Q8FX16 (NOSZ_BRUSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 65.
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: Nitrous-oxide reductase EC=1.7.2.4 Alternative name(s): N(2)OR N2O reductase | ||||
| Gene names |
| ||||
| Organism | Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 204722 [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. HAMAP MF_00716 |
| Catalytic activity | Nitrogen + H2O + 2 cytochrome c = nitrous oxide + 2 reduced cytochrome c. HAMAP MF_00716 |
| Cofactor | Binds 2 calcium ions per subunit By similarity. HAMAP MF_00716 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. HAMAP MF_00716 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00716 |
| Subcellular location | Periplasm By similarity HAMAP MF_00716. |
| Post-translational modification | Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. HAMAP MF_00716 |
| Sequence similarities | Belongs to the nosZ family. In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Calcium Copper Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular component | membrane Inferred from electronic annotation. Source: InterPro periplasmic spaceInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: InterPro copper ion bindingInferred from electronic annotation. Source: InterPro cytochrome-c oxidase activityInferred from electronic annotation. Source: InterPro nitrous-oxide reductase activityInferred from electronic annotation. Source: InterPro |
| 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 HAMAP MF_00716 | PRO_0000019826 | |||||
Regions | |||||||||
| Region | 541 – 639 | 99 | COX2-like HAMAP MF_00716 | ||||||
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 Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
| [2] | "Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014292 Genomic DNA. Translation: AAN33476.1. CP002998 Genomic DNA. Translation: AEM19754.1. |
| RefSeq | NP_699471.1. NC_004311.2. |
3D structure databases | |
| ProteinModelPortal | Q8FX16. |
| SMR | Q8FX16. Positions 56-637. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1164712. |
| GenomeReviews | Gene locus BRA0275 in contig AE014292_GR. |
| KEGG | bms:BRA0275. |
| PATRIC | 17793347. VBIBruSui107850_2492. |
| TIGR | BRA0275. |
Phylogenomic databases | |
| HOGENOM | HBG308574. |
| OMA | KLVHDGP. |
| PhylomeDB | Q8FX16. |
| ProtClustDB | PRK02888. |
Enzyme and pathway databases | |
| BioCyc | BSUI204722:BR_A0275-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00716. NosZ. [Tree] |
| InterPro | IPR008972. Cupredoxin. IPR002429. Cyt_c_oxidase_su2_C. IPR011045. N2O_reductase_N. IPR023644. NO_Rdtase. IPR006311. TAT_signal. IPR015943. WD40/YVTN_repeat-like_dom. [Graphical view] |
| Gene3D | G3DSA:2.60.40.420. Cupredoxin. 1 hit. G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit. |
| KO | K00376. |
| Pfam | PF00116. COX2. 1 hit. [Graphical view] |
| SUPFAM | SSF49503. Cupredoxin. 1 hit. SSF50974. N2O_reductase_N. 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_BRUSU | ||||||||
| Accession | Primary (citable) accession number: Q8FX16 Secondary accession number(s): G0KFB0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella suis Brucella suis (strain 1330): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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