HAMAP rule MF_00220
General rule information
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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>
Triggered by |
end case
case <OC:Archaea>
Triggered by |
end case
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
Protein name |
|
Gene name |
|
Comments
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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
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Gene Ontology
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GO:0004151; Molecular function: dihydroorotase activity.
GO:0008270; Molecular function: zinc ion binding.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.
GO:0008270; Molecular function: zinc ion binding.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.
Cross-references
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Pfam | PF01979; Amidohydro_1; 1; |
NCBIfam | TIGR00857; PyrC_multi; 1; |
PROSITE | PS00482; DIHYDROOROTASE_1; 1; |
PS00483; DIHYDROOROTASE_2; 1; |
Features
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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
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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. |