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P19573 (NOSZ_PSEST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nitrous-oxide reductase
EC=1.7.2.4
Alternative name(s):
N(2)OR
N2O reductase
Gene names
Name:nosZ
OrganismPseudomonas stutzeri (Pseudomonas perfectomarina)
Taxonomic identifier316 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Ref.4

Catalytic activity

Nitrogen + H2O + 2 cytochrome c = nitrous oxide + 2 reduced cytochrome c. Ref.4

Cofactor

Binds 2 calcium ions per subunit. Ref.4

Binds 6 copper ions 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. Ref.4

Pathway

Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4. HAMAP MF_00716

Subunit structure

Homodimer. Ref.4

Subcellular location

Periplasm 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

The N-terminus is blocked. HAMAP MF_00716

Sequence similarities

Belongs to the nosZ family.

In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5252Tat-type signal Potential
Chain53 – 638586Nitrous-oxide reductase HAMAP MF_00716
PRO_0000019831

Regions

Region542 – 63897COX2-like HAMAP MF_00716

Sites

Metal binding1291Copper Z2 By similarity
Metal binding1301Copper Z3 By similarity
Metal binding1781Copper Z2 By similarity
Metal binding2561Calcium 2; via carbonyl oxygen By similarity
Metal binding2591Calcium 2 By similarity
Metal binding2671Calcium 2; via carbonyl oxygen By similarity
Metal binding2731Calcium 2 By similarity
Metal binding3241Calcium 2 By similarity
Metal binding3261Copper Z1 By similarity
Metal binding3821Copper Z1 By similarity
Metal binding4331Copper Z3 By similarity
Metal binding4541Calcium 1; via carbonyl oxygen By similarity
Metal binding4691Calcium 1 By similarity
Metal binding4941Copper Z4 By similarity
Metal binding5831Copper A1 By similarity
Metal binding6181Copper A1 By similarity
Metal binding6181Copper A2 By similarity
Metal binding6201Copper A2; via carbonyl oxygen By similarity
Metal binding6221Copper A1 By similarity
Metal binding6221Copper A2 By similarity
Metal binding6261Copper A2 By similarity
Metal binding6291Copper A1 By similarity

Experimental info

Sequence conflict141E → EE Ref.3

Secondary structure

1 ................................................................................................................... 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19573 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: C2CA79CCB556061B

FASTA63870,822
        10         20         30         40         50         60 
MSDKDSKNTP QVPEKLGLSR RGFLGASAVT GAAVAATALG GAVMTRESWA QAVKESKQKI 

        70         80         90        100        110        120 
HVGPGELDDY YGFWSGGHQG EVRVLGVPSM RELMRIPVFN VDSATGWGLT NESRHIMGDS 

       130        140        150        160        170        180 
AKFLNGDCHH PHISMTDGKY DGKYLFINDK ANSRVARIRL DIMKCDKMIT VPNVQAIHGL 

       190        200        210        220        230        240 
RLQKVPHTKY VFANAEFIIP HPNDGKVFDL QDENSYTMYN AIDAETMEMA FQVIVDGNLD 

       250        260        270        280        290        300 
NTDADYTGRF AAATCYNSEK AFDLGGMMRN ERDWVVVFDI HAVEAAVKAG DFITLGDSKT 

       310        320        330        340        350        360 
PVLDGRKKDG KDSKFTRYVP VPKNPHGCNT SSDGKYFIAA GKLSPTCSMI AIDKLPDLFA 

       370        380        390        400        410        420 
GKLADPRDVI VGEPELGLGP LHTTFDGRGN AYTTLFIDSQ VVKWNMEEAV RAYKGEKVNY 

       430        440        450        460        470        480 
IKQKLDVHYQ PGHLHASLCE TNEADGKWLV ALSKFSKDRF LPVGPLHPEN DQLIDISGDE 

       490        500        510        520        530        540 
MKLVHDGPTF AEPHDCIMAR RDQIKTKKIW DRNDPFFAPT VEMAKKDGIN LDTDNKVIRD 

       550        560        570        580        590        600 
GNKVRVYMTS MAPAFGVQEF TVKQGDEVTV TITNIDQIED VSHGFVVVNH GVSMEISPQQ 

       610        620        630 
TSSITFVADK PGLHWYYCSW FCHALHMEMV GRMMVEPA

« Hide

References

[1]"Molecular cloning, heterologous expression, and primary structure of the structural gene for the copper enzyme nitrous oxide reductase from denitrifying Pseudomonas stutzeri."
Viebrock A., Zumft W.G.
J. Bacteriol. 170:4658-4668(1988) [PubMed: 3049543] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 14405 / 218 / ZoBell.
[2]"Nitrous oxide reductase from denitrifying Pseudomonas stutzeri. Genes for copper-processing and properties of the deduced products, including a new member of the family of ATP/GTP-binding proteins."
Zumft W.G., Viebrock-Sambale A., Braun C.
Eur. J. Biochem. 192:591-599(1990) [PubMed: 2170125] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14405 / 218 / ZoBell.
[3]"NosR, a membrane-bound regulatory component necessary for expression of nitrous oxide reductase in denitrifying Pseudomonas stutzeri."
Cuypers H., Viebrock-Sambale A., Zumft W.G.
J. Bacteriol. 174:5332-5339(1992) [PubMed: 1644760] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
Strain: ATCC 14405 / 218 / ZoBell.
[4]"Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme."
Coyle C.L., Zumft W.G., Kroneck P.M., Korner H., Jakob W.
Eur. J. Biochem. 153:459-467(1985) [PubMed: 3000778] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR.
[5]"Pseudomonas stutzeri N2O reductase contains CuA-type sites."
Scott R.A., Zumft W.G., Coyle C.L., Dooley D.M.
Proc. Natl. Acad. Sci. U.S.A. 86:4082-4086(1989) [PubMed: 2542963] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance Raman spectroscopy: evidence for sulfur coordination in the catalytic cluster."
Alvarez M.L., Ai J., Zumft W.G., Sanders-Loehr J., Dooley D.M.
J. Am. Chem. Soc. 123:576-587(2001) [PubMed: 11456570] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X53676 Genomic DNA. Translation: CAA37714.2.
PIRA31845.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SBPX-ray2.10A/B/C/D/E/F/G/H1-638[»]
3SBQX-ray1.70A/B1-638[»]
3SBRX-ray2.24A/B/C/D/E/F/G/H1-638[»]
ProteinModelPortalP19573.
SMRP19573. Positions 61-638.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-243.

Family and domain databases

HAMAPMF_00716. NosZ.
[Tree]
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011045. N2O_reductase_N.
IPR023644. NO_Rdtase.
IPR006311. TAT_signal.
IPR019546. TAT_signal_bac_arc.
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]
SUPFAMSSF49503. Cupredoxin. 1 hit.
SSF50974. N2O_reductase_N. 1 hit.
TIGRFAMsTIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNOSZ_PSEST
AccessionPrimary (citable) accession number: P19573
Secondary accession number(s): P19846, Q6LAE4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: December 14, 2011
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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