BioPAX pathway converted from "orotidine 5'-monophosphate => uridine 5'-monophosphate + CO2" in the Reactome database.4.1.1.23orotidine 5'-monophosphate => uridine 5'-monophosphate + CO2orotidine 5'-monophosphate => uridine 5'-monophosphate + CO2decarboxylation of Orotidine 5'-phosphate to form Uridine 5'-phosphateThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 1116291cytosolGO0005829orotidine 5'-phosphate [ChEBI:15842]orotidine 5'-phosphateReactomehttp://www.reactome.orgChEBI15842Reactome DB_ID: 1135281carbon dioxide [ChEBI:16526]carbon dioxideChEBI16526Reactome DB_ID: 1094021uridine 5'-monophosphate [ChEBI:16695]uridine 5'-monophosphateChEBI16695PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 9937624UMPS dimer [cytosol]UMPS dimerReactome DB_ID: 99376222UniProt:E2RRY7UMPSCanis familiarisNCBI Taxonomy9615UniProtE2RRY7Chain Coordinates2EQUAL480EQUALReactome Database ID Release 759937624Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9937624ReactomeR-CFA-4195121Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-CFA-419512.1GO0004590GO molecular functionReactome Database ID Release 759937625Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9937625Reactome Database ID Release 759937627Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9937627ReactomeR-CFA-735641Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-CFA-73564.1The decarboxylation of orotidine 5'-monophosphate (OMP) to form uridine 5'-monophosphate (UMP) is catalyzed by the orotidine 5'-phosphate decarboxylase activity of the bifunctional "uridine monophosphate synthetase (orotate phosphoribosyl transferase and orotidine 5'-decarboxylase)" protein. While purified human protein has not been characterized in detail, the close similarity of the human gene to that encoding the well-studied hamster protein, and the demonstration that mutations in the human gene are associated with failure to convert orotate to UMP in vivo, provide convincing evidence that the human uridine monophosphate synthetase protein indeed catalyzes these two reactions (McClard et al. 1980; Suchi et al. 1997). The active form of the human protein is a dimer (Yablonski et al. 1996; Wittmann et al. 2008).9042911Pubmed1997Molecular cloning of the human UMP synthase gene and characterization of point mutations in two hereditary orotic aciduria familiesSuchi, MMizuno, HKawai, YTsuboi, TSumi, SOkajima, KHodgson, MEOgawa, HWada, YAm J Hum Genet 60:525-5396893554Pubmed1980Isolation and initial characterization of the single polypeptide that synthesizes uridine 5'-monophosphate from orotate in Ehrlich ascites carcinoma. Purification by tandem affinity chromatography of uridine-5'-monophosphate synthaseMcClard, RWBlack, MJLivingstone, LRJones, MEBiochemistry 19:4699-47068631878Pubmed1996Intrinsic activity and stability of bifunctional human UMP synthase and its two separate catalytic domains, orotate phosphoribosyltransferase and orotidine-5'-phosphate decarboxylaseYablonski, MJPasek, DAHan, BDJones, METraut, TWJ Biol Chem 271:10704-818184586Pubmed2008Structures of the human orotidine-5'-monophosphate decarboxylase support a covalent mechanism and provide a framework for drug designWittmann, JGHeinrich, DGasow, KFrey, ADiederichsen, URudolph, MGStructure 16:82-92inferred by electronic annotationIEAGOIEA