HAMAP

Accession	MF_00224
Dates	1-JUN-2001 (Created) 19-JUL-2011 (Last updated, Version 34)

Data class

Protein

Predictors

HAMAP; MF_00224; [distribution of match scores in UniProtKB];[seed alignment for MF_00224]

Names

DHO_dh_type1

Identifier

PYRD

Protein name

RecName: Full=Dihydroorotate dehydrogenase; Short=DHOdehase; Short=DHOD; Short=DHODase; EC=1.3.-.-;

Gene name

pyrD

FUNCTION: Catalyzes the conversion of dihydroorotate to orotate (By similarity).

CATALYTIC ACTIVITY: (S)-dihydroorotate + acceptor = orotate + reduced acceptor.

COFACTOR: Binds 1 FMN per subunit (By similarity).

PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Pfam	PF01180; DHO_dh; 1;
PIRSF	PIRSF000164; DHO_oxidase; 1;
TIGRFAMs	TIGR01037; PyrD_sub1_fam; 1;
PROSITE	PS00911; DHODEHASE_1; 1; PS00912; DHODEHASE_2; 1;

Cytoplasm, Pyrimidine biosynthesis, Oxidoreductase, Flavoprotein, FMN.

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

From: PYRDB_LACLM (P54322)
Key		From		To		Description		Condition		FTGroup
NP_BIND		48		49		FMN (By similarity)		K-[STAG]
NP_BIND		248		249		FMN (By similarity)		G-G
NP_BIND (Optional)		270		271		FMN (By similarity)		[GA]-[TS]
REGION		72		76		Substrate binding (By similarity)		N-x-[IMVN]-G-[LI]
REGION		197		198		Substrate binding (By similarity)		N-[ST]
ACT_SITE		135		135		Nucleophile		[CS]
BINDING (Optional)		24		24		FMN (By similarity)		S
BINDING		48		48		Substrate (By similarity)		K
BINDING (Optional)		104		104		FMN (By similarity)		N
BINDING		132		132		FMN (By similarity)		N
BINDING		132		132		Substrate (By similarity)		N
BINDING		170		170		FMN (By similarity)		K
BINDING		196		196		FMN; via carbonyl oxygen (By similarity)		[IV]
BINDING		222		222		FMN; via amide nitrogen (By similarity)		G

Size range:	270-318 amino acids
Related UniRules:	MF_00225 (PYRD)
Template:	P54322 (PYRDB_LACLM); A2RJT9 (PYRDA_LACLM); P25996 (PYRDB_BACSU); P0DH74 (PYRDB_ENTFA): [Recover all]
Scope:	Bacteria Archaea
Fusion:	Nter: None; Cter: None
Duplicate:	in ENTFA, LACLA, LACLM, STRPN, STRR6
Plasmid encoded:	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.