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Protein

Copper-containing nitrite reductase

Gene

nirU

Organism
Rhizobium galegae
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Cu2+By similarityNote: 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
  • Cu+By similarityNote: Binds 1 Cu+ ion. The Cu+ ion is bound within a single monomer.By similarity
  • FADBy similarity

Pathwayi: nitrate reduction (denitrification)

This protein is involved in step 2 of the subpathway that synthesizes dinitrogen from nitrate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Copper-containing nitrite reductase (nirU)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway nitrate reduction (denitrification), which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dinitrogen from nitrate, the pathway nitrate reduction (denitrification) and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi134Copper 1; type 1By similarity1
Metal bindingi139Copper 2; type 2By similarity1
Metal bindingi174Copper 2; type 2By similarity1
Metal bindingi175Copper 1; type 1By similarity1
Metal bindingi184Copper 1; type 1By similarity1
Metal bindingi189Copper 1; type 1By similarity1
Metal bindingi345Copper 2; type 2By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Nitrate assimilation

Keywords - Ligandi

Copper, FAD, Flavoprotein, Metal-binding

Enzyme and pathway databases

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:nirU
OrganismiRhizobium galegae
Taxonomic identifieri399 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupNeorhizobium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Tat-type signalPROSITE-ProRule annotationAdd BLAST32
ChainiPRO_000000298933 – 379Copper-containing nitrite reductaseAdd BLAST347

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

Structurei

3D structure databases

ProteinModelPortaliQ01537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 214Plastocyanin-like 1Add BLAST182
Domaini215 – 379Plastocyanin-like 2Add BLAST165

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

Belongs to the multicopper oxidase family.Curated
Contains 2 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

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.

Q01537-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQFRLTRR SMLAGAAVAG ALAPVVTSVA HAEGGGIKTN SAATAANIAT
60 70 80 90 100
LERVKVELVK PPFVHAHTQK AEGEPKVVEF KMTIQEKKIV VDDKGTEVHA
110 120 130 140 150
MTFDGSVPGP MMIVHQDDYV ELTLVNPDTN ELQHNIDFHS ATGALGGGAL
160 170 180 190 200
TVVNPGDTAV LRFKATKAGV FVYHCAPAGM VPWHVTSGMN GAIMVLPRDG
210 220 230 240 250
LKDHKGHELV YDKVYYVGEQ DFYVPKDENG KFKKYESAGE AYPDVLEAMK
260 270 280 290 300
TLTPTHVVFN GAVGALTGDN ALQAKVGDRV LILHSQANRD TRPHLIGGHG
310 320 330 340 350
DYVWATGKFA NPPELDQETW FIPGGAAGAA YYTFQQPGIY AYVNHNLIEA
360 370
FELGAAGHFK VTGDWNDDLM TAVVSPTSG
Length:379
Mass (Da):40,694
Last modified:February 1, 1995 - v1
Checksum:i090A3CBF6662F62F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97294 Genomic DNA. Translation: AAC79132.1.
PIRiA48936.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97294 Genomic DNA. Translation: AAC79132.1.
PIRiA48936.

3D structure databases

ProteinModelPortaliQ01537.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00652; UER00707.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiNIR_RHIGA
AccessioniPrimary (citable) accession number: Q01537
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 5, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-12 is the initiator.Curated

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.