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P94127 (NOSZ_ACHCY) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 84. 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
OrganismAchromobacter cycloclastes
Taxonomic identifier223 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Achromobacter

Protein attributes

Sequence length642 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 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4646Tat-type signal HAMAP MF_00716
Chain47 – 642596Nitrous-oxide reductase HAMAP MF_00716
PRO_0000019822

Regions

Region544 – 64299COX2-like HAMAP MF_00716

Sites

Metal binding1351Copper Z2 By similarity
Metal binding1361Copper Z3 By similarity
Metal binding1841Copper Z2 By similarity
Metal binding2611Calcium 2; via carbonyl oxygen By similarity
Metal binding2641Calcium 2 By similarity
Metal binding2721Calcium 2; via carbonyl oxygen By similarity
Metal binding2781Calcium 2 By similarity
Metal binding3251Calcium 2 By similarity
Metal binding3271Copper 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 binding5851Copper A1 By similarity
Metal binding6201Copper A1 By similarity
Metal binding6201Copper A2 By similarity
Metal binding6221Copper A2; via carbonyl oxygen By similarity
Metal binding6241Copper A1 By similarity
Metal binding6241Copper A2 By similarity
Metal binding6281Copper A2 By similarity
Metal binding6311Copper A1 By similarity

Experimental info

Sequence conflict61H → L in CAA64426. Ref.1
Sequence conflict162 – 1632AR → GA in CAA64426. Ref.1
Sequence conflict2591T → S in CAA64426. Ref.1
Sequence conflict291 – 2944AIKA → PLRR in CAA64426. Ref.1
Sequence conflict5351W → S in CAA64426. Ref.1

Secondary structure

1 ...................................................................................................................... 642
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P94127 [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: 76C9049FF5E712AB

FASTA64270,922
        10         20         30         40         50         60 
MESKEHKGLS RRALFSATAG SAILAGTVGP AALSLGAAGL ATPARAATGA DGSVAPGKLD 

        70         80         90        100        110        120 
DYYGFWSSGQ TGEMRILGIP SMRELMRVPV FNRCSATGWG QTNESIRIHQ RTMTEKTKKQ 

       130        140        150        160        170        180 
LAANGKKIHD NGDLHHVHMS FTDGKYDGRY LFMNDKANTR VARVRCDVMK TDAILEIPNA 

       190        200        210        220        230        240 
KGIHGMRPQK WPRSNYVFCN GEDEAPLVND GSTMTDVATY VNIFTAVDAD KWEVAWQVKV 

       250        260        270        280        290        300 
SGNLDNCDAD YEGKWAFSTS YNSEMGMTLE EMTKSEMDHV VVFNIAEIEK AIKAGQYEEI 

       310        320        330        340        350        360 
NGVKVVDGRK EAKSLFTRYI PIANNPHGCN MAPDRKHLCV AGKLSPTVTV LDVTKFDALF 

       370        380        390        400        410        420 
YDNAEPRSAV VAEPELGLGP LHTAFDGRGN AYTSLFLDSQ VVKWNIDEAI RAYAGEKINP 

       430        440        450        460        470        480 
IKDKLDVQYQ PGHLKTVMGE TLDAANDWLV CLCKFSKDRF LNVGPLKPEN DQLIDISGDK 

       490        500        510        520        530        540 
MVLVHDGPTF AEPHDAIAVS PSILPNIRSV WDRKDPLWAE TRKQAEADEV DIDEWTEAVI 

       550        560        570        580        590        600 
RDGNKVRVYM TSVAPSFSQP SFTVKEGDEV TVIVTNLDEI DDLTHGFTMG NHGVAMEVGP 

       610        620        630        640 
QQTSSVTFVA ANPGVYWYYC QWFCHALHME MRGRMFVEPK GA

« Hide

References

[1]Chang W.C., Liu M.Y., Chang T., Payne W.J., Legall J., Chang W.C.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the nitrous oxide reduction genes, nosZDFYL, of Achromobacter cycloclastes."
Inatomi K.
DNA Res. 5:365-371(1998) [PubMed: 10048486] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 21921 / IAM 1013.
[3]"The nos (nitrous oxide reductase) gene cluster from the soil bacterium Achromobacter cycloclastes: cloning, sequence analysis, and expression."
McGuirl M.A., Nelson L.K., Bollinger J.A., Chan Y.-K., Dooley D.M.
J. Inorg. Biochem. 70:155-169(1998) [PubMed: 9720302] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS OF THE MATURE PROTEIN.
Strain: ATCC 21921 / IAM 1013.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X94977 Genomic DNA. Translation: CAA64426.1.
Y15161 Genomic DNA. Translation: CAA75425.1.
AF047429 Genomic DNA. Translation: AAD09157.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IWFX-ray1.86A/B1-642[»]
2IWKX-ray1.70A/B1-642[»]
ProteinModelPortalP94127.
SMRP94127. Positions 50-639.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00716. NosZ.
[Tree]
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]
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.
PROSITEPS00078. COX2. False negative.
PS50857. COX2_CUA. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNOSZ_ACHCY
AccessionPrimary (citable) accession number: P94127
Secondary accession number(s): O68477
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2003
Last modified: September 21, 2011
This is version 84 of the entry and version 2 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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