HAMAP rule MF_00224
General rule information
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| Accession | MF_00224 |
| Dates | 1-JUN-2001 (Created) 19-NOV-2022 (Last updated, Version 41) |
| Name | DHO_dh_type1 |
| Scope | Bacteria
Archaea |
| Templates | P54322 (PYRDB_LACLM); A2RJT9 (PYRDA_LACLM); P25996 (PYRDB_BACSU); P0DH74 (PYRDB_ENTFA): [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 conversion of dihydroorotate to orotate. |
| Catalytic activity | RHEA:18073: (S)-dihydroorotate + A = AH2 + orotate |
| Cofactor | FMN Note: Binds 1 FMN per subunit. |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway. |
| Subcellular location | Cytoplasm. |
| Similarity | Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily. |
Keywords
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Gene Ontology
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GO:0004152; Molecular function: dihydroorotate dehydrogenase activity.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
Cross-references
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| Pfam | PF01180; DHO_dh; 1; |
| PIRSF | PIRSF000164; DHO_oxidase; 1; |
| TIGRFAMs | TIGR01037; PyrD_sub1_fam; 1; |
| PROSITE | PS00911; DHODEHASE_1; 1; |
| PS00912; DHODEHASE_2; 1; |
Features
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| From: PYRDB_LACLM (P54322) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 48 | 49 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | K-[STAG] | ||||||||
| BINDING | 248 | 249 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | G-G | ||||||||
| BINDING (Optional) | 270 | 271 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | [GA]-[TS] | ||||||||
| BINDING | 72 | 76 | /ligand="substrate | N-x-[IMVN]-G-[LI] | ||||||||
| BINDING | 197 | 198 | /ligand="substrate | N-[ST] | ||||||||
| ACT_SITE | 135 | 135 | Nucleophile | [CS] | ||||||||
| BINDING (Optional) | 24 | 24 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | S | ||||||||
| BINDING | 48 | 48 | /ligand="substrate | K | ||||||||
| BINDING (Optional) | 104 | 104 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | N | ||||||||
| BINDING | 132 | 132 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | N | ||||||||
| BINDING | 132 | 132 | /ligand="substrate | N | ||||||||
| BINDING | 170 | 170 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | K | ||||||||
| BINDING | 196 | 196 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | [IV] | ||||||||
| BINDING | 222 | 222 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210 | G | ||||||||
Additional information
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| Size range | 270-318 amino acids |
| Related rules | MF_00225 (PYRD) |
| Fusion | None |
| Comments | This is not possible to make an automatic distinction of the 2 subclasses, 1A and 1B, that constitute this family, and which differ in their structural organization and use of electron acceptors. The 1A enzyme is a homodimer of two PyrD subunits and use fumarate as the natural electron acceptor (EC 1.3.98.1). The 1B enzyme, in contrast use NAD(+) as its natural electron acceptor (EC 1.3.1.14) and is a heterotetramer composed of a central, FMN-containing, PyrD homodimer resembling the 1A homodimer, and two additional PyrK subunits which contain FAD and a 2Fe-2S cluster. In bacteria the gene coding for PyrD type B and pyrK are adjacent genes; this rule does not seem to be always verified in archaea. |