Reviewed,
UniProtKB/Swiss-Prot Q2YX89 (ISDG_STAAB)
Last modified
June 16, 2009.
Version 26.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Heme-degrading monooxygenase isdG EC=1.14.99.3 Alternative name(s): Iron-regulated surface determinant isdG Iron-responsive surface determinant isdG Heme oxygenase | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain bovine RF122 / ET3-1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 273036 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 107 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron By similarity. |
| Catalytic activity | Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. HAMAP 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 | antibiotic biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| 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: EC 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 isdG HAMAP MF_01272 | PRO_0000270080 | |||||
Sites | |||||||||
| Metal binding | 7 | 1 | Iron Potential | ||||||
| Metal binding | 77 | 1 | Iron (heme axial ligand) Potential | ||||||
| Site | 67 | 1 | Transition state stabilizer Potential | ||||||
Sequences
References
| [1] | "Molecular correlates of host specialization in Staphylococcus aureus." Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V. PLoS ONE 2:E1120-E1120(2007) [PubMed: 17971880] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AJ938182 Genomic DNA. Translation: CAI80688.1. | |
| RefSeq | YP_416484.1. |
3D structure databases | |
| SMR | Q2YX89. Positions 1-107. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3792879. |
| GenomeReviews | Gene locus SAB1000 in contig AJ938182_GR. |
| KEGG | sab:SAB1000. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q2YX89. |
| OMA | Q2YX89. RDEGTSE. |
Enzyme and pathway databases | |
| BioCyc | SAUR273036:SAB1000-MON. |
Family and domain databases | |
| HAMAP | MF_01272. [Tree] |
| InterPro | IPR007138. Antibiotic_mOase. [Graphical view] |
| Pfam | PF03992. ABM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ISDG_STAAB | ||||||||
| Accession | Primary (citable) accession number: Q2YX89 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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