HAMAP annotation rule: MF_00716
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Accession MF_00716
Dates 2-OCT-2003 (Created)
10-JUN-2011 (Last updated, Version 28)
Data class Protein
Names NosZ



Identifier NOSZ
Protein name
RecName: Full=Nitrous-oxide reductase;
EC=1.7.2.4;
AltName: Full=N(2)OR;
AltName: Full=N2O reductase;
Flags: Precursor;
Gene name nosZ
FUNCTION: Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide (By similarity).
CATALYTIC ACTIVITY: Nitrogen + H(2)O + 2 cytochrome c = nitrous oxide + 2 reduced cytochrome c.
COFACTOR: Binds 2 calcium ions per subunit (By similarity).
COFACTOR: Binds 6 copper ions per subunit. Each subunit contains 2 copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site of nitrous oxide reduction (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Periplasm (By similarity).

case <Feature:PS51318>
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
end case

SIMILARITY: Belongs to the nosZ family.
SIMILARITY: In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family.
Pfam PF00394; Cu-oxidase; 1;
TIGRFAMs TIGR01409; TAT_signal_seq; 1;
PROSITE PS00078; COX2; 1;
PS51318; TAT; 0-1; trigger=PRU00648;
case not <Feature:PS51318>
General Signal; -; 1; trigger=Yes;
end case

GO:0005509; Molecular function: calcium ion binding.
GO:0005507; Molecular function: copper ion binding.
GO:0050304; Molecular function: nitrous-oxide reductase activity.
GO:0042597; Cellular component: periplasmic space.
From: NOSZ_PARDE (Q51705)
Key     From     To       Description   Condition   FTGroup
REGION     554     Cter       COX2-like      
 
METAL     145     145       Copper Z2 (By similarity)   H   1
METAL     146     146       Copper Z3 (By similarity)   H   1
METAL     194     194       Copper Z2 (By similarity)   H   1
 
METAL     271     271       Calcium 2; via carbonyl oxygen (By similarity)   Y   3
METAL     274     274       Calcium 2 (By similarity)   E   3
METAL     282     282       Calcium 2; via carbonyl oxygen (By similarity)   M   3
METAL     288     288       Calcium 2 (By similarity)   D   3
METAL     335     335       Calcium 2 (By similarity)   [NS]   3
 
METAL     337     337       Copper Z1 (By similarity)   H   1
METAL     392     392       Copper Z1 (By similarity)   H   1
METAL     443     443       Copper Z3 (By similarity)   H   1
 
METAL     464     464       Calcium 1; via carbonyl oxygen (By similarity)   K   3
METAL     479     479       Calcium 1 (By similarity)   E   3
 
METAL     504     504       Copper Z4 (By similarity)   H   1
 
METAL     595     595       Copper A1 (By similarity)   H   2
METAL     630     630       Copper A1 (By similarity)   C   2
METAL     630     630       Copper A2 (By similarity)   C   2
METAL     632     632       Copper A2; via carbonyl oxygen (By similarity)   [WH]   2
METAL     634     634       Copper A1 (By similarity)   C   2
METAL     634     634       Copper A2 (By similarity)   C   2
METAL     638     638       Copper A2 (By similarity)   H   2
METAL     641     641       Copper A1 (By similarity)   M   2



Size range: 634-652 amino acids
Related UniRules: None
Template: Q51705 (NOSZ_PARDE); P19573 (NOSZ_PSEST): [Recover all]
Scope: Bacteria
Fusion: Nter: None; Cter: None
Duplicate: None
Plasmid encoded: in CUPNH, RALSO, RHIME

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