Q7A827 (ISDI_STAAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 55.
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 isdI EC=1.14.99.3 Alternative name(s): Heme oxygenase Iron-regulated surface determinant isdI Iron-responsive surface determinant isdI | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 158879 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 108 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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. HAMAP MF_01272 |
| Catalytic activity | Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O. HAMAP MF_01272 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01272 |
| Subcellular location | Cytoplasm By similarity HAMAP 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 | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | iron assimilation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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 – 108 | 108 | Heme-degrading monooxygenase isdI HAMAP MF_01272 | PRO_0000270092 | ||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||
| Metal binding | 6 | 1 | Iron Potential | |||||||||||||||||||||||
| Metal binding | 76 | 1 | Iron (heme axial ligand) Potential | |||||||||||||||||||||||
| Site | 66 | 1 | Transition state stabilizer Potential | |||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||
| Beta strand | 2 – 10 | 9 | ||||||||||||||||||||||||
| Helix | 15 – 20 | 6 | ||||||||||||||||||||||||
| Beta strand | 36 – 42 | 7 | ||||||||||||||||||||||||
| Beta strand | 47 – 58 | 12 | ||||||||||||||||||||||||
| Helix | 60 – 67 | 8 | ||||||||||||||||||||||||
| Helix | 70 – 75 | 6 | ||||||||||||||||||||||||
| Turn | 76 – 78 | 3 | ||||||||||||||||||||||||
| Beta strand | 92 – 101 | 10 | ||||||||||||||||||||||||
| Beta strand | 105 – 107 | 3 | ||||||||||||||||||||||||
Sequences
References
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315. |
| [2] | "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BA000018 Genomic DNA. Translation: BAB41380.1. | ||||||||||||||||||||||||||||||
| PIR | A89778. | ||||||||||||||||||||||||||||||
| RefSeq | NP_373402.1. NC_002745.2. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||
| ProteinModelPortal | Q7A827. | ||||||||||||||||||||||||||||||
| SMR | Q7A827. Positions 1-108. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| STRING | Q7A827. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| EnsemblBacteria | EBSTAT00000001858; EBSTAP00000001858; EBSTAG00000001858. | ||||||||||||||||||||||||||||||
| GeneID | 1122935. | ||||||||||||||||||||||||||||||
| GenomeReviews | Gene locus SA0160 in contig BA000018_GR. | ||||||||||||||||||||||||||||||
| KEGG | sau:SA0160. | ||||||||||||||||||||||||||||||
| PATRIC | 19572351. VBIStaAur116463_0165. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| CMR | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| eggNOG | COG2329. | ||||||||||||||||||||||||||||||
| GeneTree | EBGT00050000024362. | ||||||||||||||||||||||||||||||
| HOGENOM | HBG616589. | ||||||||||||||||||||||||||||||
| OMA | WTKSSAF. | ||||||||||||||||||||||||||||||
| ProtClustDB | PRK13313. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| BioCyc | SAUR158879:SA0160-MONOMER. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| HAMAP | MF_01272. IsdG. [Tree] | ||||||||||||||||||||||||||||||
| InterPro | IPR007138. Antibiotic_mOase. IPR011008. Dimeric_a/b-barrel. IPR023953. Heme-degrad_mOase. [Graphical view] | ||||||||||||||||||||||||||||||
| KO | K07145. | ||||||||||||||||||||||||||||||
| Pfam | PF03992. ABM. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SUPFAM | SSF54909. Dimer_A_B_barrel. 1 hit. | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | ISDI_STAAN | ||||||||
| Accession | Primary (citable) accession number: Q7A827 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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