P00691 · AMY_BACSU

Function

Catalytic activity

  • Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
    EC:3.2.1.1 (UniProtKB | ENZYME | Rhea)

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 2 calcium ions per subunit.

Features

Showing features for binding site, active site, site.

165950100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site142Ca2+ 1 (UniProtKB | ChEBI)
Binding site178Ca2+ 1 (UniProtKB | ChEBI)
Binding site187Ca2+ 1 (UniProtKB | ChEBI)
Binding site210Ca2+ 2 (UniProtKB | ChEBI)
Binding site212Ca2+ 2 (UniProtKB | ChEBI)
Active site217Nucleophile
Binding site221Ca2+ 1 (UniProtKB | ChEBI)
Active site249Proton donor
Site310Transition state stabilizer

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functionalpha-amylase activity
Molecular Functionmetal ion binding
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • CBM26Carbohydrate-Binding Module Family 26
    • GH13Glycoside Hydrolase Family 13

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-amylase
  • EC number
  • Alternative names
    • 1,4-alpha-D-glucan glucanohydrolase

Gene names

    • Name
      amyE
    • Synonyms
      amyA
    • Ordered locus names
      BSU03040

Organism names

Accessions

  • Primary accession
    P00691

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant469-477in strain: N7 AMYEN+
Natural variant478-659in strain: N7 AMYEN+

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for signal, propeptide, chain.

TypeIDPosition(s)Description
Signal1-27
PropeptidePRO_000000133528-41
ChainPRO_000000133642-659Alpha-amylase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Chemistry

Family & Domains

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    659
  • Mass (Da)
    72,378
  • Last updated
    2009-06-16 v2
  • Checksum
    16BD6CB1E7C67BD6
MFAKRFKTSLLPLFAGFLLLFHLVLAGPAAASAETANKSNELTAPSIKSGTILHAWNWSFNTLKHNMKDIHDAGYTAIQTSPINQVKEGNQGDKSMSNWYWLYQPTSYQIGNRYLGTEQEFKEMCAAAEEYGIKVIVDAVINHTTSDYAAISNEVKSIPNWTHGNTQIKNWSDRWDVTQNSLLGLYDWNTQNTQVQSYLKRFLDRALNDGADGFRFDAAKHIELPDDGSYGSQFWPNITNTSAEFQYGEILQDSASRDAAYANYMDVTASNYGHSIRSALKNRNLGVSNISHYASDVSADKLVTWVESHDTYANDDEESTWMSDDDIRLGWAVIASRSGSTPLFFSRPEGGGNGVRFPGKSQIGDRGSALFEDQAITAVNRFHNVMAGQPEELSNPNGNNQIFMNQRGSHGVVLANAGSSSVSINTATKLPDGRYDNKAGAGSFQVNDGKLTGTINARSVAVLYPDDIAKAPHVFLENYKTGVTHSFNDQLTITLRADANTTKAVYQINNGPETAFKDGDQFTIGKGDPFGKTYTIMLKGTNSDGVTRTEKYSFVKRDPASAKTIGYQNPNHWSQVNAYIYKHDGSRVIELTGSWPGKPMTKNADGIYTLTLPADTDTTNAKVIFNNGSAQVPGQNQPGFDYVLNGLYNDSGLSGSLPH

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict22in Ref. 2; CAA26086, 6; AAA22234, 7; CAA23436 and 8; AAA22230
Sequence conflict146in Ref. 2; CAA26086 and 6; AAA22234
Sequence conflict204in Ref. 2; CAA26086 and 6; AAA22234
Sequence conflict284in Ref. 2; CAA26086
Sequence conflict332in Ref. 6; AAA22234
Sequence conflict513-529in Ref. 1; CAA23437 and 3; BAA08938

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
V00101
EMBL· GenBank· DDBJ
CAA23437.1
EMBL· GenBank· DDBJ
Genomic DNA
V00100
EMBL· GenBank· DDBJ
CAA23436.1
EMBL· GenBank· DDBJ
Genomic DNA
D50453
EMBL· GenBank· DDBJ
BAA08938.1
EMBL· GenBank· DDBJ
Genomic DNA
AL009126
EMBL· GenBank· DDBJ
CAB12098.2
EMBL· GenBank· DDBJ
Genomic DNA
K00563
EMBL· GenBank· DDBJ
AAA22234.1
EMBL· GenBank· DDBJ
Genomic DNA
X02150
EMBL· GenBank· DDBJ
CAA26086.1
EMBL· GenBank· DDBJ
Genomic DNA
M35517
EMBL· GenBank· DDBJ
AAA22230.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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