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Q51705 (NOSZ_PARDE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length652 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. HAMAP-Rule MF_00716

Catalytic activity

Nitrogen + H2O + 2 ferricytochrome c = nitrous oxide + 2 ferrocytochrome c + 2 H+. HAMAP-Rule MF_00716

Cofactor

Binds 2 calcium ions per subunit.

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.

Pathway

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

Subunit structure

Homodimer.

Subcellular location

Periplasm HAMAP-Rule MF_00716.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. HAMAP-Rule 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 – 5757Tat-type signal Ref.3
Chain58 – 652595Nitrous-oxide reductase HAMAP-Rule MF_00716
PRO_0000019827

Regions

Region554 – 65299COX2-like HAMAP-Rule MF_00716

Sites

Metal binding1451Copper Z2
Metal binding1461Copper Z3
Metal binding1941Copper Z2
Metal binding2711Calcium 2; via carbonyl oxygen
Metal binding2741Calcium 2
Metal binding2821Calcium 2; via carbonyl oxygen
Metal binding2881Calcium 2
Metal binding3351Calcium 2
Metal binding3371Copper Z1
Metal binding3921Copper Z1
Metal binding4431Copper Z3
Metal binding4641Calcium 1; via carbonyl oxygen
Metal binding4791Calcium 1
Metal binding5041Copper Z4
Metal binding5951Copper A1
Metal binding6301Copper A1
Metal binding6301Copper A2
Metal binding6321Copper A2; via carbonyl oxygen
Metal binding6341Copper A1
Metal binding6341Copper A2
Metal binding6381Copper A2
Metal binding6411Copper A1
Binding site1971Chloride
Binding site3391Chloride; via amide nitrogen
Binding site3401Chloride
Binding site3921Chloride

Secondary structure

1 .................................................................................................................. 652
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q51705 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 40492A4FDE7EDEA8

FASTA65271,414
        10         20         30         40         50         60 
MESKQEKGLS RRALLGATAG GAAVAGAFGG RLALGPAALG LGTAGVATVA GSGAALAASG 

        70         80         90        100        110        120 
DGSVAPGQLD DYYGFWSSGQ SGEMRILGIP SMRELMRVPV FNRCSATGWG QTNESVRIHE 

       130        140        150        160        170        180 
RTMSERTKKF LAANGKRIHD NGDLHHVHMS FTEGKYDGRF LFMNDKANTR VARVRCDVMK 

       190        200        210        220        230        240 
CDAILEIPNA KGIHGLRPQK WPRSNYVFCN GEDETPLVND GTNMEDVANY VNVFTAVDAD 

       250        260        270        280        290        300 
KWEVAWQVLV SGNLDNCDAD YEGKWAFSTS YNSEKGMTLP EMTAAEMDHI VVFNIAEIEK 

       310        320        330        340        350        360 
AIAAGDYQEL NGVKVVDGRK EASSLFTRYI PIANNPHGCN MAPDKKHLCV AGKLSPTATV 

       370        380        390        400        410        420 
LDVTRFDAVF YENADPRSAV VAEPELGLGP LHTAFDGRGN AYTSLFLDSQ VVKWNIEDAI 

       430        440        450        460        470        480 
RAYAGEKVDP IKDKLDVHYQ PGHLKTVMGE TLDATNDWLV CLSKFSKDRF LNVGPLKPEN 

       490        500        510        520        530        540 
DQLIDISGDK MVLVHDGPTF AEPHDAIAVH PSILSDIKSV WDRNDPMWAE TRAQAEADGV 

       550        560        570        580        590        600 
DIDNWTEEVI RDGNKVRVYM SSVAPSFSIE SFTVKEGDEV TVIVTNLDEI DDLTHGFTMG 

       610        620        630        640        650 
NYGVAMEIGP QMTSSVTFVA ANPGVYWYYC QWFCHALHME MRGRMLVEPK EA

« Hide

References

[1]"Sequence and expression of the gene encoding the respiratory nitrous-oxide reductase from Paracoccus denitrificans. New and conserved structural and regulatory motifs."
Hoeren F.U., Berks B.C., Ferguson S.J., McCarthy J.E.G.
Eur. J. Biochem. 218:49-57(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NL1B8944.
[2]"The NosX and NirX proteins of Paracoccus denitrificans are functional homologues: their role in maturation of nitrous oxide reductase."
Saunders N.F.W., Hornberg J.J., Reijnders W.N.M., Westerhoff H.V., de Vries S., van Spanning R.J.M.
J. Bacteriol. 182:5211-5217(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Pd 1222.
[3]"Crystal structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 A resolution."
Haltia T., Brown K., Tegoni M., Cambillau C., Saraste M., Mattila K., Djinovic-Carugo K.
Biochem. J. 369:77-88(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 60-650, PROTEIN SEQUENCE OF 58-63.
Strain: 1657.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X74792 Genomic DNA. Translation: CAA52798.1.
AJ010260 Genomic DNA. Translation: CAB53351.1.
PIRS39409.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FWXX-ray1.60A/B/C/D58-652[»]
ProteinModelPortalQ51705.
SMRQ51705. Positions 61-650.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00652; UER00709.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
2.60.40.420. 1 hit.
HAMAPMF_00716. NosZ.
InterProIPR008972. 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]
PfamPF00116. COX2. 1 hit.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 1 hit.
SSF50974. N2O_reductase_N. 1 hit.
TIGRFAMsTIGR04244. nitrous_NosZ_RR. 1 hit.
PROSITEPS00078. COX2. False negative.
PS50857. COX2_CUA. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ51705.

Entry information

Entry nameNOSZ_PARDE
AccessionPrimary (citable) accession number: Q51705
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 90 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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