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Reviewed, UniProtKB/Swiss-Prot O18345 (AMY2_DROAN)

Last modified June 16, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-amylase 2
    EC=3.2.1.1
Gene names
Name: Amy58
Synonyms: Amy2
OrganismDrosophila ananassae (Fruit fly)
Taxonomic identifier7217 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Binds 1 chloride ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

chloride ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 494476Alpha-amylase 2
PRO_0000001361

Sites

Active site2041Nucleophile By similarity
Active site2411Proton donor By similarity
Active site3061 By similarity
Metal binding1161Calcium By similarity
Metal binding1651Calcium; via carbonyl oxygen By similarity
Metal binding1741Calcium By similarity
Metal binding2081Calcium; via carbonyl oxygen By similarity
Binding site2021Chloride By similarity
Binding site3041Chloride By similarity
Binding site3431Chloride By similarity

Amino acid modifications

Disulfide bond46 ↔ 102 By similarity
Disulfide bond153 ↔ 167 By similarity
Disulfide bond376 ↔ 382 By similarity
Disulfide bond448 ↔ 460 By similarity

Sequences

Sequence LengthMass (Da)Tools
O18345-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C01473B128C3A703

FASTA49453,588
        10         20         30         40         50         60 
MFLAKSIVCL ALLAVANAQF NTNYPSGRSG MVHLFEWKWD DIAAECENFL GPYGYAGVQV 

        70         80         90        100        110        120 
SPANENAVKD SRPWWERYQP ISYKLVTRSG NEEQFASMVR RCNNVGVRIY VDVVFNHMAA 

       130        140        150        160        170        180 
DGGTYGTAGS TASPSSKSYP GVPFSSLDFN PTCAISNYND ANQVRNCELV GLRDLNQGNS 

       190        200        210        220        230        240 
YVQEKIVEFL NHLIDLGVAG FRVDAAKHMW PADLGVIYGS LKNLNTDHGF ESGAKAYIVQ 

       250        260        270        280        290        300 
EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKAFRGKNQL QYLVNWGVSW GFAASDRSLV 

       310        320        330        340        350        360 
FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF TDTDQGPPTT 

       370        380        390        400        410        420 
DGQNIASPSF NSDNSCSGGW VCEHRWKQIY NMVGFRNAVG SDAIQNWWDN GSNQIAFSRG 

       430        440        450        460        470        480 
SKGFVAFNND NYDLNSSVQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRANISIGSS 

       490 
EDDGVLAIHV NAKL 

« Hide

References

[1]"Molecular characterization and evolution of the amylase multigene family of Drosophila ananassae."
Da Lage J.-L., Maczkowiak F., Cariou M.-L.
J. Mol. Evol. 51:391-403(2000) [PubMed: 11040291] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 371-1, Beruwala, Bouake, Brazzaville, Colombo, Guadeloupe, Korat3422, Lambir, Mauritius, Mexico, Porto Rico, Reunion, Sao Paulo and Tai 13-1610.
+Additional computationally mapped references.

Cross-references

Sequence databases

U53698 Genomic DNA. Translation: AAC79122.1.
AF238958 Genomic DNA. Translation: AAG45312.1.
AF238959 Genomic DNA. Translation: AAG45313.1.
AF238960 Genomic DNA. Translation: AAG45314.1.
AF238961 Genomic DNA. Translation: AAG45315.1.
AF238962 Genomic DNA. Translation: AAG45316.1.
AF238963 Genomic DNA. Translation: AAG45317.1.
AF238964 Genomic DNA. Translation: AAG45318.1.
AF238965 Genomic DNA. Translation: AAG45319.1.
AF238966 Genomic DNA. Translation: AAG45320.1.
AF238967 Genomic DNA. Translation: AAG45321.1.
AF238968 Genomic DNA. Translation: AAG45322.1.
AF238969 Genomic DNA. Translation: AAG45323.1.
AF238970 Genomic DNA. Translation: AAG45324.1.
AF238971 Genomic DNA. Translation: AAG45325.1.
AF238972 Genomic DNA. Translation: AAG45326.1.
AF238973 Genomic DNA. Translation: AAG45327.1.
AF238974 Genomic DNA. Translation: AAG45328.1.
AF238975 Genomic DNA. Translation: AAG45329.1.
AF238976 Genomic DNA. Translation: AAG45330.1.
AF238977 Genomic DNA. Translation: AAG45331.1.

3D structure databases

HSSPHSSP built from PDB template 1JAE based on UniProtKB P56634.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Organism-specific databases

FlyBaseFBgn0020488. Dana\Amy58.

Enzyme and pathway databases

BRENDA3.2.1.1. 278838.

Family and domain databases

InterProIPR006048. A-amylase_b_C.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMY2_DROAN
AccessionPrimary (citable) accession number: O18345
Secondary accession number(s): Q9GN73
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents