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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)DescriptionActionsGraphical viewLength
Binding sitei6Substrate1
Metal bindingi30Divalent metal cation1
Active sitei32Proton acceptor1
Metal bindingi32Divalent metal cation1
Metal bindingi63Divalent metal cation1
Binding sitei63Substrate1
Active sitei173Proton donor1
Metal bindingi173Divalent metal cation1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001715851 – 231D-allulose-6-phosphate 3-epimeraseAdd BLAST231

Proteomic databases

PaxDbiP32719.
PRIDEiP32719.

Interactioni

Subunit structurei

Homohexamer. Trimer of dimers.1 Publication

Protein-protein interaction databases

BioGridi4261233. 11 interactors.
IntActiP32719. 2 interactors.
STRINGi511145.b4085.

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi7 – 9Combined sources3
Helixi12 – 14Combined sources3
Helixi15 – 23Combined sources9
Beta strandi29 – 34Combined sources6
Beta strandi36 – 40Combined sources5
Helixi46 – 53Combined sources8
Beta strandi60 – 67Combined sources8
Helixi69 – 71Combined sources3
Helixi73 – 79Combined sources7
Beta strandi82 – 86Combined sources5
Helixi88 – 90Combined sources3
Turni92 – 94Combined sources3
Helixi95 – 104Combined sources10
Beta strandi108 – 113Combined sources6
Helixi119 – 122Combined sources4
Turni123 – 125Combined sources3
Helixi126 – 128Combined sources3
Beta strandi130 – 137Combined sources8
Helixi150 – 164Combined sources15
Beta strandi169 – 174Combined sources6
Turni178 – 180Combined sources3
Helixi181 – 187Combined sources7
Beta strandi191 – 194Combined sources4
Turni196 – 199Combined sources4
Helixi200 – 202Combined sources3
Helixi206 – 218Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP32719.
SMRiP32719.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32719.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni140 – 143Substrate binding4
Regioni173 – 175Substrate binding3
Regioni195 – 197Substrate binding3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CT7X-ray2.50A/B/C/D/E/F1-231[»]
3CTLX-ray2.20A/B/C/D/E/F1-231[»]
ProteinModelPortaliP32719.
SMRiP32719.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261233. 11 interactors.
IntActiP32719. 2 interactors.
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: November 2, 2016
This is version 114 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.