Reviewed, UniProtKB/Swiss-Prot P83833 (AMYA_DROYA)

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

Organism

Drosophila yakuba (Fruit fly)

Taxonomic identifier

7245 [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	Inferred from homology.

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.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Signal
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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	By similarity
	Chain	19 – 494	476	Alpha-amylase A		PRO_0000001366
Sites
	Active site	204	1	By similarity
	Active site	241	1	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

Sequences

	Sequence		Length	Mass (Da)
	P83833-1 [UniParc]. Last modified March 29, 2004. Version 1. Checksum: EBDC6DDB3C0041FC	FASTA	494	53,689
	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 NSGSKAYIVE 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

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: 8536970] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D17738 Genomic DNA. Translation: BAA04591.1.
PIR	S58947.
3D structure databases
HSSP	HSSP built from PDB template 1JAE based on UniProtKB P56634.
ModBase	Search...
Organism-specific databases
FlyBase	FBgn0013166. Dyak\Amy-p.
Enzyme and pathway databases
BRENDA	3.2.1.1. 278535.
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...

Entry information

Entry name

AMYA_DROYA

Accession

Primary (citable) accession number: P83833
Secondary accession number(s): P51548

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	March 29, 2004
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project