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Protein

Alpha-amylase A

Gene

Amy-p

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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+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

  • alpha-amylase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Chloride, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_313493. Digestion of dietary carbohydrate.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase A (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:Amy-p
Synonyms:AmyA
ORF Names:CG18730
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0000079. Amy-p.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 494476Alpha-amylase APRO_0000001364Add
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

Proteomic databases

PaxDbiP08144.
PRIDEiP08144.

Expressioni

Gene expression databases

GenevisibleiP08144. DM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi70922. 2 interactions.
STRINGi7227.FBpp0086155.

Structurei

3D structure databases

ProteinModelPortaliP08144.
SMRiP08144. Positions 21-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
InParanoidiP08144.
KOiK01176.
OrthoDBiEOG7RJPR2.
PhylomeDBiP08144.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
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.

P08144-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL
60 70 80 90 100
GPNGYAGVQV SPVNENAVKD SRPWWERYQP ISYKLETRSG NEEQFASMVK
110 120 130 140 150
RCNAVGVRTY VDVVFNHMAA DGGTYGTGGS TASPSSKSYP GVPYSSLDFN
160 170 180 190 200
PTCAISNYND ANEVRNCELV 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
TDTDQGPPTT DGHNIASPIF NSDNSCSGGW VCEHRWRQIY NMVAFRNTVG
410 420 430 440 450
SDEIQNWWDN GSNQISFSRG SRGFVAFNND NYDLNSSLQT GLPAGTYCDV
460 470 480 490
ISGSKSGSSC TGKTVTVGSD GRASINIGSS EDDGVLAIHV NAKL
Length:494
Mass (Da):53,746
Last modified:August 1, 1988 - v1
Checksum:iB477D3B44754C298
GO

Polymorphismi

At least 6 electrophoretic isozymes are known: Amy1, Amy2, Amy3, Amy4, Amy5 and Amy6. Strains J87 and KO123 express Amy2; KO140 and 1420#1 express Amy4; L16 expresses Amy5.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111A → S in strain: KN-28.
Natural varianti16 – 161A → V in strain: KN-22 and KN-23.
Natural varianti71 – 711S → R in strain: KN-3, KN-9, KN-10 and L16.
Natural varianti121 – 1211D → G in strain: TN256, 1420#1 and KO140.
Natural varianti121 – 1211D → N in strain: KN-3, KN-9, KN-10 and L16.
Natural varianti138 – 1381S → T in strain: JP-75, KN-7, KN-15, KN-17, KN-21 and KN-23.
Natural varianti144 – 1441Y → H in strain: Canton-S.
Natural varianti156 – 1561S → R in strain: 1420#1, KN-3, KN-9, KN-10, KO140, L16 and TN256.
Natural varianti181 – 1811Y → N in strain: Canton-S.
Natural varianti231 – 2311A → S in strain: JP-70, KN-17 and KN-21.
Natural varianti278 – 2781D → N in strain: 1420#1, KO140, KN-3, KN-9, KN-10 and L16.
Natural varianti284 – 2841T → I in strain: KN-21.
Natural varianti398 – 3981T → A in strain: 1420#1, J87, JP-60, JP-70, JP-75, KO123, KO140, KN-9, KN-15, KN-21, L16 and TN256.
Natural varianti401 – 4011S → L in strain: Berkeley.
Natural varianti403 – 4031E → A in strain: J87, JP-60 and KO123.
Natural varianti465 – 4651V → I in strain: 1420#1.
Natural varianti474 – 4741S → Y in strain: KN-23.
Natural varianti476 – 4761N → Y in strain: Berkeley, JP-1, JP-5, JP-15, JP-35, JP-55, JP-65, JP-84, KN-12, KN-22 and KN-27.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04569 Genomic DNA. Translation: CAA28238.1.
L22716 Genomic DNA. Translation: AAA92226.1.
L22719 Genomic DNA. Translation: AAA92229.1.
L22721 Genomic DNA. Translation: AAA92231.1.
L22725 Genomic DNA. Translation: AAA92235.1.
L22726 Genomic DNA. Translation: AAA92239.1.
L22729 Genomic DNA. Translation: AAA92240.1.
L22731 Genomic DNA. Translation: AAA92234.1.
L22733 Genomic DNA. Translation: AAA92241.1.
L22735 Genomic DNA. Translation: AAA92236.1.
AB042862 Genomic DNA. Translation: BAB32503.1.
AB042863 Genomic DNA. Translation: BAB32504.1.
AB042864 Genomic DNA. Translation: BAB32505.1.
AB042865 Genomic DNA. Translation: BAB32506.1.
AB042866 Genomic DNA. Translation: BAB32507.1.
AB042867 Genomic DNA. Translation: BAB32508.1.
AB042868 Genomic DNA. Translation: BAB32509.1.
AB042869 Genomic DNA. Translation: BAB32510.1.
AB042870 Genomic DNA. Translation: BAB32511.1.
AB042871 Genomic DNA. Translation: BAB32512.1.
AB042872 Genomic DNA. Translation: BAB32513.1.
AB042873 Genomic DNA. Translation: BAB32514.1.
AB042874 Genomic DNA. Translation: BAB32515.1.
AB042875 Genomic DNA. Translation: BAB32516.1.
AB042876 Genomic DNA. Translation: BAB32517.1.
AB042877 Genomic DNA. Translation: BAB32518.1.
AB042878 Genomic DNA. Translation: BAB32519.1.
AB042879 Genomic DNA. Translation: BAB32520.1.
AB042880 Genomic DNA. Translation: BAB32521.1.
AB042881 Genomic DNA. Translation: BAB32522.1.
AB042882 Genomic DNA. Translation: BAB32523.1.
AB042883 Genomic DNA. Translation: BAB32524.1.
AB042884 Genomic DNA. Translation: BAB72090.1.
AB042885 Genomic DNA. Translation: BAB72091.1.
AB042886 Genomic DNA. Translation: BAB72092.1.
AE013599 Genomic DNA. Translation: AAF57896.1.
AY051425 mRNA. Translation: AAK92849.1.
PIRiA25529.
S58953.
S58956.
S58957.
S58958.
S58961.
S58965.
RefSeqiNP_001286518.1. NM_001299589.1.
NP_536346.1. NM_080421.4.
UniGeneiDm.20319.

