| IED ID | IndEnz0018001529 |
| Enzyme Type ID | peroxidase001529 |
| Protein Name |
Reverse rubrerythrin-2 revRbr 2 NADH peroxidase NPXase Npx EC 1.11.1.1 Rubperoxin 2 Rpr 2 |
| Gene Name | rbr3B hsp21 rpr2 CA_C3597 |
| 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 | MKKFKCVVCGYIYTGEDAPEKCPVCGAGKDKFVEVKDEGEGWADEHKIGIAKGVDKEVLEGLRANFTGECTEVGMYLAMARQADREGYPEVAEAYKRIAFEEAEHASKFAELLGEVVVADTKTNLQMRVDAEKGACEGKKELATLAKKLNYDAIHDTVHEMCKDEARHGSAFRGLLNRYFK |
| Enzyme Length | 181 |
| Uniprot Accession Number | Q97D83 |
| 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 revRbr. {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 revRbr 2. Plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. Also exhibits NADH oxidase (NADH:O(2) oxidoreductase) activity in vitro, which is 100-fold lesser than that of FprA1/2 using the same electron transfer components. Therefore, its predominant function is most likely as a scavenger of its preferred substrate, H(2)O(2). {ECO:0000269|PubMed:19118342}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (2); Metal binding (11) |
| Keywords | Detoxification;Direct protein sequencing;Electron transport;Iron;Metal-binding;NAD;Oxidoreductase;Peroxidase;Reference proteome;Stress response;Transport |
| Interact With | |
| Induction | INDUCTION: Up-regulated by heat and oxidative stress (exposure to air, O(2) and H(2)O(2)) (at mRNA and protein levels). Various other environmental stress conditions such as an increase of the pH of the growth medium from 4.5 to 6.2, addition of the salt NaCl or of the solvent butanol, and lowering the incubation temperature also result in transiently increased transcript levels. Is also expressed under non-stressful conditions. Repressed by PerR. {ECO:0000269|PubMed:15280011, ECO:0000269|PubMed:15336429, ECO:0000269|PubMed:16463182, ECO:0000269|PubMed:18430081, ECO:0000269|PubMed:19648241}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 20,107 |
| Kinetics | |
| Metal Binding | METAL 6; /note=Iron 1; /evidence=ECO:0000250; METAL 9; /note=Iron 1; /evidence=ECO:0000250; METAL 22; /note=Iron 1; /evidence=ECO:0000250; METAL 25; /note=Iron 1; /evidence=ECO:0000250; METAL 69; /note=Iron 2; /evidence=ECO:0000250; METAL 102; /note=Iron 2; /evidence=ECO:0000250; METAL 102; /note=Iron 3; /evidence=ECO:0000250; METAL 132; /note=Iron 3; /evidence=ECO:0000250; METAL 165; /note=Iron 2; /evidence=ECO:0000250; METAL 165; /note=Iron 3; /evidence=ECO:0000250; METAL 168; /note=Iron 3; /evidence=ECO:0000250 |
| Rhea ID | RHEA:18509 |
| Cross Reference Brenda | 1.11.1.1; |