Nitrous-oxide reductase precursor - Pseudomonas stutzeri

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Reviewed, UniProtKB/Swiss-Prot P19573 (NOSZ_PSEST)

Last modified June 16, 2009. Version 83. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 stutzeri (Pseudomonas perfectomarina)

Taxonomic identifier

316 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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	N₂ + H₂O + acceptor = N₂O + reduced acceptor. HAMAP MF_00716
Cofactor	Binds 2 calcium ions per subunit. HAMAP MF_00716 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. HAMAP MF_00716
Pathway	Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4. HAMAP MF_00716
Subunit structure	Homodimer By similarity.
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.

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Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Calcium Copper Metal-binding
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
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: UniProtKB-SubCell
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 52

Tat-type signal Potential

Chain

53 – 638

586

Nitrous-oxide reductase HAMAP MF_00716

PRO_0000019831

Regions

Region

542 – 638

COX2-like HAMAP MF_00716

Sites

Metal binding

129

Copper Z2 By similarity

Metal binding

130

Copper Z3 By similarity

Metal binding

178

Copper Z2 By similarity

Metal binding

256

Calcium 2; via carbonyl oxygen By similarity

Metal binding

259

Calcium 2 By similarity

Metal binding

267

Calcium 2; via carbonyl oxygen By similarity

Metal binding

273

Calcium 2 By similarity

Metal binding

324

Calcium 2 By similarity

Metal binding

326

Copper Z1 By similarity

Metal binding

382

Copper Z1 By similarity

Metal binding

433

Copper Z3 By similarity

Metal binding

454

Calcium 1; via carbonyl oxygen By similarity

Metal binding

469

Calcium 1 By similarity

Metal binding

494

Copper Z4 By similarity

Metal binding

583

Copper A1 By similarity

Metal binding

618

Copper A1 By similarity

Metal binding

618

Copper A2 By similarity

Metal binding

620

Copper A2; via carbonyl oxygen By similarity

Metal binding

622

Copper A1 By similarity

Metal binding

622

Copper A2 By similarity

Metal binding

626

Copper A2 By similarity

Metal binding

629

Copper A1 By similarity

Experimental info

Sequence conflict

E → EE Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P19573-1 [UniParc].

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

638

70,822

        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

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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]	"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.
[5]	"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.

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Cross-references

Sequence databases
	X53676 Genomic DNA. Translation: CAA37714.2.
PIR	A31845.
3D structure databases
HSSP	HSSP built from PDB template 1FWX based on UniProtKB Q51705.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-243.
BRENDA	1.7.99.6. 421.
Family and domain databases
HAMAP	MF_00716. [Tree]
InterPro	IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR002429. Cyt_c_oxidase_su2_C. IPR006311. Tat. IPR017909. Twin_arg_translocation_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...

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Entry information

Entry name

NOSZ_PSEST

Accession

Primary (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:	June 16, 2009
This is version 83 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)

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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

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents