Nitrous-oxide reductase precursor - Pseudomonas aeruginosa

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot Q01710 (NOSZ2_PSEAE)

Last modified November 25, 2008. Version 65. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

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

Hide | Top

Names and origin

Protein names

Recommended name:
    Nitrous-oxide reductase
    EC=1.7.99.6
Alternative name(s):
    N(2)OR
    N2O reductase

Gene names

Name:

nosZ

Organism

Pseudomonas aeruginosa

Taxonomic identifier

287 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Hide | Top

Protein attributes

Sequence length	634 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

Hide | Top

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.
Catalytic activity	N(2) + H(2)O + acceptor = N(2)O + reduced acceptor.
Cofactor	Binds 2 calcium ions per subunit By similarity. 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.
Subunit structure	Homodimer By similarity.
Subcellular location	Periplasm.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the nosZ family. In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family.

Hide | Top

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Calcium Copper Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from electronic annotation. Source: HAMAP
Molecular function	calcium 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...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 49

Tat-type signal Potential

Chain

50 – 634

585

Nitrous-oxide reductase

PRO_0000019829

Regions

Region

538 – 634

COX2-like

Sites

Metal binding

125

Copper Z2 By similarity

Metal binding

126

Copper Z3 By similarity

Metal binding

174

Copper Z2 By similarity

Metal binding

252

Calcium 2; via carbonyl oxygen By similarity

Metal binding

255

Calcium 2 By similarity

Metal binding

263

Calcium 2; via carbonyl oxygen By similarity

Metal binding

269

Calcium 2 By similarity

Metal binding

320

Calcium 2 By similarity

Metal binding

322

Copper Z1 By similarity

Metal binding

378

Copper Z1 By similarity

Metal binding

429

Copper Z3 By similarity

Metal binding

450

Calcium 1; via carbonyl oxygen By similarity

Metal binding

465

Calcium 1 By similarity

Metal binding

490

Copper Z4 By similarity

Metal binding

579

Copper A1 By similarity

Metal binding

614

Copper A1 By similarity

Metal binding

614

Copper A2 By similarity

Metal binding

616

Copper A2; via carbonyl oxygen By similarity

Metal binding

618

Copper A1 By similarity

Metal binding

618

Copper A2 By similarity

Metal binding

622

Copper A2 By similarity

Metal binding

625

Copper A1 By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q01710-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 646BA48B28E949EE
Show »

FASTA

634

70,695

        10         20         30         40         50         60 
MSDKQTDKDE KTGLSRRGFL GASALTRSAV AASGLVGGVM TRDSWAAAAK EAQQKIHVAP 

        70         80         90        100        110        120 
GELDEYYGFW SGGHQGEVRV LGVPSMRELM RIPVFNVDSA TGWGLTNESR HILGDTAKFL 

       130        140        150        160        170        180 
NGDCHHPHIS MTDGKYDGKY LFINDKANSR VARIRLDIMK CDKITTIPNV QAIHGLRLQK 

       190        200        210        220        230        240 
VPHTKYVFCN AEFIIPHPND GKVFDLEDEN SFTMYNAVDA ETMEVAFQVI VDGNLDNTDA 

       250        260        270        280        290        300 
DYTGRFTAAT CYNSEKAFDL GGMMRNERDW VVVFDISAVE KEIKAGRFIT LGDSKVPVVD 

       310        320        330        340        350        360 
GRKKDGKDSV VTRYIPVPKN PHGLNTSTDG KYFIANGKLS PTCSMIAIDL LPDLFAGKLK 

       370        380        390        400        410        420 
DPRDVVVGEP ELGLGPLHTT FDGRGNAYTT LFIDSQVVKW NMEEARRAYK GEKVNYIKQK 

       430        440        450        460        470        480 
LDVHYQPGHL HASLCETSEA DGKWLVALSK FSKDRFLPTG PLHPENDQLI DISGDVMKLV 

       490        500        510        520        530        540 
HDGPTFAEPH DCIMARRDQI KTRKIWDRND PFFAPTVAMA KKDGINLEED NKVIRDGNKV 

       550        560        570        580        590        600 
RVYMTSMAPA YGLTEFKVKQ GNEVTVVITN MDQIEDVSHG FVMVNHGVSM EISPQQTSSI 

       610        620        630 
TFIADKPGLH WYYCSWFCHA LHMEMVGRMM VEPA

« Hide

Hide | Top

References

[1]

"Derived amino acid sequences of the nosZ gene (respiratory N2O reductase) from Alcaligenes eutrophus, Pseudomonas aeruginosa and Pseudomonas stutzeri reveal potential copper-binding residues. Implications for the CuA site of N2O reductase and cytochrome-c oxidase."
Zumft W.G., Dreusch A., Loechelt S., Cuypers H., Friedrich B., Schneider B.
Eur. J. Biochem. 208:31-40(1992) [PubMed: 1324835] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NCIMB 8295.

Hide | Top

Cross-references

Sequence databases
	X65277 Genomic DNA. Translation: CAA46381.1.
3D structure databases
HSSP	HSSP built from PDB template 1FWX based on UniProtKB Q51705.
ModBase	Search...
Family and domain databases
HAMAP	MF_00716. [Tree]
InterPro	IPR001505. Copper_CuA. IPR002429. COX2_C. IPR008972. Cupredoxin. IPR006311. Tat. IPR015943. WD40/YVTN_repeat-like. [Graphical view]
Gene3D	G3DSA:2.60.40.420. Cupredoxin. 1 hit. G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
Pfam	PF00116. COX2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

NOSZ2_PSEAE

Accession

Primary (citable) accession number: Q01710

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	November 25, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

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

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Family and domain databases

Entry information

Relevant documents