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Uridine 5'-monophosphate synthase (UMP synthase) [Includes: Orotate phosphoribosyltransferase (OPRT) (OPRTase) (EC 2.4.2.10); Orotidine 5'-phosphate decarboxylase (ODC) (EC 4.1.1.23) (OMPdecase)]

 UMPS_HUMAN              Reviewed;         480 AA.
P11172; B5LY68; B5LY72; O00758; O00759; O00760; Q16862; Q9H3Q2;
Q9UG49;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
28-MAR-2018, entry version 202.
RecName: Full=Uridine 5'-monophosphate synthase;
Short=UMP synthase;
Includes:
RecName: Full=Orotate phosphoribosyltransferase;
Short=OPRT;
Short=OPRTase;
EC=2.4.2.10;
Includes:
RecName: Full=Orotidine 5'-phosphate decarboxylase;
Short=ODC;
EC=4.1.1.23;
AltName: Full=OMPdecase;
Name=UMPS; ORFNames=OK/SW-cl.21;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3279416; DOI=10.1073/pnas.85.6.1754;
Suttle D.P., Bugg B.Y., Winkler J.K., Kanalas J.J.;
"Molecular cloning and nucleotide sequence for the complete coding
region of human UMP synthase.";
Proc. Natl. Acad. Sci. U.S.A. 85:1754-1758(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2624233;
Suchi M., Harada N., Tsuboi T., Asai K., Okajima K., Wada Y.,
Takagi Y.;
"Molecular cloning of human UMP synthase.";
Adv. Exp. Med. Biol. 253A:511-518(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ORAC1 GLY-96; GLY-109 AND
ARG-429, AND VARIANT ALA-213.
TISSUE=Leukocyte;
PubMed=9042911;
Suchi M., Mizuno H., Kawai Y., Tsuboi T., Sumi S., Okajima K.,
Hodgson M.E., Ogawa H., Wada Y.;
"Molecular cloning of the human UMP synthase gene and characterization
of point mutations in two hereditary orotic aciduria families.";
Am. J. Hum. Genet. 60:525-539(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
Griffith M., Pugh T.J., Tang M.J., Asano J.K., Ally A., Chan S.Y.,
Taylor G., Morin G.B., Tai I.T., Marra M.A.;
"Genomic analysis of UMPS expression and sequence reveals novel
isoforms and sequence polymorphisms associated with 5-FU resistance.";
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-30; ALA-213 AND
VAL-446.
NIEHS SNPs program;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 13-480 (ISOFORM 1).
Suchi M.;
"Molecular genetic studies on hereditary orotic aciduria: I.
Purification of human orotidine 5'-monophosphate decarboxylase and
cloning of its cDNA.";
Nagoya Med. J. 32:207-220(1988).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-37 AND SER-214, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 224-480 IN COMPLEX WITH
SUBSTRATE, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF ASP-312.
PubMed=18184586; DOI=10.1016/j.str.2007.10.020;
Wittmann J.G., Heinrich D., Gasow K., Frey A., Diederichsen U.,
Rudolph M.G.;
"Structures of the human orotidine-5'-monophosphate decarboxylase
support a covalent mechanism and provide a framework for drug
design.";
Structure 16:82-92(2008).
-!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate
+ 5-phospho-alpha-D-ribose 1-diphosphate.
-!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2).
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; UMP from orotate: step 1/2.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; UMP from orotate: step 2/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18184586}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P11172-1; Sequence=Displayed;
Name=2;
IsoId=P11172-2; Sequence=VSP_009273;
Note=No experimental confirmation available.;
Name=3;
IsoId=P11172-3; Sequence=VSP_047611;
Name=4;
IsoId=P11172-4; Sequence=VSP_009273, VSP_047612;
-!- DISEASE: Orotic aciduria 1 (ORAC1) [MIM:258900]: A disorder of
pyrimidine metabolism resulting in megaloblastic anemia and orotic
acid crystalluria that is frequently associated with some degree
of physical and mental retardation. A minority of cases have
additional features, particularly congenital malformations and
immune deficiencies. {ECO:0000269|PubMed:9042911}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: In the N-terminal section; belongs to the
purine/pyrimidine phosphoribosyltransferase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the OMP
decarboxylase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB45710.3; Type=Erroneous termination; Positions=430; Note=Translated as Gln.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/umps/";
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EMBL; J03626; AAA61255.1; -; mRNA.
EMBL; D86227; BAA19920.1; -; mRNA.
EMBL; D86228; BAA19921.1; -; mRNA.
