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Protein

Alpha-amylase

Gene
N/A
Organism
Dermatophagoides pteronyssinus (European house dust mite)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Aids in the digestion of starch and glycogen derived from food, such as skin scales, fungi and bacteria.

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+CuratedNote: Binds 1 Ca2+ ion per subunit.Curated
  • chlorideCuratedNote: Binds 1 Cl- ion per subunit.Curated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase (EC:3.2.1.1)
Alternative name(s):
Allergen Der p IV
Allergen: Der p 4
OrganismiDermatophagoides pteronyssinus (European house dust mite)
Taxonomic identifieri6956 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariAcariformesSarcoptiformesAstigmataPsoroptidiaAnalgoideaPyroglyphidaeDermatophagoidinaeDermatophagoides

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei318. Der p 4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000542841 – ›19Alpha-amylaseAdd BLAST›19

Post-translational modificationi

Disulfide bonds are present.

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Sequencei

Sequence statusi: Fragment.

P49274-1 [UniParc]FASTAAdd to basket

« Hide

        10 
KYXNPHFIGX RSVITXLME
Length:19
Mass (Da):2,239
Last modified:February 1, 1996 - v1
Checksum:i7AB769619A256F99
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei191

Sequence databases

PIRiA39729.

Cross-referencesi

Sequence databases

PIRiA39729.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei318. Der p 4.
CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiAMY_DERPT
AccessioniPrimary (citable) accession number: P49274
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. 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.