IED ID | IndEnz0018001091 |
Enzyme Type ID | peroxidase001091 |
Protein Name |
Catalase-1 EC 1.11.1.6 |
Gene Name | cat-1 NCU08791 |
Organism | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora Neurospora crassa Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
Enzyme Sequence | MSNIISQAGQKAKEALTSAPSSKKVDDLKNEFKETDKSARLTTDYGVKQTTADDWLRIVSDDKIGPSLLEDPFARERIMRFDHERIPERVVHARGSGAFGKFKVYESASDLTMAPVLTDTSRETPVFVRFSTVLGSRGSADTVRDVRGFAVKFYTEEGNWDLVGNNIPVFFIQDAIKFPDVIHAGKPEPHNEVPQAQSAHNNFWDFQFNHTEATHMFTWAMSDRAIPRSLRMMQGFGVNTYTLINAQGKRHFVKFHWTPELGVHSLVWDEALKLAGQDPDFHRKDLWEAIENGAYPKWKFGIQAIAEEDEHKFDFDILDATKIWPEDLVPVRYIGEMELNRNPDEFFPQTEQIAFCTSHVVNGIGFSDDPLLQGRNFSYFDTQISRLGVNFQELPINRPVCPVMNFNRDGAMRHTISRGTVNYYPNRFDACPPASLKEGGYLEYAQKVAGIKARARSAKFKEHFSQAQLFYNSMSPIEKQHMINAFGFELDHCEDPVVYGRMVQRLADIDLGLAQTIAEMVGGEAPTTTNHPNHGRKTINLSQTEFPPATPTIKSRRVAIIIADGYDNVAYDAAYAAISANQAIPLVIGPRRSKVTAANGSTVQPHHHLEGFRSTMVDAIFIPGGAKAAETLSKNGRALHWIREAFGHLKAIGATGEAVDLVAKAIALPQVTVSSEAEVHESYGVVTLKKVKPESFTDAVKIAKGAAGFLGEFFYAIAQHRNWDRELDGLHSMIAY |
Enzyme Length | 736 |
Uniprot Accession Number | Q9C168 |
Absorption | |
Active Site | ACT_SITE 92; /evidence="ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:15342250"; ACT_SITE 165; /evidence="ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:15342250" |
Activity Regulation | |
Binding Site | BINDING 89; /note=Heme; /evidence=ECO:0000269|PubMed:15342250; BINDING 129; /note=Heme; /evidence=ECO:0000269|PubMed:15342250; BINDING 178; /note=Heme; /evidence=ECO:0000269|PubMed:15342250; BINDING 375; /note=Heme; /evidence=ECO:0000269|PubMed:15342250; BINDING 386; /note=Heme; /evidence=ECO:0000269|PubMed:15342250 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:11728803, ECO:0000269|PubMed:12160934}; |
DNA Binding | |
EC Number | 1.11.1.6 |
Enzyme Function | FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active from pH 4 to 12. {ECO:0000269|PubMed:11728803}; |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (26); Binding site (5); Chain (1); Compositional bias (1); Cross-link (1); Erroneous initiation (1); Helix (30); Metal binding (1); Region (1); Turn (9) |
Keywords | 3D-structure;Cell wall;Direct protein sequencing;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Oxidoreductase;Peroxidase;Reference proteome;Secreted;Thioether bond |
Interact With | |
Induction | INDUCTION: During prestationary growth. By ethanol and in the presence of air by heat shock. Inactivated by isopropanol and 20 mM 3-amino-1,2,4-triazole. {ECO:0000269|PubMed:11728803, ECO:0000269|PubMed:12160934}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:11728803}. Note=Principally associated with the cell wall of conidia. |
Modified Residue | |
Post Translational Modification | PTM: Glycosylated; with alpha-glucose and/or alpha-mannose. {ECO:0000269|PubMed:11728803}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1SY7; |
Mapped Pubmed ID | 16697373; |
Motif | |
Gene Encoded By | |
Mass | 82,268 |
Kinetics | |
Metal Binding | METAL 379; /note=Iron (heme axial ligand); /evidence=ECO:0000269|PubMed:15342250 |
Rhea ID | RHEA:20309 |
Cross Reference Brenda | 1.11.1.6; |