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HAMAP rule MF_01989

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General rule information [?]

Accession MF_01989
Dates 24-MAR-2017 (Created)
1-JUN-2023 (Last updated, Version 11)
Name Cyc_amidohydrol
Scope
Bacteria
Eukaryota; Fungi
Templates P58329 (CAH_PSESD); A8IKD2 (CAH_AZOC5); E3JD18 (CYAH_PSEI1); Q8RSQ2 (BAH_RHOER): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

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 [?]

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 RHEA:70363: cyanurate + H2O = 1-carboxybiuret + H(+)
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 RHEA:18653: barbiturate + H2O = 3-oxo-3-ureidopropanoate
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 [?]

Hydrolase
case <FTGroup:1>
Magnesium
Metal-binding
end case

Gene Ontology [?]

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
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 [?]

Pfam PF09663; Amido_AtzD_TrzD; 1;
NCBIfam TIGR02714; amido_AtzD_TrzD; 1;

Features [?]

From: CAH_PSESD (P58329)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     Nter     103       RU A        
BINDING     83     84       /ligand="substrate     S-G  
REGION     112     249       RU B        
BINDING     232     233       /ligand="substrate     S-[SAG]  
REGION     255     Cter       RU C        
BINDING (Optional)     343     344       /ligand="substrate   CAH3   S-G  
BINDING (Optional)     343     344       /ligand="substrate   BAH3   S-V  
BINDING (Optional)     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 (Optional)     194     194       /ligand="substrate   CAH1   R  
BINDING (Optional)     194     194       /ligand="substrate   BAH1   N  
BINDING (Optional)     324     324       /ligand="substrate   CAH2   R  
BINDING (Optional)     324     324       /ligand="substrate   BAH2   K  
SITE (Optional)     320     320       Important for substrate specificity   CAH4   [ST]  
SITE (Optional)     320     320       Important for substrate specificity   BAH4   [H]  
From: CAH_AZOC5 (A8IKD2)
ACT_SITE     156     156             K  
ACT_SITE     226     226       Nucleophile     S  
From: CYAH_FRAIE (E3JD18)
DISULFID (Optional)     303     303       Interchain (with #{Cys-304})     C   2
DISULFID (Optional)     304     304       Interchain (with #{Cys-303})     C   2

Additional information [?]

Size range 341-390 amino acids
Related rules None
Fusion None


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