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Q01537

- NIR_RHIGA

UniProt

Q01537 - NIR_RHIGA

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Protein
Copper-containing nitrite reductase
Gene
nirU
Organism
Rhizobium galegae
Status
Reviewed - Annotation score: 4 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 bindingi134 – 1341Copper 1; type 1 By similarity
Metal bindingi139 – 1391Copper 2; type 2 By similarity
Metal bindingi174 – 1741Copper 2; type 2 By similarity
Metal bindingi175 – 1751Copper 1; type 1 By similarity
Metal bindingi184 – 1841Copper 1; type 1 By similarity
Metal bindingi189 – 1891Copper 1; type 1 By similarity
Metal bindingi345 – 3451Copper 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

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 groupRhizobium

Subcellular locationi

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 – 3232Tat-type signal Reviewed prediction
Add
BLAST
Chaini33 – 379347Copper-containing nitrite reductase
PRO_0000002989Add
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.

Structurei

3D structure databases

ProteinModelPortaliQ01537.
SMRiQ01537. Positions 47-378.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 214182Plastocyanin-like 1
Add
BLAST
Domaini215 – 379165Plastocyanin-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

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

MSEQFRLTRR SMLAGAAVAG ALAPVVTSVA HAEGGGIKTN SAATAANIAT    50
LERVKVELVK PPFVHAHTQK AEGEPKVVEF KMTIQEKKIV VDDKGTEVHA 100
MTFDGSVPGP MMIVHQDDYV ELTLVNPDTN ELQHNIDFHS ATGALGGGAL 150
TVVNPGDTAV LRFKATKAGV FVYHCAPAGM VPWHVTSGMN GAIMVLPRDG 200
LKDHKGHELV YDKVYYVGEQ DFYVPKDENG KFKKYESAGE AYPDVLEAMK 250
TLTPTHVVFN GAVGALTGDN ALQAKVGDRV LILHSQANRD TRPHLIGGHG 300
DYVWATGKFA NPPELDQETW FIPGGAAGAA YYTFQQPGIY AYVNHNLIEA 350
FELGAAGHFK VTGDWNDDLM TAVVSPTSG 379
Length:379
Mass (Da):40,694
Last modified:February 1, 1995 - v1
Checksum:i090A3CBF6662F62F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97294 Genomic DNA. Translation: AAC79132.1.
PIRiA48936.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M97294 Genomic DNA. Translation: AAC79132.1 .
PIRi A48936.

3D structure databases

ProteinModelPortali Q01537.
SMRi Q01537. Positions 47-378.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00652 ; UER00707 .

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. "Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers."
    Ye R.W., Fries M.R., Bezborodnikov S.G., Averill B.A., Tiedje J.M.
    Appl. Environ. Microbiol. 59:250-254(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: G-179.

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 16, 2013
This is version 78 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.

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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