Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

D-allulose-6-phosphate 3-epimerase

Gene

alsE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.2 Publications

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

Pathwayi: D-allose degradation

This protein is involved in the pathway D-allose degradation, which is part of Carbohydrate degradation.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei6 – 61Substrate
Metal bindingi30 – 301Divalent metal cation
Active sitei32 – 321Proton acceptor
Metal bindingi32 – 321Divalent metal cation
Metal bindingi63 – 631Divalent metal cation
Binding sitei63 – 631Substrate
Active sitei173 – 1731Proton donor
Metal bindingi173 – 1731Divalent metal cation

GO - Molecular functioni

  • allulose 6-phosphate 3-epimerase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB
  • ribulose-phosphate 3-epimerase activity Source: GO_Central

GO - Biological processi

  • cellular carbohydrate metabolic process Source: UniProtKB
  • D-allose catabolic process Source: EcoCyc
  • pentose catabolic process Source: GO_Central
  • pentose-phosphate shunt, non-oxidative branch Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Cobalt, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG11957-MONOMER.
ECOL316407:JW4046-MONOMER.
MetaCyc:EG11957-MONOMER.
SABIO-RKP32719.
UniPathwayiUPA00361.

Names & Taxonomyi

Protein namesi
Recommended name:
D-allulose-6-phosphate 3-epimerase (EC:5.1.3.-)
Gene namesi
Name:alsE
Synonyms:yjcU
Ordered Locus Names:b4085, JW4046
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11957. alsE.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi196 – 1961Missing : Shortens the substrate-binding pocket. Slightly lower activity towards allulose 6-phosphate and increased activity towards ribulose 5-phosphate. 1 Publication
Mutagenesisi197 – 1971Missing : Shortens the substrate-binding pocket. Slightly lower activity towards allulose 6-phosphate and increased activity towards ribulose 5-phosphate. 1 Publication
Mutagenesisi198 – 1981Missing : Shortens the substrate-binding pocket. Slightly lower activity towards allulose 6-phosphate and increased activity towards ribulose 5-phosphate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231D-allulose-6-phosphate 3-epimerasePRO_0000171585Add
BLAST

Proteomic databases

PaxDbiP32719.
PRIDEiP32719.

Interactioni

Subunit structurei

Homohexamer. Trimer of dimers.1 Publication

Protein-protein interaction databases

BioGridi4261233. 11 interactions.
IntActiP32719. 2 interactions.
STRINGi511145.b4085.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi7 – 93Combined sources
Helixi12 – 143Combined sources
Helixi15 – 239Combined sources
Beta strandi29 – 346Combined sources
Beta strandi36 – 405Combined sources
Helixi46 – 538Combined sources
Beta strandi60 – 678Combined sources
Helixi69 – 713Combined sources
Helixi73 – 797Combined sources
Beta strandi82 – 865Combined sources
Helixi88 – 903Combined sources
Turni92 – 943Combined sources
Helixi95 – 10410Combined sources
Beta strandi108 – 1136Combined sources
Helixi119 – 1224Combined sources
Turni123 – 1253Combined sources
Helixi126 – 1283Combined sources
Beta strandi130 – 1378Combined sources
Helixi150 – 16415Combined sources
Beta strandi169 – 1746Combined sources
Turni178 – 1803Combined sources
Helixi181 – 1877Combined sources
Beta strandi191 – 1944Combined sources
Turni196 – 1994Combined sources
Helixi200 – 2023Combined sources
Helixi206 – 21813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CT7X-ray2.50A/B/C/D/E/F1-231[»]
3CTLX-ray2.20A/B/C/D/E/F1-231[»]
ProteinModelPortaliP32719.
SMRiP32719. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32719.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 1434Substrate binding
Regioni173 – 1753Substrate binding
Regioni195 – 1973Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105UP7. Bacteria.
COG0036. LUCA.
HOGENOMiHOG000259348.
InParanoidiP32719.
KOiK17195.
OMAiPQDYISQ.
PhylomeDBiP32719.

Family and domain databases

CDDicd00429. RPE. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i8FA92458D714D4B0
GO

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_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77046; AAC77046; b4085.
BAE78088; BAE78088; BAE78088.
GeneIDi948595.
KEGGiecj:JW4046.
eco:b4085.
PATRICi32123725. VBIEscCol129921_4211.

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_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CT7X-ray2.50A/B/C/D/E/F1-231[»]
3CTLX-ray2.20A/B/C/D/E/F1-231[»]
ProteinModelPortaliP32719.
SMRiP32719. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261233. 11 interactions.
IntActiP32719. 2 interactions.
STRINGi511145.b4085.

Proteomic databases

PaxDbiP32719.
PRIDEiP32719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77046; AAC77046; b4085.
BAE78088; BAE78088; BAE78088.
GeneIDi948595.
KEGGiecj:JW4046.
eco:b4085.
PATRICi32123725. VBIEscCol129921_4211.

Organism-specific databases

EchoBASEiEB1900.
EcoGeneiEG11957. alsE.

Phylogenomic databases

eggNOGiENOG4105UP7. Bacteria.
COG0036. LUCA.
HOGENOMiHOG000259348.
InParanoidiP32719.
KOiK17195.
OMAiPQDYISQ.
PhylomeDBiP32719.

Enzyme and pathway databases

UniPathwayiUPA00361.
BioCyciEcoCyc:EG11957-MONOMER.
ECOL316407:JW4046-MONOMER.
MetaCyc:EG11957-MONOMER.
SABIO-RKP32719.

Miscellaneous databases

EvolutionaryTraceiP32719.
PROiP32719.

Family and domain databases

CDDicd00429. RPE. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALSE_ECOLI
AccessioniPrimary (citable) accession number: P32719
Secondary accession number(s): Q2M6L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 7, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.