HAMAP rule MF_00219
General rule information
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Accession | MF_00219 |
Dates | 1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 40) |
Name | PyrC_classII |
Scope | Bacteria |
Templates | P05020 (PYRC_ECOLI); A6T7D6 (PYRC_KLEP7); B1IV40 (PYRC_ECOLC); P06204 (PYRC_SALTY); Q8ZFU4 (PYRC_YERPE): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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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. |
Subunit | Homodimer. |
Similarity | Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II 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; |
PIRSF | PIRSF001237; DHOdimr; 1; |
NCBIfam | TIGR00856; PyrC_dimer; 1; |
PROSITE | PS00482; DIHYDROOROTASE_1; 1; |
PS00483; DIHYDROOROTASE_2; 1; |
Features
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From: PYRC_ECOLI (P05020) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING (Optional) | 19 | 21 | /ligand="substrate | H-[LFV]-R | ||||||||
ACT_SITE | 251 | 251 | D | |||||||||
BINDING | 17 | 17 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 | H | ||||||||
BINDING | 19 | 19 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 | H | ||||||||
BINDING | 103 | 103 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1" /note="via carbamate group | K | ||||||||
BINDING | 103 | 103 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2" /note="via carbamate group | K | ||||||||
BINDING | 140 | 140 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 | H | ||||||||
BINDING | 178 | 178 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 | H | ||||||||
BINDING | 251 | 251 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 | D | ||||||||
BINDING (Optional) | 45 | 45 | /ligand="substrate | N | ||||||||
BINDING (Optional) | 140 | 140 | /ligand="substrate | H | ||||||||
BINDING (Optional) | 223 | 223 | /ligand="substrate | L | ||||||||
BINDING (Optional) | 255 | 255 | /ligand="substrate | H | ||||||||
BINDING (Optional) | 267 | 267 | /ligand="substrate | A | ||||||||
MOD_RES | 103 | 103 | N6-carboxylysine | K |
Additional information
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Size range | 300-400 amino acids |
Related rules | MF_00220 (PYRC) |
Fusion | None |
Comments | Classification into subfamilies was done according to PubMed:24332717 |