Detail Information for IndEnz0018001091
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;