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 27-MAR-2024, entry version 97. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd11020; CuRO_1_CuNIR; 1. DR CDD; cd04208; CuRO_2_CuNIR; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 2. DR InterPro; IPR011707; Cu-oxidase-like_N. DR InterPro; IPR001117; Cu-oxidase_2nd. DR InterPro; IPR045087; Cu-oxidase_fam. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR001287; NO2-reductase_Cu. DR NCBIfam; TIGR02376; Cu_nitrite_red; 1. DR PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1. DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR PRINTS; PR00695; CUNO2RDTASE. DR SUPFAM; SSF49503; Cupredoxins; 2. 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 //