Reviewed, UniProtKB/Swiss-Prot O18345 (AMY2_DROAN)

Names and origin

Protein names

Recommended name:
    Alpha-amylase 2
    EC=3.2.1.1

Gene names

Name:	Amy58
Synonyms:	Amy2

Organism

Drosophila ananassae (Fruit fly)

Taxonomic identifier

7217 [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
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	Potential
	Chain	19 – 494	476	Alpha-amylase 2		PRO_0000001361
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
	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)
	O18345-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C01473B128C3A703	FASTA	494	53,588
	10 20 30 40 50 60 MFLAKSIVCL ALLAVANAQF NTNYPSGRSG MVHLFEWKWD DIAAECENFL GPYGYAGVQV 70 80 90 100 110 120 SPANENAVKD SRPWWERYQP ISYKLVTRSG NEEQFASMVR RCNNVGVRIY VDVVFNHMAA 130 140 150 160 170 180 DGGTYGTAGS TASPSSKSYP GVPFSSLDFN PTCAISNYND ANQVRNCELV GLRDLNQGNS 190 200 210 220 230 240 YVQEKIVEFL NHLIDLGVAG FRVDAAKHMW PADLGVIYGS LKNLNTDHGF ESGAKAYIVQ 250 260 270 280 290 300 EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKAFRGKNQL QYLVNWGVSW GFAASDRSLV 310 320 330 340 350 360 FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF TDTDQGPPTT 370 380 390 400 410 420 DGQNIASPSF NSDNSCSGGW VCEHRWKQIY NMVGFRNAVG SDAIQNWWDN GSNQIAFSRG 430 440 450 460 470 480 SKGFVAFNND NYDLNSSVQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRANISIGSS 490 EDDGVLAIHV NAKL

References

[1]

"Molecular characterization and evolution of the amylase multigene family of Drosophila ananassae." Da Lage J.-L., Maczkowiak F., Cariou M.-L. J. Mol. Evol. 51:391-403(2000) [PubMed: 11040291] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 371-1, Beruwala, Bouake, Brazzaville, Colombo, Guadeloupe, Korat3422, Lambir, Mauritius, Mexico, Porto Rico, Reunion, Sao Paulo and Tai 13-1610.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U53698 Genomic DNA. Translation: AAC79122.1. AF238958 Genomic DNA. Translation: AAG45312.1. AF238959 Genomic DNA. Translation: AAG45313.1. AF238960 Genomic DNA. Translation: AAG45314.1. AF238961 Genomic DNA. Translation: AAG45315.1. AF238962 Genomic DNA. Translation: AAG45316.1. AF238963 Genomic DNA. Translation: AAG45317.1. AF238964 Genomic DNA. Translation: AAG45318.1. AF238965 Genomic DNA. Translation: AAG45319.1. AF238966 Genomic DNA. Translation: AAG45320.1. AF238967 Genomic DNA. Translation: AAG45321.1. AF238968 Genomic DNA. Translation: AAG45322.1. AF238969 Genomic DNA. Translation: AAG45323.1. AF238970 Genomic DNA. Translation: AAG45324.1. AF238971 Genomic DNA. Translation: AAG45325.1. AF238972 Genomic DNA. Translation: AAG45326.1. AF238973 Genomic DNA. Translation: AAG45327.1. AF238974 Genomic DNA. Translation: AAG45328.1. AF238975 Genomic DNA. Translation: AAG45329.1. AF238976 Genomic DNA. Translation: AAG45330.1. AF238977 Genomic DNA. Translation: AAG45331.1.
3D structure databases
HSSP	HSSP built from PDB template 1JAE based on UniProtKB P56634.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Organism-specific databases
FlyBase	FBgn0020488. Dana\Amy58.
Enzyme and pathway databases
BRENDA	3.2.1.1. 278838.
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

AMY2_DROAN

Accession

Primary (citable) accession number: O18345
Secondary accession number(s): Q9GN73

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project