AC MF_00224; DC Protein; auto TR HAMAP; MF_00224; -; 1; level=0 XX Names: DHO_dh_type1 XX ID PYRD DE RecName: Full=Dihydroorotate dehydrogenase; DE Short=DHOdehase; DE Short=DHOD; DE Short=DHODase; DE EC=1.3.-.-; GN Name=pyrD; XX CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-dihydroorotate + A = AH2 + orotate; Xref=Rhea:RHEA:18073, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:30839, CC ChEBI:CHEBI:30864; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Note=Binds 1 FMN per subunit.; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 CC subfamily. XX DR Pfam; PF01180; DHO_dh; 1; trigger=no DR PIRSF; PIRSF000164; DHO_oxidase; 1; trigger=no DR NCBIfam; TIGR01037; PyrD_sub1_fam; 1; trigger=no DR PROSITE; PS00911; DHODEHASE_1; 1; trigger=no DR PROSITE; PS00912; DHODEHASE_2; 1; trigger=no XX KW Cytoplasm KW Pyrimidine biosynthesis KW Oxidoreductase KW Flavoprotein KW FMN XX GO GO:0004152; F:dihydroorotate dehydrogenase activity GO GO:0006221; P:pyrimidine nucleotide biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: PYRDB_LACLM (P54322) FT BINDING 48..49 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: K-[STAG] FT BINDING 248..249 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: G-G FT BINDING 270..271 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: [GA]-[TS] FT BINDING 72..76 FT /ligand="substrate" FT Condition: N-x-[IMVN]-G-[LI] FT BINDING 197..198 FT /ligand="substrate" FT Condition: N-[ST] FT ACT_SITE 135 FT /note="Nucleophile" FT Condition: [CS] FT BINDING 24 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: S FT BINDING 48 FT /ligand="substrate" FT Condition: K FT BINDING 104 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Optional; Condition: N FT BINDING 132 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: N FT BINDING 132 FT /ligand="substrate" FT Condition: N FT BINDING 170 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: K FT BINDING 196 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: [IV] FT BINDING 222 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: G XX Size: 270-318; Related: MF_00225; Template: P54322; A2RJT9; P25996; P0DH74; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in ENTFA, LACLA, LACLM, STRPN, STRR6 Plasmid: 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. XX # Revision 1.42 2023/06/01 //