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Protein

Alpha-amylase A

Gene

Amy-d

more
Organism
Drosophila mauritiana (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 1 Cl- ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi116 – 1161CalciumBy similarity
Metal bindingi165 – 1651Calcium; via carbonyl oxygenBy similarity
Metal bindingi174 – 1741CalciumBy similarity
Binding sitei202 – 2021ChlorideBy similarity
Active sitei204 – 2041NucleophileBy similarity
Metal bindingi208 – 2081Calcium; via carbonyl oxygenBy similarity
Active sitei241 – 2411Proton donorBy similarity
Binding sitei304 – 3041ChlorideBy similarity
Sitei306 – 3061Transition state stabilizerBy similarity
Binding sitei343 – 3431ChlorideBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase A (EC:3.2.1.1By similarity)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:Amy-d
AND
Name:Amy-p
OrganismiDrosophila mauritiana (Fruit fly)
Taxonomic identifieri7226 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Organism-specific databases

FlyBaseiFBgn0012498. Dmau\Amy-d.
FBgn0012499. Dmau\Amy-p.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 494476Alpha-amylase APRO_0000001363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acidBy similarity
Disulfide bondi46 ↔ 102By similarity
Disulfide bondi153 ↔ 167By similarity
Disulfide bondi376 ↔ 382By similarity
Disulfide bondi448 ↔ 460By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP54215.
SMRiP54215. Positions 21-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54215-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLAKSLVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL
60 70 80 90 100
GPNGFAGVQV SPVNENAVKD SRPWWERYQP ISYKLETRSG NEQQFASMVK
110 120 130 140 150
RCNAVGVRIY VDVIFNHMAA DGGTYGTGGS TASPSSKSYP GVPYSSLDFN
160 170 180 190 200
PTCAINNYND ANQVRNCELV GLRDLNQGNS YVQDKVVEFL DHLIDLGVAG
210 220 230 240 250
FRVDAAKHMW PADLAVIYGR LKNLNTDHGF ASGSKAYIVQ EVIDMGGEAI
260 270 280 290 300
SKSEYTGLGA ITEFRHSDSI GKVFRGKDQL QYLTNWGTAW GFAASDRSLV
310 320 330 340 350
FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF
360 370 380 390 400
SDTDQGPPTT DGHNIASPVF NSDNSCSGGW VCEHRWRQIY NMVAFRNTVG
410 420 430 440 450
SDAIQNWWDN GSNQISFSRG SRGFVAFNND NYDLNSSLQT GLPAGTYCDV
460 470 480 490
ISGSKSGSSC TGKTVSVGSD GRASIYIGSS EDDGVLAIHV NAKL
Length:494
Mass (Da):53,730
Last modified:October 1, 1996 - v1
Checksum:iF557075877241E56
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71L → I in Amy-P.
Natural varianti398 – 3981T → A in Amy-P.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17729 Genomic DNA. Translation: BAA04583.1.
D17730 Genomic DNA. Translation: BAA04584.1.
PIRiS58939.
S58940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17729 Genomic DNA. Translation: BAA04583.1.
D17730 Genomic DNA. Translation: BAA04584.1.
PIRiS58939.
S58940.

3D structure databases

ProteinModelPortaliP54215.
SMRiP54215. Positions 21-494.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

FlyBaseiFBgn0012498. Dmau\Amy-d.
FBgn0012499. Dmau\Amy-p.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase/branching_C.
IPR031319. A-amylase_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiAMYA_DROMA
AccessioniPrimary (citable) accession number: P54215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Documents

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