| IED ID | IndEnz0018001580 |
| Enzyme Type ID | peroxidase001580 |
| Protein Name |
Rubrerythrin-1 Rr 1 NADH peroxidase NPXase Npx EC 1.11.1.1 |
| Gene Name | rbr1 rubY CA_C2575 |
| Organism | Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Eubacteriales Clostridiaceae Clostridium Clostridium acetobutylicum Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) |
| Enzyme Sequence | MKSLKGTKTAENLMKAFAGESQARNRYTFYSNTAKKEGYVQISNIFLETAENERMHAKRFFKFLSEGLDDEAVEINGASYPTTLGDTKKNLIAAAKGENEEWTDLYPSFAKTAEDEGFKGVAAAFRLIAAVEKEHEKRYNALLKNIEENKVFEKDEVKFWKCIKCGYIFEGKTAPKVCPACLHPQAYFEILSENY |
| Enzyme Length | 195 |
| Uniprot Accession Number | Q97FZ9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Rubredoxin (Rd) increases the NADH consumption rate by serving as an intermediary electron-transfer shuttle between NROR and RubY. {ECO:0000269|PubMed:19118342}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H(+) + H2O2 + NADH = 2 H2O + NAD(+); Xref=Rhea:RHEA:18509, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.11.1.1; Evidence={ECO:0000269|PubMed:19118342}; |
| DNA Binding | |
| EC Number | 1.11.1.1 |
| Enzyme Function | FUNCTION: Functions as the terminal component of an NADH peroxidase (NADH:H(2)O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) as the electron transport intermediary from NADH to RubY. {ECO:0000269|PubMed:19118342}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (2); Metal binding (12) |
| Keywords | Electron transport;Iron;Metal-binding;NAD;Oxidoreductase;Peroxidase;Reference proteome;Transport |
| Interact With | |
| Induction | INDUCTION: Various environmental stress conditions, e.g. oxidative stress (exposure to air or H(2)O(2)) and other stress factors such as salt, increased pH, high concentration of solvents or cold shock, do not lead to increased transcript levels of this gene. Is not repressed by PerR. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,158 |
| Kinetics | |
| Metal Binding | METAL 20; /note=Fe(3+) 1; /evidence=ECO:0000250|UniProtKB:P24931; METAL 53; /note=Fe(3+) 1; /evidence=ECO:0000250|UniProtKB:P24931; METAL 53; /note=Fe(3+) 2; /evidence=ECO:0000250|UniProtKB:P24931; METAL 98; /note=Fe(3+) 2; /evidence=ECO:0000250|UniProtKB:P24931; METAL 101; /note=Fe(3+) 1; /evidence=ECO:0000250|UniProtKB:P24931; METAL 132; /note=Fe(3+) 1; /evidence=ECO:0000250|UniProtKB:P24931; METAL 132; /note=Fe(3+) 2; /evidence=ECO:0000250|UniProtKB:P24931; METAL 135; /note=Fe(3+) 2; /evidence=ECO:0000250|UniProtKB:P24931; METAL 162; /note=Fe(3+) 3; /evidence=ECO:0000250|UniProtKB:P24931; METAL 165; /note=Fe(3+) 3; /evidence=ECO:0000250|UniProtKB:P24931; METAL 178; /note=Fe(3+) 3; /evidence=ECO:0000250|UniProtKB:P24931; METAL 181; /note=Fe(3+) 3; /evidence=ECO:0000250|UniProtKB:P24931 |
| Rhea ID | RHEA:18509 |
| Cross Reference Brenda |