ID B5LY71_HUMAN Unreviewed; 480 AA. AC B5LY71; DT 14-OCT-2008, integrated into UniProtKB/TrEMBL. DT 14-OCT-2008, sequence version 1. DT 03-OCT-2012, entry version 25. DE RecName: Full=Orotate phosphoribosyltransferase D; DE Short=OPRT D; DE Short=OPRTase D; DE EC=2.4.2.10; GN Name=UMPS; Synonyms=PYRED; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [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 RT isoforms and sequence polymorphisms associated with 5-FU resistance."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from CC 5-phosphoribose 1-diphosphate to orotate, leading to the formation CC of orotidine monophosphate (OMP) (By similarity). CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate CC + 5-phospho-alpha-D-ribose 1-diphosphate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 1/2. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. PyrE subfamily. 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 IPI; IPI00003923; -. DR UniGene; Hs.2057; -. DR STRING; B5LY71; -. DR PRIDE; B5LY71; -. DR HOVERGEN; HBG000870; -. DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:InterPro. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:InterPro. DR Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 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; IPR004467; Or_phspho_trans_clade-1. DR InterPro; IPR023031; Orotate_PribosylTferase. DR InterPro; IPR000836; PRibTrfase. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00215; OMPdecase; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; RibP_bind_barrel; 1. DR TIGRFAMs; TIGR00336; pyrE; 1. DR TIGRFAMs; TIGR01740; pyrF; 1. DR PROSITE; PS00156; OMPDECASE; 1. PE 2: Evidence at transcript level; KW Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase. 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 //