Detail Information for IndEnz0018000472
IED ID IndEnz0018000472
Enzyme Type ID peroxidase000472
Protein Name Hydroxylamine reductase
EC 1.7.99.1
Hybrid-cluster protein
HCP
Prismane protein
Gene Name hcp ybjW b0873 JW0857
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MFCVQCEQTIRTPAGNGCSYAQGMCGKTAETSDLQDLLIAALQGLSAWAVKAREYGIINHDVDSFAPRAFFSTLTNVNFDSPRIVGYAREAIALREALKAQCLAVDANARVDNPMADLQLVSDDLGELQRQAAEFTPNKDKAAIGENILGLRLLCLYGLKGAAAYMEHAHVLGQYDNDIYAQYHKIMAWLGTWPADMNALLECSMEIGQMNFKVMSILDAGETGKYGHPTPTQVNVKATAGKCILISGHDLKDLYNLLEQTEGTGVNVYTHGEMLPAHGYPELRKFKHLVGNYGSGWQNQQVEFARFPGPIVMTSNCIIDPTVGAYDDRIWTRSIVGWPGVRHLDGDDFSAVITQAQQMAGFPYSEIPHLITVGFGRQTLLGAADTLIDLVSREKLRHIFLLGGCDGARGERHYFTDFATSVPDDCLILTLACGKYRFNKLEFGDIEGLPRLVDAGQCNDAYSAIILAVTLAEKLGCGVNDLPLSLVLSWFEQKAIVILLTLLSLGVKNIVTGPTAPGFLTPDLLAVLNEKFGLRSITTVEEDMKQLLSA
Enzyme Length 550
Uniprot Accession Number P75825
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Inhibited by oxygen. Activated by cyanide except in the prolonged presence of excess cyanide, where the enzyme is inactivated. {ECO:0000269|PubMed:12374823}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine; Xref=Rhea:RHEA:22052, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15429, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938; EC=1.7.99.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000269|PubMed:12374823};
DNA Binding
EC Number 1.7.99.1
Enzyme Function FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. {ECO:0000255|HAMAP-Rule:MF_00069, ECO:0000269|PubMed:10651802, ECO:0000269|PubMed:12374823}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:12374823};
Pathway
nucleotide Binding
Features Chain (1); Metal binding (12); Modified residue (1); Sequence conflict (1)
Keywords 2Fe-2S;3D-structure;Cytoplasm;Iron;Iron-sulfur;Metal-binding;Oxidoreductase;Reference proteome
Interact With
Induction INDUCTION: By Fnr, NarL and NarP under anaerobic conditions in the presence of either nitrate or nitrite. {ECO:0000269|PubMed:15667305}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069}.
Modified Residue MOD_RES 405; /note=Cysteine persulfide; /evidence=ECO:0000255|HAMAP-Rule:MF_00069
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 7DE4;
Mapped Pubmed ID 15690043; 16606699; 24561554; 34101368;
Motif
Gene Encoded By
Mass 60,064
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 mM for hydroxylamine (at pH 9) {ECO:0000269|PubMed:12374823}; Vmax=92 umol/min/mg enzyme (at pH 7.5) {ECO:0000269|PubMed:12374823}; Vmax=458 umol/min/mg enzyme (at pH 9) {ECO:0000269|PubMed:12374823};
Metal Binding METAL 3; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 6; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 18; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 25; /note=Iron-sulfur (2Fe-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 249; /note=Iron-oxo-sulfur (4Fe-2O-2S); via tele nitrogen; /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 273; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 317; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 405; /note=Iron-oxo-sulfur (4Fe-2O-2S); via persulfide group; /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 433; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 458; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 492; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069; METAL 494; /note=Iron-oxo-sulfur (4Fe-2O-2S); /evidence=ECO:0000255|HAMAP-Rule:MF_00069
Rhea ID RHEA:22052
Cross Reference Brenda