Alpha-amylase 1 precursor - Drosophila ananassae (Fruit fly)

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Q23835 (AMY1_DROAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-amylase 1
EC=3.2.1.1

Gene names

Name:	Amy35
Synonyms:	Amy1
ORF Names:	GF18844

Organism

Drosophila ananassae (Fruit fly) [Complete proteome]

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	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 polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
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
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC metal 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

Potential

Chain

19 – 494

476

Alpha-amylase 1

PRO_0000001360

Sites

Active site

204

Nucleophile By similarity

Active site

241

Proton donor By similarity

Metal binding

116

Calcium By similarity

Metal binding

165

Calcium; via carbonyl oxygen By similarity

Metal binding

174

Calcium By similarity

Metal binding

208

Calcium; via carbonyl oxygen By similarity

Binding site

202

Chloride By similarity

Binding site

304

Chloride By similarity

Binding site

343

Chloride By similarity

Site

306

Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond

46 ↔ 102

By similarity

Disulfide bond

153 ↔ 167

By similarity

Disulfide bond

376 ↔ 382

By similarity

Disulfide bond

448 ↔ 460

By similarity

Natural variations

Natural variant

F → L in strain: Taka5. Ref.3

Experimental info

Sequence conflict

121

N → D in AAC79123. Ref.1

Sequence conflict

121

N → D in AAC47353. Ref.4

Sequence conflict

128

G → A in AAC79123. Ref.1

Sequence conflict

128

G → A in AAC47353. Ref.4

Sequence conflict

387

K → R in AAC79123. Ref.1

Sequence conflict

394

G → D in AAC79123. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q23835 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 9884FB907BE8E6B0
Show »

FASTA

494

53,575

        10         20         30         40         50         60 
MFLAKSIVCL ALLAVANAQF NTNYASGRSG MVHLFEWKWD DIAAECENFL GPYGYAGVQV 

        70         80         90        100        110        120 
SPVNENAVKD SRPWWERYQP ISYKLVTRSG NEEQFASMVR RCNNVGVRIY VDVVFNHMAA 

       130        140        150        160        170        180 
NGGTYGTGGS TASPSSKSYP GVPFSSLDFN PTCAISNYND ANQVRNCELV GLRDLNQGNS 

       190        200        210        220        230        240 
YVQEKIVEFL NHLIDLGVAG FRVDAAKHMW PADLGVIYGS LKNLNTDHGF ESGAKAYIVQ 

       250        260        270        280        290        300 
EVIDMGGEAI SKSEYTGLGA ITEFRHSDSI GKAFRGKNQL QYLVNWGVSW GFAASDRSLV 

       310        320        330        340        350        360 
FVDNHDNQRG HGAGGADVLT YKVPKQYKMA SAFMLAHPFG TPRVMSSFSF TDTDQGPPTT 

       370        380        390        400        410        420 
DGQNIASPSF NSDNSCSGGW VCEHRWKQIY NMVGFRNAVG SDAIQNWWDN GSNQIAFSRG 

       430        440        450        460        470        480 
SKGFVAFNND NYDLNSSVQT GLPAGTYCDV ISGSKSGSSC TGKTVTVGSD GRANISIGSS 

