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HAMAP rule MF_00219

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General rule information [?]

Accession MF_00219
Dates 1-JUN-2001 (Created)
14-MAY-2024 (Last updated, Version 41)
Name PyrC_classII
Scope(s) Bacteria
Template(s) P05020 (PYRC_ECOLI); A6T7D6 (PYRC_KLEP7); B1IV40 (PYRC_ECOLC); P06204 (PYRC_SALTY); Q8ZFU4 (PYRC_YERPE); [ Recover all ]
Triggered by HAMAP; MF_00219 (Get profile general information and statistics)

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.
SUBUNITHomodimer.
SIMILARITYBelongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.

Keywords [?]


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;
PIRSF PIRSF001237; DHOdimr; 1;
NCBIfam TIGR00856; PyrC_dimer; 1;
PROSITE PS00482; DIHYDROOROTASE_1; 1;
PROSITE PS00483; DIHYDROOROTASE_2; 1;

Features [?]

From: PYRC_ECOLI (P05020)
Key From To Description Tag Condition FTGroup
BINDING 19 21 /ligand="substrate" H-[LFV]-R
ACT_SITE 251 251 D
BINDING 17 17 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
H
BINDING 19 19 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
H
BINDING 103 103 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/note="via carbamate group"
K
BINDING 103 103 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
/note="via carbamate group"
K
BINDING 140 140 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
H
BINDING 178 178 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
H
BINDING 251 251 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
D
BINDING 45 45 /ligand="substrate" N
BINDING 140 140 /ligand="substrate" H
BINDING 223 223 /ligand="substrate" L
BINDING 255 255 /ligand="substrate" H
BINDING 267 267 /ligand="substrate" A
MOD_RES 103 103 /note="N6-carboxylysine" K

Additional information [?]

Size range 300-400 amino acids
Related rules MF_00220
Fusion Nter: None Cter: None
Comments Classification into subfamilies was done according to PubMed:24332717



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