H2N0D4 · AMY_ORYLA

Function

function

Catalyzes the hydrolysis of alpha-1,4 glycosidic linkages in starch, glycogen and similar oligosaccharides.

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

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.
chloride (UniProtKB | Rhea| CHEBI:17996 )

Note: Binds 1 Cl- ion per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1.18 mg/mlpotato amylopectin
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
2560 μmol/min/mg

pH Dependence

Optimum pH is 7.1.

Temperature Dependence

Optimum temperature is 50 degrees Celsius.

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site115Ca2+ (UniProtKB | ChEBI)
Binding site173Ca2+ (UniProtKB | ChEBI)
Binding site182Ca2+ (UniProtKB | ChEBI)
Binding site210chloride (UniProtKB | ChEBI)
Active site212Nucleophile
Binding site216Ca2+ (UniProtKB | ChEBI)
Active site248Proton donor
Site315Transition state stabilizer
Binding site352chloride (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular space
Molecular Functionalpha-amylase activity
Molecular Functionmetal ion binding
Biological Processcarbohydrate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-amylase
  • EC number

Organism names

  • Taxonomic identifier
  • Strain
    • Hd-rR
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Atherinomorphae > Beloniformes > Adrianichthyidae > Oryziinae > Oryzias

Accessions

  • Primary accession
    H2N0D4

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Signal1-15
ChainPRO_501299449316-512Alpha-amylase
Disulfide bond43↔101
Disulfide bond85↔130
Disulfide bond156↔175
Disulfide bond394↔400
Disulfide bond466↔478
Glycosylation496N-linked (GlcNAc...) asparagine

Keywords

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

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
    512
  • Mass (Da)
    57,167
  • Last updated
    2012-03-21 v1
  • MD5 Checksum
    55E37258B3E85C1A22F0488993FCDF70
MKLFVLIALFGLGFAQHNPNTRDGRTAIVHLFEWRWADIAAECERFLGPKGFAGVQISPPNEHILVSSPWRPWWQRYQPISYNLCSRSGGENELRDMITRCNNVGVNVYVDAVINHMCGAGGGEGTHSSCGSWFNANNKDFPSVPYSNLDFNDGKCKTGSGNIENYGDPYQVRDCRLVGLLDLALEKDYVRGKVADFMNKLIDMGVAGFRVDACKHMWPGDLDNVYRRLNNLNTKWFPGGSRPFIFQEVIDLGGEPITTGEYVGLGRVTEFKYGARLGELFRKWNGQKLSYTKNWGEGWGFMADGNAVVFTDNHDNQRGHGAGGASILTFWDPRLYKMAVGYMLAHPYGFTRVMSSYSWDRNFVNGKDENDWIGPPSNGDGSTKPVPINPDQTCGDGWVCEHRWRQIMNMVQFRNVVNGQPHANWWDNGNNQVAFGRGNRGFIVFNNDDWALDVTLNTGLPGGTYCDVISGNKDGGSCTGKQITVGGDGRAHFYINNSEEDPFIAIHADSKL

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help