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P53354 (AMY1_AEDAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-amylase I
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:AMY1
Synonyms:AMY I
ORF Names:AAEL006719
OrganismAedes aegypti (Yellowfever mosquito) (Culex aegypti)
Taxonomic identifier7159 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Culicinae › Aedini › Aedes › Stegomyia

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Subcellular location

Secreted.

Tissue specificity

Expressed specifically in the proximal-lateral lobes of the adult female salivary gland. Ref.3

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
Glycoprotein
   Technical termComplete proteome
Reference proteome
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

metal 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 – 1616 Potential
Chain17 – 737721Alpha-amylase I
PRO_0000001359

Regions

Region17 – 260244Not found in other alpha-amylases

Sites

Active site4471Nucleophile By similarity
Active site4841Proton donor By similarity
Metal binding3561Calcium By similarity
Metal binding4081Calcium; via carbonyl oxygen By similarity
Metal binding4171Calcium By similarity
Metal binding4511Calcium; via carbonyl oxygen By similarity
Binding site4451Chloride By similarity
Binding site5501Chloride By similarity
Binding site5891Chloride By similarity
Site5521Transition state stabilizer By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation3881N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation5321N-linked (GlcNAc...) Potential
Glycosylation5951N-linked (GlcNAc...) Potential
Glycosylation6191N-linked (GlcNAc...) Potential
Glycosylation6731N-linked (GlcNAc...) Potential
Disulfide bond286 ↔ 342 By similarity
Disulfide bond396 ↔ 410 By similarity
Disulfide bond622 ↔ 628 By similarity
Disulfide bond693 ↔ 705 By similarity

Experimental info

Sequence conflict191L → F in AAA29343. Ref.3
Sequence conflict1371R → H in AAA29343. Ref.3
Sequence conflict1581G → A in AAA29343. Ref.3
Sequence conflict1731N → K in AAB60935. Ref.1
Sequence conflict1781M → I in AAB60935. Ref.1
Sequence conflict1781M → I in AAA29343. Ref.3
Sequence conflict1841K → T in AAB60935. Ref.1
Sequence conflict1971A → D in AAA29343. Ref.3
Sequence conflict2301M → I in AAB60935. Ref.1
Sequence conflict2451L → V in AAB60935. Ref.1
Sequence conflict2881N → K in AAB60935. Ref.1
Sequence conflict2881N → K in AAA29343. Ref.3
Sequence conflict3781Q → L in AAB60935. Ref.1
Sequence conflict4531R → Q in AAA29343. Ref.3
Sequence conflict4621V → D in AAB60935. Ref.1
Sequence conflict4621V → D in AAA29343. Ref.3
Sequence conflict5121A → V in AAB60935. Ref.1
Sequence conflict5121A → V in AAA29343. Ref.3
Sequence conflict5711R → P in AAB60935. Ref.1
Sequence conflict5711R → P in AAA29343. Ref.3
Sequence conflict6121K → R in AAB60935. Ref.1
Sequence conflict6121K → R in AAA29343. Ref.3
Sequence conflict6171A → V in AAB60935. Ref.1
Sequence conflict6171A → V in AAA29343. Ref.3
Sequence conflict6181A → V in AAB60935. Ref.1
Sequence conflict6241N → T in AAB60935. Ref.1
Sequence conflict6241N → T in AAA29343. Ref.3
Sequence conflict7271I → V in AAB60935. Ref.1
Sequence conflict7271I → V in AAA29345. Ref.3
Sequence conflict7321V → I in AAB60935. Ref.1
Sequence conflict7321V → I in AAA29345. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P53354 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 682A1F42055AC753

FASTA73780,891
        10         20         30         40         50         60 
MKQLLVILYS ALVVTNAQLP GFSFGPSGFG GFSLSNPLFN ASFAPANPVD RISDIASRFR 

        70         80         90        100        110        120 
DVANNVQRNL PKIPQFTNPL SAFSRFARPT SSSGSTNANS NNNQNFNSNQ ANEGTSGARN 

