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| Annotation rule MF_00219 |
General rule information
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| Accession | MF_00219 |
| Dates | 1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 36) |
| 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; |
| TIGRFAMs | 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 | ||||||
| REGION (Optional) | 19 | 21 | Substrate binding | H-[LFV]-R | ||||||||
| ACT_SITE | 251 | 251 | D | |||||||||
| METAL | 17 | 17 | Zinc 1; via tele nitrogen | H | ||||||||
| METAL | 19 | 19 | Zinc 1; via tele nitrogen | H | ||||||||
| METAL | 103 | 103 | Zinc 1; via carbamate group | K | ||||||||
| METAL | 103 | 103 | Zinc 2; via carbamate group | K | ||||||||
| METAL | 140 | 140 | Zinc 2; via pros nitrogen | H | ||||||||
| METAL | 178 | 178 | Zinc 2; via tele nitrogen | H | ||||||||
| METAL | 251 | 251 | Zinc 1 | D | ||||||||
| BINDING (Optional) | 45 | 45 | Substrate | N | ||||||||
| BINDING (Optional) | 140 | 140 | Substrate | H | ||||||||
| BINDING (Optional) | 223 | 223 | Substrate; via amide nitrogen and carbonyl oxygen | L | ||||||||
| BINDING (Optional) | 255 | 255 | Substrate | H | ||||||||
| BINDING (Optional) | 267 | 267 | Substrate; via carbonyl oxygen | 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 |