Reviewed,
UniProtKB/Swiss-Prot Q7WUM8 (HMP_RHIME)
Last modified
November 25, 2008.
Version 40.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
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| Encoded on | Plasmid pSymA (megaplasmid 1) | ||||||||
| Organism | Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 382 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium |
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)
| Function | Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress By similarity. |
| Catalytic activity | 2 NO + 2 O(2) + NAD(P)H = 2 NO(3)(-) + NAD(P)(+). |
| 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. |
| 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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 403 | 403 | Flavohemoprotein | PRO_0000052442 | |||||
Regions | |||||||||
| Domain | 152 – 262 | 111 | FAD-binding FR-type | ||||||
| Nucleotide binding | 206 – 209 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 275 – 280 | 6 | NADP By similarity | ||||||
| Nucleotide binding | 395 – 398 | 4 | FAD By similarity | ||||||
| Region | 1 – 138 | 138 | Globin | ||||||
| Region | 149 – 403 | 255 | Reductase | ||||||
| Region | 266 – 403 | 138 | NAD or NADP-binding | ||||||
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 | 394 | 1 | Influences the redox potential of the prosthetic heme and FAD groups By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 41 | 1 | N → D in AAP93662. Ref.1 | ||||||
| Sequence conflict | 88 | 1 | L → I in AAP93662. Ref.1 | ||||||
| Sequence conflict | 142 | 1 | E → G in AAP93662. Ref.1 | ||||||
| Sequence conflict | 250 | 1 | L → P in AAP93662. Ref.1 | ||||||
| Sequence conflict | 353 | 1 | K → N in AAP93662. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "In silico analysis of a flavohemoglobin from Sinorhizobium meliloti strain 1021." Lira-Ruan V., Sarath G., Klucas R.V., Arredondo-Peter R. Microbiol. Res. 158:215-227(2003) [PubMed: 14521231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1021. |
| [2] | "Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid." Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H. Long S.R.Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021. |
Cross-references
Sequence databases | |
|---|---|
| AY328026 Genomic DNA. Translation: AAP93662.1. AE006469 Genomic DNA. Translation: AAK65307.1. | |
| PIR | A95343. |
| RefSeq | NP_435895.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CQX based on UniProtKB P39662. |
| SMR | Q7WUM8. Positions 1-403. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1235685. |
| GenomeReviews | Gene locus RA0649 in contig AE006469_GR. |
| KEGG | sme:SMa1191. |
| NMPDR | fig|266834.1.peg.649. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q7WUM8. |
Enzyme and pathway databases | |
| BioCyc | SMEL266834:SMA1191-MON. |
Family and domain databases | |
| HAMAP | MF_01252. [Tree] |
| InterPro | IPR001709. FPN_cyt_redctse. IPR012292. Globin. IPR000971. Globin_subset. IPR000778. GP91PhoX. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. [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. PR00466. GP91PHOX. PR00410. PHEHYDRXLASE. |
| PROSITE | PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HMP_RHIME | ||||||||
| Accession | Primary (citable) accession number: Q7WUM8 Secondary accession number(s): Q92Z48 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