       130        140        150        160        170        180 
AINEVLNRIP GLSGVPRVPE IPKVPEIPSF GNPSDVFGPF VNSLRNMTNQ GINDPGQMFN 

       190        200        210        220        230        240 
QVNKFLPDVS RIANSVANYA KSAANSGIWK NISNDIKHEM QNRIESMTQM LSNITSAMKN 

       250        260        270        280        290        300 
IAQSLPNLMQ DQSLNTTLRN QPFFFPGHSG IVHLFEWKFS DIAEECENVL GPNGYGGVQV 

       310        320        330        340        350        360 
SPINEYLVSP SRAWWERYQP ISFEIKSRSG NEKQFSDMVK RCMKAGVRIY VDVVVNHMAA 

       370        380        390        400        410        420 
PGASAPLYGT AGSTCDPQAR DYPGVPFNRS HFHADCQIND YNNATNVRNC ELAALPDLDQ 

       430        440        450        460        470        480 
SNRFVQNKII QYLNHLLDLG VAGFRMDACK HMRPEDLKSI YVRLKPVNAM FLFPPGARPF 

       490        500        510        520        530        540 
IFQEVIDLGT EGVSAKEYTN LGVVTEFNWC IAVGGVFRGT TNADALELLT KNGSAGVLLP 

       550        560        570        580        590        600 
SSQALVFVDN HDNQRGHGAG GDSILTYKTK RQYIQAVAFT LATDYGIARV MSSYNFSDPD 

       610        620        630        640        650        660 
QGPPQDTVQV IKSPGFAANN SCSNGWVCEH RWPEIRKMIQ FKNFVAGSSL DHIQATQNTF 

       670        680        690        700        710        720 
AFCRGEKGFI VFNNSENTIT QQYHTCLPQG QYCDIISGEV SQSTCTGTVV NVDANGDAEI 

       730 
TLPKNSIVAI YVPSRLS

« Hide

References

« Hide 'large scale' references
[1]"Evidence for two distinct members of the amylase gene family in the yellow fever mosquito, Aedes aegypti."
Grossman G.L., Campos Y., Severson D.W., James A.A.
Insect Biochem. Mol. Biol. 27:769-781(1997) [PubMed: 9443377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Rockefeller.
[2]"Genome sequence of Aedes aegypti, a major arbovirus vector."
Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J., Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F., Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P. expand/collapse author list , Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L., Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J., Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E., El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I., Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H., Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S., Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P., Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J., Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W., Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O., Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R., Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B., Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T., Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.
Science 316:1718-1723(2007) [PubMed: 17510324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LVPib12.
[3]"The salivary glands of the vector mosquito, Aedes aegypti, express a novel member of the amylase gene family."
Grossman G.L., James A.A.
Insect Mol. Biol. 1:223-232(1993) [PubMed: 7505701] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-726, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13 AND 722-737, TISSUE SPECIFICITY.
Strain: Rockefeller.
Tissue: Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF000569 Genomic DNA. Translation: AAB60935.1.
CH477404 Genomic DNA. Translation: EAT41631.1.
L03637 mRNA. Translation: AAA29343.1.
L03638 mRNA. Translation: AAA29344.1.
L03639 Genomic DNA. Translation: AAA29345.1.
L03640 Genomic DNA. Translation: AAA29346.1.
RefSeqXP_001652172.1. XM_001652122.1.
UniGeneAae.20631.

3D structure databases

ProteinModelPortalP53354.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaAAEL006719-RA; AAEL006719-PA; AAEL006719.
GeneID5568295.
KEGGaag:AaeL_AAEL006719.

Phylogenomic databases

eggNOGinNOG06322.
GeneTreeEMGT00050000007262.
InParanoidP53354.
OMAVSPINEY.
OrthoDBEOG4JDFP9.
PhylomeDBP53354.

Family and domain databases

InterProIPR006048. 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]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 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]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY1_AEDAE
AccessionPrimary (citable) accession number: P53354
Secondary accession number(s): O02413, Q175A0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents