HAMAP rule MF_00225
General rule information
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Accession | MF_00225 |
Dates | 1-JUN-2001 (Created)
14-MAY-2024 (Last updated, Version 44) |
Name | DHO_dh_type2 |
Scope(s) |
Archaea Halobacteriales Bacteria |
Template(s) | P0A7E1 (PYRD_ECOLI); [ Recover all ] |
Triggered by |
HAMAP; MF_00225 (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 (quinone); EC=1.3.5.2; AltName: Full=DHOdehase; Short=DHOD; Short=DHODase; AltName: Full=Dihydroorotate oxidase; |
Gene name | Name=pyrD; |
Comments
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FUNCTION | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. |
CATALYTIC ACTIVITY | Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate; Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2; |
COFACTOR | Name=FMN; Xref=ChEBI:CHEBI:58210; Note=Binds 1 FMN per subunit.; |
PATHWAY | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. |
SUBUNIT | Monomer. |
SUBCELLULAR LOCATION | Cell membrane; Peripheral membrane protein. |
SIMILARITY | Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. |
Keywords
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Gene Ontology
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GO:0004152; Molecular function:dihydroorotate dehydrogenase activity |
GO:0044205; Biological process:'de novo' UMP biosynthetic process |
GO:0005886; Cellular component:plasma membrane |
Cross-references
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Pfam | PF01180; DHO_dh; 1; |
PIRSF | PIRSF000164; DHO_oxidase; 1; |
NCBIfam | TIGR01036; PyrD_sub2; 1; |
PROSITE | PS00911; DHODEHASE_1; 1; |
PROSITE | PS00912; DHODEHASE_2; 1; |
Features
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From: PYRD_ECOLI (P0A7E1) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 62 | 66 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
[AP]-x-x-x-K | ||||||||
BINDING | 318 | 319 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
[YF]-[ST] | ||||||||
BINDING | 111 | 115 | /ligand="substrate" | N-x-[MYLFN]-G-[FL] | ||||||||
BINDING | 246 | 247 | /ligand="substrate" | N-T | ||||||||
ACT_SITE | 175 | 175 | /note="Nucleophile" | [SC] | ||||||||
BINDING | 66 | 66 | /ligand="substrate" | K | ||||||||
BINDING | 86 | 86 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
[TASG] | ||||||||
BINDING | 139 | 139 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
[NS] | ||||||||
BINDING | 172 | 172 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
N | ||||||||
BINDING | 172 | 172 | /ligand="substrate" | N | ||||||||
BINDING | 177 | 177 | /ligand="substrate" | N | ||||||||
BINDING | 217 | 217 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
K | ||||||||
BINDING | 245 | 245 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
[TASGV] | ||||||||
BINDING | 268 | 268 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
G | ||||||||
BINDING | 297 | 297 | /ligand="FMN" /ligand_id="ChEBI:CHEBI:58210" |
G |
Additional information
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Size range | 333-396 amino acids |
Related rules |
MF_00224 |
Fusion | Nter: None Cter: None |