HAMAP rule MF_00220

General rule information [?]

Accession	MF_00220
Dates	1-JUN-2001 (Created) 1-JUN-2023 (Last updated, Version 41)

Name	PyrC_classI

Scope

Bacteria

Archaea

Templates

Q81WF0 (PYRC_BACAN); Q5SK67 (PYRC_THET8); O66990 (PYRC_AQUAE); Q5HGN1 (PYRC_STAAC): [Recover all]

case <OC:Bacteria>

Triggered by

HAMAP; MF_00220_B (Get profile general information and statistics)

end case

case <OC:Archaea>

Triggered by

HAMAP; MF_00220_A (Get profile general information and statistics)

end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier

PYRC

Protein name

RecName:		Full=Dihydroorotase;
		Short=DHOase;
		EC 3.5.2.3;

Gene name

pyrC

Comments [?]

Function	Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic activity	RHEA:24296: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate EC 3.5.2.3
Cofactor	Zn(2+) Note: Binds 2 Zn(2+) ions per subunit.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Similarity	Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.

Keywords [?]

Hydrolase
Metal-binding
Pyrimidine biosynthesis
Zinc

Gene Ontology [?]

GO:0004151; Molecular function: dihydroorotase activity.
GO:0008270; Molecular function: zinc ion binding.
GO:0006221; Biological process: pyrimidine nucleotide biosynthetic process.

Cross-references [?]

Pfam	PF01979; Amidohydro_1; 1;
NCBIfam	TIGR00857; PyrC_multi; 1;
PROSITE	PS00482; DIHYDROOROTASE_1; 1;
	PS00483; DIHYDROOROTASE_2; 1;

Features [?]

case <OC:Bacteria>

From: PYRC_BACAN (Q81WF0)

Key From To Description Tag Condition FTGroup

BINDING 61 63 /ligand="substrate H-x-R

BINDING 322 323 /ligand="substrate [FP]-G

ACT_SITE 304 304 D

BINDING 59 59 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 H

BINDING 61 61 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 H

BINDING 151 151 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 D

BINDING 151 151 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 D

BINDING 178 178 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 H

BINDING 231 231 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 H

BINDING 304 304 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 D

BINDING 93 93 /ligand="substrate N

BINDING 277 277 /ligand="substrate N

BINDING 308 308 /ligand="substrate H

end case

case <OC:Archaea>

From: PYRC_PYRAB (Q9UXV6)

BINDING (Optional) 59 61 /ligand="substrate H-x-R

BINDING (Optional) 286 287 /ligand="substrate [FPA]-G

ACT_SITE 272 272 D

BINDING 57 57 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 H

BINDING 59 59 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 H

BINDING 135 135 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 [KE]

BINDING 135 135 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 [KE]

BINDING 164 164 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 H

BINDING 204 204 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="2 H

BINDING 272 272 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="1 D

MOD_RES (Optional) 135 135 N6-carboxylysine K

BINDING (Optional) 91 91 /ligand="substrate N

BINDING (Optional) 276 276 /ligand="substrate H

end case

Additional information [?]

case <OC:Bacteria>

Size range

370-500 amino acids

end case

case <OC:Archaea>

Size range

380-480 amino acids

end case

Related rules	MF_00219 (PYRC)
Fusion	None
Comments	Classification into subfamilies was done according to PubMed:24332717.

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