AC MF_00716; DC Protein; auto TR HAMAP; MF_00716; -; 1; level=0 XX Names: NosZ XX ID NOSZ 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; XX 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. CC -!- CATALYTIC ACTIVITY: CC Reaction=N2 + 2 Fe(III)-[cytochrome c] + H2O = nitrous oxide + 2 CC Fe(II)-[cytochrome c] + 2 H(+); Xref=Rhea:RHEA:43108, Rhea:RHEA- CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17045, ChEBI:CHEBI:17997, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.4; CC -!- COFACTOR: CC Name=binuclear copper center (CuA); Xref=ChEBI:CHEBI:47357; CC -!- COFACTOR: CC Name=[4Cu-S] cluster; Xref=ChEBI:CHEBI:33730; CC Note=Each subunit contains 2 copper centers; Cu(A) (binuclear) and CC Cu(Z) (tetranuclear, a [4Cu-S] cluster). Cu(Z) is thought to be the CC site of nitrous oxide reduction.; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 2 calcium ions per subunit. The calcium ions appear to have CC a role in dimer formation.; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Periplasm. case CC -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has not been experimentally proven. end case CC -!- SIMILARITY: Belongs to the NosZ family. XX DR Pfam; PF00116; COX2; 0-1; trigger=no DR Pfam; PF13473; Cupredoxin_1; 0-1; trigger=no DR Pfam; PF18764; nos_propeller; 1; trigger=no DR Pfam; PF18793; nos_propeller_2; 1; trigger=no DR NCBIfam; TIGR04244; nitrous_NosZ_RR; 1; trigger=no DR NCBIfam; TIGR01409; TAT_signal_seq; 0-1; trigger=no DR PROSITE; PS00078; COX2; 0-1; trigger=no DR PROSITE; PS50857; COX2_CUA; 1; trigger=no DR PROSITE; PS51318; TAT; 0-1; trigger=yes case not DR General; Signal; -; 1; trigger=yes end case XX KW Calcium KW Copper KW Metal-binding KW Oxidoreductase KW Periplasm KW Signal XX GO GO:0005509; F:calcium ion binding GO GO:0005507; F:copper ion binding GO GO:0050304; F:nitrous-oxide reductase activity GO GO:0042597; C:periplasmic space XX FT From: NOSZ_PARDE (Q51705) FT REGION 554..Cter FT /note="COX2-like" FT BINDING 145 FT /ligand="[4Cu-S] cluster" FT /ligand_id="ChEBI:CHEBI:33730" FT /ligand_label="(CuZ)" FT Group: 1; Condition: H FT BINDING 146 FT /ligand="[4Cu-S] cluster" FT /ligand_id="ChEBI:CHEBI:33730" FT /ligand_label="(CuZ)" FT Group: 1; Condition: H FT BINDING 194 FT /ligand="[4Cu-S] cluster" FT /ligand_id="ChEBI:CHEBI:33730" FT /ligand_label="(CuZ)" FT Group: 1; Condition: H FT BINDING 271 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT Group: 3; Condition: Y FT BINDING 274 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT Group: 3; Condition: E FT BINDING 282 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT Optional; Group: 3; Condition: M FT BINDING 288 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT Group: 3; Condition: D FT BINDING 335 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT Group: 3; Condition: [NS] FT BINDING 337 FT /ligand="[4Cu-S] cluster" FT /ligand_id="ChEBI:CHEBI:33730" FT /ligand_label="(CuZ)" FT Group: 1; Condition: H FT BINDING 392 FT /ligand="[4Cu-S] cluster" FT /ligand_id="ChEBI:CHEBI:33730" FT /ligand_label="(CuZ)" FT Group: 1; Condition: H FT BINDING 443 FT /ligand="[4Cu-S] cluster" FT /ligand_id="ChEBI:CHEBI:33730" FT /ligand_label="(CuZ)" FT Group: 1; Condition: H FT BINDING 464 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT Group: 4; Condition: K FT BINDING 479 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT Group: 4; Condition: [ED] FT BINDING 504 FT /ligand="[4Cu-S] cluster" FT /ligand_id="ChEBI:CHEBI:33730" FT /ligand_label="(CuZ)" FT Group: 1; Condition: H FT BINDING 595 FT /ligand="binuclear copper center (CuA)" FT /ligand_id="ChEBI:CHEBI:47357" FT Group: 2; Condition: H FT BINDING 630 FT /ligand="binuclear copper center (CuA)" FT /ligand_id="ChEBI:CHEBI:47357" FT Group: 2; Condition: C FT BINDING 632 FT /ligand="binuclear copper center (CuA)" FT /ligand_id="ChEBI:CHEBI:47357" FT Group: 2; Condition: [WNH] FT BINDING 634 FT /ligand="binuclear copper center (CuA)" FT /ligand_id="ChEBI:CHEBI:47357" FT Group: 2; Condition: C FT BINDING 638 FT /ligand="binuclear copper center (CuA)" FT /ligand_id="ChEBI:CHEBI:47357" FT Group: 2; Condition: H FT BINDING 641 FT /ligand="binuclear copper center (CuA)" FT /ligand_id="ChEBI:CHEBI:47357" FT Group: 2; Condition: M XX Size: 610-670; Related: None; Template: Q51705; P19573; Scope: Bacteria; Pseudomonadati Fusion: Nter: None Cter: None Duplicate: None Plasmid: in CUPNH, RALN1, RHIME Comments: None XX # Version: 40 # Last updated date: 2025-10-02 # Created date: 2005-02-28 //