ID Q8YQ92_NOSS1 Unreviewed; 338 AA.
AC Q8YQ92;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Copper-containing nitrite reductase {ECO:0000256|ARBA:ARBA00017290};
DE EC=1.7.2.1 {ECO:0000256|ARBA:ARBA00011882};
GN OrderedLocusNames=all3942 {ECO:0000313|EMBL:BAB75641.1};
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB75641.1, ECO:0000313|Proteomes:UP000002483};
RN [1] {ECO:0000313|EMBL:BAB75641.1, ECO:0000313|Proteomes:UP000002483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576
RC {ECO:0000313|Proteomes:UP000002483};
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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}.
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DR EMBL; BA000019; BAB75641.1; -; Genomic_DNA.
DR PIR; AG2298; AG2298.
DR RefSeq; WP_010998083.1; NZ_RSCN01000045.1.
DR AlphaFoldDB; Q8YQ92; -.
DR STRING; 103690.gene:10495984; -.
DR KEGG; ana:all3942; -.
DR eggNOG; COG2132; Bacteria.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd11024; CuRO_1_2DMCO_NIR_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 2.
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:SF218; 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.
PE 4: Predicted;
KW Copper {ECO:0000256|PIRSR:PIRSR601287-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601287-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..198
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 202..329
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT BINDING 136
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 141
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 175
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 176
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 184
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 338 AA; 38409 MW; AFBF1BB9D01627F7 CRC64;
MPNNFNLGRR EFWTRRQLLK LGLGGIGVAG AAALWQTLNS QGKSIVKVPQ MKMDAADKVA
QPMRMLREFD YGTLKQENGR TIREFQLTAG TSVIQLNSAV SYNIWDLNGR IPGPTLRAKQ
GDRIRVLFHN QAGHSHSLHF HGVHPAEMDG VRPVSNNSAT IYEFDAEPYG VHLYHCHIEP
VTRHIAKGLY GMFIIDPPTP RPPADEIVLV MAGYDVDDNS HNDFYAFNGL PHHYMDNPIQ
IYQNQLIRLY VLNIIEYDPA VTFHLHANFF DVYRYGMSMK ASEKTDVITM GVAERHILEF
AFRYPGKYMF HPHQDAIAEN GCMGQFEVVA NNNQNHSN
//
