Detail Information for IndEnz0018001218
IED ID IndEnz0018001218
Enzyme Type ID peroxidase001218
Protein Name Cytochrome c-552
Gene Name nirB
Organism Pseudomonas stutzeri (Pseudomonas perfectomarina)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas stutzeri group Pseudomonas stutzeri subgroup Pseudomonas stutzeri (Pseudomonas perfectomarina)
Enzyme Sequence MKKTLMASAVGAVIAFGTHGAMAAAPADWSSVAATDVTLFYPGVSPVEWITKGTEHGGARALKKGETCAGCHSEEASDMGEKMASGKKLEPSPIAGKAPFINAKVQAANDGENLYLRFTWKQPAASGAAPMDADNPVKIAYMLEGGSKVELAEAGGCWGSCHGDARTMPGAADTKTKYVKDGSLANGVYYDLNQWRSGENKAFDGYVATERVMEGGQALVDAQGKLDGDTWTVVFTRKFAGGEGDVTLAPGNLYNFGFAIHDDSATGRYHHVSLGYSLGIDAQGDITAAKQ
Enzyme Length 291
Uniprot Accession Number P24037
Absorption
Active Site
Activity Regulation
Binding Site BINDING 68; /note=heme c 1; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 71; /note=heme c 1; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 157; /note=heme c 2; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; BINDING 161; /note=heme c 2; covalent; /evidence=ECO:0000255|PROSITE-ProRule:PRU00433
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: May play a role in nitrite reduction. Shows peroxidase activity on proteolytic modification.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Binding site (4); Chain (1); Metal binding (2); Sequence conflict (3); Signal peptide (1)
Keywords Direct protein sequencing;Electron transport;Heme;Iron;Metal-binding;Periplasm;Repeat;Signal;Transport
Interact With
Induction INDUCTION: By anaerobic conditions.
Subcellular Location SUBCELLULAR LOCATION: Periplasm.
Modified Residue
Post Translational Modification PTM: Binds 2 heme c groups per subunit.
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000269|PubMed:2539041
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 30,426
Kinetics
Metal Binding METAL 72; /note=Iron (heme c 1 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433; METAL 162; /note=Iron (heme c 2 axial ligand); /evidence=ECO:0000255|PROSITE-ProRule:PRU00433
Rhea ID
Cross Reference Brenda