AC   MF_00225;
DC   Protein; auto
TR   HAMAP; MF_00225; -; 1; level=0
XX
Names: DHO_dh_type2
XX
ID   PYRD
DE   RecName: Full=Dihydroorotate dehydrogenase (quinone);
DE            EC=1.3.5.2;
DE   AltName: Full=DHOdehase;
DE            Short=DHOD;
DE            Short=DHODase;
DE   AltName: Full=Dihydroorotate oxidase;
GN   Name=pyrD;
XX
CC   -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with
CC       quinone as electron acceptor.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + a quinone = a quinol + orotate;
CC         Xref=Rhea:RHEA:30187, ChEBI:CHEBI:24646, ChEBI:CHEBI:30839,
CC         ChEBI:CHEBI:30864, ChEBI:CHEBI:132124; EC=1.3.5.2;
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       orotate from (S)-dihydroorotate (quinone route): step 1/1.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2
CC       subfamily.
XX
DR   Pfam; PF01180; DHO_dh; 1; trigger=no
DR   PIRSF; PIRSF000164; DHO_oxidase; 1; trigger=no
DR   NCBIfam; TIGR01036; PyrD_sub2; 1; trigger=no
DR   PROSITE; PS00911; DHODEHASE_1; 1; trigger=no
DR   PROSITE; PS00912; DHODEHASE_2; 1; trigger=no
XX
KW   Cell membrane
KW   Flavoprotein
KW   FMN
KW   Membrane
KW   Oxidoreductase
KW   Pyrimidine biosynthesis
XX
GO   GO:0004152; F:dihydroorotate dehydrogenase activity
GO   GO:0006221; P:pyrimidine nucleotide biosynthetic process
GO   GO:0005886; C:plasma membrane
XX
FT   From: PYRD_ECOLI (P0A7E1)
FT   BINDING         62..66
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [AP]-x-x-x-K
FT   BINDING         318..319
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [YF]-[ST]
FT   BINDING         111..115
FT                   /ligand="substrate"
FT   Condition: N-x-[MYLFN]-G-[FL]
FT   BINDING         246..247
FT                   /ligand="substrate"
FT   Condition: N-T
FT   ACT_SITE        175
FT                   /note="Nucleophile"
FT   Condition: [SC]
FT   BINDING         66
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         86
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [TASG]
FT   BINDING         139
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [NS]
FT   BINDING         172
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: N
FT   BINDING         172
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         177
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         217
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: K
FT   BINDING         245
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: [TASGV]
FT   BINDING         268
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: G
FT   BINDING         297
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: G
XX
Size: 333-396;
Related: MF_00224;
Template: P0A7E1;
Scope:
 Archaea; Halobacteriales
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in CORST
Comments: None
XX
# Revision 1.43 2023/06/01
//