ID A0A1W6VP04_GEOTD Unreviewed; 352 AA. AC A0A1W6VP04; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 24-JAN-2024, entry version 24. DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290}; DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882}; GN Name=nirK {ECO:0000313|EMBL:ARP41763.1}; GN ORFNames=GTHT12_00198 {ECO:0000313|EMBL:ARP41763.1}; OS Geobacillus thermodenitrificans. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=33940 {ECO:0000313|EMBL:ARP41763.1, ECO:0000313|Proteomes:UP000194134}; RN [1] {ECO:0000313|EMBL:ARP41763.1, ECO:0000313|Proteomes:UP000194134} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T12 {ECO:0000313|EMBL:ARP41763.1, RC ECO:0000313|Proteomes:UP000194134}; RA Daas M.J.A., Vriesendorp B., van de Weijer A.H.P., van der Oost J., RA van Kranenburg R.; RT "Complete genome sequence of Geobacillus thermodenitrificans T12, a RT potential host for biotechnological applications."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:5YTL, ECO:0007829|PDB:5YTM} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 31-352. RX PubMed=30082512; DOI=10.1107/S2059798318010082; RA Fukuda Y., Matsusaki T., Tse K.M., Mizohata E., Murphy M.E.P., Inoue T.; RT "Crystallographic study of dioxygen chemistry in a copper-containing RT nitrite reductase from Geobacillus thermodenitrificans."; RL Acta Crystallogr. D Struct. Biol. 74:769-777(2018). RN [3] {ECO:0007829|PDB:6L46} RP STRUCTURE (1.30 ANGSTROMS) OF 31-352. RX PubMed=32041886; DOI=10.1073/pnas.1918125117; RA Fukuda Y., Hirano Y., Kusaka K., Inoue T., Tamada T.; RT "High-resolution neutron crystallography visualizes an OH-bound resting RT state of a copper-containing nitrite reductase."; RL Proc. Natl. Acad. Sci. U.S.A. 117:4071-4077(2020). 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 Evidence={ECO:0000256|ARBA:ARBA00029301}; CC -!- COFACTOR: CC Name=Cu(+); Xref=ChEBI:CHEBI:49552; CC Evidence={ECO:0000256|ARBA:ARBA00001960, CC ECO:0000256|PIRSR:PIRSR601287-1}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000256|ARBA:ARBA00001973, CC ECO:0000256|PIRSR:PIRSR601287-1}; CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}. 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; CP020030; ARP41763.1; -; Genomic_DNA. DR RefSeq; WP_008879019.1; NZ_PIZS01000077.1. DR PDB; 5YTL; X-ray; 1.40 A; A=31-352. DR PDB; 5YTM; X-ray; 1.50 A; A=31-352. DR PDB; 5YTN; X-ray; 1.75 A; A=31-352. DR PDB; 6L46; Other; 1.30 A; A=31-352. DR PDBsum; 5YTL; -. DR PDBsum; 5YTM; -. DR PDBsum; 5YTN; -. DR PDBsum; 6L46; -. DR AlphaFoldDB; A0A1W6VP04; -. DR SMR; A0A1W6VP04; -. DR STRING; 33940.GTHT12_00198; -. DR OMA; PFIRVRE; -. DR Proteomes; UP000194134; Chromosome. 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:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR CDD; cd11020; CuRO_1_CuNIR; 1. DR CDD; cd04208; CuRO_2_CuNIR; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1. DR InterPro; IPR011707; Cu-oxidase-like_N. DR InterPro; IPR011706; Cu-oxidase_C. DR InterPro; IPR045087; Cu-oxidase_fam. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR001287; NO2-reductase_Cu. DR PANTHER; PTHR11709:SF394; FI03373P-RELATED; 1. DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1. DR Pfam; PF07731; Cu-oxidase_2; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR PRINTS; PR00695; CUNO2RDTASE. DR SUPFAM; SSF49503; Cupredoxins; 2. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:5YTL, ECO:0007829|PDB:5YTM}; KW Copper {ECO:0000256|PIRSR:PIRSR601287-1}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601287-1}; KW Oxidoreductase {ECO:0000313|EMBL:ARP41763.1}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..352 FT /note="Copper-containing nitrite reductase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5038966358" FT DOMAIN 78..187 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07732" FT DOMAIN 220..339 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07731" FT BINDING 124 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000256|PIRSR:PIRSR601287-1" FT BINDING 129 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000256|PIRSR:PIRSR601287-1" 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:0000256|PIRSR:PIRSR601287-1" FT BINDING 164 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000256|PIRSR:PIRSR601287-1" FT BINDING 172 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000256|PIRSR:PIRSR601287-1" FT BINDING 177 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000256|PIRSR:PIRSR601287-1" FT BINDING 323 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000256|PIRSR:PIRSR601287-1" SQ SEQUENCE 352 AA; 38382 MW; 5C243800B5B14094 CRC64; MNRNVYAVLS TVLAASLLAA CNSGGEQVKA ESKNKTAATQ QSEPNVIAAH KGVNQAPVPL KMERVGPHDV HIEMTAQITD IEIDKGKIYK AWTFNGQAPG PLVVVNEGDT IHFTLKNMDP VVPHSMDFHA VHASPSKDFI DVMPNKSGTF TYPANKPGVF MYHCGTKPVL QHIANGMHGV IIVKPKNGYP TDKEVDREYV LIQNEWYKYN DMNDFQNGVP SYVVFSSKAL KPGDPNTNGD TFTLKEKPLL AKVGEKIRLY INNVGPNEVS SFHVVGTVFD DVYLDGNPNN HLQGMQTVML PASGGAVVEF TVTRPGTYPI VTHQFNHAQK GAVAMLKVTE TGEDDGTETS GH //