Q9BN01 (AMYB_DROYA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase B
EC=3.2.1.1

Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase

Gene names

Name:	Amy-d
ORF Names:	GE11648

Organism

Drosophila yakuba (Fruit fly) [Complete proteome]

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 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.
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 Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC metal 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 B		PRO_0000001367
Sites
	Active site	204	1	By similarity
	Active site	241	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
	Site	306	1	Transition state stabilizer 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	179 – 180	2	NS → DP in strain: LO4.
	Natural variant	195	1	D → N in strain: LO4.
	Natural variant	330	1	A → V in strain: LO4.
	Natural variant	381	1	V → A in strain: LO4.
	Natural variant	405	1	Q → P in strain: LO4.
	Natural variant	427	1	F → Y in strain: LO4.

Sequences

	Sequence		Length	Mass (Da)
	Q9BN01 [UniParc]. Last modified March 29, 2004. Version 2. Checksum: EBDC615F3C0044B8	FASTA	494	53,688
	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 NSGSKAYIVQ 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

	« Hide 'large scale' referencesShow 'large scale' 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].
[2]	"Divergence between Drosophila santomea and allopatric or sympatric populations of D. yakuba using paralogous amylase genes and migration scenarios along the Cameroon volcanic line." Cariou M.-L., Silvain J.-F., Daubin V., Da Lage J.-L., Lachaise D. Mol. Ecol. 10:649-660(2001) [PubMed: 11298976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LBV1, LO4, SA2 and SA3.
[3]	"Evolution of genes and genomes on the Drosophila phylogeny." Drosophila 12 genomes consortium Nature 450:203-218(2007) [PubMed: 17994087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tai18E2 / Tucson 14021-0261.01.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D17737 Genomic DNA. Translation: BAA04590.1. AF280886 Genomic DNA. Translation: AAG60011.1. AF280887 Genomic DNA. Translation: AAG60012.1. AF280888 Genomic DNA. Translation: AAG60013.1. AF280889 Genomic DNA. Translation: AAG60014.1. CM000158 Genomic DNA. Translation: EDW92184.1.
PIR	S58946.
RefSeq	XP_002092472.1. XM_002092436.1.
3D structure databases
ProteinModelPortal	Q9BN01.
SMR	Q9BN01. Positions 21-494.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9BN01.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0258166; FBpp0256658; FBgn0013165.
GeneID	6531681.
KEGG	dya:Dyak_GE11648.
Organism-specific databases
FlyBase	FBgn0013165. Dyak\Amy-d.
Phylogenomic databases
GeneTree	EMGT00050000007262.
PhylomeDB	Q9BN01.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR015902. Alpha_amylase. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K01176.
PANTHER	PTHR10357. Alpha_amylase. 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]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMYB_DROYA

Accession

Primary (citable) accession number: Q9BN01
Secondary accession number(s): B4P8G7, P51548

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	March 29, 2004
Last modified:	December 14, 2011
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project