Q01537 (NIR_RHIGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Copper-containing nitrite reductase
EC=1.7.2.1

Alternative name(s):
Cu-NIR

Gene names

Name:

nirU

Organism

Rhizobium galegae

Taxonomic identifier

399 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Rhizobium

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+.
Cofactor	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.
Pathway	Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4.
Subunit structure	Homotrimer By similarity.
Subcellular location	Periplasm.
Domain	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.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 2 plastocyanin-like domains.
Caution	It is uncertain whether Met-1 or Met-12 is the initiator.

Ontologies

Keywords
Biological process	Nitrate assimilation
Cellular component	Periplasm
Domain	Repeat Signal
Ligand	Copper FAD Flavoprotein Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	denitrification pathway Inferred from electronic annotation. Source: UniProtKB-UniPathway nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro nitrite reductase (NO-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	Tat-type signal Potential
	Chain	33 – 379	347	Copper-containing nitrite reductase		PRO_0000002989
Regions
	Domain	33 – 214	182	Plastocyanin-like 1
	Domain	215 – 379	165	Plastocyanin-like 2
Sites
	Metal binding	134	1	Copper 1; type 1 By similarity
	Metal binding	139	1	Copper 2; type 2 By similarity
	Metal binding	174	1	Copper 2; type 2 By similarity
	Metal binding	175	1	Copper 1; type 1 By similarity
	Metal binding	184	1	Copper 1; type 1 By similarity
	Metal binding	189	1	Copper 1; type 1 By similarity
	Metal binding	345	1	Copper 2; type 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01537 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 090A3CBF6662F62F	FASTA	379	40,694
	10 20 30 40 50 60 MSEQFRLTRR SMLAGAAVAG ALAPVVTSVA HAEGGGIKTN SAATAANIAT LERVKVELVK 70 80 90 100 110 120 PPFVHAHTQK AEGEPKVVEF KMTIQEKKIV VDDKGTEVHA MTFDGSVPGP MMIVHQDDYV 130 140 150 160 170 180 ELTLVNPDTN ELQHNIDFHS ATGALGGGAL TVVNPGDTAV LRFKATKAGV FVYHCAPAGM 190 200 210 220 230 240 VPWHVTSGMN GAIMVLPRDG LKDHKGHELV YDKVYYVGEQ DFYVPKDENG KFKKYESAGE 250 260 270 280 290 300 AYPDVLEAMK TLTPTHVVFN GAVGALTGDN ALQAKVGDRV LILHSQANRD TRPHLIGGHG 310 320 330 340 350 360 DYVWATGKFA NPPELDQETW FIPGGAAGAA YYTFQQPGIY AYVNHNLIEA FELGAAGHFK 370 VTGDWNDDLM TAVVSPTSG

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M97294 Genomic DNA. Translation: AAC79132.1.
PIR	A48936.
3D structure databases
ProteinModelPortal	Q01537.
SMR	Q01537. Positions 47-378.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00652; UER00707.
Family and domain databases
Gene3D	2.60.40.420. 2 hits.
InterPro	IPR001117. Cu-oxidase. IPR011707. Cu-oxidase_3. IPR008972. Cupredoxin. IPR001287. NO2-reductase_Cu. IPR006311. TAT_signal. [Graphical view]
Pfam	PF00394. Cu-oxidase. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view]
PRINTS	PR00695. CUNO2RDTASE.
SUPFAM	SSF49503. Cupredoxin. 2 hits.
TIGRFAMs	TIGR02376. Cu_nitrite_red. 1 hit.
PROSITE	PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NIR_RHIGA

Accession

Primary (citable) accession number: Q01537

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program