| IED ID | IndEnz0007000665 |
| Enzyme Type ID | catalase000665 |
| Protein Name |
Cell surface superoxide dismutase Cu-Zn 4 EC 1.15.1.1 GPI-anchored protein 2 |
| Gene Name | SOD4 PGA2 SOD32 CAALFM_C200660CA CaO19.2062 CaO19.9609 |
| Organism | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Candida Candida albicans (Yeast) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Enzyme Sequence | MKYLSIISIVALALAGDSPISTDSKGKAPLVARFKKTSKSDIEGTIKFEPANNGTVLVSVDLTGLPSGVGPYPYHVHEKPVPESKNCTATGMHFNPFNGSTTAKTPAALELGDLSGRHGNITSESFEVEYDDSYISLNKDSKAYIGGLSIVVHSNNNTRLNCANITTLDEGDDTASAATWSNSSSSSSSSSKNSTNGSSGSSTSASQGSGAGRAEISGFLAAGIAGVVAALI |
| Enzyme Length | 232 |
| Uniprot Accession Number | Q5AD05 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 213; /note=Substrate; /evidence=ECO:0000250 |
| 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; |
| 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. Degrades host-derived reactive oxygen species to escape innate immune surveillance. Involved in the occurrence of miconazole-tolerant persisters in biofilms. Persisters are cells that survive high doses of an antimicrobial agent. {ECO:0000269|PubMed:19019164, ECO:0000269|PubMed:21746956}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (1); Chain (1); Glycosylation (9); Lipidation (1); Metal binding (6); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Antioxidant;Cell wall;Copper;GPI-anchor;Glycoprotein;Lipoprotein;Membrane;Metal-binding;Oxidoreductase;Reference proteome;Secreted;Signal;Virulence;Zinc |
| Interact With | |
| Induction | INDUCTION: Induced by farnesol and ciclopirox. Expression is higher in opaque cells compared to white cells. {ECO:0000269|PubMed:15790671, ECO:0000269|PubMed:16215173, ECO:0000269|PubMed:20735781, ECO:0000269|PubMed:22205973}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:15302828}. Membrane {ECO:0000305|PubMed:15302828}; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). {ECO:0000269|PubMed:15302828}. |
| 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. |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,726 |
| Kinetics | |
| Metal Binding | METAL 75; /note=Copper; catalytic; /evidence=ECO:0000250; METAL 77; /note=Copper; catalytic; /evidence=ECO:0000250; METAL 93; /note=Copper; catalytic; /evidence=ECO:0000250; METAL 93; /note=Zinc; structural; /evidence=ECO:0000250; METAL 113; /note=Zinc; structural; /evidence=ECO:0000250; METAL 153; /note=Copper; catalytic; /evidence=ECO:0000250 |
| Rhea ID | RHEA:20696 |
| Cross Reference Brenda |