Q9K7R6 (HDOX_BACHD) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 66.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Heme-degrading monooxygenase EC=1.14.99.3 Alternative name(s): Heme oxygenase Iron-regulated surface determinant Iron-responsive surface determinant | ||||
| Gene names |
| ||||
| Organism | Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272558 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 116 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring to the biliverdin in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron By similarity. HAMAP-Rule MF_01272 |
| Catalytic activity | Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. HAMAP-Rule MF_01272 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the antibiotic biosynthesis monooxygenase family. Heme-degrading monooxygenase IsdG subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | heme catabolic process Inferred from electronic annotation. Source: HAMAP iron assimilationInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | heme binding Inferred from electronic annotation. Source: HAMAP heme oxygenase (decyclizing) activityInferred from electronic annotation. Source: HAMAP iron ion bindingInferred from electronic annotation. Source: HAMAP monooxygenase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 116 | 116 | Heme-degrading monooxygenase HAMAP-Rule MF_01272 | PRO_0000270075 | |||||
Sites | |||||||||
| Metal binding | 6 | 1 | Iron By similarity | ||||||
| Metal binding | 76 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Site | 66 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
References
| [1] | "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000004 Genomic DNA. Translation: BAB07012.1. |
| PIR | E84061. |
| RefSeq | NP_244159.1. NC_002570.2. |
3D structure databases | |
| ProteinModelPortal | Q9K7R6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272558.BH3293. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB07012; BAB07012; BAB07012. |
| GeneID | 891123. |
| KEGG | bha:BH3293. |
| PATRIC | 18943862. VBIBacHal18977_3430. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2329. |
| HOGENOM | HOG000008026. |
| KO | K07145. |
| OMA | VTNTSKI. |
| ProtClustDB | PRK13314. |
Enzyme and pathway databases | |
| BioCyc | BHAL272558:GJC5-3392-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01272. Heme_degrading_monooxygenase. |
| InterPro | IPR007138. Antibiotic_mOase. IPR011008. Dimeric_a/b-barrel. IPR023953. Heme-degrad_mOase. [Graphical view] |
| Pfam | PF03992. ABM. 1 hit. [Graphical view] |
| SUPFAM | SSF54909. Dimer_A_B_barrel. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HDOX_BACHD | ||||||||
| Accession | Primary (citable) accession number: Q9K7R6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
