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Database: UniProt
Entry: P11172
LinkDB: P11172
Original site: P11172 
ID   UMPS_HUMAN              Reviewed;         480 AA.
AC   P11172; B5LY68; B5LY72; O00758; O00759; O00760; Q16862; Q9H3Q2;
AC   Q9UG49;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   26-NOV-2014, entry version 174.
DE   RecName: Full=Uridine 5'-monophosphate synthase;
DE            Short=UMP synthase;
DE   Includes:
DE     RecName: Full=Orotate phosphoribosyltransferase;
DE              Short=OPRT;
DE              Short=OPRTase;
DE              EC=2.4.2.10;
DE   Includes:
DE     RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE              Short=ODC;
DE              EC=4.1.1.23;
DE     AltName: Full=OMPdecase;
GN   Name=UMPS; ORFNames=OK/SW-cl.21;
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 [MRNA] (ISOFORM 1).
RX   PubMed=3279416; DOI=10.1073/pnas.85.6.1754;
RA   Suttle D.P., Bugg B.Y., Winkler J.K., Kanalas J.J.;
RT   "Molecular cloning and nucleotide sequence for the complete coding
RT   region of human UMP synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1754-1758(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2624233;
RA   Suchi M., Harada N., Tsuboi T., Asai K., Okajima K., Wada Y.,
RA   Takagi Y.;
RT   "Molecular cloning of human UMP synthase.";
RL   Adv. Exp. Med. Biol. 253A:511-518(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ORAC1 GLY-96; GLY-109 AND
RP   ARG-429, AND VARIANT ALA-213.
RC   TISSUE=Leukocyte;
RX   PubMed=9042911;
RA   Suchi M., Mizuno H., Kawai Y., Tsuboi T., Sumi S., Okajima K.,
RA   Hodgson M.E., Ogawa H., Wada Y.;
RT   "Molecular cloning of the human UMP synthase gene and characterization
RT   of point mutations in two hereditary orotic aciduria families.";
RL   Am. J. Hum. Genet. 60:525-539(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
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.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon adenocarcinoma;
RA   Shichijo S., Itoh K.;
RT   "Identification of immuno-peptidmics that are recognized by tumor-
RT   reactive CTL generated from TIL of colon cancer patients.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-30; ALA-213 AND
RP   VAL-446.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-480 (ISOFORM 1).
RA   Suchi M.;
RT   "Molecular genetic studies on hereditary orotic aciduria: I.
RT   Purification of human orotidine 5'-monophosphate decarboxylase and
RT   cloning of its cDNA.";
RL   Nagoya Med. J. 32:207-220(1988).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 224-480 IN COMPLEX WITH
RP   SUBSTRATE, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF ASP-312.
RX   PubMed=18184586; DOI=10.1016/j.str.2007.10.020;
RA   Wittmann J.G., Heinrich D., Gasow K., Frey A., Diederichsen U.,
RA   Rudolph M.G.;
RT   "Structures of the human orotidine-5'-monophosphate decarboxylase
RT   support a covalent mechanism and provide a framework for drug
RT   design.";
RL   Structure 16:82-92(2008).
CC   -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate
CC       + 5-phospho-alpha-D-ribose 1-diphosphate.
CC   -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 1/2.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; UMP from orotate: step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18184586}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P11172-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P11172-2; Sequence=VSP_009273;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=P11172-3; Sequence=VSP_047611;
CC       Name=4;
CC         IsoId=P11172-4; Sequence=VSP_009273, VSP_047612;
CC   -!- DISEASE: Orotic aciduria 1 (ORAC1) [MIM:258900]: A disorder of
CC       pyrimidine metabolism resulting in megaloblastic anemia and orotic
CC       acid crystalluria that is frequently associated with some degree
CC       of physical and mental retardation. A minority of cases have
CC       additional features, particularly congenital malformations and
CC       immune deficiencies. {ECO:0000269|PubMed:9042911}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       purine/pyrimidine phosphoribosyltransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the OMP
CC       decarboxylase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB45710.3; Type=Erroneous termination; Positions=430; Note=Translated as Gln.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/umps/";
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DR   EMBL; J03626; AAA61255.1; -; mRNA.
