| IED ID | IndEnz0018001323 |
| Enzyme Type ID | peroxidase001323 |
| Protein Name |
Rubrerythrin Rr |
| Gene Name | rbr DVU_3094 |
| Organism | Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Deltaproteobacteria Desulfovibrionales Desulfovibrionaceae Desulfovibrio Desulfovibrio vulgaris Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough) |
| Enzyme Sequence | MKSLKGSRTEKNILTAFAGESQARNRYNYFGGQAKKDGFVQISDIFAETADQEREHAKRLFKFLEGGDLEIVAAFPAGIIADTHANLIASAAGEHHEYTEMYPSFARIAREEGYEEIARVFASIAVAEEFHEKRFLDFARNIKEGRVFLREQATKWRCRNCGYVHEGTGAPELCPACAHPKAHFELLGINW |
| Enzyme Length | 191 |
| Uniprot Accession Number | P24931 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (4); Chain (1); Domain (2); Helix (6); Metal binding (12); Turn (2) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Electron transport;Iron;Metal-binding;Reference proteome;Transport;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (10) |
| Cross Reference PDB | 1B71; 1DVB; 1JYB; 1LKM; 1LKO; 1LKP; 1QYB; 1RYT; 1S2Z; 1S30; |
| Mapped Pubmed ID | 15023070; 15134924; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,544 |
| Kinetics | |
| Metal Binding | METAL 20; /note="Fe(3+) 1"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 53; /note="Fe(3+) 1"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 53; /note="Fe(3+) 2"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 94; /note="Fe(3+) 2"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 97; /note="Fe(3+) 1"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 128; /note="Fe(3+) 1"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 128; /note="Fe(3+) 2"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 131; /note="Fe(3+) 2"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 158; /note="Fe(3+) 3"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 161; /note="Fe(3+) 3"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 174; /note="Fe(3+) 3"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM"; METAL 177; /note="Fe(3+) 3"; /evidence="ECO:0000269|PubMed:12175244, ECO:0007744|PDB:1LKM" |
| Rhea ID | |
| Cross Reference Brenda |