IED ID | IndEnz0018001649 |
Enzyme Type ID | peroxidase001649 |
Protein Name |
Rubredoxin Rd EC 1.-.-.- |
Gene Name | rd CA_C2778 |
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 | MKKYVCVVCGYIYDPAEGDPDNGVNPGTSFEDIPDDWVCPLCGVGKDQFEPSEE |
Enzyme Length | 54 |
Uniprot Accession Number | Q9AL94 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 1.-.-.- |
Enzyme Function | FUNCTION: Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Functions as an intermediate component in the electron transfer chain: NADH->NROR->Rd->FprA1/2 in which Rd serves as the proximal electron donor to the FDPs that exhibit H(2)O-forming NADH oxidase activity. Also functions as the proximal electron donor to the Dfx and revRbr proteins that display superoxide reductase (SOR) and NADH peroxidase activity, respectively. Therefore, is a key electron carrier in an efficient multienzyme complex that can scavenge O(2) and reactive oxygen species (ROS), and thus plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. {ECO:0000269|PubMed:18005665, ECO:0000269|PubMed:19084524, ECO:0000269|PubMed:19118342, ECO:0000269|PubMed:19124587}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Domain (1); Metal binding (4) |
Keywords | Detoxification;Direct protein sequencing;Electron transport;Iron;Metal-binding;Oxidoreductase;Reference proteome;Stress response;Transport |
Interact With | |
Induction | INDUCTION: Up-regulated upon exposure to O(2). Repressed by PerR. {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 | 5,930 |
Kinetics | |
Metal Binding | METAL 6; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00241; METAL 9; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00241; METAL 39; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00241; METAL 42; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00241 |
Rhea ID | |
Cross Reference Brenda |