Reviewed, UniProtKB/Swiss-Prot O76263 (AMYR_DROWI)

Names and origin

Protein names

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

Gene names

Name:

Amyrel

Organism

Drosophila willistoni (Fruit fly)

Taxonomic identifier

7260 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	492 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 – 18	18	By similarity
	Chain	19 – 492	474	Alpha-amylase-related protein		PRO_0000001393
Sites
	Active site	206	1	Nucleophile By similarity
	Active site	243	1	Proton donor By similarity
	Active site	308	1	By similarity
	Metal binding	116	1	Calcium By similarity
	Metal binding	167	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	176	1	Calcium By similarity
	Metal binding	210	1	Calcium; via carbonyl oxygen By similarity
	Binding site	204	1	Chloride By similarity
	Binding site	306	1	Chloride By similarity
	Binding site	341	1	Chloride By similarity
Amino acid modifications
	Modified residue	19	1	Pyrrolidone carboxylic acid By similarity
	Disulfide bond	46 ↔ 102		By similarity
	Disulfide bond	155 ↔ 169		By similarity
	Disulfide bond	374 ↔ 380		By similarity
	Disulfide bond	416 ↔ 439		Potential
	Disulfide bond	446 ↔ 458		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O76263-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: DFC711A762D8715D	FASTA	492	55,641
	10 20 30 40 50 60 MRLSLSVLLC LGLALTLAQH NPHWWGNRNT IVHLFEWKWT DIADKCERFL GPRGYAGVQV 70 80 90 100 110 120 SPANENIISE GRPWWERYQP ISYKLVTRSG NELEFASMVK RCNDVGVRIY VDVLLNHMSA 130 140 150 160 170 180 DFEGLATGTG GSVAEPAKKS FPSVPYTADD FHETCEITDW NDRFQVQQCE LVGLKDLNQN 190 200 210 220 230 240 RDWVRTKLIE FLDHLIELGV AGFRVDAAKH MASEDLSFIY SSVRDLNINH GFPNNARPFI 250 260 270 280 290 300 YQEVIDHGHE TVTREEYNEL GAVTEFRFSE EIGKAFRGNN ALKWLQSWGT DWGFLSSGQA 310 320 330 340 350 360 LTFVDNHDNQ RDSGDVLNYK SPKQYKMATA FHLAYPYGIS RVMSSFGFDD RDQAPPQDAQ 370 380 390 400 410 420 EQLISPEFDA DGGCTNGWIC EHRWRQIYNM VEFKNTVRDT ELTNWWDNGD NQIAFCRGSK 430 440 450 460 470 480 GFIAINNNLY NLSETLQTCL PAGEYCDVIS GSLVDGACTG KSVSVDGNGY GYIHIGTEDF 490 DGVLAIHTDA KL

References

[1]	Da Lage J.-L. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF039560 Genomic DNA. Translation: AAC39095.1.
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	FBgn0025016. Dwil\Amyrel.
Enzyme and pathway databases
BRENDA	3.2.1.1. 278536.
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_DROWI

Accession

Primary (citable) accession number: O76263

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project