Q4L849 (HDOX_STAHJ) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 56.
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.- Alternative name(s): Heme oxygenase Iron-regulated surface determinant Iron-responsive surface determinant | ||||
| Gene names |
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| Organism | Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279808 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 104 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 oxo-bilirubin chromophore staphylobilin (a mixture of the linear tetrapyrroles 5-oxo-delta-bilirubin and 15-oxo-beta-bilirubin) 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 = staphylobilins + 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 – 104 | 104 | Heme-degrading monooxygenase HAMAP-Rule MF_01272 | PRO_0000270099 | |||||
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] | "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCSC1435. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP006716 Genomic DNA. Translation: BAE04176.1. |
| RefSeq | YP_252782.1. NC_007168.1. |
3D structure databases | |
| ProteinModelPortal | Q4L849. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 279808.SH0867. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAE04176; BAE04176; SH0867. |
| GeneID | 3483823. |
| KEGG | sha:SH0867. |
| PATRIC | 19617754. VBIStaHae67511_0853. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2329. |
| HOGENOM | HOG000008026. |
| KO | K07145. |
| OMA | GFAEKMA. |
| ProtClustDB | PRK13315. |
Enzyme and pathway databases | |
| BioCyc | SHAE279808:GJX7-869-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_STAHJ | ||||||||
| Accession | Primary (citable) accession number: Q4L849 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