DR   EMBL; D86227; BAA19920.1; -; mRNA.
DR   EMBL; D86228; BAA19921.1; -; mRNA.
DR   EMBL; D86230; BAA19923.1; -; mRNA.
DR   EMBL; AB041359; BAB20663.1; -; Genomic_DNA.
DR   EMBL; EU921891; ACH48229.1; -; mRNA.
DR   EMBL; EU921895; ACH48233.1; -; mRNA.
DR   EMBL; AB062285; BAB93468.1; -; mRNA.
DR   EMBL; CR456787; CAG33068.1; -; mRNA.
DR   EMBL; AL080099; CAB45710.3; ALT_SEQ; mRNA.
DR   EMBL; AY691629; AAT85801.1; -; Genomic_DNA.
DR   EMBL; AC022336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000364; AAH00364.1; -; mRNA.
DR   EMBL; BC007511; AAH07511.1; -; mRNA.
DR   EMBL; M36661; AAA61256.1; -; mRNA.
DR   CCDS; CCDS3029.1; -. [P11172-1]
DR   PIR; A30148; A30148.
DR   RefSeq; NP_000364.1; NM_000373.3. [P11172-1]
DR   UniGene; Hs.2057; -.
DR   PDB; 2EAW; X-ray; 2.88 A; A/B=190-480.
DR   PDB; 2JGY; X-ray; 1.95 A; A/B=224-479.
DR   PDB; 2P1F; X-ray; 1.76 A; A=190-480.
DR   PDB; 2QCC; X-ray; 1.85 A; A/B=224-480.
DR   PDB; 2QCD; X-ray; 2.03 A; A/B=224-480.
DR   PDB; 2QCE; X-ray; 1.43 A; A=224-480.
DR   PDB; 2QCF; X-ray; 1.22 A; A=224-480.
DR   PDB; 2QCG; X-ray; 1.75 A; A/B=224-480.
DR   PDB; 2QCH; X-ray; 1.95 A; A/B=224-480.
DR   PDB; 2QCL; X-ray; 1.85 A; A/B=224-480.
DR   PDB; 2QCM; X-ray; 1.67 A; A=224-480.
DR   PDB; 2QCN; X-ray; 1.85 A; A/B=224-480.
DR   PDB; 2V30; X-ray; 2.00 A; A/B=224-479.
DR   PDB; 2WNS; X-ray; 1.90 A; A/B=7-203.
DR   PDB; 3BGG; X-ray; 1.93 A; A=190-480.
DR   PDB; 3BGJ; X-ray; 2.00 A; A/B=190-480.
DR   PDB; 3BK0; X-ray; 1.60 A; A/B=223-480.
DR   PDB; 3BVJ; X-ray; 1.80 A; A/B=190-480.
DR   PDB; 3DBP; X-ray; 1.50 A; A/B=223-480.
DR   PDB; 3EWU; X-ray; 1.60 A; A/B=224-480.
DR   PDB; 3EWW; X-ray; 1.10 A; A/B=224-480.
DR   PDB; 3EWX; X-ray; 1.40 A; A=224-480.
DR   PDB; 3EWY; X-ray; 1.10 A; A=224-480.
DR   PDB; 3EWZ; X-ray; 1.40 A; A/B/C/D=224-480.
DR   PDB; 3EX1; X-ray; 1.40 A; A/B=224-480.
DR   PDB; 3EX2; X-ray; 1.55 A; A/B=224-480.
DR   PDB; 3EX3; X-ray; 1.45 A; A/B=224-480.
DR   PDB; 3EX4; X-ray; 1.24 A; A=224-480.
DR   PDB; 3EX6; X-ray; 1.30 A; A/B=224-480.
DR   PDB; 3G3D; X-ray; 1.70 A; A/B=190-480.
DR   PDB; 3G3M; X-ray; 1.40 A; A=223-480.
DR   PDB; 3L0K; X-ray; 1.34 A; A/B=224-480.
