Reviewed, UniProtKB/Swiss-Prot Q9NJP0 (AMYR_DROEL)

Names and origin

Protein names

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

Gene names

Name:

Amyrel

Organism

Drosophila elegans (Fruit fly)

Taxonomic identifier

30023 [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 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.
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 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 – 19	19	By similarity
	Chain	20 – 493	474	Alpha-amylase-related protein		PRO_0000001376
Sites
	Active site	207	1	Nucleophile By similarity
	Active site	244	1	Proton donor By similarity
	Active site	309	1	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
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

Sequences

	Sequence		Length	Mass (Da)
	Q9NJP0-1 [UniParc]. Last modified May 30, 2003. Version 2. Checksum: F80F6F903992445A	FASTA	493	55,572
	10 20 30 40 50 60 MFKFALALTL CLAGSLSLAQ HNPHWWGNRN TIVHLFEWKW SDIAEECESF LGPRGFAGVQ 70 80 90 100 110 120 VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGDMV RRCNEVGVRI YVDVLLNHMS 130 140 150 160 170 180 GDFDGVAIGT AGTEAEPSKK SFPGVPFSAQ DFPPSCEITD WNNRFQVQQC ELVGLKDLDQ 190 200 210 220 230 240 SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YRSLSDLNTD HGFPHNARPF 250 260 270 280 290 300 IFQEVIDHGH ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALRWLQSWG TGWGFLPSGQ 310 320 330 340 350 360 ALTFVDNHDN QRDAGAVLNY KSPRQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA 370 380 390 400 410 420 QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEMAEWWDNG DSQISFCRGN 430 440 450 460 470 480 KGFLAVNNNQ YDLSQELNTC LPAGEYCDVI SGSLINGSCT GKSVTVKDNG YGYIHIGVDD 490 FDGMMALHVD AKV

References

[1]	"Origin and evolution of the Amyrel gene in Drosophila." Da Lage J.-L., Renard E., Chartois F., Cariou M.-L. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF136930 Genomic DNA. Translation: AAF25712.2.
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	FBgn0029435. Dele\Amyrel.
Enzyme and pathway databases
BRENDA	3.2.1.1. 262510.
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

AMYR_DROEL

Accession

Primary (citable) accession number: Q9NJP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	May 30, 2003
Last modified:	June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project