Reviewed, UniProtKB/Swiss-Prot Q23834 (AM4N_DROAN)

Names and origin

Protein names

Recommended name:
    Alpha-amylase 4N
    EC=3.2.1.1

Gene names

Name:	Amy4N
ORF Names:	GF13835

Organism

Drosophila ananassae (Fruit fly)

Taxonomic identifier

7217 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	495 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.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Signal
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	alpha-amylase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB 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	Potential
	Chain	20 – 495	476	Alpha-amylase 4N		PRO_0000001362
Sites
	Active site	205	1	Nucleophile By similarity
	Active site	242	1	Proton donor By similarity
	Active site	307	1	By similarity
	Metal binding	117	1	Calcium By similarity
	Metal binding	166	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	175	1	Calcium By similarity
	Metal binding	209	1	Calcium; via carbonyl oxygen By similarity
	Binding site	203	1	Chloride By similarity
	Binding site	305	1	Chloride By similarity
	Binding site	344	1	Chloride By similarity
Amino acid modifications
	Disulfide bond	47 ↔ 103		By similarity
	Disulfide bond	154 ↔ 168		By similarity
	Disulfide bond	377 ↔ 383		By similarity
	Disulfide bond	449 ↔ 461		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q23834-1 [UniParc]. Last modified November 1, 1998. Version 2. Checksum: 529B3E61F00A41C9	FASTA	495	53,781
	10 20 30 40 50 60 MRGLTKSLVC LALLAVANAQ FNTNYASGRS GMVHLFEWKW DDIASECENF LGPNGFAGVQ 70 80 90 100 110 120 VSPVNENAVK DSRPWWERYQ PISYKLVTRS GNEEQFASMV RRCNNAGVRI YVDVVFNHMA 130 140 150 160 170 180 ADGGTYGTGG STASPSSKSY PGVPYSSLDF NPTCAISNYN DANQVRNCEL VGLRDLNQGN 190 200 210 220 230 240 SYVQEKVAEF LNHLIDLGVA GFRVDAAKHM WPADLGTIYG RLKTLNTDHG FQSGAKAYIV 250 260 270 280 290 300 QEVIDMGGEA ISKSEYTGLG AITEFRHSDS IGKVFRGKNQ LKYLTNWGTA WGFAASDRSL 310 320 330 340 350 360 VFVDNHDNQR GHGAGGADVL TYKVAKQYKM ASAFMLAHPF GTPRVMSSFS FSDTDQGPPT 370 380 390 400 410 420 TDGHNIASPV FNSDNSCSGG WVCEHRWRQI YNMVAFRNTV GSDEIQNWWD NGSNQIAFSR 430 440 450 460 470 480 GGKGFVAFNN DNYDLNSSLQ TGLPAGTYCD VISGMKNGSS CTGKTVTVGS DGRANISIGS 490 SEDDGVLAIH VSAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization and evolution of the amylase multigene family of Drosophila ananassae." Da Lage J.-L., Maczkowiak F., Cariou M.-L. J. Mol. Evol. 51:391-403(2000) [PubMed: 11040291] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Tai 13-1610.
[2]	"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: Tucson 14024-0371.13.
[3]	"Distribution and evolution of introns in Drosophila amylase genes." Da Lage J.-L., Wegnez M., Cariou M.-L. J. Mol. Evol. 43:334-347(1996) [PubMed: 8798339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-202. Strain: Tai 13-1610.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U53477 Genomic DNA. Translation: AAC48343.1. CH902619 Genomic DNA. Translation: EDV38192.1. U31121 Genomic DNA. Translation: AAC47352.1.
RefSeq	XP_001961370.1.
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	6496670.
KEGG	dan:Dana_GF13835.
Organism-specific databases
FlyBase	FBgn0259988. Dana\Amy4N.
Enzyme and pathway databases
BRENDA	3.2.1.1. 278838.
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

AM4N_DROAN

Accession

Primary (citable) accession number: Q23834
Secondary accession number(s): B3MBP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	November 1, 1998
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