BioPAX pathway converted from "orotidine 5'-monophosphate => uridine 5'-monophosphate + CO2" in the Reactome database.LEFT-TO-RIGHT4.1.1.23orotidine 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>orotidylic acidorotidine 5'-monophosphateorotidine 5'-phosphateReactome DB_ID: 111629cytosolGENE ONTOLOGYGO:0005829orotidine 5'-phosphate [ChEBI:15842]orotidine 5'-phosphateChEBICHEBI:15842Reactome Database ID Release 75111629Database 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=111629ReactomeR-ALL-1116293Reactome 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-ALL-111629.3Reactomehttp://www.reactome.orgCOMPOUNDC01103additional informationMIMI:0361CO2carbon dioxideReactome DB_ID: 113528carbon dioxide [ChEBI:16526]carbon dioxideChEBICHEBI:16526Reactome Database ID Release 75113528Database 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=113528ReactomeR-ALL-1135283Reactome 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-ALL-113528.3COMPOUNDC00011UMPuridine 5'-monophosphateuridylic acidUridine monophosphate5'Uridylic acidReactome DB_ID: 109402uridine 5'-monophosphate [ChEBI:16695]uridine 5'-monophosphateChEBICHEBI:16695Reactome Database ID Release 75109402Database 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=109402ReactomeR-ALL-1094024Reactome 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-ALL-109402.4COMPOUNDC00105ACTIVATIONUMPS dimerReactome DB_ID: 10095104UMPSUMPSF1SQ55Reactome DB_ID: 10095102UniProt:F1SQ55UMPSSus scrofaNCBI Taxonomy9823UniProtF1SQ552EQUAL480EQUALReactome Database ID Release 7510095102Database 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=10095102ReactomeR-SSC-734871Reactome 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-SSC-73487.12Reactome Database ID Release 7510095104Database 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=10095104ReactomeR-SSC-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-SSC-419512.1GENE ONTOLOGYGO:0004590gene ontology term for cellular functionMIMI:0355Same Catalyst ActivityReactome Database ID Release 7510095105Database 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=10095105Reactome Database ID Release 7510095107Database 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=10095107ReactomeR-SSC-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-SSC-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 from electronic annotationEVIDENCE CODEECO:0000203