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NOSZ_RALSO
ID   NOSZ_RALSO              Reviewed;         646 AA.
AC   Q8XQB8;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Nitrous-oxide reductase;
DE            EC=1.7.2.4;
DE   AltName: Full=N(2)OR;
DE   AltName: Full=N2O reductase;
DE   Flags: Precursor;
GN   Name=nosZ; OrderedLocusNames=RSp1368; ORFNames=RS02090;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
CC   -!- FUNCTION: Nitrous-oxide reductase is part of a bacterial respiratory
CC       system which is activated under anaerobic conditions in the presence of
CC       nitrate or nitrous oxide. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c]
CC         + 2 H(+) + nitrous oxide; Xref=Rhea:RHEA:43108, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17045, ChEBI:CHEBI:17997, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=1.7.2.4;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 6 Cu cations per subunit. Each subunit contains 2 copper
CC       centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought
CC       to be the site of nitrous oxide reduction. {ECO:0000250};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC       dinitrogen from nitrate: step 4/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
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 NosZ family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC       oxidase subunit 2 family. {ECO:0000305}.
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DR   EMBL; AL646053; CAD18519.1; -; Genomic_DNA.
DR   RefSeq; WP_011004618.1; NC_003296.1.
DR   AlphaFoldDB; Q8XQB8; -.
DR   SMR; Q8XQB8; -.
DR   STRING; 267608.RSp1368; -.
DR   PRIDE; Q8XQB8; -.
DR   EnsemblBacteria; CAD18519; CAD18519; RSp1368.
DR   GeneID; 60504275; -.
DR   KEGG; rso:RSp1368; -.
DR   PATRIC; fig|267608.8.peg.4846; -.
DR   eggNOG; COG4263; Bacteria.
DR   HOGENOM; CLU_016420_0_0_4; -.
DR   OMA; HQEMQGY; -.
DR   UniPathway; UPA00652; UER00709.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0050304; F:nitrous-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR   CDD; cd04223; N2OR_C; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   HAMAP; MF_00716; NosZ; 1.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR028096; EfeO_Cupredoxin.
DR   InterPro; IPR011045; N2O_reductase_N.
DR   InterPro; IPR034205; N2OR_C.
DR   InterPro; IPR023644; NO_Rdtase.
DR   InterPro; IPR041114; Nos_propeller.
DR   InterPro; IPR041142; NOS_propeller_2.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF13473; Cupredoxin_1; 1.
DR   Pfam; PF18764; nos_propeller; 1.
DR   Pfam; PF18793; nos_propeller_2; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   SUPFAM; SSF50974; SSF50974; 1.
DR   TIGRFAMs; TIGR04244; nitrous_NosZ_RR; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Calcium; Copper; Metal-binding; Oxidoreductase; Periplasm; Plasmid;
KW   Reference proteome; Signal.
FT   SIGNAL          1..52
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255"
FT   CHAIN           53..646
FT                   /note="Nitrous-oxide reductase"
FT                   /id="PRO_0000019832"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..646
FT                   /note="COX2-like"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z2"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z3"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z2"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         275
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z1"
FT                   /evidence="ECO:0000250"
FT   BINDING         400
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z1"
FT                   /evidence="ECO:0000250"
FT   BINDING         452
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z3"
FT                   /evidence="ECO:0000250"
FT   BINDING         473
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         513
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z4"
FT                   /evidence="ECO:0000250"
FT   BINDING         592
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250"
FT   BINDING         627
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250"
FT   BINDING         627
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250"
FT   BINDING         629
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250"
FT   BINDING         631
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250"
FT   BINDING         631
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250"
FT   BINDING         635
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT                   /evidence="ECO:0000250"
FT   BINDING         638
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   646 AA;  71307 MW;  82A70B60D48271E0 CRC64;
     MMSKHPHSPS TPQDETPSVP GRRRFMNSAA LAGLATVVAC TDKGAPAGSA AATGVAATAE
     EHTVAGLHPK PGQLDTYYGL WSGGHTGDMR VMGMPSGREI HRIPMFVPDA LVGWGITNES
     KKVMGTRPDG RLKYTVGDTH HVHASYKDGN YDGRYAWIND KINSRLGRVR LDYFICDKIT
     ELPNVQGFHG IFPDKRDPVD PQINYTTRVF CGGEFAIPLP NTAGIDDPAK YRSLFTCVDA
     ESMEVRWQVL IDGNCDLVAT SYDGKLAATN QYNTEMGAHY EDMMSAERDA CLFFNVARIE
     AAVKAGRFKT IGDSKVPVVD GTHAANQDPK TALTAYVSVP KNPHGVNASP DQKYFICAGK
     LSPTATVIEL ARVLDWFDGK LAKIDDAIVA EVELGLGPLH TAFDGRGNAY TTLFLDSQIV
     KWNIDAAIRF HKGDKNAKYV VDRLDVHYQP GHLNASQSET VAADGKFLAV GCKFSKDRFL
     PVGPLHPENE QFIDISGDKM VLLQDHPIRS EPHDFIIFKR ELLHPKQIYS LDDFPLATKD
     PKQSGVVRNG KKVTVRLTSQ APSYSLREFK LKKGDEVTLI LTNLDKVEDL THGFAIPKYD
     INFIVNPQET ASVTFIADKP GVFWCYCTHF CHALHLEMRS RMIVEA
 
 
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