| IED ID | IndEnz0015000113 |
| Enzyme Type ID | laccase000113 |
| Protein Name |
Copper acquisition factor BIM1 BCS-inducible membrane protein 1 Lytic polysaccharide monooxygenase-like protein BIM1 LPMO-like protein BIM1 EC 1.14.99.- |
| Gene Name | BIM CNAG_02775 |
| Organism | Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Agaricomycotina Tremellomycetes Tremellales (jelly fungi) Cryptococcaceae Cryptococcus Cryptococcus neoformans species complex Cryptococcus neoformans (Filobasidiella neoformans) Cryptococcus neoformans var. grubii (Filobasidiella neoformans var. grubii) Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) |
| Enzyme Sequence | MFALKSILVTSLITSTALAHFTLDYPQSRGFVDDTENQFCGGFNTVEARQPFPLGSGPVHIDSHHALATIVAFISTSSNPTSFDDFNTTSNGTAIPLASSIFQVPQGEKCFNIDLQSLNVGLTNGSEVTLQIQYDGGDGNLYQCSDLVLIEGYEVPSNETCTNDASKASNATSTSSGSATATSAAATSSSSGTSGAIKEVVGFGALSLALGIAGLIIL |
| Enzyme Length | 218 |
| Uniprot Accession Number | J9VHN6 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 1.14.99.- |
| Enzyme Function | FUNCTION: Cell surface-bound protein that functions in the copper-accumulation pathway shared by the CUF1-dependent copper transporter CTR1 (PubMed:31932719). Binds Cu(2+) with an estimated 1:1 stoichiometry and might serve as an extracellular copper ligand (PubMed:31932719). FRE4 and FRE7 metalloreductases probably function together with CTR1 and BIM1 to liberate the Cu(2+) bound to the BIM1 copper-binding site for subsequent import of Cu(+) into the cell by CTR1, via the reduction of BIM1-bound Cu(2+) to Cu(+) to reduce binding affinity for BIM1 but increase affinity for CTR1 (Probable). Facilitates copper acquisition in the brain of mammalian hosts and acts as a copper-dependent virulence trait in fungal meningitis (PubMed:31932719). While BIM1 plays a critical role in cryptococcal meningitis, at least in part through its role in copper acquisition, it could play additional roles during copper limitation or as a means to invade and colonize host tissues in the brain, by compromising host carbohydrate integrity via its lytic polysaccharide monooxygenase (LPMO) activity, which has still to be determined (Probable). {ECO:0000269|PubMed:31932719, ECO:0000305|PubMed:31932719}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (5); Lipidation (1); Metal binding (3); Mutagenesis (4); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Cell membrane;Copper;GPI-anchor;Glycoprotein;Lipoprotein;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Signal |
| Interact With | |
| Induction | INDUCTION: Expression is highly induced in response to copper limitation by the copper-specific chelator bathocuproine disulfonic acid (BCS) (PubMed:31932719). The BIM1 promoter harbors three conserved Cu-responsive elements (CuRE), which are critical for CUF1 binding and activation under copper-limiting conditions, beginning at positions -239, -268 and -516 (PubMed:31932719). Consistent with their presence, binding of the CUF1 copper-sensing transcription factor to the BIM1 promoter is strongly induced under copper-limiting conditions and expression of BIM1 under these conditions is CUF1-dependent (PubMed:31932719). {ECO:0000269|PubMed:31932719}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31932719}; Lipid-anchor, GPI-anchor {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 | 22,460 |
| Kinetics | |
| Metal Binding | METAL 20; /note=Copper; /evidence=ECO:0000305|PubMed:31932719; METAL 65; /note=Copper; /evidence=ECO:0000305|PubMed:31932719; METAL 138; /note=Copper; /evidence=ECO:0000305|PubMed:31932719 |
| Rhea ID | |
| Cross Reference Brenda |