HAMAP rule MF_00219
General rule information
[?]
| Accession | MF_00219 |
| Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 40) |
| Name | PyrC_classII |
| Scope(s) |
Bacteria |
| Template(s) | P05020 (PYRC_ECOLI); A6T7D6 (PYRC_KLEP7); B1IV40 (PYRC_ECOLC); P06204 (PYRC_SALTY); Q8ZFU4 (PYRC_YERPE); [ Recover all ] |
| Triggered by |
HAMAP; MF_00219 (Get profile general information and statistics) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Identifier | PYRC |
| Protein name | RecName: Full=Dihydroorotase; Short=DHOase; EC=3.5.2.3; |
| Gene name | Name=pyrC; |
Comments
[?]
| FUNCTION | Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. |
| CATALYTIC ACTIVITY | Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; 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
[?]
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; |
| PIRSF | PIRSF001237; DHOdimr; 1; |
| NCBIfam | TIGR00856; PyrC_dimer; 1; |
| PROSITE | PS00482; DIHYDROOROTASE_1; 1; |
| PROSITE | PS00483; DIHYDROOROTASE_2; 1; |
Features
[?]
| From: PYRC_ECOLI (P05020) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 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 | 45 | 45 | /ligand="substrate" | N | ||||||||
| BINDING | 140 | 140 | /ligand="substrate" | H | ||||||||
| BINDING | 223 | 223 | /ligand="substrate" | L | ||||||||
| BINDING | 255 | 255 | /ligand="substrate" | H | ||||||||
| BINDING | 267 | 267 | /ligand="substrate" | A | ||||||||
| MOD_RES | 103 | 103 | /note="N6-carboxylysine" | K | ||||||||
Additional information
[?]
| Size range | 300-400 amino acids |
| Related rules |
MF_00220 |
| Fusion | Nter: None Cter: None |
| Comments | Classification into subfamilies was done according to PubMed:24332717 |