ANIA_NEIMA
ID ANIA_NEIMA Reviewed; 386 AA.
AC Q9JTB8; A1IT94;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Copper-containing nitrite reductase;
DE EC=1.7.2.1;
DE Flags: Precursor;
GN Name=aniA; OrderedLocusNames=NMA1887;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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 (By similarity). {ECO:0000250}.
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}.
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DR EMBL; AL157959; CAM09006.1; -; Genomic_DNA.
DR PIR; B81816; B81816.
DR RefSeq; WP_002237256.1; NC_003116.1.
DR AlphaFoldDB; Q9JTB8; -.
DR SMR; Q9JTB8; -.
DR PRIDE; Q9JTB8; -.
DR EnsemblBacteria; CAM09006; CAM09006; NMA1887.
DR KEGG; nma:NMA1887; -.
DR HOGENOM; CLU_031740_1_1_4; -.
DR OMA; APCVGCK; -.
DR BioCyc; NMEN122587:NMA_RS09535-MON; -.
DR Proteomes; UP000000626; 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:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR001287; NO2-reductase_Cu.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR PRINTS; PR00695; CUNO2RDTASE.
DR SUPFAM; SSF49503; SSF49503; 2.
DR TIGRFAMs; TIGR02376; Cu_nitrite_red; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Copper; Lipoprotein; Membrane; Metal-binding;
KW Oxidoreductase; Palmitate; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..386
FT /note="Copper-containing nitrite reductase"
FT /id="PRO_0000002998"
FT DOMAIN 97..191
FT /note="Plastocyanin-like 1"
FT DOMAIN 241..342
FT /note="Plastocyanin-like 2"
FT REPEAT 367..371
FT /note="1"
FT REPEAT 372..376
FT /note="2"
FT REPEAT 377..381
FT /note="3"
FT REGION 363..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..381
FT /note="3 X 5 AA tandem repeats of A-A-S-A-P"
FT BINDING 130
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 135
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 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
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 171
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 179
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 184
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 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 325
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 386 AA; 40390 MW; D0624ED3A3979E88 CRC64;
MKRQALAAII ASMFALAACG GEPAAQTPAA SAEAASSAAQ TAAETPAGEL PVIDAVTTHA
PEVPPAIDRD YPAKVRVKME TVEKTMKMDD GVEYRYWTFD GDVPGRMIRV REGDTVEVEF
SNNPSSTVPH NVDFHAATGQ GGGAAATFTA PGRTSTFSFK ALQPGLYIYH CAVAPVGMHI
ANGMYGLILV EPKEGLPKVD KEFYIVQGDF YTKGKKGAQG LQPFDMDKAI AEQPEYVVFN
GHVGAIAGDN ALKAKAGETV RMYVGNGGPN LVSSFHVIGE IFDKVYVEGG KLINENVQST
IVPAGGSAIV EFKVDIPGSY TLVDHSIFRA FNKGALGQLK VEGAENPEIM TQKLSDTAYA
GNGAAPAASA PAASAPAASA PAKSDY