DR   PDB; 3L0N; X-ray; 1.74 A; A/B=224-480.
DR   PDB; 3MI2; X-ray; 1.20 A; A/B=223-480.
DR   PDB; 3MO7; X-ray; 1.35 A; A=223-480.
DR   PDB; 3MW7; X-ray; 2.32 A; A/B=190-480.
DR   PDB; 4HIB; X-ray; 1.80 A; A/B=190-480.
DR   PDB; 4HKP; X-ray; 1.75 A; A/B=190-480.
DR   PDBsum; 2EAW; -.
DR   PDBsum; 2JGY; -.
DR   PDBsum; 2P1F; -.
DR   PDBsum; 2QCC; -.
DR   PDBsum; 2QCD; -.
DR   PDBsum; 2QCE; -.
DR   PDBsum; 2QCF; -.
DR   PDBsum; 2QCG; -.
DR   PDBsum; 2QCH; -.
DR   PDBsum; 2QCL; -.
DR   PDBsum; 2QCM; -.
DR   PDBsum; 2QCN; -.
DR   PDBsum; 2V30; -.
DR   PDBsum; 2WNS; -.
DR   PDBsum; 3BGG; -.
DR   PDBsum; 3BGJ; -.
DR   PDBsum; 3BK0; -.
DR   PDBsum; 3BVJ; -.
DR   PDBsum; 3DBP; -.
DR   PDBsum; 3EWU; -.
DR   PDBsum; 3EWW; -.
DR   PDBsum; 3EWX; -.
DR   PDBsum; 3EWY; -.
DR   PDBsum; 3EWZ; -.
DR   PDBsum; 3EX1; -.
DR   PDBsum; 3EX2; -.
DR   PDBsum; 3EX3; -.
DR   PDBsum; 3EX4; -.
DR   PDBsum; 3EX6; -.
DR   PDBsum; 3G3D; -.
DR   PDBsum; 3G3M; -.
DR   PDBsum; 3L0K; -.
DR   PDBsum; 3L0N; -.
DR   PDBsum; 3MI2; -.
DR   PDBsum; 3MO7; -.
DR   PDBsum; 3MW7; -.
DR   PDBsum; 4HIB; -.
DR   PDBsum; 4HKP; -.
DR   ProteinModelPortal; P11172; -.
DR   SMR; P11172; 7-203, 224-479.
DR   BioGrid; 113218; 13.
DR   DIP; DIP-29595N; -.
DR   IntAct; P11172; 12.
DR   MINT; MINT-1397000; -.
DR   STRING; 9606.ENSP00000232607; -.
DR   BindingDB; P11172; -.
DR   ChEMBL; CHEMBL5216; -.
DR   DrugBank; DB00544; Fluorouracil.
DR   PhosphoSite; P11172; -.
DR   MaxQB; P11172; -.
DR   PaxDb; P11172; -.
DR   PeptideAtlas; P11172; -.
DR   PRIDE; P11172; -.
DR   DNASU; 7372; -.
DR   Ensembl; ENST00000232607; ENSP00000232607; ENSG00000114491. [P11172-1]
DR   GeneID; 7372; -.
DR   KEGG; hsa:7372; -.
DR   UCSC; uc003ehl.4; human. [P11172-1]
DR   UCSC; uc011bkd.2; human.
DR   CTD; 7372; -.
DR   GeneCards; GC03P124449; -.
DR   HGNC; HGNC:12563; UMPS.
DR   HPA; HPA036178; -.
DR   HPA; HPA036179; -.
DR   MIM; 258900; phenotype.
DR   MIM; 613891; gene.
DR   neXtProt; NX_P11172; -.
DR   Orphanet; 30; Hereditary orotic aciduria.
DR   PharmGKB; PA363; -.
DR   eggNOG; COG0284; -.
DR   GeneTree; ENSGT00390000001856; -.
DR   HOVERGEN; HBG000870; -.
DR   KO; K13421; -.
DR   OMA; SMKPEFL; -.
DR   OrthoDB; EOG754HPB; -.
