HAMAP rule MF_01989

General rule information [?]

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 [?]

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	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 [?]

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

Description

Tag

Condition

FTGroup

REGION

Nter

103

/note="RU A"

BINDING

/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