O77016 (AMYR_DROSI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase-related protein
EC=3.2.1.1

Gene names

Name:

Amyrel

Organism

Drosophila simulans (Fruit fly)

Taxonomic identifier

7240 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	493 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.
Subcellular location	Secreted Probable.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
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
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 19	19	By similarity
	Chain	20 – 493	474	Alpha-amylase-related protein		PRO_0000001387
Sites
	Active site	207	1	Nucleophile By similarity
	Active site	244	1	Proton donor By similarity
	Metal binding	117	1	Calcium By similarity
	Metal binding	168	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	177	1	Calcium By similarity
	Metal binding	211	1	Calcium; via carbonyl oxygen By similarity
	Binding site	205	1	Chloride By similarity
	Binding site	307	1	Chloride By similarity
	Binding site	342	1	Chloride By similarity
	Site	309	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	20	1	Pyrrolidone carboxylic acid By similarity
	Disulfide bond	47 ↔ 103		By similarity
	Disulfide bond	156 ↔ 170		By similarity
	Disulfide bond	375 ↔ 381		By similarity
	Disulfide bond	417 ↔ 440		Potential
	Disulfide bond	447 ↔ 459		By similarity
Natural variations
	Natural variant	50	1	F → L in strain: Isolate SIM2.
	Natural variant	324	1	K → R in strain: Isolate SIM2.

Sequences

	Sequence		Length	Mass (Da)
	O77016 [UniParc]. Last modified May 16, 2003. Version 3. Checksum: 388EA33DFBDFCDEE	FASTA	493	55,551
	10 20 30 40 50 60 MFKFALTLTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAQECESF LGPRGFAGVQ 70 80 90 100 110 120 VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNDVGVRI YVDVLLNHMS 130 140 150 160 170 180 GDFDGVAVGT AGTEAEPRKK SFPGVPYTAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLDQ 190 200 210 220 230 240 SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNID HGFPHNSRPF 250 260 270 280 290 300 IFQEVIDHGH ETVSRDEYKE LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ 310 320 330 340 350 360 ALTFVDNHDN QRDAGAVLNY KSPKQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA 370 380 390 400 410 420 QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQISFCRGN 430 440 450 460 470 480 KGFLAINNNQ YDLSQDLNTC LPTGTYCDVI SGSLIDGSCT GKSVTVNENG YGYIHIGSDD 490 FDGVLALHVD AKV

References

[1]	Da Lage J.-L. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONES SIM1/SIM92 AND SIM2).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U96159 Genomic DNA. Translation: AAC39109.4. U96160 Genomic DNA. Translation: AAC39110.2.
3D structure databases
ProteinModelPortal	O77016.
SMR	O77016. Positions 20-493.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
FlyBase	FBgn0021128. Dsim\Amyrel.
Phylogenomic databases
GeneTree	EMGT00050000007262.
OrthoDB	EOG4XD26M.
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.
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

AMYR_DROSI

Accession

Primary (citable) accession number: O77016
Secondary accession number(s): O77017

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	May 16, 2003
Last modified:	December 14, 2011
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project