Q2FHU5 (HDOX1_STAA3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 52.
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 1 EC=1.14.99.- Alternative name(s): Heme oxygenase 1 Iron-regulated surface determinant 1 Iron-responsive surface determinant 1 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain USA300) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 367830 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 107 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. HAMAP-Rule MF_01272 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_01272. |
| 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 – 107 | 107 | Heme-degrading monooxygenase 1 HAMAP-Rule MF_01272 | PRO_0000270095 | |||||
Regions | |||||||||
| Region | 22 – 29 | 8 | Heme binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 7 | 1 | Iron By similarity | ||||||
| Metal binding | 77 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Site | 67 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
References
| [1] | "Complete genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus." Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., Perdreau-Remington F. Lancet 367:731-739(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USA300. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000255 Genomic DNA. Translation: ABD22802.1. |
| RefSeq | YP_493733.1. NC_007793.1. |
3D structure databases | |
| ProteinModelPortal | Q2FHU5. |
| SMR | Q2FHU5. Positions 1-107. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 451515.SAUSA300_1035. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABD22802; ABD22802; SAUSA300_1035. |
| GeneID | 3913448. |
| KEGG | saa:SAUSA300_1035. |
| PATRIC | 19591409. VBIStaAur129981_1133. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG2329. |
| HOGENOM | HOG000008026. |
| KO | K00510. |
| OMA | GEGERIM. |
| ProtClustDB | PRK13312. |
Enzyme and pathway databases | |
| BioCyc | SAUR451515:GH3C-1035-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 | HDOX1_STAA3 | ||||||||
| Accession | Primary (citable) accession number: Q2FHU5 | ||||||||
| 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
