Detail Information for IndEnz0001000595
IED ID IndEnz0001000595
Enzyme Type ID amylase000595
Protein Name Alpha-amylase
EC 3.2.1.1
1,4-alpha-D-glucan glucanohydrolase
Gene Name amyA
Organism Butyrivibrio fibrisolvens
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Lachnospiraceae Butyrivibrio Butyrivibrio fibrisolvens
Enzyme Sequence MKRGKLWGRLVSAAGLSLSIFLSSIGNVSTAYAMESNDALVLDETKENTESATDASSNEASDAEADNDTDEAITDASSKELSAENDGASESDSSFDEYDHTALPETDEITVTAAGELSTAKAELYTLAPREAREADNSLVTRDSIHDGAILHAFCWSFNTIADNMADIADAGYTAVQTSPINECLSTNPGMNLHGPDGMWYYHYQPTDWVIGNYQLGSRDEFKHMCDVADEYGVAVIVDILPNHTTPSTGSIAKALMEAAGGSDALYHATGKIGGGYTDRLELTYYSMGGLPDVDTENTGFQQYFYEFLKDCVYLGADGFRIDTAKHISLPDDPVPSDYSDAGRNTFYPNMREALNEYSEEVGTKSYDELFVYGEVLQGTNDRLAAYQQYIGGTTASNYGSSLRSALSSGNLSVNRLLDYQIYDDTAYGSTYTADTEKLVTWVESHDNYMNDSESCWKSIDDDMVIMGWSIIAARDAGTPLFFSRPNNSSAENPYGDNLIGAAGSPIYKAPEVKAVNLFREKMGEADEYLSNPGGNIQTLMIERYNDTVQGAVIVNAAQTRTTISTETHLSDGIYPDQVEGSNSVFLVKDGVLSGSVEGEGVVVLSEKMDGTGKVVSFYNNKNWNGVVARVDNAEETLDTIDENDGWFQVTVLDDEFTIRFESADGKEVSPEFQITAESGTFATPDSSELYYSKAEAEEGLGIHTYPVYFFNTENWGSVYTYGWLDGGAQLFGGWPGTVAVNEGSGWYRADVKTTGEITAFNLIFNNGNGIQTVNVEGITPDSKDIYLAVDAEKSNGQLIVNRYEDKESAEKALGVSGSYTTAYFYNTEGWDKVCAYTWGATALGDWPGKELTQDEDGWYSVVLPAGPSEDLNIIFNNGNNGKQTNDMKISDMKYRFILNNGISYQKYGSKKDAMEAIAGAGDVTYETVYFYNEKADDANWKNVYLYVFGGTDGEYNNLVGTWPGKLMEKEEDSNG
Enzyme Length 976
Uniprot Accession Number P30269
Absorption
Active Site ACT_SITE 323; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 375; /note=Proton donor; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=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;
DNA Binding
EC Number 3.2.1.1
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (4); Region (1); Signal peptide (1); Site (1)
Keywords Calcium;Carbohydrate metabolism;Glycosidase;Hydrolase;Metal-binding;Signal
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..33; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 106,695
Kinetics
Metal Binding METAL 243; /note=Calcium; /evidence=ECO:0000250; METAL 284; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 293; /note=Calcium; /evidence=ECO:0000250; METAL 327; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda