Nitrous-oxide reductase precursor - Paracoccus denitrificans

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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

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

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Protein attributes

Sequence length	652 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. HAMAP MF_00716
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 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.

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Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Calcium Chloride Copper Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure 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 chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 57

57

Tat-type signal Ref.3

Chain

58 – 652

595

Nitrous-oxide reductase HAMAP MF_00716

PRO_0000019827

Regions

Region

554 – 652

99

COX2-like HAMAP MF_00716

Sites

Metal binding

145

1

Copper Z2 HAMAP MF_00716

Metal binding

146

1

Copper Z3 HAMAP MF_00716

Metal binding

194

1

Copper Z2 HAMAP MF_00716

Metal binding

271

1

Calcium 2; via carbonyl oxygen HAMAP MF_00716

Metal binding

274

1

Calcium 2 HAMAP MF_00716

Metal binding

282

1

Calcium 2; via carbonyl oxygen HAMAP MF_00716

Metal binding

288

1

Calcium 2 HAMAP MF_00716

Metal binding

335

1

Calcium 2 HAMAP MF_00716

Metal binding

337

1

Copper Z1 HAMAP MF_00716

Metal binding

392

1

Copper Z1 HAMAP MF_00716

Metal binding

443

1

Copper Z3 HAMAP MF_00716

Metal binding

464

1

Calcium 1; via carbonyl oxygen HAMAP MF_00716

Metal binding

479

1

Calcium 1 HAMAP MF_00716

Metal binding

504

1

Copper Z4 HAMAP MF_00716

Metal binding

595

1

Copper A1 HAMAP MF_00716

Metal binding

630

1

Copper A1 HAMAP MF_00716

Metal binding

630

1

Copper A2 HAMAP MF_00716

Metal binding

632

1

Copper A2; via carbonyl oxygen HAMAP MF_00716

Metal binding

634

1

Copper A1 HAMAP MF_00716

Metal binding

634

1

Copper A2 HAMAP MF_00716

Metal binding

638

1

Copper A2 HAMAP MF_00716

Metal binding

641

1

Copper A1 HAMAP MF_00716

Binding site

197

1

Chloride HAMAP MF_00716

Binding site

339

1

Chloride; via amide nitrogen HAMAP MF_00716

Binding site

340

1

Chloride HAMAP MF_00716

Binding site

392

1

Chloride HAMAP MF_00716

Secondary structure

1

.

652

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q51705-1 [UniParc].

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

652

71,414

        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

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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: 8243476] [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: 10960107] [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: 12356332] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 60-650, PROTEIN SEQUENCE OF 58-63. Strain: 1657.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X74792 Genomic DNA. Translation: CAA52798.1.
AJ010260 Genomic DNA. Translation: CAB53351.1.

PIR

S39409.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FWX	X-ray	1.60	A/B/C/D	58-652	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.7.99.6. 59.

Family and domain databases

HAMAP

MF_00716.
[Tree]

InterPro

IPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
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]

PROSITE

PS00078. COX2. False negative.
PS50857. COX2_CUA. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

NOSZ_PARDE

Accession

Primary (citable) accession number: Q51705

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 68 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families