Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 127 (13 Nov 2019)
Sequence version 1 (01 Oct 1993)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

D-allulose-6-phosphate 3-epimerase

Gene

alsE

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 reversible epimerization of D-allulose 6-phosphate to D-fructose 6-phosphate. Can also catalyze with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.UniRule annotation2 Publications

<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

Co2+1 Publication, Mn2+1 Publication, Zn2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Activity is highest with Co2+ > Mn2+ > Zn2+.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: D-allose degradation

This protein is involved in the pathway D-allose degradation, which is part of Carbohydrate degradation.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway D-allose degradation and in Carbohydrate degradation.

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 sitei6SubstrateUniRule annotationCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi30Divalent metal cation; via tele nitrogenUniRule annotationCombined sources1 Publication1
<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 sitei32Proton acceptorUniRule annotationCombined sources1 Publication1
Metal bindingi32Divalent metal cationUniRule annotationCombined sources1 Publication1
Metal bindingi63Divalent metal cation; via pros nitrogenUniRule annotationCombined sources1 Publication1
Binding sitei63SubstrateUniRule annotationCombined sources1 Publication1
Active sitei173Proton donorUniRule annotationCombined sources1 Publication1
Metal bindingi173Divalent metal cationUniRule annotationCombined sources1 Publication1

<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

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 functionIsomerase
Biological processCarbohydrate metabolism
LigandCobalt, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11957-MONOMER
ECOL316407:JW4046-MONOMER
MetaCyc:EG11957-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P32719

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

More...
UniPathwayi
UPA00361

<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:
D-allulose-6-phosphate 3-epimeraseUniRule annotation (EC:5.1.3.-UniRule annotation1 Publication)
<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:alsEUniRule annotation
Synonyms:yjcU
Ordered Locus Names:b4085, JW4046
<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi196Missing : Shortens the substrate-binding pocket. Slightly lower activity towards allulose 6-phosphate and increased activity towards ribulose 5-phosphate. 1 Publication1
Mutagenesisi197Missing : Shortens the substrate-binding pocket. Slightly lower activity towards allulose 6-phosphate and increased activity towards ribulose 5-phosphate. 1 Publication1
Mutagenesisi198Missing : Shortens the substrate-binding pocket. Slightly lower activity towards allulose 6-phosphate and increased activity towards ribulose 5-phosphate. 1 Publication1

<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_00001715851 – 231D-allulose-6-phosphate 3-epimeraseAdd BLAST231

Proteomic databases

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

More...
PaxDbi
P32719

PRoteomics IDEntifications database

More...
PRIDEi
P32719

<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

Homohexamer. Trimer of dimers.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261233, 11 interactors

Protein interaction database and analysis system

More...
IntActi
P32719, 2 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b4085

<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

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P32719

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P32719

<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>Regioni140 – 143Substrate bindingUniRule annotationCombined sources1 Publication4
Regioni173 – 175Substrate bindingUniRule annotationCombined sources1 Publication3
Regioni195 – 197Substrate bindingUniRule annotationCombined sources1 Publication3

<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 ribulose-phosphate 3-epimerase family. AlsE subfamily.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105UP7 Bacteria
COG0036 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000259348

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32719

KEGG Orthology (KO)

More...
KOi
K17195

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P32719

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00429 RPE, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_02226 AlluloseP_3_epimer, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785 Aldolase_TIM
IPR000056 Ribul_P_3_epim-like
IPR011060 RibuloseP-bd_barrel

The PANTHER Classification System

More...
PANTHERi
PTHR11749 PTHR11749, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00834 Ribul_P_3_epim, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51366 SSF51366, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01085 RIBUL_P_3_EPIMER_1, 1 hit
PS01086 RIBUL_P_3_EPIMER_2, 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.

P32719-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKISPSLMCM DLLKFKEQIE FIDSHADYFH IDIMDGHFVP NLTLSPFFVS
60 70 80 90 100
QVKKLATKPL DCHLMVTRPQ DYIAQLARAG ADFITLHPET INGQAFRLID
110 120 130 140 150
EIRRHDMKVG LILNPETPVE AMKYYIHKAD KITVMTVDPG FAGQPFIPEM
160 170 180 190 200
LDKLAELKAW REREGLEYEI EVDGSCNQAT YEKLMAAGAD VFIVGTSGLF
210 220 230
NHAENIDEAW RIMTAQILAA KSEVQPHAKT A
Length:231
Mass (Da):26,109
Last modified:October 1, 1993 - v1
<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:i8FA92458D714D4B0
GO

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
U00006 Genomic DNA Translation: AAC43179.1
U00096 Genomic DNA Translation: AAC77046.1
AP009048 Genomic DNA Translation: BAE78088.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D65217

NCBI Reference Sequences

More...
RefSeqi
NP_418509.1, NC_000913.3
WP_001311314.1, NZ_STEB01000014.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77046; AAC77046; b4085
BAE78088; BAE78088; BAE78088

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948595

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4046
eco:b4085

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2615

<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
U00006 Genomic DNA Translation: AAC43179.1
U00096 Genomic DNA Translation: AAC77046.1
AP009048 Genomic DNA Translation: BAE78088.1
PIRiD65217
RefSeqiNP_418509.1, NC_000913.3
WP_001311314.1, NZ_STEB01000014.1

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
3CT7X-ray2.50A/B/C/D/E/F1-231[»]
3CTLX-ray2.20A/B/C/D/E/F1-231[»]
SMRiP32719
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4261233, 11 interactors
IntActiP32719, 2 interactors
STRINGi511145.b4085

Proteomic databases

PaxDbiP32719
PRIDEiP32719

Genome annotation databases

EnsemblBacteriaiAAC77046; AAC77046; b4085
BAE78088; BAE78088; BAE78088
GeneIDi948595
KEGGiecj:JW4046
eco:b4085
PATRICifig|1411691.4.peg.2615

Organism-specific databases

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

More...
EchoBASEi
EB1900

Phylogenomic databases

eggNOGiENOG4105UP7 Bacteria
COG0036 LUCA
HOGENOMiHOG000259348
InParanoidiP32719
KOiK17195
PhylomeDBiP32719

Enzyme and pathway databases

UniPathwayiUPA00361
BioCyciEcoCyc:EG11957-MONOMER
ECOL316407:JW4046-MONOMER
MetaCyc:EG11957-MONOMER
SABIO-RKiP32719

Miscellaneous databases

EvolutionaryTraceiP32719

Protein Ontology

More...
PROi
PR:P32719

Family and domain databases

CDDicd00429 RPE, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_02226 AlluloseP_3_epimer, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000056 Ribul_P_3_epim-like
IPR011060 RibuloseP-bd_barrel
PANTHERiPTHR11749 PTHR11749, 1 hit
PfamiView protein in Pfam
PF00834 Ribul_P_3_epim, 1 hit
SUPFAMiSSF51366 SSF51366, 1 hit
PROSITEiView protein in PROSITE
PS01085 RIBUL_P_3_EPIMER_1, 1 hit
PS01086 RIBUL_P_3_EPIMER_2, 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 nameiALSE_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: P32719
Secondary accession number(s): Q2M6L8
<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, 1993
Last sequence update: October 1, 1993
Last modified: November 13, 2019
This is version 127 of the entry and version 1 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. 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
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again