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Reviewed, UniProtKB/Swiss-Prot Q8FX16 (NOSZ_BRUSU)

Last modified February 9, 2010. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Nitrous-oxide reductase
    EC=1.7.99.6
Alternative name(s):
    N(2)OR
    N2O reductase
Gene names
Name: nosZ
Ordered Locus Names: BRA0275
OrganismBrucella suis [Complete proteome] [HAMAP]
Taxonomic identifier29461 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

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Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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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

N2 + H2O + acceptor = N2O + reduced acceptor. 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. HAMAP MF_00716

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.

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Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandCalcium
Copper
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmembrane

Inferred from electronic annotation. Source: InterPro

periplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: HAMAP

copper ion binding

Inferred from electronic annotation. Source: HAMAP

cytochrome-c oxidase activity

Inferred from electronic annotation. Source: InterPro

nitrous-oxide reductase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4444Tat-type signal Potential
Chain45 – 639595Nitrous-oxide reductase HAMAP MF_00716
PRO_0000019826

Regions

Region541 – 63999COX2-like HAMAP MF_00716

Sites

Metal binding1361Copper Z2 By similarity
Metal binding1371Copper Z3 By similarity
Metal binding1851Copper Z2 By similarity
Metal binding2621Calcium 2; via carbonyl oxygen By similarity
Metal binding2651Calcium 2 By similarity
Metal binding2731Calcium 2; via carbonyl oxygen By similarity
Metal binding2791Calcium 2 By similarity
Metal binding3241Calcium 2 By similarity
Metal binding3261Copper Z1 By similarity
Metal binding3811Copper Z1 By similarity
Metal binding4321Copper Z3 By similarity
Metal binding4531Calcium 1; via carbonyl oxygen By similarity
Metal binding4681Calcium 1 By similarity
Metal binding4931Copper Z4 By similarity
Metal binding5821Copper A1 By similarity
Metal binding6171Copper A1 By similarity
Metal binding6171Copper A2 By similarity
Metal binding6191Copper A2; via carbonyl oxygen By similarity
Metal binding6211Copper A1 By similarity
Metal binding6211Copper A2 By similarity
Metal binding6251Copper A2 By similarity
Metal binding6281Copper A1 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8FX16-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: DFB2E8DBB372B057

FASTA63971,071
        10         20         30         40         50         60 
MTEETRKSQL SRRQLLGTSA FVAAAGASGL GGALLAGSSE TALAAGAAKG GMSPEVKPGE 

        70         80         90        100        110        120 
LDEYYVFFSS GQCGEVRIVG LPSMRELMRI PVFNRDSATG WGLTNESRKV LTEGLLPQDR 

       130        140        150        160        170        180 
EFLKDRGDIF LNGDLHHPHP SFTDGTYDGR YLYANDKANT RVCRIRLDVM KCDKIIQLPN 

       190        200        210        220        230        240 
QHTVHGLRVQ KYPKTGYVFC NGEDRVPIPN DGSHLNDVKQ YHAIFTAVDG ETMKVAWQVM 

       250        260        270        280        290        300 
VDGNLDNVDC DYQGKYAFST CYNSEEGTTL AEMMSSEQDW IVVFNLKRIE EAVANGDFKE 

       310        320        330        340        350        360 
MNGVPVIDGR HGSKYTRYIP VPNSPHGINT APDGIHVVAN GKLSPTVTVF DVRKFDDLFD 

       370        380        390        400        410        420 
DKIKPRDAVV AEPELGLGPL HTAYDDKGNA YTTLFIDSQI CKWNIEDAKR AFKGEKVDPI 

       430        440        450        460        470        480 
RQKLDVHYQP GHNHSSMGQT KEVDGKWLIS LNKFSKDRYL NVGPLKPEND QLIDISGDKM 

       490        500        510        520        530        540 
VIVHDGPSFA EPHDATIVHR SKINPVSFWS REDPFFADAV AQAKADGLDL MEANEVVRDG 

       550        560        570        580        590        600 
NKVRVYMTSS APAFGLTEFT VQQDDEVTVY VTNIDEIEDL THGFAIVNYG VNMEVAPQAT 

       610        620        630 
ASVTFKASKP GVWWYYCSWF CHAMHMEMQG RMLVEPKKA

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014292 Genomic DNA. Translation: AAN33476.1.
RefSeqNP_699471.1.

3D structure databases

SMRQ8FX16. Positions 56-637.
ModBaseSearch...

Genome annotation databases

GeneID1164712.
GenomeReviewsGene locus BRA0275 in contig AE014292_GR.
KEGGbms:BRA0275.
TIGRBRA0275.

Phylogenomic databases

HOGENOMHBG308574.
OMASKDRFLP.

Enzyme and pathway databases

BioCycBSUI204722:BR_A0275-MONOMER.
BRENDA1.7.99.6. 281610.

Family and domain databases

HAMAPMF_00716. NosZ.
[Tree]
InterProIPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011045. N2O_reductase_N.
IPR006311. TAT_signal.
IPR017909. Twin_arg_translocation_Tat.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 1 hit.
G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PfamPF00116. COX2. 1 hit.
[Graphical view]
TIGRFAMsTIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS00078. COX2. False negative.
PS50857. COX2_CUA. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameNOSZ_BRUSU
AccessionPrimary (citable) accession number: Q8FX16
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: March 1, 2003
Last modified: February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents