ID A0A0N0MBW9_9HYPH Unreviewed; 376 AA. AC A0A0N0MBW9; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 03-MAY-2023, entry version 21. DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290, ECO:0000256|RuleBase:RU365025}; DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882, ECO:0000256|RuleBase:RU365025}; GN ORFNames=AE618_13735 {ECO:0000313|EMBL:KPH80379.1}; OS Bosea vaviloviae. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; Boseaceae; OC Bosea. OX NCBI_TaxID=1526658 {ECO:0000313|EMBL:KPH80379.1, ECO:0000313|Proteomes:UP000037822}; RN [1] {ECO:0000313|EMBL:KPH80379.1, ECO:0000313|Proteomes:UP000037822} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SD260 {ECO:0000313|EMBL:KPH80379.1, RC ECO:0000313|Proteomes:UP000037822}; RA Tan N.E.H., Lee Y.P., Gan H.M., Barton H., Savka M.A.; RT "Whole genome sequencing of Bosea vaviloviae isolated from cave pool."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. 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 ECO:0000256|RuleBase:RU365025}; CC -!- COFACTOR: CC Name=Cu(+); Xref=ChEBI:CHEBI:49552; CC Evidence={ECO:0000256|RuleBase:RU365025}; CC Note=Binds 1 Cu(+) ion. {ECO:0000256|RuleBase:RU365025}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000256|RuleBase:RU365025}; CC Note=Binds 1 Cu(+) ion. {ECO:0000256|RuleBase:RU365025}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974}; CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification); CC dinitrogen from nitrate: step 2/4. {ECO:0000256|ARBA:ARBA00005127}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233, CC ECO:0000256|RuleBase:RU365025}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC {ECO:0000256|ARBA:ARBA00010609, ECO:0000256|RuleBase:RU365025}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KPH80379.1}. 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; LGSZ01000042; KPH80379.1; -; Genomic_DNA. DR RefSeq; WP_054209634.1; NZ_LGSZ01000042.1. DR AlphaFoldDB; A0A0N0MBW9; -. DR EnsemblBacteria; KPH80379; KPH80379; AE618_13735. DR PATRIC; fig|1526658.3.peg.2674; -. DR OrthoDB; 9757546at2; -. DR UniPathway; UPA00652; UER00707. DR Proteomes; UP000037822; Unassembled WGS sequence. 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 Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 2. DR InterPro; IPR001117; Cu-oxidase_2nd. DR InterPro; IPR011707; Cu-oxidase_N. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR001287; NO2-reductase_Cu. DR InterPro; IPR006311; TAT_signal. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07732; Cu-oxidase_3; 1. DR PRINTS; PR00695; CUNO2RDTASE. DR SUPFAM; SSF49503; Cupredoxins; 2. DR TIGRFAMs; TIGR02376; Cu_nitrite_red; 1. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|PIRSR:PIRSR601287-1, ECO:0000256|RuleBase:RU365025}; KW FAD {ECO:0000256|ARBA:ARBA00022827}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR601287-1, KW ECO:0000256|RuleBase:RU365025}; KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063}; KW Oxidoreductase {ECO:0000256|RuleBase:RU365025}; KW Signal {ECO:0000256|RuleBase:RU365025}. FT SIGNAL 1..31 FT /evidence="ECO:0000256|RuleBase:RU365025" FT CHAIN 32..376 FT /note="Copper-containing nitrite reductase" FT /evidence="ECO:0000256|RuleBase:RU365025" FT /id="PRO_5015211562" FT DOMAIN 89..195 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07732" FT DOMAIN 211..361 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF00394" FT BINDING 131 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 136 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 copper site" FT /evidence="ECO:0000256|PIRSR:PIRSR601287-1" FT BINDING 171 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 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 181 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 186 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 342 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 copper site" FT /evidence="ECO:0000256|PIRSR:PIRSR601287-1" SQ SEQUENCE 376 AA; 40354 MW; E6F1A754D03B6BB0 CRC64; MGEDFKLSRR TVLAGAAAAG ALAQSAATAQ AQAPAVLTGA TAADIAKLPR VKPKLVDPPF VQAHQQVATD GPKVVEFEMT IHEKKIVLDD AGTETFAFTF NGTVPGPLMV VHEGDYVELT LINADTNELM HNIDFHSSTG ALGGGALTEV GPGEKVVLRW KATRPGVFVY HCAPPGMVPW HVTAGMNGAV MVLPRDGLKD HQGKPLKYDR VYYVGEQDFY VPRGADGKFK RYASPGEAHE DVIKTMRTLT PSHIVFNGKV GALTGKNALT AKVGETVLIV HSQANRDTRP HLIGGHGDYV WASGKFRNPP ERDLETWFIP GGCAGAALYT FLQPGIYAYV NHNLIEAFEL GAAGHFKVEG AWNDALMKQI RAPAGI //