NIR_PSECL
ID NIR_PSECL Reviewed; 363 AA.
AC Q06006;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Copper-containing nitrite reductase;
DE EC=1.7.2.1;
DE AltName: Full=Cu-NIR;
DE Flags: Precursor;
GN Name=nirK;
OS Pseudomonas chlororaphis (Pseudomonas aureofaciens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-41.
RC STRAIN=ATCC 13985 / DSM 6698 / CIP 103295 / NBRC 3521 / NCIMB 9030 / NCTC
RC 10686 / NRRL B-1576 / Stanier 38;
RX PubMed=8352648; DOI=10.1007/bf00258141;
RA Glockner A.B., Juengst A., Zumft W.G.;
RT "Copper-containing nitrite reductase from Pseudomonas aureofaciens is
RT functional in a mutationally cytochrome cd1-free background (NirS-) of
RT Pseudomonas stutzeri.";
RL Arch. Microbiol. 160:18-26(1993).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-
CC [cytochrome c] + 2 H(+) + nitrite; Xref=Rhea:RHEA:15233, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.1;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 Cu(2+) ion. The Cu(2+) ion is held by residues from each
CC of 2 monomers of the trimer. Nitrite is bound to the Cu(2+) ion site.
CC Pseudoazurin is the physiological electron donor for the Cu-NIR in
CC vitro.;
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Note=Binds 1 Cu(+) ion. The Cu(+) ion is bound within a single
CC monomer.;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 2/4.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- DOMAIN: The type I copper site in NIR plays a crucial role for electron
CC transfer from pseudoazurin to the type II copper site of NIR, which
CC comprises the catalytic center of NIR for the reduction of nitrite.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; Z21945; CAA79939.1; -; Genomic_DNA.
DR PIR; S32112; S32112.
DR AlphaFoldDB; Q06006; -.
DR SMR; Q06006; -.
DR UniPathway; UPA00652; UER00707.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 2.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR001287; NO2-reductase_Cu.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR PRINTS; PR00695; CUNO2RDTASE.
DR SUPFAM; SSF49503; SSF49503; 2.
DR TIGRFAMs; TIGR02376; Cu_nitrite_red; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; FAD; Flavoprotein; Metal-binding;
KW Nitrate assimilation; Oxidoreductase; Periplasm; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8352648"
FT CHAIN 25..363
FT /note="Copper-containing nitrite reductase"
FT /id="PRO_0000002988"
FT DOMAIN 25..193
FT /note="Plastocyanin-like 1"
FT DOMAIN 194..363
FT /note="Plastocyanin-like 2"
FT BINDING 113
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 39248 MW; 50DDB60CC4DC3E00 CRC64;
MSVFRSVLGA CVLLGSCASS LALAGGAEGL QRVKVDLVAP PLVHPHEQVV SGPPKVVQFR
MSIEEKKMVI DDQGTTLQAM TFNGSMPGPT LVVHEGDYIE LTLVNPATNS MPHNVDFHAA
TGALGGAGLT QVVPGQEVVL RFKADRSGTF VYHCAPQGMV PWHVVSGMNG ALMVLPRDGL
RDPQGKLLHY DRVYTIGESD LYIPKDKDGH YKDYPDLASS YQDTRAVMRT LTPSHVVFNG
RVGALTGANA LTSKVGESVL FIHSQANRDS RPHLIGGHGD WVWTTGKFAN PPQRNMETWF
IPGGSAVAAL YTFKQPGTYV YLSHNLIEAM ELGALAQIKV EGQWDDDLMT QVKAPGPIVE
PKQ
