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Reviewed, UniProtKB/Swiss-Prot O76265 (AMYR_DROER)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-amylase-related protein
    EC=3.2.1.1
Gene names
Name: Amyrel
OrganismDrosophila erecta (Fruit fly)
Taxonomic identifier7220 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Chloride
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Pyrrolidone carboxylic acid
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalpha-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 493474Alpha-amylase-related protein
PRO_0000001377

Sites

Active site2071Nucleophile By similarity
Active site2441Proton donor By similarity
Active site3091 By similarity
Metal binding1171Calcium By similarity
Metal binding1681Calcium; via carbonyl oxygen By similarity
Metal binding1771Calcium By similarity
Metal binding2111Calcium; via carbonyl oxygen By similarity
Binding site2051Chloride By similarity
Binding site3071Chloride By similarity
Binding site3421Chloride By similarity

Amino acid modifications

Modified residue201Pyrrolidone carboxylic acid By similarity
Disulfide bond47 ↔ 103 By similarity
Disulfide bond156 ↔ 170 By similarity
Disulfide bond375 ↔ 381 By similarity
Disulfide bond417 ↔ 440 Potential
Disulfide bond447 ↔ 459 By similarity

Sequences

Sequence LengthMass (Da)Tools
O76265-1 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: 4F7FEC32130662B7

FASTA49355,364
        10         20         30         40         50         60 
MFKLAFTLTL CLAGGLSLAQ HNPHWWGNRN TIVHLFEWKW LDIAQECESF LAPRGFAGVQ 

        70         80         90        100        110        120 
VSPVNENIIS AGRPWWERYQ PISYKLTTRS GNEEEFGEMV RRCNDVGVRI YVDVLLNHMS 

       130        140        150        160        170        180 
GDFDGVAVGT AGTQAEPRKK SFPGVPYSAQ DFHPTCEITD WNDRFQVQQC ELVGLKDLNQ 

       190        200        210        220        230        240 
SSDWVRSKLI EFLDHLIELG VAGFRVDAAK HMASEDLEYI YSSLSNLNIA HGFPHNSRPF 

       250        260        270        280        290        300 
IFQEVIDHGH ETVSRDEYRD LGAVTEFRFS EEIGNAFRGN NALKWLQSWG TGWGFLPSGQ 

       310        320        330        340        350        360 
ALTFVDNHDN QRDAGAVLNY KSPKPYKMAT AFHLAYPYGI SRVMSSFAFD DHDTPPPQDA 

       370        380        390        400        410        420 
QERIISPEFD ADGACVNGWI CEHRWRQVYA MVGFKNAVRD TEITGWWDNG DSQISFCRGT 

       430        440        450        460        470        480 
KGFLALNNNL YDLSQDLNTC LPAGTYCDVI SGSLIDGSCT GKSVTVNEHG YGYIHIGSDD 

       490 
FDGVLALHVD AKV 

« Hide

References

[1]Da Lage J.-L.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

AF039562 Genomic DNA. Translation: AAC39091.2.

3D structure databases

HSSPHSSP built from PDB template 1JAE based on UniProtKB P56634.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Organism-specific databases

FlyBaseFBgn0025090. Dere\Amyrel.

Enzyme and pathway databases

BRENDA3.2.1.1. 278534.

Family and domain databases

InterProIPR006048. 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]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02806. Alpha-amylase_C. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYR_DROER
AccessionPrimary (citable) accession number: O76265
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents