ID PYRF_BACC0 Reviewed; 238 AA.
AC B7JJX0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200};
DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200};
GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200};
GN OrderedLocusNames=BCAH820_3897;
OS Bacillus cereus (strain AH820).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH820.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-
CC Rule:MF_01200}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01200};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01200}.
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DR EMBL; CP001283; ACK89834.1; -; Genomic_DNA.
DR RefSeq; WP_000083501.1; NC_011773.1.
DR AlphaFoldDB; B7JJX0; -.
DR SMR; B7JJX0; -.
DR KEGG; bcu:BCAH820_3897; -.
DR HOGENOM; CLU_067069_1_1_9; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000001363; Chromosome.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04725; OMP_decarboxylase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01200_B; OMPdecase_type1_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR047596; OMPdecase_bac.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR01740; pyrF; 1.
DR PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR32119:SF2; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1..238
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000138511"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 59..68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
SQ SEQUENCE 238 AA; 26201 MW; 1A7E376152A3C3CE CRC64;
MSQSLIVALD FPGKQDVEQF LRHFEGEELF VKVGMELFYK EGPAIITYLK EKGHKIFLDL
KLHDIPNTVK SAMRSLASLD VDMVNVHAAG GSSMMKAAIE GLEEGKQEGK ERPICIAVTQ
LTSTSETMMK KEIGIEKTLE EAVAHYAKLT KESGLDGVVC STLEVPKLRE VCGSEFVTVT
PGIRLASDDV NDQVRVATPK RARELGSSYI VVGRSITKAE NPLEAYKTVK QQWEGVTV
//
