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Reviewed, UniProtKB/Swiss-Prot P56271 (AMYA_ASPNG)

Last modified June 16, 2009. Version 55. 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

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Names and origin

Protein namesRecommended name:
    Acid alpha-amylase
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.

Cofactor

Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.

Subunit structure

Monomer.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcarbohydrate catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Acid alpha-amylase
PRO_0000054289

Sites

Active site2061Nucleophile
Active site2301Proton donor
Active site2971
Metal binding1211Calcium 1
Metal binding1621Calcium 1; via carbonyl oxygen
Metal binding1751Calcium 1
Metal binding2061Calcium 2
Metal binding2101Calcium 1; via carbonyl oxygen
Metal binding2301Calcium 2

Amino acid modifications

Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 38
Disulfide bond150 ↔ 164
Disulfide bond240 ↔ 283
Disulfide bond440 ↔ 475

Secondary structure

1 .............................................................................................. 484
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P56271-1 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 04D596E34680656D

FASTA48452,935
        10         20         30         40         50         60 
LSAASWRTQS IYFLLTDRFG RTDNSTTATC NTGNEIYCGG SWQGIIDHLD YIEGMGFTAI 

        70         80         90        100        110        120 
WISPITEQLP QDTADGEAYH GYWQQKIYDV NSNFGTADNL KSLSDALHAR GMYLMVDVVP 

       130        140        150        160        170        180 
DHMGYAGNGN DVDYSVFDPF DSSSYFHPYC LITDWDNLTM VEDCWEGDTI VSLPDLDTTE 

       190        200        210        220        230        240 
TAVRTIWYDW VADLVSNYSV DGLRIDSVLE VQPDFFPGYN KASGVYCVGE IDNGNPASDC 

       250        260        270        280        290        300 
PYQKVLDGVL NYPIYWQLLY AFESSSGSIS NLYNMIKSVA SDCSDPTLLG NFIENHDNPR 

       310        320        330        340        350        360 
FAKYTSDYSQ AKNVLSYIFL SDGIPIVYAG EEQHYAGGKV PYNREATWLS GYDTSAELYT 

       370        380        390        400        410        420 
WIATTNAIRK LAIAADSAYI TYANDAFYTD SNTIAMAKGT SGSQVITVLS NKGSSGSSYT 

       430        440        450        460        470        480 
LTLSGSGYTS GTKLIEAYTC TSVTVDSSGD IPVPMASGLP RVLLPASVVD SSSLCGGSGR 


LYVE

« Hide

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References

[1]"Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus."
Boel E., Brady L., Brzozowski A.M., Derewenda Z., Dodson G.G., Jensen V.J., Petersen S.B., Swift H., Thim L., Woldike H.F.
Biochemistry 29:6244-6249(1990) [PubMed: 2207069] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

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Cross-references

Sequence databases

PIRA35282.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2AAAX-ray2.10A1-484[»]
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Enzyme and pathway databases

BRENDA3.2.1.1. 277.

Family and domain databases

InterProIPR013777. A-amylase_fun.
IPR015340. Alpha_amylase_DUF1966_C.
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.
PF09260. DUF1966. 1 hit.
[Graphical view]
PIRSFPIRSF001024. Alph-amyl_fung. 1 hit.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMYA_ASPNG
AccessionPrimary (citable) accession number: P56271
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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