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=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;
CC       Note=Binds 2 calcium ions per subunit.;
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
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.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
case <Feature:PS51318>
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.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC       oxidase subunit 2 family.
XX
DR   Pfam; PF00394; Cu-oxidase; 1; trigger=no
DR   NCBIfam; TIGR04244; nitrous_NosZ_RR; 1; trigger=no
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1; trigger=no
DR   PROSITE; PS00078; COX2; 1; trigger=no
DR   PROSITE; PS51318; TAT; 0-1; trigger=yes
case not <Feature:PS51318>
DR   General; Signal; -; 1; trigger=yes
end case
XX
KW   Oxidoreductase
KW   Periplasm
KW   Metal-binding
KW   Calcium
KW   Copper
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="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z2"
FT   Group: 1; Condition: H
FT   BINDING         146
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z3"
FT   Group: 1; Condition: H
FT   BINDING         194
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z2"
FT   Group: 1; Condition: H
FT   BINDING         271
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Group: 3; Condition: Y
FT   BINDING         274
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Group: 3; Condition: E
FT   BINDING         282
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Group: 3; Condition: M
FT   BINDING         288
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Group: 3; Condition: D
FT   BINDING         335
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Group: 3; Condition: [NS]
FT   BINDING         337
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z1"
FT   Group: 1; Condition: H
FT   BINDING         392
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z1"
FT   Group: 1; Condition: H
FT   BINDING         443
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z3"
FT   Group: 1; Condition: H
FT   BINDING         464
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   Group: 3; Condition: K
FT   BINDING         479
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   Group: 3; Condition: E
FT   BINDING         504
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="Z4"
FT   Group: 1; Condition: H
FT   BINDING         595
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT   Group: 2; Condition: H
FT   BINDING         630
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT   Group: 2; Condition: C
FT   BINDING         630
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT   Group: 2; Condition: C
FT   BINDING         632
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT   Group: 2; Condition: [WH]
FT   BINDING         634
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT   Group: 2; Condition: C
FT   BINDING         634
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT   Group: 2; Condition: C
FT   BINDING         638
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A2"
FT   Group: 2; Condition: H
FT   BINDING         641
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A1"
FT   Group: 2; Condition: M
XX
Size: 634-652;
Related: None;
Template: Q51705; P19573;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in CUPNH, RALN1, RHIME
Comments: None
XX
# Revision 1.41 2023/11/28
//