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Q59746 (NOSZ_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nitrous-oxide reductase
EC=1.7.2.4
Alternative name(s):
N(2)OR
N2O reductase
Gene names
Name:nosZ
Ordered Locus Names:RA0643
ORF Names:SMa1182
Encoded onPlasmid pSymA (megaplasmid 1)
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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

Nitrogen + H2O + 2 cytochrome c = nitrous oxide + 2 reduced cytochrome c. 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.

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.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandCalcium
Copper
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Cellular componentmembrane

Inferred from electronic annotation. Source: InterPro

periplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

copper ion binding

Inferred from electronic annotation. Source: InterPro

cytochrome-c oxidase activity

Inferred from electronic annotation. Source: InterPro

nitrous-oxide reductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4646Tat-type signal Potential
Chain47 – 639593Nitrous-oxide reductase HAMAP MF_00716
PRO_0000019833

Regions

Region541 – 63999COX2-like HAMAP MF_00716

Sites

Metal binding1361Copper Z2 By similarity
Metal binding1371Copper Z3 By similarity
Metal binding1851Copper Z2 By similarity
Metal binding2621Calcium 2; via carbonyl oxygen By similarity
Metal binding2651Calcium 2 By similarity
Metal binding2731Calcium 2; via carbonyl oxygen By similarity
Metal binding2791Calcium 2 By similarity
Metal binding3241Calcium 2 By similarity
Metal binding3261Copper Z1 By similarity
Metal binding3811Copper Z1 By similarity
Metal binding4321Copper Z3 By similarity
Metal binding4531Calcium 1; via carbonyl oxygen By similarity
Metal binding4681Calcium 1 By similarity
Metal binding4931Copper Z4 By similarity
Metal binding5821Copper A1 By similarity
Metal binding6171Copper A1 By similarity
Metal binding6171Copper A2 By similarity
Metal binding6191Copper A2; via carbonyl oxygen By similarity
Metal binding6211Copper A1 By similarity
Metal binding6211Copper A2 By similarity
Metal binding6251Copper A2 By similarity
Metal binding6281Copper A1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59746 [UniParc].

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

FASTA63970,760
        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

« Hide

References

« Hide '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. expand/collapse author list , Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., 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.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed: 11474104] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U47133 Genomic DNA. Translation: AAC44023.1.
AE006469 Genomic DNA. Translation: AAK65301.1.
PIRC95342.
RefSeqNP_435889.1. NC_003037.1.

3D structure databases

ProteinModelPortalQ59746.
SMRQ59746. Positions 56-635.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1235679.
GenomeReviewsGene locus RA0643 in contig AE006469_GR.
KEGGsme:SMa1182.
NMPDRfig|266834.1.peg.643.
PATRIC23627768. VBISinMel96828_0663.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG308574.
OMAKLVHDGP.
ProtClustDBPRK02888.

Enzyme and pathway databases

BioCycSMEL266834:SMA1182-MONOMER.

Family and domain databases

HAMAPMF_00716. NosZ.
[Tree]
InterProIPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011045. N2O_reductase_N.
IPR023644. NO_Rdtase.
IPR006311. TAT_signal.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 1 hit.
G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KOK00376.
PfamPF00116. COX2. 1 hit.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 1 hit.
SSF50974. N2O_reductase_N. 1 hit.
PROSITEPS00078. COX2. False negative.
PS50857. COX2_CUA. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNOSZ_RHIME
AccessionPrimary (citable) accession number: Q59746
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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