| IED ID | IndEnz0007000654 |
| Enzyme Type ID | catalase000654 |
| Protein Name |
Cell surface Cu-only superoxide dismutase 5 EC 1.15.1.1 Predicted GPI-anchored protein 3 |
| Gene Name | SOD5 PGA3 SOD31 CAALFM_C200680CA CaO19.2060 CaO19.9607 |
| 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 | MKYLSIFLLATFALAGDAPISTDSKGSPSLIAKFEKTSKSNIEGTIKFTPANNGTVSVSVDLKGLPSDIGPFPYHVHEKPVPASKNCSATENHFNPYNGTVRAATPAAHEVGDLAGKHGNIMGESYKTEYDDSYISLNEKSRSYIGGLSIVIHANNGTRLNCANITLLDEGHGNANTTMSNSSSSSSQSAVNTSSSMASTAPQGNGAERAVVNGLLAAGVVGVIAALI |
| Enzyme Length | 228 |
| Uniprot Accession Number | Q5AD07 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Secreted in a disulfide-oxidized form and apo-pools of secreted SOD5 can readily capture extracellular copper for rapid induction of enzyme activity. {ECO:0000269|PubMed:24711423}. |
| 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:0000269|PubMed:24711423}; |
| 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. 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. {ECO:0000269|PubMed:14617819, ECO:0000269|PubMed:19019164, ECO:0000269|PubMed:21746956, ECO:0000269|PubMed:24711423}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (8); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (8); Helix (4); Lipidation (1); Metal binding (4); Propeptide (1); Region (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Antioxidant;Cell wall;Copper;Disulfide bond;GPI-anchor;Glycoprotein;Lipoprotein;Membrane;Metal-binding;Oxidoreductase;Reference proteome;Secreted;Signal;Virulence |
| Interact With | |
| Induction | INDUCTION: Induced during yeast-to-hyphal transition and by osmotic and oxidative stresses. Expression is also increased when cells were grown on nonfermentable substrates as the only carbon source, in serum, and in the presence of neutrophils. Down-regulated by shikonin. Expression is controlled by EFG1, NRG1 and RIM101. {ECO:0000269|PubMed:14617819, ECO:0000269|PubMed:15813733, ECO:0000269|PubMed:15814840, ECO:0000269|PubMed:23123467, ECO:0000269|PubMed:23125349, ECO:0000269|PubMed:23136884, ECO:0000269|PubMed:23285201, ECO:0000269|PubMed:23948566}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:23136884}. Membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). {ECO:0000250}. |
| 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 (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 4N3T; 4N3U; 5CU9; 5KBK; 5KBL; 5KBM; |
| Mapped Pubmed ID | 27535222; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,589 |
| Kinetics | |
| Metal Binding | METAL 75; /note=Copper; catalytic; METAL 77; /note=Copper; catalytic; METAL 93; /note=Copper; catalytic; METAL 153; /note=Copper; catalytic |
| Rhea ID | RHEA:20696 |
| Cross Reference Brenda |