Reviewed, UniProtKB/Swiss-Prot Q06006 (NIR_PSECL)

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

Pseudomonas chlororaphis (Pseudomonas aureofaciens)

Taxonomic identifier

333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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. Binds 1 Cu+ ion. The Cu+ ion is bound within a single monomer. FAD.
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.
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
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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: UniProtKB-KW 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 – 24	24	Ref.1
	Chain	25 – 363	339	Copper-containing nitrite reductase		PRO_0000002988
Regions
	Domain	25 – 193	169	Plastocyanin-like 1
	Domain	194 – 363	170	Plastocyanin-like 2
Sites
	Metal binding	113	1	Copper 1; type 1 By similarity
	Metal binding	118	1	Copper 2; type 2 By similarity
	Metal binding	153	1	Copper 2; type 2 By similarity
	Metal binding	154	1	Copper 1; type 1 By similarity
	Metal binding	163	1	Copper 1; type 1 By similarity
	Metal binding	168	1	Copper 1; type 1 By similarity
	Metal binding	324	1	Copper 2; type 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q06006-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 50DDB60CC4DC3E00	FASTA	363	39,248
	10 20 30 40 50 60 MSVFRSVLGA CVLLGSCASS LALAGGAEGL QRVKVDLVAP PLVHPHEQVV SGPPKVVQFR 70 80 90 100 110 120 MSIEEKKMVI DDQGTTLQAM TFNGSMPGPT LVVHEGDYIE LTLVNPATNS MPHNVDFHAA 130 140 150 160 170 180 TGALGGAGLT QVVPGQEVVL RFKADRSGTF VYHCAPQGMV PWHVVSGMNG ALMVLPRDGL 190 200 210 220 230 240 RDPQGKLLHY DRVYTIGESD LYIPKDKDGH YKDYPDLASS YQDTRAVMRT LTPSHVVFNG 250 260 270 280 290 300 RVGALTGANA LTSKVGESVL FIHSQANRDS RPHLIGGHGD WVWTTGKFAN PPQRNMETWF 310 320 330 340 350 360 IPGGSAVAAL YTFKQPGTYV YLSHNLIEAM ELGALAQIKV EGQWDDDLMT QVKAPGPIVE PKQ

References

[1]

"Copper-containing nitrite reductase from Pseudomonas aureofaciens is functional in a mutationally cytochrome cd1-free background (NirS-) of Pseudomonas stutzeri." Glockner A.B., Juengst A., Zumft W.G. Arch. Microbiol. 160:18-26(1993) [PubMed: 8352648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-41. Strain: ATCC 13985 / DSM 50082 / NRRL B-1576 / Stanier 38.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z21945 Genomic DNA. Translation: CAA79939.1.
PIR	S32112.
3D structure databases
HSSP	HSSP built from PDB template 1OE2 based on UniProtKB O68601.
SMR	Q06006. Positions 27-358.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.7.2.1. 20327.
Family and domain databases
InterPro	IPR001117. Cu-oxidase. IPR011707. Cu-oxidase_3. IPR001287. Cu_NO2-reductase_N. IPR008972. Cupredoxin. IPR012746. Nitrite_red_Cu. [Graphical view]
Gene3D	G3DSA:2.60.40.420. Cupredoxin. 2 hits.
Pfam	PF00394. Cu-oxidase. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view]
PRINTS	PR00695. CUNO2RDTASE.
ProDom	PD001235. Copper_blue_sub. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02376. Cu_nitrite_red. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NIR_PSECL

Accession

Primary (citable) accession number: Q06006

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)