF ESGMRKTVQW YLANESWWKQ VQDGSYQGER

LGLKG
Length:355
Mass (Da):39,754
Last modified:November 23, 2004 - v3
<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:i34DBD1EFB42DB9B3
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 conflicti314 – 315WL → CV in AAA67588 (PubMed:1379743).Curated2

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
M87049 Genomic DNA Translation: AAA67588.1
U00096 Genomic DNA Translation: AAT48213.1
AP009048 Genomic DNA Translation: BAE77510.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G65182

NCBI Reference Sequences

More...
RefSeqi
WP_001226601.1, NZ_LN832404.1
YP_026255.1, NC_000913.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAT48213; AAT48213; b3788
BAE77510; BAE77510; BAE77510

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948300

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5598
eco:b3788

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.3904

<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
M87049 Genomic DNA Translation: AAA67588.1
U00096 Genomic DNA Translation: AAT48213.1
AP009048 Genomic DNA Translation: BAE77510.1
PIRiG65182
RefSeqiWP_001226601.1, NZ_LN832404.1
YP_026255.1, NC_000913.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BXKX-ray1.90A/B1-355[»]
ProteinModelPortaliP27830
SMRiP27830
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262077, 235 interactors
STRINGi316385.ECDH10B_3977

Proteomic databases

PaxDbiP27830
PRIDEiP27830

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48213; AAT48213; b3788
BAE77510; BAE77510; BAE77510
GeneIDi948300
KEGGiecj:JW5598
eco:b3788
PATRICifig|511145.12.peg.3904

Organism-specific databases

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

More...
EchoBASEi
EB1422
EcoGeneiEG11453 rffG

Phylogenomic databases

eggNOGiENOG4105C1B Bacteria
COG1088 LUCA
HOGENOMiHOG000168006
InParanoidiP27830
KOiK01710
PhylomeDBiP27830

Enzyme and pathway databases

UniPathwayi
UPA00566

UPA00817

BioCyciEcoCyc:DTDPGLUCDEHYDRAT2-MONOMER
MetaCyc:DTDPGLUCDEHYDRAT2-MONOMER
BRENDAi4.2.1.46 2026
SABIO-RKiP27830

Miscellaneous databases

EvolutionaryTraceiP27830

Protein Ontology

More...
PROi
PR:P27830

Family and domain databases

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...

<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 nameiRMLB2_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: P27830
Secondary accession number(s): P76754, Q2M896, Q6BF01
<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: August 1, 1992
Last sequence update: November 23, 2004
Last modified: December 5, 2018
This is version 151 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

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