HAMAP rule MF_00716
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00716 |
| Accession | MF_00716 |
| Dates | 28-FEB-2005 (Created)
02-SEP-2024 (Last updated, Version 39) |
| Name | NosZ |
| Scope(s) |
Bacteria |
| Template(s) | Q51705; P19573; [ Recover all ] |
| Triggered by |
HAMAP; MF_00716 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| 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 | Name=nosZ; |
Comments
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| 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. |
| CATALYTIC ACTIVITY | Reaction=N2 + 2 Fe(III)-[cytochrome c] + H2O = nitrous oxide + 2 Fe(II)-[cytochrome c] + 2 H(+); Xref=Rhea:RHEA:43108, Rhea:RHEA- COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17045, ChEBI:CHEBI:17997, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.4; |
| COFACTOR | Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; |
| COFACTOR | Name=Cu cation; Xref=ChEBI:CHEBI:23378; Note=Binds 6 Cu cations 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.; |
| SUBUNIT | Homodimer. |
| SUBCELLULAR LOCATION | Periplasm. |
| 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. |
Keywords
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Gene Ontology
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| 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 |
Cross-references
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| Pfam | PF00394; Cu-oxidase; 1; |
| NCBIfam | TIGR04244; nitrous_NosZ_RR; 1; |
| NCBIfam | TIGR01409; TAT_signal_seq; 1; |
| PROSITE | PS00078; COX2; 1; |
| PROSITE | PS51318; TAT; 0-1; |
| General | Signal; -; 1; |
Features
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| From: NOSZ_PARDE (Q51705) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| REGION | 554 | Cter | /note="COX2-like" | |||||||||
| BINDING | 145 | 145 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="Z2" |
H | 1 | |||||||
| BINDING | 146 | 146 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="Z3" |
H | 1 | |||||||
| BINDING | 194 | 194 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="Z2" |
H | 1 | |||||||
| BINDING | 271 | 271 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="2" |
Y | 3 | |||||||
| BINDING | 274 | 274 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="2" |
E | 3 | |||||||
| BINDING | 282 | 282 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="2" |
M | 3 | |||||||
| BINDING | 288 | 288 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="2" |
D | 3 | |||||||
| BINDING | 335 | 335 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="2" |
[NS] | 3 | |||||||
| BINDING | 337 | 337 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="Z1" |
H | 1 | |||||||
| BINDING | 392 | 392 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="Z1" |
H | 1 | |||||||
| BINDING | 443 | 443 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="Z3" |
H | 1 | |||||||
| BINDING | 464 | 464 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="1" |
K | 3 | |||||||
| BINDING | 479 | 479 | /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="1" |
E | 3 | |||||||
| BINDING | 504 | 504 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="Z4" |
H | 1 | |||||||
| BINDING | 595 | 595 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="A1" |
H | 2 | |||||||
| BINDING | 630 | 630 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="A1" |
C | 2 | |||||||
| BINDING | 630 | 630 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="A2" |
C | 2 | |||||||
| BINDING | 632 | 632 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="A2" |
[WH] | 2 | |||||||
| BINDING | 634 | 634 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="A1" |
C | 2 | |||||||
| BINDING | 634 | 634 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="A2" |
C | 2 | |||||||
| BINDING | 638 | 638 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="A2" |
H | 2 | |||||||
| BINDING | 641 | 641 | /ligand="Cu cation" /ligand_id="ChEBI:CHEBI:23378" /ligand_label="A1" |
M | 2 | |||||||
Additional information
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| Size range | 634-652 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |