| IED ID | IndEnz0007000707 |
| Enzyme Type ID | catalase000707 |
| Protein Name |
Cell surface Cu-only superoxide dismutase ARB_03674 EC 1.15.1.1 |
| Gene Name | ARB_03674 |
| Organism | Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Arthroderma benhamiae (Trichophyton mentagrophytes) Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
| Enzyme Sequence | MIWKQPPRRMGEMGGSLSRRFGNAAASWAVWRVSRSCFSLLFFFYFFLFFSSSSLLPTTNNYQHLQLHSLIPTLNTTAHLPHQQASSASMKASLFLACSALGLALATPTQDAPETVNNPLGIVYQAKLPETSRTGIRGTINATAHSSGRGVVFNLDLWGFDNTEGPFRKLHTCFDQTNKQTNKIVKLTTTTAYHIHVDPVPTDGSCGPTKDHLDPFGRGQTPPCDDSLPQTCEPGDLSGKFGRLTTSSMEEHFNQTFHDLYTSTRPGLGTFFGNRSIVIHHRNSTRLTCANFTLVEQPGTSTTYVPRPTGTGIISSIFPTGTGAISTSGHAPTISATYTPTPTPSPPAQNNGAGRLVGFSLGAIMAALVPLAL |
| Enzyme Length | 373 |
| Uniprot Accession Number | D4B5D4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000250|UniProtKB:Q5AD07}; |
| DNA Binding | |
| EC Number | 1.15.1.1 |
| Enzyme Function | FUNCTION: Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action (By similarity). Degrades host-derived reactive oxygen species to escape innate immune surveillance (By similarity). Involved in the occurrence of miconazole-tolerant persisters in biofilms (By similarity). Persisters are cells that survive high doses of an antimicrobial agent. The unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface (By similarity). {ECO:0000250|UniProtKB:Q5AD07}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Glycosylation (6); Lipidation (1); Metal binding (4); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Antioxidant;Cell membrane;Cell wall;Copper;Disulfide bond;GPI-anchor;Glycoprotein;Lipoprotein;Membrane;Metal-binding;Oxidoreductase;Reference proteome;Secreted;Signal;Virulence |
| Interact With | |
| Induction | INDUCTION: Expression is down-regulated in presence of human keratinocytes. {ECO:0000269|PubMed:21247460}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250|UniProtKB:Q5AD07}. Secreted {ECO:0000269|PubMed:21919205}. Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). {ECO:0000250|UniProtKB:Q5AD07}. |
| Modified Residue | |
| Post Translational Modification | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. {ECO:0000305}. |
| Signal Peptide | SIGNAL 1..55; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,234 |
| Kinetics | |
| Metal Binding | METAL 194; /note=Copper; catalytic; /evidence=ECO:0000250|UniProtKB:Q5AD07; METAL 196; /note=Copper; catalytic; /evidence=ECO:0000250|UniProtKB:Q5AD07; METAL 212; /note=Copper; catalytic; /evidence=ECO:0000250|UniProtKB:Q5AD07; METAL 280; /note=Copper; catalytic; /evidence=ECO:0000250|UniProtKB:Q5AD07 |
| Rhea ID | RHEA:20696 |
| Cross Reference Brenda |