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Q51700 (NIRS_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Nitrite reductase
EC=1.7.2.1
Alternative name(s):
Cytochrome cd1
Cytochrome oxidase
Hydroxylamine reductase
EC=1.7.99.1
Gene names
Name:nirS
Ordered Locus Names:Pden_2487
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus ›

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Inactivation of this cytochrome oxidase results in the loss of nitrite and nitric oxide reductase activities, but not of nitrous oxide reductase activity.

Catalytic activity

Nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+.

NH3 + H2O + acceptor = hydroxylamine + reduced acceptor.

Cofactor

Binds 2 heme groups per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Periplasm By similarity.

Sequence similarities

Contains 1 cytochrome c domain.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

hydroxylamine reductase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nitrite reductase (NO-forming) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 By similarity
Chain30 – 596567Nitrite reductase
PRO_0000006574

Regions

Domain77 – 16286Cytochrome c
Region30 – 7647N-terminal tail
Region163 – 596434D1-heme domain

Sites

Metal binding461Iron (heme axial ligand) By similarity
Metal binding981Iron (heme axial ligand) By similarity
Metal binding2291Iron (heme D1 proximal ligand) By similarity
Binding site941Heme (covalent) By similarity
Binding site971Heme (covalent) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q51700 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 90C981B688A74BD3

FASTA59665,440
        10         20         30         40         50         60 
MRQRTPFARP GLLASAALAL VLGPLAVAAQ EQAAPPKDPA AALEDHKTKT DNRYEPSLDN 

        70         80         90        100        110        120 
LAQQDVAALG APEGIPALSD AQYNEANKIY FERCAGCHGV LRKGATGKAL TPDLTRDLGF 

       130        140        150        160        170        180 
DYLQSFITYG SPAGMPNWGT SGELTAEQVD LMANYLLLDP AAPPEFGMKE MRESWQVHVA 

       190        200        210        220        230        240 
PEDRPTQQEN DWDLENLFSV TLRDAGQIAL IDGTTYEIKS VLDTGYAVHI SRMSASGRYL 

       250        260        270        280        290        300 
FVIGRDGKVN MIDLWMKEPA TVAEIKIGSE ARSIETSKME GWEDKYAIAG AYWPPQYVIM 

       310        320        330        340        350        360 
DGETLEPMKI QSTRGMIYDE QEYHPEPRVA AILASHYRPE FIVNVKETGK ILLVDYTDLK 

       370        380        390        400        410        420 
NLKTTEIEAE RFLHDGGLDG SHRYFITAAN ARNKLVVIDT KEGKLVAIED TGGQTPHPGR 

       430        440        450        460        470        480 
GANFVHPTFG PVWATSHMGD DSVALIGTDP EGHPDNAWKI LDSFPALGGG SLFIKTHPNS 

       490        500        510        520        530        540 
QYLYVDATLN PEAEISGSVA VFDTKAMTGD GSDPEFKTLP IAEWAGIAEG QPRVVQGEFN 

       550        560        570        580        590 
KDGTEVWFSV WNGKDQESAL VVVDDKTLEL KHVIKDERLV TPTGKFNVYN TMTDTY

« Hide

References

« Hide 'large scale' references
[1]"Isolation, sequencing and mutational analysis of a gene cluster involved in nitrite reduction in Paracoccus denitrificans."
de Boer A.P.N., Reijnders W.N.M., Kuenen J.G., Stouthamer A.H., van Spanning R.J.M.
Antonie Van Leeuwenhoek 66:111-127(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U05002 Genomic DNA. Translation: AAA93118.1.
CP000489 Genomic DNA. Translation: ABL70574.1.
RefSeqYP_916270.1. NC_008686.1.

3D structure databases

ProteinModelPortalQ51700.
SMRQ51700. Positions 38-596.
ModBaseSearch...

Protein-protein interaction databases

STRING318586.Pden_2487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL70574; ABL70574; Pden_2487.
GeneID4580125.
KEGGpde:Pden_2487.
PATRIC22856095. VBIParDen97112_2412.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2010.
HOGENOMHOG000225986.
KOK15864.
OMAAGMPNWG.
ProtClustDBCLSK865915.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
2.140.10.20. 1 hit.
InterProIPR009056. Cyt_c_dom.
IPR011048. Cyt_cd1_nitrite_Rdtase_haem_C.
IPR003143. Cyt_d1_haem_dom.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
SUPFAMSSF51004. Cyt_cd1_haem_C. 1 hit.
SSF46626. Cytochrome_c. 1 hit.
PROSITEPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNIRS_PARDP
AccessionPrimary (citable) accession number: Q51700
Secondary accession number(s): A1B4Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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