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HAMAP rule MF_00220

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General rule information [?]

Accession MF_00220
Dates 1-JUN-2001 (Created)
14-MAY-2024 (Last updated, Version 42)
Name PyrC_classI
Scope(s) Bacteria
Archaea
Template(s) Q81WF0 (PYRC_BACAN); Q5SK67 (PYRC_THET8); O66990 (PYRC_AQUAE); Q5HGN1 (PYRC_STAAC); [ Recover all ]
Triggered by
case c? <OC:Bacteria>
HAMAP; MF_00220_B (Get profile general information and statistics)
end case
case c? <OC:Archaea>
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 Name=pyrC;

Comments [?]

FUNCTIONCatalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
CATALYTIC ACTIVITY Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
PATHWAYPyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
SIMILARITYBelongs 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:0044205; Biological process:'de novo' UMP biosynthetic process

Cross-references [?]

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

Features [?]

From: PYRC_BACAN (Q81WF0)
Key From To Description Tag Condition FTGroup
case <OC:Bacteria>
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
From: PYRC_PYRAB (Q9UXV6)
Key From To Description Tag Condition FTGroup
case <OC:Archaea>
BINDING 59 61 /ligand="substrate" H-x-R
BINDING 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 135 135 /note="N6-carboxylysine" K
BINDING 91 91 /ligand="substrate" N
BINDING 276 276 /ligand="substrate" H
end case

Additional information [?]

Size range 380-480 amino acids
Related rules MF_00219
Fusion Nter: None Cter: None
Comments Classification into subfamilies was done according to PubMed:24332717.



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