ID PYRF_YERPY Reviewed; 245 AA.
AC B1JKQ0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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}; OrderedLocusNames=YPK_2024;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-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; CP000950; ACA68311.1; -; Genomic_DNA.
DR RefSeq; WP_012304080.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JKQ0; -.
DR SMR; B1JKQ0; -.
DR KEGG; ypy:YPK_2024; -.
DR PATRIC; fig|502800.11.peg.2701; -.
DR UniPathway; UPA00070; UER00120.
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..245
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000138576"
FT ACT_SITE 73
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 71..80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
SQ SEQUENCE 245 AA; 26179 MW; 2883471EBE1E381A CRC64;
MTSATKTNNS GSISSPIVVA LDYANKDAAL AFADQVSPQD CRLKVGKEMF TLYGPELIRD
LHQRGFDVFL DLKFHDIPNT TARAVAAAAE LGVWMVNVHA SGGARMMSAA KEALLPYGAQ
APLLIAVTVL TSMDGEDLRD IGITISPAEQ AERLAKLTWD CGLDGVVCSA HEAVRLKQVC
GEDFSLVTPG IRPQGSEAGD QRRIMTPEQA VAAGVDYMVI GRPITQSPDP EKTLREILAS
LTKVA
//
