Reviewed,
UniProtKB/Swiss-Prot Q8YBC6 (NOSZ_BRUME)
Last modified
November 25, 2008.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Nitrous-oxide reductase EC=1.7.99.6 Alternative name(s): N(2)OR N2O reductase | ||||
| Gene names |
| ||||
| Organism | Brucella melitensis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 29459 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 639 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide By similarity. |
| Catalytic activity | N(2) + H(2)O + acceptor = N(2)O + reduced acceptor. |
| Cofactor | Binds 2 calcium ions per subunit By similarity. Binds 6 copper ions per subunit. Each subunit contains 2 copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site of nitrous oxide reduction By similarity. |
| Pathway | Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | PeriplasmBy similarity. |
| Post-translational modification | Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. |
| Sequence similarities | Belongs to the nosZ family. In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family. |
| Sequence caution | The sequence AAL54215.1 differs from that shown. Reason: Erroneous termination at position 253. Translated as Gln. The sequence AAL54216.1 differs from that shown. Reason: Erroneous termination at position 253. Translated as Gln. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Calcium Copper Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | membrane Inferred from electronic annotation. Source: InterPro periplasmic spaceInferred from electronic annotation. Source: HAMAP |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: HAMAP copper ion bindingInferred from electronic annotation. Source: HAMAP cytochrome-c oxidase activityInferred from electronic annotation. Source: InterPro nitrous-oxide reductase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 44 | 44 | Tat-type signal Potential | ||||||
| Chain | 45 – 639 | 595 | Nitrous-oxide reductase | PRO_0000019825 | |||||
Regions | |||||||||
| Region | 541 – 639 | 99 | COX2-like | ||||||
Sites | |||||||||
| Metal binding | 136 | 1 | Copper Z2 By similarity | ||||||
| Metal binding | 137 | 1 | Copper Z3 By similarity | ||||||
| Metal binding | 185 | 1 | Copper Z2 By similarity | ||||||
| Metal binding | 262 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 265 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 273 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 279 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 324 | 1 | Calcium 2 By similarity | ||||||
| Metal binding | 326 | 1 | Copper Z1 By similarity | ||||||
| Metal binding | 381 | 1 | Copper Z1 By similarity | ||||||
| Metal binding | 432 | 1 | Copper Z3 By similarity | ||||||
| Metal binding | 453 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 468 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 493 | 1 | Copper Z4 By similarity | ||||||
| Metal binding | 582 | 1 | Copper A1 By similarity | ||||||
| Metal binding | 617 | 1 | Copper A1 By similarity | ||||||
| Metal binding | 617 | 1 | Copper A2 By similarity | ||||||
| Metal binding | 619 | 1 | Copper A2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 621 | 1 | Copper A1 By similarity | ||||||
| Metal binding | 621 | 1 | Copper A2 By similarity | ||||||
| Metal binding | 625 | 1 | Copper A2 By similarity | ||||||
| Metal binding | 628 | 1 | Copper A1 By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. Overbeek R.Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1. |
Cross-references
Sequence databases | |
|---|---|
| AE009730 Genomic DNA. Translation: AAL54215.1. Sequence problems. AE009730 Genomic DNA. Translation: AAL54216.1. Sequence problems. | |
| PIR | AD3631. AE3631. |
| RefSeq | NP_541951.1. NP_541952.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FWX based on UniProtKB Q51705. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1198745. 1198746. |
| GenomeReviews | Gene locus nosZ in contig AE008918_GR. |
| KEGG | bme:BMEII0973. bme:BMEII0974. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8YBC6. |
Enzyme and pathway databases | |
| BioCyc | BMEL224914:BMEII0973-MON. BMEL224914:BMEII0974-MON. |
Family and domain databases | |
| HAMAP | MF_00716. [Tree] |
| InterPro | IPR001505. Copper_CuA. IPR002429. COX2_C. IPR008972. Cupredoxin. IPR006311. Tat. IPR015943. WD40/YVTN_repeat-like. [Graphical view] |
| Gene3D | G3DSA:2.60.40.420. Cupredoxin. 1 hit. G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit. |
| Pfam | PF00116. COX2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01409. TAT_signal_seq. 1 hit. |
| PROSITE | PS00078. COX2. False negative. PS50857. COX2_CUA. 1 hit. PS51318. TAT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NOSZ_BRUME | ||||||||
| Accession | Primary (citable) accession number: Q8YBC6 Secondary accession number(s): Q8YBC7 | ||||||||
| 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
| Brucella melitensis Brucella melitensis (strain 16M): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


