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B6I385 (TREF_ECOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic trehalase

EC=3.2.1.28
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
Gene names
Name:treF
Ordered Locus Names:ECSE_3788
OrganismEscherichia coli (strain SE11) [Complete proteome] [HAMAP]
Taxonomic identifier409438 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolyzes trehalose to glucose. Could be involved, in cells returning to low osmolarity conditions, in the utilization of the accumulated cytoplasmic trehalose, which was synthesized in response to high osmolarity By similarity. HAMAP MF_01059

Catalytic activity

Alpha,alpha-trehalose + H2O = 2 D-glucose. HAMAP MF_01059

Pathway

Glycan degradation; trehalose degradation; D-glucose from alpha,alpha-trehalose: step 1/1. HAMAP MF_01059

Subunit structure

Monomer By similarity. HAMAP MF_01059

Subcellular location

Cytoplasm By similarity HAMAP MF_01059.

Sequence similarities

Belongs to the glycosyl hydrolase 37 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular hyperosmotic response

Inferred from electronic annotation. Source: InterPro

trehalose catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha,alpha-trehalase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 549549Cytoplasmic trehalase HAMAP MF_01059
PRO_1000136405

Sequences

Sequence LengthMass (Da)Tools
B6I385 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 543B83F6BFC1CB9D

FASTA54963,715
        10         20         30         40         50         60 
MLNQKIQNPN PDELMIEVDL CYELDPYELK LDEMIEAEPE PEMIEGLPAS DALTPADRYL 

        70         80         90        100        110        120 
ELFEHVQSAK IFPDSKTFPD CAPKMDPLDI LIRYRKVRRH RDFDLRKFVE NHFWLPEVYS 

       130        140        150        160        170        180 
SEYVSDPQNS LKEHIDQLWP VLTREPQDHI PWSSLLALPQ SYIVPGGRFS ETYYWDSYFT 

       190        200        210        220        230        240 
MLGLAESGRE DLLKCMADNF AWMIENYGHI PNGNRTYYLS RSQPPVFALM VELFEEDGVR 

       250        260        270        280        290        300 
GARRYLDHLK MEYAFWMDGA ESLIPNQAYR HVVRMPDGSL LNRYWDDRDT PRDESWLEDV 

       310        320        330        340        350        360 
ETAKHSGRPP NEVYRDLRAG AASGWDYSSR WLRDTGRLAS IRTTQFIPID LNAFLFKLES 

       370        380        390        400        410        420 
AIANISALKG EKETEALFRQ KASARRDAVN RYLWDDENGI YRDYDWRREQ LALFSAAAIV 

       430        440        450        460        470        480 
PLYVGMANHE QADRLANAVR SRLLTPGGIL ASEYETGEQW DKPNGWAPLQ WMAIQGFKMY 

       490        500        510        520        530        540 
GDDLLGDEIA RSWLKTVNQF YLEQHKMIEK YHIADGVPRE GGGGEYPLQD GFGWTNGVVR 


RLIGLYGEP 

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References

[1]"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
DNA Res. 15:375-386(2008) [PubMed: 18931093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SE11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009240 Genomic DNA. Translation: BAG79312.1.
RefSeqYP_002295063.1. NC_011415.1.

3D structure databases

ProteinModelPortalB6I385.
SMRB6I385. Positions 53-548.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6I385.

Protein family/group databases

CAZyGH37. Glycoside Hydrolase Family 37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000110649; EBESCP00000102607; EBESCG00000105426.
GeneID7002173.
GenomeReviewsGene locus ECSE_3788 in contig AP009240_GR.
KEGGecy:ECSE_3788.
PATRIC18426219. VBIEscCol83070_3962.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010574.
HOGENOMHBG485982.
OMAFWMDGAD.
ProtClustDBPRK13270.

Enzyme and pathway databases

BioCycECOL409438:ECSE_3788-MONOMER.

Family and domain databases

HAMAPMF_01059. Cyt_trehalase.
[Tree]
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR023715. Cyt_trehalase.
IPR001661. Glyco_hydro_37.
IPR018232. Glyco_hydro_37_CS.
[Graphical view]
KOK01194.
PANTHERPTHR23403. Glyco_hydro_37. 1 hit.
PfamPF01204. Trehalase. 1 hit.
[Graphical view]
PRINTSPR00744. GLHYDRLASE37.
SUPFAMSSF48208. Glyco_trans_6hp. 1 hit.
PROSITEPS00927. TREHALASE_1. 1 hit.
PS00928. TREHALASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTREF_ECOSE
AccessionPrimary (citable) accession number: B6I385
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: January 25, 2012
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families