Nitrous-oxide reductase precursor

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Reviewed, UniProtKB/Swiss-Prot Q59746 (NOSZ_RHIME)

Last modified January 19, 2010. Version 77. 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
Ordered Locus Names:	RA0643
ORF Names:	SMa1182

Encoded on

Plasmid pSymA (megaplasmid 1)

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

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Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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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 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. HAMAP MF_00716
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 not 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 Copper Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Plasmid
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 – 46

Tat-type signal Potential

Chain

47 – 639

593

Nitrous-oxide reductase HAMAP MF_00716

PRO_0000019833

Regions

Region

541 – 639

COX2-like HAMAP MF_00716

Sites

Metal binding

136

Copper Z2 By similarity

Metal binding

137

Copper Z3 By similarity

Metal binding

185

Copper Z2 By similarity

Metal binding

262

Calcium 2; via carbonyl oxygen By similarity

Metal binding

265

Calcium 2 By similarity

Metal binding

273

Calcium 2; via carbonyl oxygen By similarity

Metal binding

279

Calcium 2 By similarity

Metal binding

324

Calcium 2 By similarity

Metal binding

326

Copper Z1 By similarity

Metal binding

381

Copper Z1 By similarity

Metal binding

432

Copper Z3 By similarity

Metal binding

453

Calcium 1; via carbonyl oxygen By similarity

Metal binding

468

Calcium 1 By similarity

Metal binding

493

Copper Z4 By similarity

Metal binding

582

Copper A1 By similarity

Metal binding

617

Copper A1 By similarity

Metal binding

617

Copper A2 By similarity

Metal binding

619

Copper A2; via carbonyl oxygen By similarity

Metal binding

621

Copper A1 By similarity

Metal binding

621

Copper A2 By similarity

Metal binding

625

Copper A2 By similarity

Metal binding

628

Copper A1 By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q59746-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EBCF5EDFAFF70B96
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FASTA

639

70,760

        10         20         30         40         50         60 
MSNEETKMRL NRRQMLGTTA FMAAAGAVGA GGALTLSGGT ATPARAQETS GSSYEVKPGE 

        70         80         90        100        110        120 
LDEYYVFFSS GQSGEIRIVG APSMREMMRI PVFNRCSATG WGQTNESRKV MTEGLLPETV 

       130        140        150        160        170        180 
EFLKDQGGLY LNGDLHHPHP SFTDGTYDGR YLYANDKSNS RVCRIRLDVM KCDKIIQLPN 

       190        200        210        220        230        240 
QHTVHGLRVQ KYPKTGYVFC NGEDAVPVPN DGKTMGDKNS YQAIFTAVDG ETMEVAWQVM 

       250        260        270        280        290        300 
VDGNLDNVDA DYQGKYCFAT CYNSEEGFTL ADMMASEQDW VVIFNLKRIE EAVAKGDYKE 

       310        320        330        340        350        360 
IGGVPVLDGR KGSPYTRYVP VPNSPHGINT APDGIHVVAN GKLSPTVTVF DVRKFDDLFD 

       370        380        390        400        410        420 
DKIQARDTVV AEPELGLGPL HTAYDGKGNA YTTLFIDSQV CKWNIEDAKR AYAGEKVDPI 

       430        440        450        460        470        480 
RHKLDVHYQP GHNHTSMGQT KEADGKWLIS LNKFSKDRYL NVGPLKPEND QLIDISGDEM 

       490        500        510        520        530        540 
VLVHDNPTFA EPHDATIVHA SKINPVHVWN RDDPFFADAV AQAKADNIDL MVDSEVIRDG 

       550        560        570        580        590        600 
NKVRVYMTSA APAFGLDDFT VKQGDEVTVY VTNIDEVEDL THGFCIVNYG INMEVAPQAT 

       610        620        630 
ASVTFKASRP GVYWYYCTWF CHAMHMEMKG RMLVEAQGA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and analysis of the dissimilatory nitrous oxide reduction genes, nosRZDFY, of Rhizobium meliloti." Holloway P., McCormick W., Watson R.J., Chan Y.K. J. Bacteriol. 178:1505-1514(1996) [PubMed: 8626275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: JJ1c10.
[2]	"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid." Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H. Long S.R. Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	U47133 Genomic DNA. Translation: AAC44023.1. AE006469 Genomic DNA. Translation: AAK65301.1.
PIR	C95342.
RefSeq	NP_435889.1.
3D structure databases
SMR	Q59746. Positions 56-635.
ModBase	Search...
Genome annotation databases
GeneID	1235679.
GenomeReviews	Gene locus RA0643 in contig AE006469_GR.
KEGG	sme:SMa1182.
NMPDR	fig\|266834.1.peg.643.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG308574.
OMA	SKDRFLP.
Enzyme and pathway databases
BioCyc	SMEL266834:SMA1182-MONOMER.
BRENDA	1.7.99.6. 142.
Family and domain databases
HAMAP	MF_00716. NosZ. [Tree]
InterPro	IPR008972. Cupredoxin. IPR002429. Cyt_c_oxidase_su2_C. IPR011045. N2O_reductase_N. IPR017909. Twin_arg_translocation_Tat. IPR015943. WD40/YVTN_repeat-like_dom. [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_RHIME

Accession

Primary (citable) accession number: Q59746

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 77 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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents