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HAMAP rule MF_00224

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General rule information [?]

Accession MF_00224
Dates 1-JUN-2001 (Created)
19-NOV-2022 (Last updated, Version 41)
Name DHO_dh_type1
Templates P54322 (PYRDB_LACLM); A2RJT9 (PYRDA_LACLM); P25996 (PYRDB_BACSU); P0DH74 (PYRDB_ENTFA): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Dihydroorotate dehydrogenase;
EC 1.3.-.-;
Gene name

Comments [?]

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 [?]

Gene Ontology [?]

GO:0004152; Molecular function: dihydroorotate dehydrogenase activity.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF01180; DHO_dh; 1;
PIRSF PIRSF000164; DHO_oxidase; 1;
TIGRFAMs TIGR01037; PyrD_sub1_fam; 1;
PS00912; DHODEHASE_2; 1;

Features [?]

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 [?]

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 The 1B enzyme, in contrast use NAD(+) as its natural electron acceptor (EC 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.