       490 
EDDGVLAIHV NAKL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A nested alpha-amylase gene in Drosophila ananassae." Da Lage J.-L., Maisonhaute C., Maczkowiak F., Cariou M.L. J. Mol. Evol. 57:355-362(2003) [PubMed: 14629045] [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]	"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] OF 1-34, VARIANT LEU-2. Strain: 371-1, Bangalore, Beruwala, Bouake, Brazzaville, Colombo, Cuba, Djeffa, Guadeloupe, Korat, Korat3422, Lambir, Mauritius, Mexico, Porto Rico, Reunion, Sao Paulo, Tai 13-1610, Taka5 and Yaounde.
[4]	"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 57-206. Strain: Tai 13-1610.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U53698 Genomic DNA. Translation: AAC79123.1. CH902617 Genomic DNA. Translation: EDV44151.1. AF238900 Genomic DNA. Translation: AAG45254.1. AF238901 Genomic DNA. Translation: AAG45255.1. AF238902 Genomic DNA. Translation: AAG45256.1. AF238903 Genomic DNA. Translation: AAG45257.1. AF238904 Genomic DNA. Translation: AAG45258.1. AF238905 Genomic DNA. Translation: AAG45259.1. AF238906 Genomic DNA. Translation: AAG45260.1. AF238907 Genomic DNA. Translation: AAG45261.1. AF238908 Genomic DNA. Translation: AAG45262.1. AF238909 Genomic DNA. Translation: AAG45263.1. AF238910 Genomic DNA. Translation: AAG45264.1. AF238911 Genomic DNA. Translation: AAG45265.1. AF238912 Genomic DNA. Translation: AAG45266.1. AF238913 Genomic DNA. Translation: AAG45267.1. AF238914 Genomic DNA. Translation: AAG45268.1. AF238915 Genomic DNA. Translation: AAG45269.1. AF238916 Genomic DNA. Translation: AAG45270.1. AF238917 Genomic DNA. Translation: AAG45271.1. AF238918 Genomic DNA. Translation: AAG45272.1. AF238919 Genomic DNA. Translation: AAG45273.1. AF238920 Genomic DNA. Translation: AAG45274.1. AF238921 Genomic DNA. Translation: AAG45275.1. AF238922 Genomic DNA. Translation: AAG45276.1. AF238923 Genomic DNA. Translation: AAG45277.1. AF238924 Genomic DNA. Translation: AAG45278.1. AF238925 Genomic DNA. Translation: AAG45279.1. AF238926 Genomic DNA. Translation: AAG45280.1. AF238927 Genomic DNA. Translation: AAG45281.1. AF238928 Genomic DNA. Translation: AAG45282.1. AF238929 Genomic DNA. Translation: AAG45283.1. AF238930 Genomic DNA. Translation: AAG45284.1. AF238931 Genomic DNA. Translation: AAG45285.1. AF238932 Genomic DNA. Translation: AAG45286.1. AF238933 Genomic DNA. Translation: AAG45287.1. AF238934 Genomic DNA. Translation: AAG45288.1. AF238935 Genomic DNA. Translation: AAG45289.1. AF238936 Genomic DNA. Translation: AAG45290.1. AF238937 Genomic DNA. Translation: AAG45291.1. AF238938 Genomic DNA. Translation: AAG45292.1. AF238939 Genomic DNA. Translation: AAG45293.1. AF238940 Genomic DNA. Translation: AAG45294.1. AF238941 Genomic DNA. Translation: AAG45295.1. AF238942 Genomic DNA. Translation: AAG45296.1. AF238943 Genomic DNA. Translation: AAG45297.1. AF238944 Genomic DNA. Translation: AAG45298.1. AF238945 Genomic DNA. Translation: AAG45299.1. AF238946 Genomic DNA. Translation: AAG45300.1. AF238947 Genomic DNA. Translation: AAG45301.1. AF238948 Genomic DNA. Translation: AAG45302.1. AF238949 Genomic DNA. Translation: AAG45303.1. AF238950 Genomic DNA. Translation: AAG45304.1. AF238951 Genomic DNA. Translation: AAG45305.1. AF238952 Genomic DNA. Translation: AAG45306.1. AF238953 Genomic DNA. Translation: AAG45307.1. AF238954 Genomic DNA. Translation: AAG45308.1. AF238955 Genomic DNA. Translation: AAG45309.1. AF238956 Genomic DNA. Translation: AAG45310.1. AF238957 Genomic DNA. Translation: AAG45311.1. U31122 Genomic DNA. Translation: AAC47353.1.
RefSeq	XP_001955590.1. XM_001955554.1.
3D structure databases
ProteinModelPortal	Q23835.
ModBase	Search...
Protein-protein interaction databases
STRING	Q23835.
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0123544; FBpp0122036; FBgn0021703.
GeneID	6492910.
KEGG	dan:Dana_GF18844.
Organism-specific databases
FlyBase	FBgn0261677. Dana\Amy35.
Phylogenomic databases
GeneTree	EMGT00050000007262.
PhylomeDB	Q23835.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR015902. Alpha_amylase. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K01176.
PANTHER	PTHR10357. Alpha_amylase. 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]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMY1_DROAN

Accession

Primary (citable) accession number: Q23835
Secondary accession number(s): B3LZH2, Q9GN69, Q9GN73

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents