Reviewed, UniProtKB/Swiss-Prot O76261 (AMYR_DROSE)

Names and origin

Protein names

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

Gene names

Name:	Amyrel
ORF Names:	GM20043

Organism

Drosophila sechellia (Fruit fly)

Taxonomic identifier

7238 [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_0000001386
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
Natural variations
	Natural variant	143	1	P → T in strain: Seychelles-1 and Seychelles-15. Ref.2
	Natural variant	152	1	F → S in strain: Seychelles-12. Ref.2
	Natural variant	293	1	W → L in strain: Seychelles-7 and Seychelles-8. Ref.2
	Natural variant	423	1	F → S in strain: Seychelles-8 and Seychelles-10. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O76261-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 5E02E633FFB270EB	FASTA	493	55,461
	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 ETVSRDEYKD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ 310 320 330 340 350 360 ALTFVDNHDN QRDAGAVLSY KSPRQYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA 370 380 390 400 410 420 QERIISPEFD EDGACVNGWI CEHRWRQIYA MVGFKNAVRD TEITGWWDNG DNQIAFCRGN 430 440 450 460 470 480 KGFLAINNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNENG FGYIHIGSDD 490 FDGVLALHVD AKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Da Lage J.-L. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Multilocus patterns of nucleotide diversity in Drosophila sechellia: the evolutionary history of the least variable Drosophila species." Legrand D., Tenaillon M., Lachaise D., Cariou M.-L. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-143; SER-152; LEU-293 AND SER-423. Strain: Seychelles-1, Seychelles-10, Seychelles-11, Seychelles-12, Seychelles-13, Seychelles-14, Seychelles-15, Seychelles-2, Seychelles-3, Seychelles-4, Seychelles-5, Seychelles-6, Seychelles-7, Seychelles-8 and Seychelles-9.
[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: Rob3c / Tucson 14021-0248.25.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF039558 Genomic DNA. Translation: AAC39093.1. EU018418 Genomic DNA. Translation: ABW69388.1. EU018419 Genomic DNA. Translation: ABW69389.1. EU018420 Genomic DNA. Translation: ABW69390.1. EU018421 Genomic DNA. Translation: ABW69391.1. EU018422 Genomic DNA. Translation: ABW69392.1. EU018423 Genomic DNA. Translation: ABW69393.1. EU018424 Genomic DNA. Translation: ABW69394.1. EU018425 Genomic DNA. Translation: ABW69395.1. EU018426 Genomic DNA. Translation: ABW69396.1. EU018427 Genomic DNA. Translation: ABW69397.1. EU018428 Genomic DNA. Translation: ABW69398.1. EU018429 Genomic DNA. Translation: ABW69399.1. EU018430 Genomic DNA. Translation: ABW69400.1. EU018431 Genomic DNA. Translation: ABW69401.1. EU018432 Genomic DNA. Translation: ABW69402.1. CH480816 Genomic DNA. Translation: EDW48174.1.
RefSeq	XP_002034161.1.
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.
Genome annotation databases
GeneID	6609476.
KEGG	dse:Dsec_GM20043.
Organism-specific databases
FlyBase	FBgn0025060. Dsec\Amyrel.
Enzyme and pathway databases
BRENDA	3.2.1.1. 300118.
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_DROSE

Accession

Primary (citable) accession number: O76261
Secondary accession number(s): B4HT73 , B6C8H3, B6C8H4, B6C8H9, B6C8I0, B6C8I2, B6C8I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project