DR   PhylomeDB; P11172; -.
DR   TreeFam; TF314694; -.
DR   BRENDA; 4.1.1.23; 2681.
DR   Reactome; REACT_21376; Pyrimidine biosynthesis.
DR   UniPathway; UPA00070; UER00119.
DR   UniPathway; UPA00070; UER00120.
DR   ChiTaRS; UMPS; human.
DR   EvolutionaryTrace; P11172; -.
DR   GeneWiki; Uridine_monophosphate_synthetase; -.
DR   GenomeRNAi; 7372; -.
DR   NextBio; 28866; -.
DR   PRO; PR:P11172; -.
DR   Bgee; P11172; -.
DR   CleanEx; HS_UMPS; -.
DR   ExpressionAtlas; P11172; baseline and differential.
DR   Genevestigator; P11172; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IDA:UniProtKB.
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   GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; TAS:Reactome.
DR   GO; GO:0046134; P:pyrimidine nucleoside biosynthetic process; TAS:Reactome.
DR   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0006222; P:UMP biosynthetic process; IDA:UniProtKB.
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   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Decarboxylase; Disease mutation; Glycosyltransferase; Lyase;
KW   Multifunctional enzyme; Phosphoprotein; Polymorphism;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:19413330}.
FT   CHAIN         2    480       Uridine 5'-monophosphate synthase.
FT                                /FTId=PRO_0000139649.
FT   REGION        2    214       OPRTase.
FT   REGION      215    220       Domain linker.
FT   REGION      221    480       OMPdecase.
FT   ACT_SITE    312    312       For OMPdecase activity.
FT                                {ECO:0000269|PubMed:18184586}.
FT   ACT_SITE    314    314       For OMPdecase activity.
FT                                {ECO:0000269|PubMed:18184586}.
FT   ACT_SITE    317    317       For OMPdecase activity.
FT                                {ECO:0000269|PubMed:18184586}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:19413330}.
FT   MOD_RES     214    214       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648,
FT                                ECO:0000269|PubMed:20068231}.
FT   VAR_SEQ       1    178       Missing (in isoform 2 and isoform 4).
FT                                {ECO:0000303|PubMed:17974005,
FT                                ECO:0000303|Ref.4}.
FT                                /FTId=VSP_009273.
FT   VAR_SEQ       1     92       Missing (in isoform 3).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_047611.
FT   VAR_SEQ     328    424       Missing (in isoform 4).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_047612.
FT   VARIANT      30     30       S -> G (in dbSNP:rs17843776).
FT                                {ECO:0000269|Ref.8}.
FT                                /FTId=VAR_020614.
FT   VARIANT      96     96       R -> G (in ORAC1).
FT                                {ECO:0000269|PubMed:9042911}.
FT                                /FTId=VAR_006807.
FT   VARIANT     109    109       V -> G (in ORAC1).
FT                                {ECO:0000269|PubMed:9042911}.
FT                                /FTId=VAR_006808.
FT   VARIANT     213    213       G -> A (in dbSNP:rs1801019).
FT                                {ECO:0000269|PubMed:9042911,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_006809.
FT   VARIANT     429    429       G -> R (in ORAC1).
FT                                {ECO:0000269|PubMed:9042911}.
FT                                /FTId=VAR_006810.
FT   VARIANT     446    446       I -> V (in dbSNP:rs3772809).
FT                                {ECO:0000269|Ref.8}.
FT                                /FTId=VAR_020615.
FT   MUTAGEN     312    312       D->N: Loss of OMPdecase activity.
FT                                {ECO:0000269|PubMed:18184586}.
FT   CONFLICT     13     13       T -> G (in Ref. 11; AAA61256).
FT                                {ECO:0000305}.
FT   CONFLICT    377    377       L -> Q (in Ref. 11; AAA61256).
FT                                {ECO:0000305}.
FT   HELIX         8     16       {ECO:0000244|PDB:2WNS}.
FT   TURN         17     19       {ECO:0000244|PDB:2WNS}.
