| IED ID | IndEnz0018001608 |
| Enzyme Type ID | peroxidase001608 |
| Protein Name |
Group 2 truncated hemoglobin GlbO Hemoglobin-like protein HbO Truncated hemoglobin trHbO |
| Gene Name | glbO Rv2470 MTV008.26 |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Enzyme Sequence | MPKSFYDAVGGAKTFDAIVSRFYAQVAEDEVLRRVYPEDDLAGAEERLRMFLEQYWGGPRTYSEQRGHPRLRMRHAPFRISLIERDAWLRCMHTAVASIDSETLDDEHRRELLDYLEMAAHSLVNSPF |
| Enzyme Length | 128 |
| Uniprot Accession Number | P9WN23 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: When expressed in E.coli and M.smegmatis, HbO increases oxygen uptake. Membrane vesicles of E.coli carrying HbO show a respiration activity about twice that of membranes without HbO. HbO seems to interact with a terminal oxidase. Therefore, HbO could participate in oxygen/electron-transfer process, suggesting a function related to the facilitation of oxygen transfer during aerobic metabolism of M.tuberculosis. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Cross-link (1); Helix (8); Metal binding (1); Modified residue (1); Turn (2) |
| Keywords | 3D-structure;Cell membrane;Heme;Hydroxylation;Iron;Membrane;Metal-binding;Oxygen transport;Reference proteome;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. |
| Modified Residue | MOD_RES 36; /note="3',4'-dihydroxyphenylalanine; alternate"; /evidence="ECO:0000269|PubMed:12719529" |
| Post Translational Modification | PTM: Contains L-DOPA (3',4'-dihydroxyphenylalanine). |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1NGK; 2QRW; |
| Mapped Pubmed ID | 17887774; |
| Motif | |
| Gene Encoded By | |
| Mass | 14,950 |
| Kinetics | |
| Metal Binding | METAL 75; /note=Iron (heme proximal ligand) |
| Rhea ID | |
| Cross Reference Brenda |