ID ANIA_NEIMB Reviewed; 390 AA. AC Q9JYE1; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=Copper-containing nitrite reductase; DE EC=1.7.2.1; DE Flags: Precursor; GN Name=aniA; OrderedLocusNames=NMB1623; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). RN [2] RP FUNCTION. RC STRAIN=MC58; RX PubMed=12003939; DOI=10.1128/jb.184.11.2987-2993.2002; RA Anjum M.F., Stevanin T.M., Read R.C., Moir J.W.B.; RT "Nitric oxide metabolism in Neisseria meningitidis."; RL J. Bacteriol. 184:2987-2993(2002). CC -!- FUNCTION: Catalyzes the reduction of nitrite to nitric oxide (NO). It CC could be essential for growth and survival in oxygen-depleted CC environments. {ECO:0000269|PubMed:12003939}. 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(+); Xref=ChEBI:CHEBI:49552; Evidence={ECO:0000250}; CC Note=Binds 1 Cu(+) ion. {ECO:0000250}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250}; CC Note=Binds 1 Cu(2+) ion. {ECO:0000250}; CC -!- SUBUNIT: Homotrimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}. 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; AE002098; AAF41975.1; -; Genomic_DNA. DR PIR; E81062; E81062. DR RefSeq; NP_274629.1; NC_003112.2. DR RefSeq; WP_002225006.1; NC_003112.2. DR AlphaFoldDB; Q9JYE1; -. DR SMR; Q9JYE1; -. DR STRING; 122586.NMB1623; -. DR PaxDb; 122586-NMB1623; -. DR KEGG; nme:NMB1623; -. DR PATRIC; fig|122586.8.peg.2084; -. DR HOGENOM; CLU_031740_1_1_4; -. DR InParanoid; Q9JYE1; -. DR OrthoDB; 9757546at2; -. DR BRENDA; 1.7.2.1; 3593. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0009279; C:cell outer membrane; 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:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0071281; P:cellular response to iron ion; EXP:CollecTF. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro. DR CDD; cd04201; CuRO_1_CuNIR_like; 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; 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; PF07732; Cu-oxidase_3; 1. DR PRINTS; PR00695; CUNO2RDTASE. DR SUPFAM; SSF49503; Cupredoxins; 2. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell outer membrane; Copper; Lipoprotein; Membrane; Metal-binding; KW Oxidoreductase; Palmitate; Reference proteome; Repeat; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303" FT CHAIN 19..390 FT /note="Copper-containing nitrite reductase" FT /id="PRO_0000002999" FT DOMAIN 101..195 FT /note="Plastocyanin-like 1" FT DOMAIN 245..346 FT /note="Plastocyanin-like 2" FT REPEAT 371..375 FT /note="1" FT REPEAT 376..380 FT /note="2" FT REPEAT 381..385 FT /note="3" FT REGION 30..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 367..390 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 371..385 FT /note="3 X 5 AA tandem repeats of A-A-S-A-P" FT BINDING 134 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 copper site" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 174 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 copper site" FT /evidence="ECO:0000250" FT BINDING 175 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000250" FT BINDING 183 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000250" FT BINDING 188 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="1" FT /note="type 1 copper site" FT /evidence="ECO:0000250" FT BINDING 280 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 329 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="2" FT /note="type 2 copper site" FT /evidence="ECO:0000250" FT LIPID 19 FT /note="N-palmitoyl cysteine" FT /evidence="ECO:0000305" FT LIPID 19 FT /note="S-diacylglycerol cysteine" FT /evidence="ECO:0000305" SQ SEQUENCE 390 AA; 40763 MW; C503F9D47DD1169D CRC64; MKRQALAAMI ASLFALAACG GEPAAQAPAE TPAAAAEAAS SAAQTAAETP SGELPVIDAV TTHAPEVPPA IDRDYPAKVR VKMETVEKTM TMEDGVEYRY WTFDGDVPGR MIRVREGDTV EVEFSNNPSS TVPHNVDFHA ATGQGGGAAA TFTAPGRTST FSFKALQPGL YIYHCAVAPV GMHIANGMYG LILVEPKEGL PKVDKEFYIV QGDFYTKGKK GAQGLQPFDM DKAVAEQPEY VVFNGHVGAI AGDNALKAKA GETVRMYVGN GGPNLVSSFH VIGEIFDKVY VEGGKLINEN VQSTIVPAGG SAIVEFKVDI PGSYTLVDHS IFRAFNKGAL GQLKVEGAEN PEIMTQKLSD TAYAGNGAAP AASAPAASAP AASASEKSVY //