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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(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 [?]

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>
FUNCTIONResponsible 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 REGULATIONInhibited by barbituric acid.
PATHWAYXenobiotic degradation; atrazine degradation; biuret from cyanurate: step 1/1.
DOMAINThe 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>
FUNCTIONResponsible 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 REGULATIONInhibited by cyanuric acid.
PATHWAYPyrimidine metabolism; uracil degradation via oxidative pathway; malonate and urea from uracil: step 2/3.
DOMAINThe 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
FUNCTIONCyclic amide hydrolase of unknown substrate specificity. Catalyzes the hydrolytic ring-opening of a cyclic amide. Does not act on cyanuric acid nor barbituric acid.
DOMAINThe 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>
SUBUNITHomotetramer; disulfide-linked. The disufides form between 2 monomers in the tetramer, such that each tetramer contains 2 sets of vicinal disulfides.
else
SUBUNITHomotetramer.
end case
SIMILARITYBelongs 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; 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 [?]

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 /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_FRAIE (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 [?]

Size range 341-390 amino acids
Related rules None
Fusion Nter: None Cter: None



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