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P08144 (AMYA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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 A

EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:Amy-p
Synonyms:AmyA
ORF Names:CG18730
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Polymorphism

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.

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
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement Ref.3. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay PubMed 15466469. Source: FlyBase

   Molecular_functionalpha-amylase activity

Traceable author statement Ref.3. Source: UniProtKB

calcium ion binding

Traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 494476Alpha-amylase A
PRO_0000001364

Sites

Active site2041Nucleophile By similarity
Active site2411Proton donor 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 variant111A → S in strain: KN-28.
Natural variant161A → V in strain: KN-22 and KN-23.
Natural variant711S → R in strain: KN-3, KN-9, KN-10 and L16.
Natural variant1211D → G in strain: TN256, 1420#1 and KO140.
Natural variant1211D → N in strain: KN-3, KN-9, KN-10 and L16.
Natural variant1381S → T in strain: JP-75, KN-7, KN-15, KN-17, KN-21 and KN-23.
Natural variant1441Y → H in strain: Canton-S.
Natural variant1561S → R in strain: 1420#1, KN-3, KN-9, KN-10, KO140, L16 and TN256.
Natural variant1811Y → N in strain: Canton-S.
Natural variant2311A → S in strain: JP-70, KN-17 and KN-21.
Natural variant2781D → N in strain: 1420#1, KO140, KN-3, KN-9, KN-10 and L16.
Natural variant2841T → I in strain: KN-21.
Natural variant3981T → A in strain: 1420#1, J87, JP-60, JP-70, JP-75, KO123, KO140, KN-9, KN-15, KN-21, L16 and TN256.
Natural variant4011S → L in strain: Berkeley.
Natural variant4031E → A in strain: J87, JP-60 and KO123.
Natural variant4651V → I in strain: 1420#1.
Natural variant4741S → Y in strain: KN-23.
Natural variant4761N → 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.

Sequences

Sequence LengthMass (Da)Tools
P08144 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: B477D3B44754C298

FASTA49453,746
        10         20         30         40         50         60 
MFLAKSIVCL ALLAVANAQF DTNYASGRSG MVHLFEWKWD DIAAECENFL GPNGYAGVQV 

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

       130        140        150        160        170        180 
DGGTYGTGGS TASPSSKSYP GVPYSSLDFN PTCAISNYND ANEVRNCELV GLRDLNQGNS 

       190        200        210        220        230        240 
YVQDKVVEFL DHLIDLGVAG FRVDAAKHMW PADLAVIYGR LKNLNTDHGF ASGSKAYIVQ 

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

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

       370        380        390        400        410        420 
DGHNIASPIF NSDNSCSGGW VCEHRWRQIY NMVAFRNTVG SDEIQNWWDN GSNQISFSRG 

       430        440        450        460        470        480 
SRGFVAFNND NYDLNSSLQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRASINIGSS 

       490 
EDDGVLAIHV NAKL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[6]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA25529.
S58953.
S58956.
S58957.
S58958.
S58961.
S58965.
RefSeqNP_536346.1. NM_080421.3.
UniGeneDm.20319.

3D structure databases

ProteinModelPortalP08144.
SMRP08144. Positions 21-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid70922. 2 interactions.

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Proteomic databases

PaxDbP08144.
PRIDEP08144.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID47764.
KEGGdme:Dmel_CG18730.

Organism-specific databases

CTD47764.
FlyBaseFBgn0000079. Amy-p.

Phylogenomic databases

eggNOGCOG0366.
InParanoidP08144.
KOK01176.
OrthoDBEOG7RJPR2.
PhylomeDBP08144.

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...

Other

GenomeRNAi47764.
NextBio839119.

Entry information

Entry nameAMYA_DROME
AccessionPrimary (citable) accession number: P08144
Secondary accession number(s): Q27582 expand/collapse secondary AC list , Q27583, Q27584, Q27887, Q961R0, Q969D2, Q9BH42, Q9BH55, Q9BPT4, Q9BPT5, Q9BPT6, Q9BPT7, Q9BPT8, Q9BPT9, Q9BPU0, Q9BPU1, Q9V7Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 136 of the entry and version 1 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