UMPS_MOUSE
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 03-AUG-2022, entry version 176.
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, Spleen,
RC 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; 6.
DR IntAct; P13439; 2.
DR MINT; P13439; -.
DR STRING; 10090.ENSMUSP00000023510; -.
DR iPTMnet; P13439; -.
DR PhosphoSitePlus; P13439; -.
DR SwissPalm; P13439; -.
DR EPD; P13439; -.
DR jPOST; P13439; -.
DR PaxDb; P13439; -.
DR PeptideAtlas; P13439; -.
DR PRIDE; P13439; -.
DR ProteomicsDB; 297867; -.
DR Antibodypedia; 32990; 223 antibodies from 32 providers.
DR DNASU; 22247; -.
DR Ensembl; ENSMUST00000023510; ENSMUSP00000023510; ENSMUSG00000022814.
DR GeneID; 22247; -.
DR KEGG; mmu:22247; -.
DR UCSC; uc007zap.1; mouse.
DR CTD; 7372; -.
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; DHLGQQY; -.
DR OrthoDB; 1303452at2759; -.
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; 27 hits in 71 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 246 other tissues.
DR ExpressionAtlas; P13439; baseline and differential.
DR Genevisible; P13439; MM.
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; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.2020; -; 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 Pfam; PF00215; OMPdecase; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00336; pyrE; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
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
