ID B5LY71_HUMAN Unreviewed; 480 AA. AC B5LY71; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 14-DEC-2022, entry version 63. DE RecName: Full=Uridine 5'-monophosphate synthase {ECO:0000256|ARBA:ARBA00015047}; DE EC=2.4.2.10 {ECO:0000256|ARBA:ARBA00011971}; DE EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321}; GN Name=UMPS {ECO:0000313|EMBL:ACH48232.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ACH48232.1}; RN [1] {ECO:0000313|EMBL:ACH48232.1} RP NUCLEOTIDE SEQUENCE. RA Griffith M., Pugh T.J., Tang M.J., Asano J.K., Ally A., Chan S.Y., RA Taylor G., Morin G.B., Tai I.T., Marra M.A.; RT "Genomic analysis of UMPS expression and sequence reveals novel isoforms RT and sequence polymorphisms associated with 5-FU resistance."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861}. CC -!- SIMILARITY: In the C-terminal section; belongs to the OMP decarboxylase CC family. {ECO:0000256|ARBA:ARBA00009769}. CC -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00006221}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU921894; ACH48232.1; -; mRNA. DR AlphaFoldDB; B5LY71; -. DR UniPathway; UPA00070; UER00119. DR ChiTaRS; UMPS; human. DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC. 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; 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; SSF53271; PRTase-like; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1. DR TIGRFAMs; TIGR00336; pyrE; 1. DR TIGRFAMs; TIGR01740; pyrF; 1. DR PROSITE; PS00156; OMPDECASE; 1. PE 2: Evidence at transcript level; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}. FT DOMAIN 253..466 FT /note="OMPdecase" FT /evidence="ECO:0000259|SMART:SM00934" SQ SEQUENCE 480 AA; 52277 MW; 2DF6CC127054018C CRC64; MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF IQENVFVAAN HNASPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVEILNDF TLDVMKELIT LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLNRLGV //