HAMAP rule MF_00224
General rule information
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| Accession | MF_00224 |
| Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 42) |
| Name | DHO_dh_type1 |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P54322 (PYRDB_LACLM); A2RJT9 (PYRDA_LACLM); P25996 (PYRDB_BACSU); P0DH74 (PYRDB_ENTFA); [ Recover all ] |
| Triggered by |
HAMAP; MF_00224 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | PYRD |
| Protein name | RecName: Full=Dihydroorotate dehydrogenase; Short=DHOdehase; Short=DHOD; Short=DHODase; EC=1.3.-.-; |
| Gene name | Name=pyrD; |
Comments
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| FUNCTION | Catalyzes the conversion of dihydroorotate to orotate. |
| CATALYTIC ACTIVITY | Reaction=(S)-dihydroorotate + A = AH2 + orotate; Xref=Rhea:RHEA:18073, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864; |
| COFACTOR | Name=FMN; Xref=ChEBI:CHEBI:58210; 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 |
Cross-references
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| Pfam | PF01180; DHO_dh; 1; |
| PIRSF | PIRSF000164; DHO_oxidase; 1; |
| NCBIfam | TIGR01037; PyrD_sub1_fam; 1; |
| PROSITE | PS00911; DHODEHASE_1; 1; |
| PROSITE | 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 | 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 | /note="Nucleophile" | [CS] | ||||||||
| BINDING | 24 | 24 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
S | ||||||||
| BINDING | 48 | 48 | /ligand="substrate" | K | ||||||||
| BINDING | 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 |
| Fusion | Nter: None Cter: 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. |