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Q92Z29

- NIRK_RHIME

UniProt

Q92Z29 - NIRK_RHIME

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Protein
Copper-containing nitrite reductase
Gene
nirK, RA0681, SMa1250
Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Binds 1 Cu2+ ion. The Cu2+ ion is held by residues from each of 2 monomers of the trimer. Nitrite is bound to the Cu2+ ion site. Pseudoazurin is the physiological electron donor for the Cu-NIR in vitro By similarity.
Binds 1 Cu+ ion. The Cu+ ion is bound within a single monomer By similarity.
FAD By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi131 – 1311Copper 1; type 1 By similarity
Metal bindingi136 – 1361Copper 2; type 2 By similarity
Metal bindingi171 – 1711Copper 2; type 2 By similarity
Metal bindingi172 – 1721Copper 1; type 1 By similarity
Metal bindingi181 – 1811Copper 1; type 1 By similarity
Metal bindingi186 – 1861Copper 1; type 1 By similarity
Metal bindingi342 – 3421Copper 2; type 2 By similarity

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. nitrite reductase (NO-forming) activity Source: UniProtKB-EC

GO - Biological processi

  1. denitrification pathway Source: UniProtKB-UniPathway
  2. nitrate assimilation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

Copper, FAD, Flavoprotein, Metal-binding

Enzyme and pathway databases

BioCyciSMEL266834:GJF6-5689-MONOMER.
UniPathwayiUPA00652; UER00707.

Names & Taxonomyi

Protein namesi
Recommended name:
Copper-containing nitrite reductase (EC:1.7.2.1)
Alternative name(s):
Cu-NIR
Gene namesi
Name:nirK
Ordered Locus Names:RA0681
ORF Names:SMa1250
Encoded oniPlasmid pSymA (megaplasmid 1)0 Publication
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001976: Plasmid pSymA

Subcellular locationi

Periplasm By similarity

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Tat-type signal Reviewed prediction
Add
BLAST
Chaini34 – 376343Copper-containing nitrite reductase
PRO_0000002991Add
BLAST

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Interactioni

Subunit structurei

Homotrimer By similarity.

Protein-protein interaction databases

STRINGi266834.SMa1250.

Structurei

3D structure databases

ProteinModelPortaliQ92Z29.
SMRiQ92Z29. Positions 45-376.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 19396Plastocyanin-like 1
Add
BLAST
Domaini258 – 359102Plastocyanin-like 2
Add
BLAST

Domaini

The type I copper site in NIR plays a crucial role for electron transfer from pseudoazurin to the type II copper site of NIR, which comprises the catalytic center of NIR for the reduction of nitrite.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2132.
HOGENOMiHOG000217143.
KOiK00368.
OMAiNIDFHSA.
OrthoDBiEOG66B40C.

Family and domain databases

Gene3Di2.60.40.420. 2 hits.
InterProiIPR001117. Cu-oxidase.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PRINTSiPR00695. CUNO2RDTASE.
SUPFAMiSSF49503. SSF49503. 2 hits.
TIGRFAMsiTIGR02376. Cu_nitrite_red. 1 hit.
PROSITEiPS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92Z29-1 [UniParc]FASTAAdd to Basket

« Hide

MSEQFQMTRR SMLAGAAIAG AVTPLIGAVS AHAEEAVAKT AHINVASLPR    50
VKVDLVKPPF VHAHTQKAEG GPKVVEFTLT IEEKKIVIDE QGTELHAMTF 100
NGSVPGPLMV VHQDDYVELT LINPDTNTLQ HNIDFHSATG ALGGGALTVV 150
NPGDTTVLRF KASKAGVFVY HCAPPGMVPW HVTSGMNGAI MVLPREGLTD 200
GKGNSITYDK VYYVGEQDFY VPRDANGKFK KYESVGEAYA DTLEVMRTLT 250
PSHIVFNGAV GALTGDSALK AAVGEKVLIV HSQANRDTRP HLIGGHGDYV 300
WATGKFRNAP DVDQETWFIP GGTAGAAFYT FEQPGIYAYV NHNLIEAFEL 350
GAAAHFAVTG DWNDDLMTSV RAPSGT 376
Length:376
Mass (Da):40,259
Last modified:December 1, 2001 - v1
Checksum:i9B7999273001DC63
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006469 Genomic DNA. Translation: AAK65339.1.
PIRiA95347.
RefSeqiNP_435927.1. NC_003037.1.

Genome annotation databases

EnsemblBacteriaiAAK65339; AAK65339; SMa1250.
GeneIDi1235717.
KEGGisme:SMa1250.
PATRICi23627844. VBISinMel96828_0701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE006469 Genomic DNA. Translation: AAK65339.1 .
PIRi A95347.
RefSeqi NP_435927.1. NC_003037.1.

3D structure databases

ProteinModelPortali Q92Z29.
SMRi Q92Z29. Positions 45-376.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266834.SMa1250.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK65339 ; AAK65339 ; SMa1250 .
GeneIDi 1235717.
KEGGi sme:SMa1250.
PATRICi 23627844. VBISinMel96828_0701.

Phylogenomic databases

eggNOGi COG2132.
HOGENOMi HOG000217143.
KOi K00368.
OMAi NIDFHSA.
OrthoDBi EOG66B40C.

Enzyme and pathway databases

UniPathwayi UPA00652 ; UER00707 .
BioCyci SMEL266834:GJF6-5689-MONOMER.

Family and domain databases

Gene3Di 2.60.40.420. 2 hits.
InterProi IPR001117. Cu-oxidase.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
IPR001287. NO2-reductase_Cu.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF00394. Cu-oxidase. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view ]
PRINTSi PR00695. CUNO2RDTASE.
SUPFAMi SSF49503. SSF49503. 2 hits.
TIGRFAMsi TIGR02376. Cu_nitrite_red. 1 hit.
PROSITEi PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1021.

Entry informationi

Entry nameiNIRK_RHIME
AccessioniPrimary (citable) accession number: Q92Z29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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