HAMAP rule MF_01989
General rule information
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Accession | MF_01989 |
Dates | 24-MAR-2017 (Created)
29-NOV-2023 (Last updated, Version 12) |
Name | Cyc_amidohydrol |
Scope(s) |
Bacteria Eukaryota Fungi |
Template(s) | P58329 (CAH_PSESD); A8IKD2 (CAH_AZOC5); E3JD18 (CYAH_PSEI1); Q8RSQ2 (BAH_RHOER); [ Recover all ] |
Triggered by |
HAMAP; MF_01989 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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case <FTTag:CAH1> and <FTTag:CAH2> and <FTTag:CAH3> and <FTTag:CAH4> | |
Identifier | CAH |
Protein name | RecName: Full=Cyanuric acid amidohydrolase; Short=CAH; EC=3.5.2.15; |
else case <FTTag:BAH1> and <FTTag:BAH2> and <FTTag:BAH3> and <FTTag:BAH4> | |
Identifier | BAH |
Protein name | RecName: Full=Barbiturase; EC=3.5.2.1; AltName: Full=Barbituric acid hydrolase; Short=BAH; |
else | |
Identifier | CYAH |
Protein name | RecName: Full=Cyclic amide hydrolase; Short=CyAH; EC=3.5.2.-; AltName: Full=Ring-opening amidohydrolase; |
end case |
Comments
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case <FTTag:CAH1> and <FTTag:CAH2> and <FTTag:CAH3> and <FTTag:CAH4> | |
FUNCTION | Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6- trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret. |
CATALYTIC ACTIVITY | Reaction=cyanurate + H2O = 1-carboxybiuret + H(+); Xref=Rhea:RHEA:70363, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:38028, ChEBI:CHEBI:142864; EC=3.5.2.15; |
ACTIVITY REGULATION | Inhibited by barbituric acid. |
PATHWAY | Xenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1. |
DOMAIN | The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer, the active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. It is possible that any or all of the three active- site serines may act as nucleophile (albeit only one can do so per catalytic cycle). |
else case <FTTag:BAH1> and <FTTag:BAH2> and <FTTag:BAH3> and <FTTag:BAH4> | |
FUNCTION | Responsible for the hydrolysis of barbituric acid (2,4,6- trihydroxy-1,3-pyrimidine), an intermediate in the oxidative catabolism of pyrimidines. Catalyzes the hydrolytic opening of the pyrimidine ring of barbituric acid to yield ureidomalonic acid. |
CATALYTIC ACTIVITY | Reaction=barbiturate + H2O = 3-oxo-3-ureidopropanoate; Xref=Rhea:RHEA:18653, ChEBI:CHEBI:15377, ChEBI:CHEBI:58775, ChEBI:CHEBI:77938; EC=3.5.2.1; |
ACTIVITY REGULATION | Inhibited by cyanuric acid. |
PATHWAY | Pyrimidine metabolism; uracil degradation via oxidative pathway; malonate and urea from uracil: step 2/3. |
DOMAIN | The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer and the active site possess nearly threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads, but one of the 3 active site surfaces varies in composition suggesting it is involved in confering substrate specificity. |
else | |
FUNCTION | Cyclic amide hydrolase of unknown substrate specificity. Catalyzes the hydrolytic ring-opening of a cyclic amide. Does not act on cyanuric acid nor barbituric acid. |
DOMAIN | The monomer structure is formed from three repeating units (RUs) that share the same structure as one another. The monomer and the active site possess nearly threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads, but one of the 3 active site surfaces varies in composition suggesting it is involved in confering substrate specificity. |
end case | |
case <FTGroup:2> | |
SUBUNIT | Homotetramer; disulfide-linked. The disufides form between 2 monomers in the tetramer, such that each tetramer contains 2 sets of vicinal disulfides. |
else | |
SUBUNIT | Homotetramer. |
end case | |
SIMILARITY | Belongs to the cyclic amide hydrolase (CyAH) family. |
Keywords
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Hydrolase | |
case <FTGroup:1> | |
Magnesium | |
Metal-binding | |
end case |
Gene Ontology
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case <FTTag:CAH1> and <FTTag:CAH2> and <FTTag:CAH3> and <FTTag:CAH4> | |
GO:0018753; Molecular function:cyanuric acid amidohydrolase activity | |
GO:0019381; Biological process:atrazine catabolic process | |
else case <FTTag:BAH1> and <FTTag:BAH2> and <FTTag:BAH3> and <FTTag:BAH4> | |
GO:0047694; Molecular function:barbiturase activity | |
GO:0006212; Biological process:uracil catabolic process | |
else; https://www.ebi.ac.uk/QuickGO/term/else | |
GO:0016812; Molecular function:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | |
end case | |
case <FTGroup:1> | |
GO:0046872; Molecular function:metal ion binding | |
end case |
Cross-references
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Features
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From: CAH_PSESD (P58329) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
REGION | Nter | 103 | /note="RU A" | |||||||||
BINDING | 83 | 84 | /ligand="substrate" | S-G | ||||||||
REGION | 112 | 249 | /note="RU B" | |||||||||
BINDING | 232 | 233 | /ligand="substrate" | S-[SAG] | ||||||||
REGION | 255 | Cter | /note="RU C" | |||||||||
BINDING | 343 | 344 | /ligand="substrate" | CAH3 | S-G | |||||||
BINDING | 343 | 344 | /ligand="substrate" | BAH3 | S-V | |||||||
BINDING | 343 | 344 | /ligand="substrate" | S-[AT] | ||||||||
BINDING | 297 | 297 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="structural" |
[ED] | 1 | |||||||
BINDING | 346 | 346 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="structural" |
[ASG] | 1 | |||||||
BINDING | 349 | 349 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="structural" |
Q | 1 | |||||||
BINDING | 350 | 350 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="structural" |
G | 1 | |||||||
BINDING | 351 | 351 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="structural" |
P | 1 | |||||||
BINDING | 354 | 354 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_note="structural" |
G | 1 | |||||||
BINDING | 52 | 52 | /ligand="substrate" | R | ||||||||
BINDING | 194 | 194 | /ligand="substrate" | CAH1 | R | |||||||
BINDING | 194 | 194 | /ligand="substrate" | BAH1 | N | |||||||
BINDING | 324 | 324 | /ligand="substrate" | CAH2 | R | |||||||
BINDING | 324 | 324 | /ligand="substrate" | BAH2 | K | |||||||
SITE | 320 | 320 | /note="Important for substrate specificity" | CAH4 | [ST] | |||||||
SITE | 320 | 320 | /note="Important for substrate specificity" | BAH4 | [H] | |||||||
From: CAH_AZOC5 (A8IKD2) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 156 | 156 | K | |||||||||
ACT_SITE | 226 | 226 | /note="Nucleophile" | S | ||||||||
From: CYAH_PSEI1 (E3JD18) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DISULFID | 303 | 303 | /note="Interchain (with #{Cys-304})" | C | 2 | |||||||
DISULFID | 304 | 304 | /note="Interchain (with #{Cys-303})" | C | 2 |
Additional information
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Size range | 341-390 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |