HAMAP rule MF_02236
General rule information
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| Accession | MF_02236 |
| Dates | 16-OCT-2019 (Created)
2-SEP-2024 (Last updated, Version 5) |
| Name | ACDase |
| Scope(s) |
Bacteria |
| Template(s) | Q8P8J5 (ACDAS_XANCP); [ Recover all ] |
| Triggered by |
HAMAP; MF_02236 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | ACDAS |
| Protein name | RecName: Full=N-acetyl-L-citrulline deacetylase; Short=ACDase; Short=Acetylcitrulline deacetylase; EC=3.5.1.-; |
| Gene name | Name=argE'; |
Comments
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| FUNCTION | Catalyzes the deacetylation of N-acetyl-L-citrulline to produce L-citrulline. This is a step in an alternative arginine biosynthesis pathway. |
| CATALYTIC ACTIVITY | Reaction=N(2)-acetyl-L-citrulline + H2O = L-citrulline + acetate; Xref=Rhea:RHEA:61092, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57743, ChEBI:CHEBI:58765; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61093; |
| COFACTOR | Name=Co(2+); Xref=ChEBI:CHEBI:48828; Note=Binds 1 Co(2+) ion per subunit.; |
| PATHWAY | Amino-acid biosynthesis; L-arginine biosynthesis. |
| SIMILARITY | Belongs to the peptidase M20A family. N-acetylcitrulline deacetylase subfamily. |
Keywords
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Gene Ontology
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| GO:0016811; Molecular function:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| GO:0050897; Molecular function:cobalt ion binding |
| GO:0006526; Biological process:arginine biosynthetic process |
Cross-references
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Features
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| From: ACDAS_XANCP (Q8P8J5) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 130 | 130 | /note="Proton donor/acceptor" | E | ||||||||
| BINDING | 72 | 72 | /ligand="Co(2+)" /ligand_id="ChEBI:CHEBI:48828" |
H | ||||||||
| BINDING | 103 | 103 | /ligand="Co(2+)" /ligand_id="ChEBI:CHEBI:48828" |
D | ||||||||
| BINDING | 155 | 155 | /ligand="Co(2+)" /ligand_id="ChEBI:CHEBI:48828" |
E | ||||||||
Additional information
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| Size range | 335-420 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |