ID NIR_ACHCY Reviewed; 378 AA. AC P25006; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 04-NOV-2026, entry version 141. 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 Achromobacter cycloclastes. OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Alcaligenaceae; Achromobacter. OX NCBI_TaxID=223; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC RC 102459 / An-17; RX PubMed=8605003; DOI=10.1006/bbrc.1996.0249; RA Chen J.-Y., Chang W.-C., Chang T., Chang W.-C., Liu M.-Y., Payne W.J., RA le Gall J.; RT "Cloning, characterization, and expression of the nitric oxide-generating RT nitrite reductase and of the blue copper protein genes of Achromobacter RT cycloclastes."; RL Biochem. Biophys. Res. Commun. 219:423-428(1996). RN [2] RP PROTEIN SEQUENCE OF 39-378. RC STRAIN=ATCC 21921 / JCM 20009 / IAM 1013 / KCTC 2947 / LMG 1127 / NBRC RC 102459 / An-17; RX PubMed=1830217; DOI=10.1021/bi00243a020; RA Fenderson F.F., Kumar S., Adman E.T., Liu M.-Y., Payne W.J., le Gall J.; RT "Amino acid sequence of nitrite reductase: a copper protein from RT Achromobacter cycloclastes."; RL Biochemistry 30:7180-7185(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=1862344; DOI=10.1126/science.1862344; RA Godden J.W., Turley S., Teller D.C., Adman E.T., Liu M.-Y., Payne W.J., RA le Gall J.; RT "The 2.3-A X-ray structure of nitrite reductase from Achromobacter RT cycloclastes."; RL Science 253:438-442(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=7499203; DOI=10.1074/jbc.270.46.27458; RA Adman E.T., Godden J.W., Turley S.; RT "The structure of copper-nitrite reductase from Achromobacter cycloclastes RT at five pH values, with NO2-bound and with type II copper depleted."; RL J. Biol. Chem. 270:27458-27474(1995). CC -!- CATALYTIC ACTIVITY: CC Reaction=nitric oxide + Fe(III)-[cytochrome c] + H2O = Fe(II)- CC [cytochrome c] + nitrite + 2 H(+); 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(+); Xref=ChEBI:CHEBI:49552; CC Note=Binds 1 Cu(+) ion.; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Note=Binds 1 Cu(2+) ion.; 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. 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 -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has been experimentally proven. 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 EMBL; Z48635; CAA88564.1; -; Genomic_DNA. DR PIR; JC4648; JC4648. DR PDB; 1KCB; X-ray; 1.65 A; A=39-378. DR PDB; 1NIA; X-ray; 2.50 A; A/B/C=39-378. DR PDB; 1NIB; X-ray; 2.70 A; A/B/C=39-378. DR PDB; 1NIC; X-ray; 1.90 A; A=39-378. DR PDB; 1NID; X-ray; 2.20 A; A=39-378. DR PDB; 1NIE; X-ray; 1.90 A; A=39-378. DR PDB; 1NIF; X-ray; 1.70 A; A=39-378. DR PDB; 1RZP; X-ray; 1.90 A; A/B/C=39-373. DR PDB; 1RZQ; X-ray; 2.20 A; A/B/C=39-373. DR PDB; 2AVF; X-ray; 2.60 A; A/B/C/D/E/F=39-367. DR PDB; 2BW4; X-ray; 0.90 A; A=39-378. DR PDB; 2BW5; X-ray; 1.12 A; A=39-378. DR PDB; 2BWD; X-ray; 1.15 A; A=39-378. DR PDB; 2BWI; X-ray; 1.10 A; A=39-378. DR PDB; 2NRD; X-ray; 2.10 A; A=39-378. DR PDB; 2Y1A; X-ray; 1.95 A; A=39-378. DR PDB; 5AKR; X-ray; 0.87 A; A=1-378. DR PDB; 5I6K; X-ray; 1.07 A; A=45-378. DR PDB; 5I6L; X-ray; 1.08 A; A=46-377. DR PDB; 5I6M; X-ray; 1.09 A; A=46-377. DR PDB; 5I6N; X-ray; 1.22 A; A=46-377. DR PDB; 5I6O; X-ray; 1.45 A; A=46-377. DR PDB; 5I6P; X-ray; 1.56 A; A=46-377. DR PDB; 5N8F; X-ray; 1.38 A; A=45-378. DR PDB; 5N8G; X-ray; 1.47 A; A=45-378. DR PDB; 5N8H; X-ray; 1.65 A; A=45-378. DR PDB; 5N8I; X-ray; 1.40 A; A=45-378. DR PDB; 5OF5; X-ray; 1.08 A; A=45-378. DR PDB; 5OF6; X-ray; 1.08 A; A=45-378. DR PDB; 5OF7; X-ray; 1.27 A; A=45-378. DR PDB; 5OF8; X-ray; 1.34 A; A=45-378. DR PDB; 5OFC; X-ray; 1.68 A; A=45-378. DR PDB; 5OFD; X-ray; 1.77 A; A=45-378. DR PDB; 5OFE; X-ray; 1.84 A; A=45-378. DR PDB; 5OFF; X-ray; 1.41 A; A=45-378. DR PDB; 5OFG; X-ray; 1.49 A; A=45-378. DR PDB; 5OFH; X-ray; 1.58 A; A=45-378. DR PDB; 5OG2; X-ray; 1.64 A; A=45-378. DR PDB; 5OG3; X-ray; 1.70 A; A=45-378. DR PDB; 5OG4; X-ray; 1.76 A; A=45-378. DR PDB; 5OG5; X-ray; 1.82 A; A=45-378. DR PDB; 5OG6; X-ray; 1.85 A; A=45-378. DR PDB; 5OGF; X-ray; 1.88 A; A=46-378. DR PDB; 5OGG; X-ray; 1.91 A; A=45-378. DR PDB; 6GB8; X-ray; 1.48 A; A=39-378. DR PDB; 6GBB; X-ray; 1.48 A; A=39-378. DR PDB; 6GBY; X-ray; 1.48 A; A=1-378. DR PDB; 6GCG; X-ray; 1.80 A; A=1-378. DR PDB; 6GSQ; X-ray; 1.50 A; A=1-378. DR PDB; 6GT0; X-ray; 1.50 A; A=1-378. DR PDB; 6GT2; X-ray; 1.60 A; A=1-378. DR PDB; 6GTI; X-ray; 1.50 A; A=1-378. DR PDB; 6GTJ; Neutron; 1.80 A; A=39-378. DR PDB; 6GTK; X-ray; 1.50 A; A=1-378. DR PDB; 6GTL; X-ray; 1.50 A; A=1-378. DR PDB; 6GTN; X-ray; 1.50 A; A=1-378. DR PDB; 6KNF; EM; 2.99 A; A/B/C=45-378. DR PDB; 6KNG; EM; 2.85 A; A/B/C=45-378. DR PDB; 6QWG; X-ray; 1.90 A; A=46-378. DR PDB; 6ZU6; X-ray; 1.15 A; A=45-378. DR PDB; 6ZUA; X-ray; 1.14 A; A=45-378. DR PDB; 6ZUB; X-ray; 1.08 A; A=45-378. DR PDB; 6ZUD; X-ray; 1.10 A; A=45-378. DR PDB; 6ZUT; X-ray; 1.15 A; A=45-378. DR PDB; 9RLL; X-ray; 0.95 A; A=45-378. DR PDB; 9RN0; X-ray; 0.95 A; A=45-378. DR PDB; 9T6O; X-ray; 1.60 A; A=1-378. DR PDB; 9T6P; X-ray; 2.01 A; A=1-378. DR PDB; 9T6Q; X-ray; 1.47 A; A=1-378. DR PDB; 9T6U; X-ray; 1.50 A; A=1-378. DR AlphaFoldDB; P25006; -. DR EMDB; EMD-0730; -. DR EMDB; EMD-0731; -. DR SMR; P25006; -. DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid. DR KEGG; ag:CAA88564; -. DR BRENDA; 1.7.2.1; 69. DR SABIO-RK; P25006; -. DR UniPathway; UPA00652; UER00707. DR EvolutionaryTrace; P25006; -. 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 CDD; cd11020; CuRO_1_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 InterPro; IPR006311; TAT_signal. DR NCBIfam; TIGR02376; Cu_nitrite_red; 1. DR PANTHER; PTHR11709:SF394; 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. DR PROSITE; PS51318; TAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Copper; Direct protein sequencing; FAD; Flavoprotein; KW Metal-binding; Nitrate assimilation; Oxidoreductase; Periplasm; Repeat; KW Signal. FT SIGNAL 1..38 FT /note="Tat-type signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, FT ECO:0000269|PubMed:1830217" FT CHAIN 39..378 FT /note="Copper-containing nitrite reductase" FT /id="PRO_0000002986" FT DOMAIN 39..213 FT /note="Plastocyanin-like 1" FT DOMAIN 214..378 FT /note="Plastocyanin-like 2" FT BINDING 133 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT BINDING 138 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 copper site" FT BINDING 173 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 copper site" FT BINDING 174 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT BINDING 183 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT BINDING 188 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT BINDING 344 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 copper site" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 76..89 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:6KNG" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 118..125 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:2AVF" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:5AKR" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 156..163 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 168..173 FT /evidence="ECO:0007829|PDB:5AKR" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:2AVF" FT HELIX 180..185 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 189..195 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:6KNG" FT STRAND 211..221 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:5N8I" FT HELIX 237..249 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 254..258 FT /evidence="ECO:0007829|PDB:5AKR" FT TURN 262..265 FT /evidence="ECO:0007829|PDB:5AKR" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 271..274 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 278..288 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 313..317 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 325..332 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 337..345 FT /evidence="ECO:0007829|PDB:5AKR" FT HELIX 346..350 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 355..362 FT /evidence="ECO:0007829|PDB:5AKR" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:5AKR" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:1RZP" SQ SEQUENCE 378 AA; 40771 MW; A70B52B814090EA5 CRC64; MTEQLQMTRR TMLAGAALAG AVAPLLHTAQ AHAAGAAAAA GAAPVDISTL PRVKVDLVKP PFVHAHDQVA KTGPRVVEFT MTIEEKKLVI DREGTEIHAM TFNGSVPGPL MVVHENDYVE LRLINPDTNT LLHNIDFHAA TGALGGGALT QVNPGEETTL RFKATKPGVF VYHCAPEGMV PWHVTSGMNG AIMVLPRDGL KDEKGQPLTY DKIYYVGEQD FYVPKDEAGN YKKYETPGEA YEDAVKAMRT LTPTHIVFNG AVGALTGDHA LTAAVGERVL VVHSQANRDT RPHLIGGHGD YVWATGKFRN PPDLDQETWL IPGGTAGAAF YTFRQPGVYA YVNHNLIEAF ELGAAGHFKV TGEWNDDLMT SVVKPASM //