NIR_RHISU
ID NIR_RHISU Reviewed; 377 AA.
AC Q60214;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Rhizobium sullae (Rhizobium hedysari).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=50338;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HCNT1;
RX PubMed=8899992; DOI=10.1128/aem.62.11.4019-4025.1996;
RA Toffanin A., Wu Q., Maskus M., Caselia S., Abruna H.D., Shapleigh J.P.;
RT "Characterization of the gene encoding nitrite reductase and the
RT physiological consequences of its expression in the nondenitrifying
RT Rhizobium 'hedysari' strain HCNT1.";
RL Appl. Environ. Microbiol. 62:4019-4025(1996).
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(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 1 Cu(2+) ion. The Cu(2+) ion is held by residues from each
CC of 2 monomers of the trimer. Nitrite is bound to the Cu(2+) ion site.
CC Pseudoazurin is the physiological electron donor for the Cu-NIR in
CC vitro. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552; Evidence={ECO:0000250};
CC Note=Binds 1 Cu(+) ion. The Cu(+) ion is bound within a single monomer.
CC {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC dinitrogen from nitrate: step 2/4.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
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 not been experimentally proven.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; U65658; AAB05880.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60214; -.
DR SMR; Q60214; -.
DR STRING; 1041146.ATZB01000007_gene3032; -.
DR UniPathway; UPA00652; UER00707.
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 Gene3D; 2.60.40.420; -; 2.
DR InterPro; IPR001117; Cu-oxidase.
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; SSF49503; 2.
DR TIGRFAMs; TIGR02376; Cu_nitrite_red; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Copper; FAD; Flavoprotein; Metal-binding; Nitrate assimilation;
KW Oxidoreductase; Periplasm; Repeat; Signal.
FT SIGNAL 1..35
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 36..377
FT /note="Copper-containing nitrite reductase"
FT /id="PRO_0000002990"
FT DOMAIN 99..194
FT /note="Plastocyanin-like 1"
FT DOMAIN 259..360
FT /note="Plastocyanin-like 2"
FT BINDING 132
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 137
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 172
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 173
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 182
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 187
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 343
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
SQ SEQUENCE 377 AA; 40719 MW; C7AFEE9AE639E2F8 CRC64;
MTNTLQMTRR TMLTGAAVAG ALTPILTSGG GNASPTPVRK LSATEIAALP RRKLDLVKPP
FVHVHTQKAE GGPKVVEVTL TIEEKKLVID GKGTEVNAMT FDGSVPGPLI VVHQDDYVEV
TLVNPETNTL QHNIDFHSAT GALGGGALTV VNPGESAVLR FKATKAGVFV YHCAPPGMVP
WHVTSGMNGA IMVLPREGLT DGHGKELVYD KVYYLGEQDF YIPRDEKGEF KKYDSPGEAY
EDTVAVMRTL TPTHIVFNGA VGALTGENAL TAAVGERVLI VHSQANRDTR PHLIGGHGEY
VWRTGKFVNV PDRDQETWFI PGPTRGAAYY TFEQPGIYAY VNHNLIEAFE LGAAAHFKVT
GDWNDDLMTT VRSPSGS
