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Q9BN01 (AMYB_DROYA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. 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:
Alpha-amylase B

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:Amy-d
ORF Names:GE11648
OrganismDrosophila yakuba (Fruit fly) [Complete proteome]
Taxonomic identifier7245 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

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 polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

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
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionalpha-amylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal 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 By similarity
Chain19 – 494476Alpha-amylase B
PRO_0000001367

Sites

Active site2041 By similarity
Active site2411 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
Site3061Transition state stabilizer By similarity

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid By similarity
Disulfide bond46 ↔ 102 By similarity
Disulfide bond153 ↔ 167 By similarity
Disulfide bond376 ↔ 382 By similarity
Disulfide bond448 ↔ 460 By similarity

Natural variations

Natural variant179 – 1802NS → DP in strain: LO4.
Natural variant1951D → N in strain: LO4.
Natural variant3301A → V in strain: LO4.
Natural variant3811V → A in strain: LO4.
Natural variant4051Q → P in strain: LO4.
Natural variant4271F → Y in strain: LO4.

Sequences

Sequence LengthMass (Da)Tools
Q9BN01 [UniParc].

Last modified March 29, 2004. Version 2.
Checksum: EBDC615F3C0044B8

FASTA49453,688
        10         20         30         40         50         60 
MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGFAGVQV 

        70         80         90        100        110        120 
SPVNENAVKD SRPWWERYQP ISYKLETRSG NEQQFASMVK RCNAVGVRTY VDVVFNHMAA 

       130        140        150        160        170        180 
DGGTYGTGGS TASPSTKSFP GVPYSSLDFN PTCSINNYND ANQVRNCELV GLRDLNQGNS 

       190        200        210        220        230        240 
YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKTLNTDHGF NSGSKAYIVQ 

       250        260        270        280        290        300 
EVIDMGGEAI SKSEYTGLGA VTEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV 

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

       370        380        390        400        410        420 
DGHNIASPVF NSDNSCSGGW VCEHRWRQIY NMVAFRNAVG SDAIQNWWDN GSNQIAFSRG 

       430        440        450        460        470        480 
SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVSVGSD GRASIYLGSS 

       490 
EDDGVLAIHV NAKL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular evolution of the duplicated Amy locus in the Drosophila melanogaster species subgroup: concerted evolution only in the coding region and an excess of nonsynonymous substitutions in speciation."
Shibata H., Yamazaki T.
Genetics 141:223-236(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Divergence between Drosophila santomea and allopatric or sympatric populations of D. yakuba using paralogous amylase genes and migration scenarios along the Cameroon volcanic line."
Cariou M.-L., Silvain J.-F., Daubin V., Da Lage J.-L., Lachaise D.
Mol. Ecol. 10:649-660(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LBV1, LO4, SA2 and SA3.
[3]"Evolution of genes and genomes on the Drosophila phylogeny."
Drosophila 12 genomes consortium
Nature 450:203-218(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tai18E2 / Tucson 14021-0261.01.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17737 Genomic DNA. Translation: BAA04590.1.
AF280886 Genomic DNA. Translation: AAG60011.1.
AF280887 Genomic DNA. Translation: AAG60012.1.
AF280888 Genomic DNA. Translation: AAG60013.1.
AF280889 Genomic DNA. Translation: AAG60014.1.
CM000158 Genomic DNA. Translation: EDW92184.1.
PIRS58946.
RefSeqXP_002092472.1. XM_002092436.1.

3D structure databases

ProteinModelPortalQ9BN01.
SMRQ9BN01. Positions 21-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7245.FBpp0256658.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0258166; FBpp0256658; FBgn0013165.
GeneID6531681.
KEGGdya:Dyak_GE11648.

Organism-specific databases

FlyBaseFBgn0013165. Dyak\Amy-d.

Phylogenomic databases

eggNOGCOG0366.
KOK01176.
OrthoDBEOG7RJPR2.
PhylomeDBQ9BN01.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 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]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMYB_DROYA
AccessionPrimary (citable) accession number: Q9BN01
Secondary accession number(s): B4P8G7, P51548
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: July 9, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Drosophila

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