Reviewed,
UniProtKB/Swiss-Prot Q7WUM8 (HMP_RHIME)
Last modified
January 19, 2010.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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 |
| ||||||||
| 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. |
| 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 O2 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. HAMAP MF_01252 |
| 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. HAMAP MF_01252 Binds 1 FAD per subunit By similarity. HAMAP MF_01252 |
| 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 | Detoxification Oxygen transport Transport |
| Ligand | FAD Flavoprotein Heme Iron Metal-binding NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Plasmid |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transportInferred from electronic annotation. Source: HAMAP response to toxinInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | heme binding Inferred 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_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 HAMAP MF_01252 | ||||||
| Region | 149 – 403 | 255 | Reductase HAMAP MF_01252 | ||||||
| Region | 266 – 403 | 138 | 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 | 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 | |
|---|---|
| EMBL GenBank DDBJ | AY328026 Genomic DNA. Translation: AAP93662.1. AE006469 Genomic DNA. Translation: AAK65307.1. |
| PIR | A95343. |
| RefSeq | NP_435895.1. |
3D structure databases | |
| 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 | HBG623097. |
| OMA | YSISCAP. |
Enzyme and pathway databases | |
| BioCyc | SMEL266834:SMA1191-MONOMER. |
| BRENDA | 1.14.12.17. 142. |
Family and domain databases | |
| HAMAP | MF_01252. Hmp. [Tree] |
| InterPro | IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012292. Globin. IPR009050. Globin-like. IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. IPR017938. Riboflavin_synthase-like_b-brl. [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. 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) | ||||||||

Clusters with


