Q60214 (NIR_RHIHE) 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:

nirK

Organism

Rhizobium hedysari

Taxonomic identifier

50338 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	377 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 By similarity.
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.

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 – 35	35	Tat-type signal Potential
	Chain	36 – 377	342	Copper-containing nitrite reductase		PRO_0000002990
Regions
	Domain	99 – 194	96	Plastocyanin-like 1
	Domain	259 – 360	102	Plastocyanin-like 2
Sites
	Metal binding	132	1	Copper 1; type 1 By similarity
	Metal binding	137	1	Copper 2; type 2 By similarity
	Metal binding	172	1	Copper 2; type 2 By similarity
	Metal binding	173	1	Copper 1; type 1 By similarity
	Metal binding	182	1	Copper 1; type 1 By similarity
	Metal binding	187	1	Copper 1; type 1 By similarity
	Metal binding	343	1	Copper 2; type 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q60214 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C7AFEE9AE639E2F8	FASTA	377	40,719
	10 20 30 40 50 60 MTNTLQMTRR TMLTGAAVAG ALTPILTSGG GNASPTPVRK LSATEIAALP RRKLDLVKPP 70 80 90 100 110 120 FVHVHTQKAE GGPKVVEVTL TIEEKKLVID GKGTEVNAMT FDGSVPGPLI VVHQDDYVEV 130 140 150 160 170 180 TLVNPETNTL QHNIDFHSAT GALGGGALTV VNPGESAVLR FKATKAGVFV YHCAPPGMVP 190 200 210 220 230 240 WHVTSGMNGA IMVLPREGLT DGHGKELVYD KVYYLGEQDF YIPRDEKGEF KKYDSPGEAY 250 260 270 280 290 300 EDTVAVMRTL TPTHIVFNGA VGALTGENAL TAAVGERVLI VHSQANRDTR PHLIGGHGEY 310 320 330 340 350 360 VWRTGKFVNV PDRDQETWFI PGPTRGAAYY TFEQPGIYAY VNHNLIEAFE LGAAAHFKVT 370 GDWNDDLMTT VRSPSGS

References

[1]

"Characterization of the gene encoding nitrite reductase and the physiological consequences of its expression in the nondenitrifying Rhizobium 'hedysari' strain HCNT1." Toffanin A., Wu Q., Maskus M., Caselia S., Abruna H.D., Shapleigh J.P. Appl. Environ. Microbiol. 62:4019-4025(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: HCNT1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U65658 Genomic DNA. Translation: AAB05880.1.
3D structure databases
ProteinModelPortal	Q60214.
SMR	Q60214. Positions 42-377.
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_RHIHE

Accession

Primary (citable) accession number: Q60214

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program