Genome annotation databases

GeneIDi47764.
KEGGidme:Dmel_CG18730.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04569 Genomic DNA. Translation: CAA28238.1.
L22716 Genomic DNA. Translation: AAA92226.1.
L22719 Genomic DNA. Translation: AAA92229.1.
L22721 Genomic DNA. Translation: AAA92231.1.
L22725 Genomic DNA. Translation: AAA92235.1.
L22726 Genomic DNA. Translation: AAA92239.1.
L22729 Genomic DNA. Translation: AAA92240.1.
L22731 Genomic DNA. Translation: AAA92234.1.
L22733 Genomic DNA. Translation: AAA92241.1.
L22735 Genomic DNA. Translation: AAA92236.1.
AB042862 Genomic DNA. Translation: BAB32503.1.
AB042863 Genomic DNA. Translation: BAB32504.1.
AB042864 Genomic DNA. Translation: BAB32505.1.
AB042865 Genomic DNA. Translation: BAB32506.1.
AB042866 Genomic DNA. Translation: BAB32507.1.
AB042867 Genomic DNA. Translation: BAB32508.1.
AB042868 Genomic DNA. Translation: BAB32509.1.
AB042869 Genomic DNA. Translation: BAB32510.1.
AB042870 Genomic DNA. Translation: BAB32511.1.
AB042871 Genomic DNA. Translation: BAB32512.1.
AB042872 Genomic DNA. Translation: BAB32513.1.
AB042873 Genomic DNA. Translation: BAB32514.1.
AB042874 Genomic DNA. Translation: BAB32515.1.
AB042875 Genomic DNA. Translation: BAB32516.1.
AB042876 Genomic DNA. Translation: BAB32517.1.
AB042877 Genomic DNA. Translation: BAB32518.1.
AB042878 Genomic DNA. Translation: BAB32519.1.
AB042879 Genomic DNA. Translation: BAB32520.1.
AB042880 Genomic DNA. Translation: BAB32521.1.
AB042881 Genomic DNA. Translation: BAB32522.1.
AB042882 Genomic DNA. Translation: BAB32523.1.
AB042883 Genomic DNA. Translation: BAB32524.1.
AB042884 Genomic DNA. Translation: BAB72090.1.
AB042885 Genomic DNA. Translation: BAB72091.1.
AB042886 Genomic DNA. Translation: BAB72092.1.
AE013599 Genomic DNA. Translation: AAF57896.1.
AY051425 mRNA. Translation: AAK92849.1.
PIRiA25529.
S58953.
S58956.
S58957.
S58958.
S58961.
S58965.
RefSeqiNP_001286518.1. NM_001299589.1.
NP_536346.1. NM_080421.4.
UniGeneiDm.20319.

3D structure databases

ProteinModelPortaliP08144.
SMRiP08144. Positions 21-494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi70922. 2 interactions.
STRINGi7227.FBpp0086155.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbiP08144.
PRIDEiP08144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi47764.
KEGGidme:Dmel_CG18730.

Organism-specific databases

CTDi47764.
FlyBaseiFBgn0000079. Amy-p.

Phylogenomic databases

eggNOGiCOG0366.
InParanoidiP08144.
KOiK01176.
OrthoDBiEOG7RJPR2.
PhylomeDBiP08144.

Enzyme and pathway databases

ReactomeiREACT_313493. Digestion of dietary carbohydrate.

Miscellaneous databases

GenomeRNAii47764.
NextBioi839119.
PROiP08144.

Gene expression databases

GenevisibleiP08144. DM.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. 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]
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

« Hide 'large scale' publications
  1. "The alpha-amylase gene in Drosophila melanogaster: nucleotide sequence, gene structure and expression motifs."
    Boer P.H., Hickey D.A.
    Nucleic Acids Res. 14:8399-8411(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S and Oregon-R.
  2. "Evolutionary relationships and sequence variation of alpha-amylase variants encoded by duplicated genes in the Amy locus of Drosophila melanogaster."
    Inomata N., Shibata H., Okuyama E., Yamazaki T.
    Genetics 141:237-244(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 1420#1, AO168, J87, KO123, KO140, L16, TN22, TN256 and TN329.
  3. "Molecular evolution of duplicated amylase gene regions in Drosophila melanogaster: evidence of positive selection in the coding regions and selective constraints in the cis-regulatory regions."
    Araki H., Inomata N., Yamazaki T.
    Genetics 157:667-677(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS.
    Strain: JP-1, JP-15, JP-169, JP-186, JP-190, JP-35, JP-5, JP-55, JP-60, JP-65, JP-70, JP-75, JP-84, KN-10, KN-12, KN-15, KN-17, KN-21, KN-22, KN-23, KN-27, KN-28, KN-3, KN-7 and KN-9.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiAMYA_DROME
AccessioniPrimary (citable) accession number: P08144
Secondary accession number(s): Q27582
, Q27583, Q27584, Q27887, Q961R0, Q969D2, Q9BH42, Q9BH55, Q9BPT4, Q9BPT5, Q9BPT6, Q9BPT7, Q9BPT8, Q9BPT9, Q9BPU0, Q9BPU1, Q9V7Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 22, 2015
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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

External Data

Dasty 3

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 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.