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UniProtKB/Swiss-Prot entry Q01710


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NOSZ2_PSEAE
Primary accession number Q01710
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 63)
Name and origin of the protein
Protein name Nitrous-oxide reductase [Precursor]
Synonyms EC 1.7.99.6
N(2)OR
N2O reductase
Gene name
Name: nosZ
From
Pseudomonas aeruginosa [TaxID: 287] 
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NCIMB 8295;
PubMed=1324835 [NCBI, ExPASy, EBI, Israel, Japan]
Zumft W.G., Dreusch A., Loechelt S., Cuypers H., Friedrich B., Schneider B.;
"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.";
Eur. J. Biochem. 208:31-40(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X65277; CAA46381.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP Q51705; 1FWX. [HSSP ENTRY / PDB]
ModBase Q01710.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from HAMAP).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from HAMAP).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from HAMAP).
GO:0050304; Molecular function: nitrous-oxide reductase activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00716; -; 1.
PBIL [Tree]
InterPro IPR001505; Copper_CuA.
IPR002429; COX2_C.
IPR008972; Cupredoxin.
IPR006311; Tat.
IPR015943; WD40/YVTN_repeat-like.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.420; Cupredoxin; 1.
G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
Pfam PF00116; COX2; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01409; TAT_signal_seq; 1.
PROSITE PS00078; COX2; 1.
PS50857; COX2_CUA; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q01710.
Other
ProtoNet Q01710.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Copper; Metal-binding; Oxidoreductase; Periplasm; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    49  49     Tat-type signal (Potential). 
CHAIN   50   634  585     Nitrous-oxide reductase. PRO_0000019829
REGION   538   634  97     COX2-like. 
METAL   125   125        Copper Z2 (By similarity). 
METAL   126   126        Copper Z3 (By similarity). 
METAL   174   174        Copper Z2 (By similarity). 
METAL   252   252        Calcium 2; via carbonyl oxygen (By similarity). 
METAL   255   255        Calcium 2 (By similarity). 
METAL   263   263        Calcium 2; via carbonyl oxygen (By similarity). 
METAL   269   269        Calcium 2 (By similarity). 
METAL   320   320        Calcium 2 (By similarity). 
METAL   322   322        Copper Z1 (By similarity). 
METAL   378   378        Copper Z1 (By similarity). 
METAL   429   429        Copper Z3 (By similarity). 
METAL   450   450        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   465   465        Calcium 1 (By similarity). 
METAL   490   490        Copper Z4 (By similarity). 
METAL   579   579        Copper A1 (By similarity). 
METAL   614   614        Copper A1 (By similarity). 
METAL   614   614        Copper A2 (By similarity). 
METAL   616   616        Copper A2; via carbonyl oxygen (By similarity). 
METAL   618   618        Copper A1 (By similarity). 
METAL   618   618        Copper A2 (By similarity). 
METAL   622   622        Copper A2 (By similarity). 
METAL   625   625        Copper A1 (By similarity). 
Sequence information
Length: 634 AA [This is the length of the unprocessed precursor] Molecular weight: 70695 Da [This is the MW of the unprocessed precursor] CRC64: 646BA48B28E949EE [This is a checksum on the sequence]
        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 

Q01710 in FASTA format

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