AC   MF_01200;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01200_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_01200_A; -; 1; level=0
XX
Names: OMPdecase_type1
XX
ID   PYRF
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE            EC=4.1.1.23;
DE   AltName: Full=OMP decarboxylase;
DE            Short=OMPDCase;
DE            Short=OMPdecase;
GN   Name=pyrF;
XX
CC   -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC       (OMP) to uridine 5'-monophosphate (UMP).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC         Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
XX
DR   PROSITE; PS00156; OMPDECASE; 1; trigger=no
DR   Pfam; PF00215; OMPdecase; 1; trigger=no
DR   NCBIfam; TIGR01740; PyrF; 1; trigger=no
XX
KW   Lyase
KW   Decarboxylase
KW   Pyrimidine biosynthesis
XX
GO   GO:0004590; F:orotidine-5'-phosphate decarboxylase activity
GO   GO:0006221; P:pyrimidine nucleotide biosynthetic process
XX
FT   From: PYRF_ECOLI (P08244)
case <OC:Bacteria>
FT   BINDING         71..80
FT                   /ligand="substrate"
FT   Condition: D-x-K-x-x-D-x-x-x-x
FT   ACT_SITE        73
FT                   /note="Proton donor"
FT   Condition: K
FT   BINDING         22
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         44
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         131
FT                   /ligand="substrate"
FT   Condition: T
FT   BINDING         192
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         201
FT                   /ligand="substrate"
FT   Condition: Q
FT   BINDING         221
FT                   /ligand="substrate"
FT   Optional; Condition: G
FT   BINDING         222
FT                   /ligand="substrate"
FT   Condition: R
end case
FT   From: PYRF_METTH (O26232)
case <OC:Archaea>
FT   BINDING         70..79
FT                   /ligand="substrate"
FT   Condition: D-x-K-x-x-D-x-x-x-x
FT   BINDING         180..190
FT                   /ligand="substrate"
FT   ACT_SITE        72
FT                   /note="Proton donor"
FT   Condition: K
FT   BINDING         20
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         42
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         127
FT                   /ligand="substrate"
FT   Condition: S
FT   BINDING         202
FT                   /ligand="substrate"
FT   Condition: G
FT   BINDING         203
FT                   /ligand="substrate"
FT   Condition: R
end case
XX
case <OC:Bacteria>
Size: 224-279;
end case
case <OC:Archaea>
Size: 208-244;
end case
Related: MF_01215;
Template: P25971; P08244; Q59654; P07691; O26232; O74110; O58462; Q9WYG7;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: MF_01208 (pyrE)
Duplicate: None
Plasmid: None
Comments: Divergent THEMA; sequence not included in alignment and not taken into account
 in size range
XX
# Revision 1.32 2023/06/01
//