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HAMAP rule MF_00220

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General rule information [?]

Accession MF_00220
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 41)
Name PyrC_classI
Scope
Bacteria
Archaea
Templates Q81WF0 (PYRC_BACAN); Q5SK67 (PYRC_THET8); O66990 (PYRC_AQUAE); Q5HGN1 (PYRC_STAAC): [Recover all]
case <OC:Bacteria>
end case

case <OC:Archaea>
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
PYRC
Protein name
RecName: Full=Dihydroorotase;
Short=DHOase;
EC 3.5.2.3;
Gene name
pyrC

Comments [?]

Function Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic activity RHEA:24296: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
EC 3.5.2.3
Cofactor Zn(2+)
Note: Binds 2 Zn(2+) ions per subunit.
Pathway Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Similarity Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.

Keywords [?]


Gene Ontology [?]

GO:0004151; Molecular function: dihydroorotase activity.
GO:0008270; Molecular function: zinc ion binding.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.

Cross-references [?]

Pfam PF01979; Amidohydro_1; 1;
NCBIfam TIGR00857; PyrC_multi; 1;
PROSITE PS00482; DIHYDROOROTASE_1; 1;
PS00483; DIHYDROOROTASE_2; 1;

Features [?]

case <OC:Bacteria>
From: PYRC_BACAN (Q81WF0)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     61     63       /ligand="substrate     H-x-R  
BINDING     322     323       /ligand="substrate     [FP]-G  
ACT_SITE     304     304             D  
BINDING     59     59       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1     H  
BINDING     61     61       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1     H  
BINDING     151     151       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1     D  
BINDING     151     151       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     D  
BINDING     178     178       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     H  
BINDING     231     231       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     H  
BINDING     304     304       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1     D  
BINDING     93     93       /ligand="substrate     N  
BINDING     277     277       /ligand="substrate     N  
BINDING     308     308       /ligand="substrate     H  
end case
case <OC:Archaea>
From: PYRC_PYRAB (Q9UXV6)
BINDING (Optional)     59     61       /ligand="substrate     H-x-R  
BINDING (Optional)     286     287       /ligand="substrate     [FPA]-G  
ACT_SITE     272     272             D  
BINDING     57     57       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1     H  
BINDING     59     59       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1     H  
BINDING     135     135       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1     [KE]  
BINDING     135     135       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     [KE]  
BINDING     164     164       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     H  
BINDING     204     204       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2     H  
BINDING     272     272       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1     D  
MOD_RES (Optional)     135     135       N6-carboxylysine     K  
BINDING (Optional)     91     91       /ligand="substrate     N  
BINDING (Optional)     276     276       /ligand="substrate     H  
end case

Additional information [?]

case <OC:Bacteria>
Size range 370-500 amino acids
end case
case <OC:Archaea>
Size range 380-480 amino acids
end case
Related rules MF_00219 (PYRC)
Fusion None
Comments Classification into subfamilies was done according to PubMed:24332717.