FT   STRAND       21     27       {ECO:0000244|PDB:2WNS}.
FT   STRAND       33     38       {ECO:0000244|PDB:2WNS}.
FT   HELIX        40     45       {ECO:0000244|PDB:2WNS}.
FT   HELIX        47     63       {ECO:0000244|PDB:2WNS}.
FT   STRAND       69     73       {ECO:0000244|PDB:2WNS}.
FT   TURN         75     78       {ECO:0000244|PDB:2WNS}.
FT   HELIX        79     89       {ECO:0000244|PDB:2WNS}.
FT   STRAND       93     96       {ECO:0000244|PDB:2WNS}.
FT   TURN         99    102       {ECO:0000244|PDB:2WNS}.
FT   STRAND      103    105       {ECO:0000244|PDB:2WNS}.
FT   STRAND      108    111       {ECO:0000244|PDB:2WNS}.
FT   STRAND      118    129       {ECO:0000244|PDB:2WNS}.
FT   HELIX       130    141       {ECO:0000244|PDB:2WNS}.
FT   STRAND      148    154       {ECO:0000244|PDB:2WNS}.
FT   HELIX       159    164       {ECO:0000244|PDB:2WNS}.
FT   TURN        165    167       {ECO:0000244|PDB:2WNS}.
FT   STRAND      169    175       {ECO:0000244|PDB:2WNS}.
FT   HELIX       176    185       {ECO:0000244|PDB:2WNS}.
FT   HELIX       191    202       {ECO:0000244|PDB:2WNS}.
FT   HELIX       227    230       {ECO:0000244|PDB:3EWW}.
FT   HELIX       238    250       {ECO:0000244|PDB:3EWW}.
FT   STRAND      254    257       {ECO:0000244|PDB:3EWW}.
FT   HELIX       263    273       {ECO:0000244|PDB:3EWW}.
FT   HELIX       274    276       {ECO:0000244|PDB:3EWW}.
FT   STRAND      278    282       {ECO:0000244|PDB:3EWW}.
FT   HELIX       284    286       {ECO:0000244|PDB:3EWW}.
FT   HELIX       292    305       {ECO:0000244|PDB:3EWW}.
FT   STRAND      308    315       {ECO:0000244|PDB:3EWW}.
FT   HELIX       319    327       {ECO:0000244|PDB:3EWW}.
FT   TURN        329    331       {ECO:0000244|PDB:3EWW}.
FT   HELIX       333    335       {ECO:0000244|PDB:3EWW}.
FT   STRAND      338    344       {ECO:0000244|PDB:3EWW}.
FT   HELIX       349    358       {ECO:0000244|PDB:3EWW}.
FT   TURN        359    362       {ECO:0000244|PDB:3EWW}.
FT   STRAND      364    368       {ECO:0000244|PDB:3EWW}.
FT   HELIX       381    392       {ECO:0000244|PDB:3EWW}.
FT   TURN        393    396       {ECO:0000244|PDB:3EWW}.
FT   STRAND      397    401       {ECO:0000244|PDB:3EWW}.
FT   STRAND      412    416       {ECO:0000244|PDB:3EWW}.
FT   STRAND      421    425       {ECO:0000244|PDB:3EWW}.
FT   STRAND      427    429       {ECO:0000244|PDB:4HIB}.
FT   STRAND      431    433       {ECO:0000244|PDB:3EWW}.
FT   HELIX       435    439       {ECO:0000244|PDB:3EWW}.
FT   TURN        440    442       {ECO:0000244|PDB:3MI2}.
FT   STRAND      445    450       {ECO:0000244|PDB:3EWW}.
FT   HELIX       451    454       {ECO:0000244|PDB:3EWW}.
FT   STRAND      456    458       {ECO:0000244|PDB:3MO7}.
FT   HELIX       459    478       {ECO:0000244|PDB:3EWW}.
SQ   SEQUENCE   480 AA;  52222 MW;  D985CD566B72F5CA CRC64;
     MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT
     AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL
     IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML
     EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA
     SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT
     LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP
     LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ
     LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV
//
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