Detail Information for IndEnz0001000057
IED ID IndEnz0001000057
Enzyme Type ID amylase000057
Protein Name Alpha-glucosidase
EC 3.2.1.20
Binary toxin-binding alpha-glucosidase
Culex pipiens maltase 1
Cpm1
Gene Name CPM1
Organism Culex pipiens (House mosquito)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Nematocera Culicomorpha Culicoidea Culicidae (mosquitos) Culicinae Culicini Culex Culex Culex pipiens complex Culex pipiens (House mosquito)
Enzyme Sequence MRPLGALSLFALLATTVSGLAIREPDAKDWYQHATFYQIYPRSFLDSNGDGIGDLAGITSKMKYLADIGIDATWLSPPFKSPLKDFGYDVSDFYAIQPEYGNLTDFDKLVEEAHKNGIKLMLDFIPNHSSDQHEWFVKSVARDPEYSEFYVWKPPATGGGPPNNWISVFGGPAWTYNAARGEYYLHQFTPQQPDLNYRNPKLLAEMTKMLFFWLDRGVDGFRLDAINHMFEDEQFRDEPVSGWGQPGEYDSLDHIYTKDIPDVYNVVYNWRDQMDKYSAEKGRTIILMTEAYSSIEGTMLYYESADRKRQGAHMPFNFQLIYDFKKEQNAVGLKSSIDWWMNNMPARHTPSWVAGSHDHSRVASRVGLDRVDQVMTLMHTLPGTSITYYGEEVAMQDFKEAQQFDNRDPNRTPMQWDSSTSAGFSTNTNTWLRVHPDYARYNVDVMQKNPQSTFHHFQHLTKLRGHRTMQSGEYVHKTVGTKVYALLRELRGEDSFLTVLNMAGAEDTVDLGDFVNLPQKMRVEVAQPNSKSKAGNEVDISKLTLGPYDSVVLRATVSSAAAINLSIGLLLAIMARYIFV
Enzyme Length 580
Uniprot Accession Number Q95WY5
Absorption
Active Site ACT_SITE 224; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:A0R6E0; ACT_SITE 290; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:A0R6E0
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; Evidence={ECO:0000305|PubMed:11483434};
DNA Binding
EC Number 3.2.1.20
Enzyme Function FUNCTION: Probably an alpha-glucosidase, it has no alpha-amylase function. {ECO:0000305|Ref.2}.; FUNCTION: (Microbial infection) Serves as the larval receptor for Lysinibacillus sphaericus BinB toxin (Ref.2). {ECO:0000269|Ref.2}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Glycosylation (3); Natural variant (7); Signal peptide (1); Site (1); Transmembrane (1)
Keywords Direct protein sequencing;Glycoprotein;Glycosidase;Hydrolase;Membrane;Signal;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 66,121
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda