ID   UMPS_MOUSE              Reviewed;         481 AA.
AC   P13439; Q99L26;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 3.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Uridine 5'-monophosphate synthase;
DE            Short=UMP synthase;
DE   Includes:
DE     RecName: Full=Orotate phosphoribosyltransferase;
DE              Short=OPRTase;
DE              EC=2.4.2.10 {ECO:0000250|UniProtKB:P11172};
DE   Includes:
DE     RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE              EC=4.1.1.23 {ECO:0000250|UniProtKB:P11172};
DE     AltName: Full=OMPdecase;
GN   Name=Umps;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 216-481.
RX   PubMed=2419341; DOI=10.1016/s0021-9258(17)35657-0;
RA   Ohmstede C.A., Langdon S.D., Chae C.B., Jones M.E.;
RT   "Expression and sequence analysis of a cDNA encoding the orotidine-5'-
RT   monophosphate decarboxylase domain from Ehrlich ascites uridylate
RT   synthase.";
RL   J. Biol. Chem. 261:4276-4282(1986).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Bifunctional enzyme catalyzing the last two steps of de novo
CC       pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT),
CC       which converts orotate to orotidine-5'-monophosphate (OMP), and
CC       orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic
CC       reaction that decarboxylates OMP to uridine monophosphate (UMP).
CC       {ECO:0000250|UniProtKB:P11172}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC         ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC         ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC         ChEBI:CHEBI:58017; EC=2.4.2.10;
CC         Evidence={ECO:0000250|UniProtKB:P11172};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10382;
CC         Evidence={ECO:0000250|UniProtKB:P11172};
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:0000250|UniProtKB:P11172};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11597;
CC         Evidence={ECO:0000250|UniProtKB:P11172};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2. {ECO:0000250|UniProtKB:P11172}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2. {ECO:0000250|UniProtKB:P11172}.
CC   -!- SUBUNIT: Homodimer; dimerization is required for enzymatic activity.
CC       {ECO:0000250|UniProtKB:P11172}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the OMP decarboxylase
CC       family. {ECO:0000305}.
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DR   EMBL; BC003887; AAH03887.1; -; mRNA.
DR   EMBL; M29395; AAA39859.1; -; mRNA.
DR   CCDS; CCDS28136.1; -.
DR   PIR; A25323; DCMSOP.
DR   RefSeq; NP_033497.1; NM_009471.3.
DR   AlphaFoldDB; P13439; -.
DR   SMR; P13439; -.
DR   BioGRID; 204442; 8.
DR   IntAct; P13439; 2.
DR   MINT; P13439; -.
DR   STRING; 10090.ENSMUSP00000023510; -.
DR   GlyGen; P13439; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P13439; -.
DR   PhosphoSitePlus; P13439; -.
DR   SwissPalm; P13439; -.
DR   EPD; P13439; -.
DR   jPOST; P13439; -.
DR   PaxDb; 10090-ENSMUSP00000023510; -.
DR   PeptideAtlas; P13439; -.
DR   ProteomicsDB; 297867; -.
DR   Pumba; P13439; -.
DR   Antibodypedia; 32990; 250 antibodies from 32 providers.
DR   DNASU; 22247; -.
DR   Ensembl; ENSMUST00000023510.7; ENSMUSP00000023510.7; ENSMUSG00000022814.7.
DR   GeneID; 22247; -.
DR   KEGG; mmu:22247; -.
DR   UCSC; uc007zap.1; mouse.
DR   AGR; MGI:1298388; -.
DR   MGI; MGI:1298388; Umps.
DR   VEuPathDB; HostDB:ENSMUSG00000022814; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   GeneTree; ENSGT00390000001856; -.
DR   HOGENOM; CLU_049275_1_0_1; -.
DR   InParanoid; P13439; -.
DR   OMA; SAKHVCG; -.
DR   OrthoDB; 922at2759; -.
DR   PhylomeDB; P13439; -.
DR   TreeFam; TF314694; -.
DR   Reactome; R-MMU-500753; Pyrimidine biosynthesis.
DR   UniPathway; UPA00070; UER00119.
DR   UniPathway; UPA00070; UER00120.
DR   BioGRID-ORCS; 22247; 28 hits in 77 CRISPR screens.
DR   ChiTaRS; Umps; mouse.
DR   PRO; PR:P13439; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P13439; Protein.
DR   Bgee; ENSMUSG00000022814; Expressed in primitive streak and 249 other cell types or tissues.
DR   ExpressionAtlas; P13439; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:MGI.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IDA:MGI.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IDA:MGI.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006225; P:UDP biosynthetic process; IDA:MGI.
DR   GO; GO:0006222; P:UMP biosynthetic process; ISO:MGI.
DR   CDD; cd04725; OMP_decarboxylase_like; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00336; pyrE; 1.
DR   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
DR   Genevisible; P13439; MM.
PE   1: Evidence at protein level;
KW   Decarboxylase; Glycosyltransferase; Lyase; Multifunctional enzyme;
KW   Phosphoprotein; Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..481
FT                   /note="Uridine 5'-monophosphate synthase"
FT                   /id="PRO_0000139650"
FT   REGION          1..214
FT                   /note="OPRTase"
FT   REGION          215..220
FT                   /note="Domain linker"
FT   REGION          221..481
FT                   /note="OMPdecase"
FT   ACT_SITE        314
FT                   /note="For OMPdecase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   ACT_SITE        317
FT                   /note="For OMPdecase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         257
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         257
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         259
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         281..283
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         281
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         314
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         317
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         317
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         321
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         321
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         372
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         372
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         430..432
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         430..432
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         450..451
FT                   /ligand="orotidine 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57538"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   BINDING         450..451
FT                   /ligand="UMP"
FT                   /ligand_id="ChEBI:CHEBI:57865"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
FT   MOD_RES         37
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P11172"
SQ   SEQUENCE   481 AA;  52292 MW;  761C7EF7960C9C59 CRC64;
     MEVASQALGP LVTELYDVQA FKFGSFVLKS GLSSPVYIDL RGIVSRPRLL SQVADILFQT
     AKNAGISFDS VCGVPYTALP LATVICSANH IPMLIRRKET KDYGTKRLVE GEINPGQTCL
     VIEDVVTSGA SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAQGIRL HAVCTLSQML
     EILQQQEKID ADMVGRVKRF IQENVFSAAN HNGLPPPEKK ACKELSFGAR AELPGTHPLA
     SKLLRLMQKK ETNLCLSADV SEARELLQLA DALGPSICML KTHVDILNDF TLDVMEELTA
     LAKRHEFLIF EDRKFADIGN TVKKQYESGT FKIASWADIV NAHVVPGSGV VKGLQEVGLP
     LHRACLLIAE MSSAGSLATG NYTKAAVGMA EEHCEFVIGF ISGSRVSMKP EFLHLTPGVQ
     LETGGDHLGQ QYNSPQEVIG KRGSDVIIVG RGILAAANRL EAAEMYRKAA WEAYLSRLAV
     Q
//