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A8J4S9 (TREA_APIME) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Trehalase
EC=3.2.1.28
Alternative name(s):
Alpha,alpha-trehalase
Alpha,alpha-trehalose glucohydrolase
OrganismApis mellifera (Honeybee)
Taxonomic identifier7460 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Apoidea › Apidae › Apis

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Alpha,alpha-trehalose + H2O = 2 D-glucose. Ref.1 Ref.2

Enzyme regulation

Inhibited by sodium, potassium and ammonium ions, and by TEMED. Ref.2

Subunit structure

Monomer. Ref.2

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Post-translational modification

Glycosylated; contains 3.1% carbohydrates. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 37 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.66 mM for alpha,alpha-trehalose (in 0.1 M sodium phosphate pH 6.75, at 35 degrees Celsius) Ref.1 Ref.2

KM=0.52 mM for alpha,alpha-trehalose (in 50 mM sodium phosphate pH 6.6, at 35 degrees Celsius) Ref.1

pH dependence:

Optimum pH is 6.7 when incubated for 5 minutes at 35 degrees Celsius. Active from pH 4.5 to 12.5 when incubated for 5 minutes at 35 degrees Celsius. Optimum pH is 7.0 when incubated for 24 hours at 4 degrees Celsius. Active from pH 5.0 to 10.5 when incubated for 24 hours at 4 degrees Celsius. Ref.1 Ref.2

Temperature dependence:

Stable up to 40 degrees Celsius, but activity is lost after 15 minutes incubation at 60 degrees Celsius. Ref.1 Ref.2

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processtrehalose metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Signal peptide1 – 3535 Potential
Chain36 – 626591Trehalase
PRO_0000314636

Regions

Topological domain36 – 595560Extracellular Potential
Transmembrane596 – 61621Helical; Potential
Topological domain617 – 62610Cytoplasmic Potential

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation3841N-linked (GlcNAc...) Potential
Glycosylation4981N-linked (GlcNAc...) Potential
Glycosylation5251N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A8J4S9 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 08DAE9FCB49D1426

FASTA62672,817
        10         20         30         40         50         60 
MASSCSIRCG SRNILVNAAA TFLALLVVLR CFANAEKPSP CQSDVYCRGE LLHTIQMASI 

        70         80         90        100        110        120 
YKDSKTFVDM KMKRPPDETL KSFREFMERH EQMPTRYQIE RFVNDTFDPE GSEFEDWDPD 

       130        140        150        160        170        180 
DWTFRPKFLS RILDDDLRNF ASELNGIWKM LGRKMKDDVR VNEELYSIIY VPHPVIVPGG 

       190        200        210        220        230        240 
RFREFYYWDS YWIVKGLLLS EMYTTVKGML TNFVSLVDKI GFIPNGGRIY YTMRSQPPML 

       250        260        270        280        290        300 
IPMVDEYLKI THDYEWLENN LYLLEKEFDF WMTNRTVEIE VDGVNYVLAR YNEQSSGPRP 

       310        320        330        340        350        360 
ESYKEDYLTS QSFRTNEEKD NYYSELKTAA ESGWDFSSRW FILDGTNKGN LTNLKTRYII 

       370        380        390        400        410        420 
PVDLNSIIYR NAVLLAQYNQ RMGNESKVAY YQKRAAEWKR AIQAVLWHDE VGAWLDYDIL 

       430        440        450        460        470        480 
NDIKRDYFYP TNILPLWTDC YDIAKREEYV SKVLKYLEKN KIMLNLGGIP TTLEHSGEQW 

       490        500        510        520        530        540 
DYPNAWPPLQ YFVIMALNKT EDPWAQRLAY EISERWVRSN YKAYNETHSM FEKYDATVSG 

       550        560        570        580        590        600 
GHGGGGEYEV QLGFGWSNGV IMDLLNRYGD KLTAEDRFVA TFHSNSTPQP VVVSTAGQVM 

       610        620 
TGILALVISL AAGFIGKMRC ANNAAQ

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References

[1]"Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris."
Lee J.-H., Saito S., Mori H., Nishimoto M., Okuyama M., Kim D., Wongchawalit J., Kimura A., Chiba S.
Biosci. Biotechnol. Biochem. 71:2256-2265(2007) [PubMed: 17827701] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-54; 128-147; 157-188; 220-239; 426-444 AND 500-519, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"Purification and identification of the essential ionizable groups of honeybee, Apis mellifera L., trehalase."
Lee J.-H., Tsuji M., Nakamura M., Nishimoto M., Okuyama M., Mori H., Kimura A., Matsui H., Chiba S.
Biosci. Biotechnol. Biochem. 65:2657-2665(2001) [PubMed: 11826961] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB301556 mRNA. Translation: BAF81545.1.
RefSeqNP_001106141.1. NM_001112671.1.
UniGeneAme.515.

3D structure databases

ProteinModelPortalA8J4S9.
ModBaseSearch...

Protein family/group databases

CAZyGH37. Glycoside Hydrolase Family 37.

Proteomic databases

PRIDEA8J4S9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID410795.
KEGGame:410795.

Family and domain databases

InterProIPR008928. 6-hairpin_glycosidase-like.
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 nameTREA_APIME
AccessionPrimary (citable) accession number: A8J4S9
Secondary accession number(s): P85151
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 4, 2007
Last modified: November 16, 2011
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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