| IED ID | IndEnz0018001519 |
| Enzyme Type ID | peroxidase001519 |
| Protein Name |
Rubrerythrin-2 Rr 2 NADH peroxidase NPXase Npx EC 1.11.1.1 |
| Gene Name | rbr2 CA_C3018 |
| 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 | MSVKNAMTADFLRSAYGGESMAHMRYLIWGEEAENSNYPNIGRLFKAIAYSEHIHAKNHFNVLKEDLYDSSVVAGAVFGSTNLIDNLQGAINGELHEIKQMYPVYLETARYQEEKEAERTFHYALEAEKIHAKLFQDAQDSAKENKDINIGKVYICPVCGFTTLDENIEQCPICGVKKDKFQAF |
| Enzyme Length | 184 |
| Uniprot Accession Number | Q97ET8 |
| 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 Rbr2. {ECO:0000250}. |
| 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; |
| 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 Rbr2. {ECO:0000250}. |
| 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 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. However, PubMed:15336429 shows that rbr2 is slightly up-regulated after exposure to air, but PubMed:19648241 shows it does not respond to the presence of O(2). Is not repressed by PerR. {ECO:0000269|PubMed:15336429}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 20,869 |
| Kinetics | |
| Metal Binding | METAL 19; /note=Fe(3+) 1; /evidence=ECO:0000250|UniProtKB:P24931; METAL 52; /note=Fe(3+) 1; /evidence=ECO:0000250|UniProtKB:P24931; METAL 52; /note=Fe(3+) 2; /evidence=ECO:0000250|UniProtKB:P24931; METAL 94; /note=Fe(3+) 2; /evidence=ECO:0000250|UniProtKB:P24931; METAL 97; /note=Fe(3+) 1; /evidence=ECO:0000250|UniProtKB:P24931; METAL 128; /note=Fe(3+) 1; /evidence=ECO:0000250|UniProtKB:P24931; METAL 128; /note=Fe(3+) 2; /evidence=ECO:0000250|UniProtKB:P24931; METAL 131; /note=Fe(3+) 2; /evidence=ECO:0000250|UniProtKB:P24931; METAL 156; /note=Fe(3+) 3; /evidence=ECO:0000250|UniProtKB:P24931; METAL 159; /note=Fe(3+) 3; /evidence=ECO:0000250|UniProtKB:P24931; METAL 171; /note=Fe(3+) 3; /evidence=ECO:0000250|UniProtKB:P24931; METAL 174; /note=Fe(3+) 3; /evidence=ECO:0000250|UniProtKB:P24931 |
| Rhea ID | RHEA:18509 |
| Cross Reference Brenda |