Reviewed, UniProtKB/Swiss-Prot P08144 (AMYA_DROME)

Names and origin

Protein names

Recommended 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

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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.
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 process	Carbohydrate metabolism
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Ref.3 Traceable author statement. Source: UniProtKB
Molecular function	alpha-amylase activity Ref.3 Traceable author statement. Source: UniProtKB calcium ion binding Ref.3 Traceable author statement. Source: UniProtKB chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18
	Chain	19 – 494	476	Alpha-amylase A		PRO_0000001364
Sites
	Active site	204	1	Nucleophile By similarity
	Active site	241	1	Proton donor By similarity
	Active site	306	1	By similarity
	Metal binding	116	1	Calcium By similarity
	Metal binding	165	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	174	1	Calcium By similarity
	Metal binding	208	1	Calcium; via carbonyl oxygen By similarity
	Binding site	202	1	Chloride By similarity
	Binding site	304	1	Chloride By similarity
	Binding site	343	1	Chloride By similarity
Amino acid modifications
	Modified residue	19	1	Pyrrolidone carboxylic acid By similarity
	Disulfide bond	46 ↔ 102		By similarity
	Disulfide bond	153 ↔ 167		By similarity
	Disulfide bond	376 ↔ 382		By similarity
	Disulfide bond	448 ↔ 460		By similarity
Natural variations
	Natural variant	11	1	A → S in strain: KN-28.
	Natural variant	16	1	A → V in strain: KN-22 and KN-23.
	Natural variant	71	1	S → R in strain: KN-3, KN-9, KN-10 and L16.
	Natural variant	121	1	D → G in strain: TN256, 1420#1 and KO140.
	Natural variant	121	1	D → N in strain: KN-3, KN-9, KN-10 and L16.
	Natural variant	138	1	S → T in strain: JP-75, KN-7, KN-15, KN-17, KN-21 and KN-23.
	Natural variant	144	1	Y → H in strain: Canton-S.
	Natural variant	156	1	S → R in strain: 1420#1, KN-3, KN-9, KN-10, KO140, L16 and TN256.
	Natural variant	181	1	Y → N in strain: Canton-S.
	Natural variant	231	1	A → S in strain: JP-70, KN-17 and KN-21.
	Natural variant	278	1	D → N in strain: 1420#1, KO140, KN-3, KN-9, KN-10 and L16.
	Natural variant	284	1	T → I in strain: KN-21.
	Natural variant	398	1	T → A in strain: 1420#1, J87, JP-60, JP-70, JP-75, KO123, KO140, KN-9, KN-15, KN-21, L16 and TN256.
	Natural variant	401	1	S → L in strain: Berkeley.
	Natural variant	403	1	E → A in strain: J87, JP-60 and KO123.
	Natural variant	465	1	V → I in strain: 1420#1.
	Natural variant	474	1	S → Y in strain: KN-23.
	Natural variant	476	1	N → 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		Length	Mass (Da)
	P08144-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: B477D3B44754C298	FASTA	494	53,746
	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

References

	« Hide 'large scale' referencesShow '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: 3024105] [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: 8536971] [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: 11156987] [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: 10731132] [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. , 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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	A25529. S58953. S58956. S58957. S58958. S58961. S58965.
RefSeq	NP_536346.1.
UniGene	Dm.20319
3D structure databases
HSSP	HSSP built from PDB template 1JAE based on UniProtKB P56634.
ModBase	Search...
Protein-protein interaction databases
STRING	P08144.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Proteomic databases
PRIDE	P08144.
Genome annotation databases
Ensembl	FBtr0086983; FBpp0086136; FBgn0000078; Drosophila melanogaster. [Genome view] FBtr0087004; FBpp0086155; FBgn0000079; Drosophila melanogaster. [Genome view]
GeneID	47764.
KEGG	dme:Dmel_CG18730.
Organism-specific databases
CTD	47764.
FlyBase	FBgn0000079. Amy-p.
Enzyme and pathway databases
BRENDA	3.2.1.1. 48.
Gene expression databases
GermOnline	CG18730. Drosophila melanogaster.
Family and domain databases
InterPro	IPR006048. 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]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02806. Alpha-amylase_C. 1 hit. [Graphical view]
PRINTS	PR00110. ALPHAAMYLASE.
SMART	SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	839119.

Entry information

Entry name

AMYA_DROME

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	September 1, 2009
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project