Reviewed,
UniProtKB/Swiss-Prot Q9RYR5 (HMP_DEIRA)
Last modified
June 16, 2009.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Flavohemoprotein Alternative name(s): Hemoglobin-like protein Flavohemoglobin Nitric oxide dioxygenase Short name=NO oxygenase Short name=NOD EC=1.14.12.17 | ||||
| Gene names |
| ||||
| Organism | Deinococcus radiodurans [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1299 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus |
Protein attributes
| Sequence length | 403 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 NO + 2 O2 + NAD(P)H = 2 NO3- + NAD(P)+. HAMAP MF_01252 |
| Cofactor | Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 1 FAD per subunit By similarity. |
| Domain | Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H. HAMAP MF_01252 |
| Sequence similarities | Belongs to the globin family. Two-domain flavohemoproteins subfamily. In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Oxygen transport Transport |
| Ligand | FAD Flavoprotein Heme Iron Metal-binding NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transportInferred from electronic annotation. Source: HAMAP |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activityInferred from electronic annotation. Source: HAMAP oxygen bindingInferred from electronic annotation. Source: InterPro oxygen transporter activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 403 | 403 | Flavohemoprotein HAMAP MF_01252 | PRO_0000052430 | |||||
Regions | |||||||||
| Domain | 152 – 257 | 106 | FAD-binding FR-type | ||||||
| Nucleotide binding | 206 – 209 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 269 – 274 | 6 | NADP By similarity | ||||||
| Nucleotide binding | 390 – 393 | 4 | FAD By similarity | ||||||
| Region | 1 – 138 | 138 | Globin HAMAP MF_01252 | ||||||
| Region | 149 – 403 | 255 | Reductase HAMAP MF_01252 | ||||||
| Region | 261 – 403 | 143 | NAD or NADP-binding HAMAP MF_01252 | ||||||
Sites | |||||||||
| Active site | 95 | 1 | Charge relay system By similarity | ||||||
| Active site | 137 | 1 | Charge relay system By similarity | ||||||
| Metal binding | 85 | 1 | Iron (heme proximal ligand) By similarity | ||||||
| Binding site | 190 | 1 | FAD By similarity | ||||||
| Site | 29 | 1 | Involved in heme-bound ligand stabilization and O-O bond activation By similarity | ||||||
| Site | 84 | 1 | Influences the redox potential of the prosthetic heme and FAD groups By similarity | ||||||
| Site | 389 | 1 | Influences the redox potential of the prosthetic heme and FAD groups By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P.  Fraser C.M.Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1. |
Cross-references
Sequence databases | |
|---|---|
| AE001825 Genomic DNA. Translation: AAF12394.1. | |
| PIR | D75577. |
| RefSeq | NP_285566.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 4VHB based on UniProtKB P04252. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1798115. |
| GenomeReviews | Gene locus DR_A0243 in contig AE001825_GR. |
| KEGG | dra:DR_A0243. |
| NMPDR | fig|243230.1.peg.3056. |
| TIGR | DR_A0243. |
Phylogenomic databases | |
| HOGENOM | Q9RYR5. |
| OMA | Q9RYR5. KHRSLGI. |
Enzyme and pathway databases | |
| BioCyc | DRAD243230:DR_A0243-MON. |
| BRENDA | 1.14.12.17. 96172. |
Family and domain databases | |
| HAMAP | MF_01252. [Tree] |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012292. Globin. IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR000951. Ph_dOase_redase_FPNCR. [Graphical view] |
| Gene3D | G3DSA:1.10.490.10. Globin_related. 1 hit. |
| Pfam | PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00371. FPNCR. PR00409. PHDIOXRDTASE. |
| PROSITE | PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HMP_DEIRA | ||||||||
| Accession | Primary (citable) accession number: Q9RYR5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
