NIR_ALCXX
ID NIR_ALCXX Reviewed; 330 AA.
AC P81445;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Copper-containing nitrite reductase;
DE EC=1.7.2.1;
DE AltName: Full=Cu-NIR;
GN Name=nirK;
OS Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=85698;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC STRAIN=LMG 1865 / CCUG 61957 / NCIMB 11015 / Iwasaki;
RX PubMed=15299906; DOI=10.1107/s0907444997002667;
RA Dodd F.E., Hasnain S.S., Abraham Z.H.L., Eady R.R., Smith B.E.;
RT "Structures of a blue-copper nitrite reductase and its substrate-bound
RT complex.";
RL Acta Crystallogr. D 53:406-418(1997).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=LMG 1865 / CCUG 61957 / NCIMB 11015 / Iwasaki;
RX PubMed=8240262; DOI=10.1042/bj2950587;
RA Abraham Z.H.L., Lowe D.J., Smith B.E.;
RT "Purification and characterization of the dissimilatory nitrite reductase
RT from Alcaligenes xylosoxidans subsp. xylosoxidans (N.C.I.M.B. 11015):
RT evidence for the presence of both type 1 and type 2 copper centres.";
RL Biochem. J. 295:587-593(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.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
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 PDB; 1NDR; X-ray; 3.00 A; A/B/C=1-329.
DR PDB; 1NDS; X-ray; 2.80 A; A/B/C=1-329.
DR PDBsum; 1NDR; -.
DR PDBsum; 1NDS; -.
DR AlphaFoldDB; P81445; -.
DR SMR; P81445; -.
DR SABIO-RK; P81445; -.
DR UniPathway; UPA00652; UER00707.
DR EvolutionaryTrace; P81445; -.
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 3D-structure; Copper; FAD; Flavoprotein; Metal-binding;
KW Nitrate assimilation; Oxidoreductase; Periplasm; Repeat.
FT CHAIN 1..330
FT /note="Copper-containing nitrite reductase"
FT /id="PRO_0000085586"
FT DOMAIN 1..165
FT /note="Plastocyanin-like 1"
FT DOMAIN 166..330
FT /note="Plastocyanin-like 2"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT BINDING 90
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT BINDING 125
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT BINDING 126
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT BINDING 135
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT BINDING 140
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 1 copper site"
FT BINDING 296
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
SQ SEQUENCE 330 AA; 34413 MW; E2C38C3A2CEBFCE8 CRC64;
GLPRVAVDLV APPLVHPHSQ VAAGAPKVVQ FRMSIEEKKM VADDDGTTAQ AMTFNGSVPG
PTLVVHEGDY IELTLVNPAT NSMPHNVDFH AATGALGGAG LTQVVPGQEA VLRFKADRSG
TFVYHCAPAG MVPWHVVSGM NGALMVLPRD GLRDAAGAAL AYDRVYTIGE SDLYVPKAAD
GNYSDYPALA SAYADTVAVM RTLTPSHAVF NGAVGALTGA NALTAAVGES VLIIHSQANR
DSRPHLIGGH GDWVWTTGKF ANPPQLNMET WFIPGGSAAA ALYTFKQPGT YAYLSHNLIE
AMELGAAAQA SVEGQWDDDL MTSVAAPGPA
