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 |