Reviewed, UniProtKB/Swiss-Prot Q9NJN8 (AMYR_DROBP)

Names and origin

Protein names

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

Gene names

Name:

Amyrel

Organism

Drosophila bipectinata (Fruit fly)

Taxonomic identifier

42026 [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 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 – 20	20	By similarity
	Chain	21 – 494	474	Alpha-amylase-related protein		PRO_0000001373
Sites
	Active site	208	1	Nucleophile By similarity
	Active site	245	1	Proton donor By similarity
	Active site	310	1	By similarity
	Metal binding	118	1	Calcium By similarity
	Metal binding	169	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	178	1	Calcium By similarity
	Metal binding	212	1	Calcium; via carbonyl oxygen By similarity
	Binding site	206	1	Chloride By similarity
	Binding site	308	1	Chloride By similarity
	Binding site	343	1	Chloride By similarity
Amino acid modifications
	Modified residue	21	1	Pyrrolidone carboxylic acid By similarity
	Disulfide bond	48 ↔ 104		By similarity
	Disulfide bond	157 ↔ 171		By similarity
	Disulfide bond	376 ↔ 382		By similarity
	Disulfide bond	418 ↔ 441		Potential
	Disulfide bond	448 ↔ 460		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9NJN8-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 60EEEF2C9F685491	FASTA	494	55,339
	10 20 30 40 50 60 MFKFATAVIL CLVAASSTLA QHNPHWWGNR NTIVHLFEWK WSDIAAECEN FLGPRGFAGV 70 80 90 100 110 120 QVSPVNENIV SAGRPWWERY QPISYKLTTR SGNEKEFADM VRRCNEVGVR IYVDVLLNHM 130 140 150 160 170 180 SGDFDGIAVG TAGSEAEPSK KSYPGVPYSA LDFHPSCEIT DWNDRFQVQQ CELVGLKDLD 190 200 210 220 230 240 QSSEWVRSKL IEFLDHLIEL GVAGFRVDAA KHMAADDLSF IYSSLSDLNI EHGFPHNARP 250 260 270 280 290 300 FIFQEVIDHG HETVSREEYN QLGAVTEFRF SEGIGNAFRG NNALKWLQSW GTGWGFLPSG 310 320 330 340 350 360 QALTFVDNHD NQRDMGAVLN YKSPKQYKMA TAFHLAYPYG ISRVMSSFAF DDHDTAPPQD 370 380 390 400 410 420 EQEKIISPEF DEEGACVNGW ICEHRWRQIY AMVGFKNAVR DTELSNWWDN GDSQISFCRG 430 440 450 460 470 480 NKGFLAVNNN LYDLSQELQT CLPAGVYCDV ISGSLVDGSC TGKSVTVDDN GYGYAHIGSD 490 DFDGVLALHV DAKV

References

[1]	"Origin and evolution of the Amyrel gene in Drosophila." Da Lage J.-L., Renard E., Chartois F., Cariou M.-L. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF136936 Genomic DNA. Translation: AAF25718.1.
3D structure databases
SMR	Q9NJN8. Positions 21-494.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Organism-specific databases
FlyBase	FBgn0029467. Dbip\Amyrel.
Enzyme and pathway databases
BRENDA	3.2.1.1. 294624.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR017853. Glyco_hydro_catalytic_core. 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_DROBP

Accession

Primary (citable) accession number: Q9NJN8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project