EMBL; D86230; BAA19923.1; -; mRNA.
EMBL; AB041359; BAB20663.1; -; Genomic_DNA.
EMBL; EU921891; ACH48229.1; -; mRNA.
EMBL; EU921895; ACH48233.1; -; mRNA.
EMBL; AB062285; BAB93468.1; -; mRNA.
EMBL; CR456787; CAG33068.1; -; mRNA.
EMBL; AL080099; CAB45710.3; ALT_SEQ; mRNA.
EMBL; AY691629; AAT85801.1; -; Genomic_DNA.
EMBL; AC022336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000364; AAH00364.1; -; mRNA.
EMBL; BC007511; AAH07511.1; -; mRNA.
EMBL; M36661; AAA61256.1; -; mRNA.
CCDS; CCDS3029.1; -. [P11172-1]
PIR; A30148; A30148.
RefSeq; NP_000364.1; NM_000373.3. [P11172-1]
UniGene; Hs.2057; -.
PDB; 2EAW; X-ray; 2.88 A; A/B=190-480.
PDB; 2JGY; X-ray; 1.95 A; A/B=224-479.
PDB; 2P1F; X-ray; 1.76 A; A=190-480.
PDB; 2QCC; X-ray; 1.85 A; A/B=224-480.
PDB; 2QCD; X-ray; 2.03 A; A/B=224-480.
PDB; 2QCE; X-ray; 1.43 A; A=224-480.
PDB; 2QCF; X-ray; 1.22 A; A=224-480.
PDB; 2QCG; X-ray; 1.75 A; A/B=224-480.
PDB; 2QCH; X-ray; 1.95 A; A/B=224-480.
PDB; 2QCL; X-ray; 1.85 A; A/B=224-480.
PDB; 2QCM; X-ray; 1.67 A; A=224-480.
PDB; 2QCN; X-ray; 1.85 A; A/B=224-480.
PDB; 2V30; X-ray; 2.00 A; A/B=224-479.
PDB; 2WNS; X-ray; 1.90 A; A/B=7-203.
PDB; 3BGG; X-ray; 1.93 A; A=190-480.
PDB; 3BGJ; X-ray; 2.00 A; A/B=190-480.
PDB; 3BK0; X-ray; 1.60 A; A/B=223-480.
PDB; 3BVJ; X-ray; 1.80 A; A/B=190-480.
PDB; 3DBP; X-ray; 1.50 A; A/B=223-480.
PDB; 3EWU; X-ray; 1.60 A; A/B=224-480.
PDB; 3EWW; X-ray; 1.10 A; A/B=224-480.
PDB; 3EWX; X-ray; 1.40 A; A=224-480.
PDB; 3EWY; X-ray; 1.10 A; A=224-480.
PDB; 3EWZ; X-ray; 1.40 A; A/B/C/D=224-480.
PDB; 3EX1; X-ray; 1.40 A; A/B=224-480.
PDB; 3EX2; X-ray; 1.55 A; A/B=224-480.
PDB; 3EX3; X-ray; 1.45 A; A/B=224-480.
PDB; 3EX4; X-ray; 1.24 A; A=224-480.
PDB; 3EX6; X-ray; 1.30 A; A/B=224-480.
PDB; 3G3D; X-ray; 1.70 A; A/B=190-480.
PDB; 3G3M; X-ray; 1.40 A; A=223-480.
PDB; 3L0K; X-ray; 1.34 A; A/B=224-480.
PDB; 3L0N; X-ray; 1.74 A; A/B=224-480.
PDB; 3MI2; X-ray; 1.20 A; A/B=223-480.
PDB; 3MO7; X-ray; 1.35 A; A=223-480.
PDB; 3MW7; X-ray; 2.32 A; A/B=190-480.
PDB; 4HIB; X-ray; 1.80 A; A/B=190-480.
PDB; 4HKP; X-ray; 1.75 A; A/B=190-480.
PDBsum; 2EAW; -.
PDBsum; 2JGY; -.
PDBsum; 2P1F; -.
PDBsum; 2QCC; -.
PDBsum; 2QCD; -.
PDBsum; 2QCE; -.
PDBsum; 2QCF; -.
PDBsum; 2QCG; -.
PDBsum; 2QCH; -.
PDBsum; 2QCL; -.
PDBsum; 2QCM; -.
PDBsum; 2QCN; -.
PDBsum; 2V30; -.
PDBsum; 2WNS; -.
PDBsum; 3BGG; -.
PDBsum; 3BGJ; -.
PDBsum; 3BK0; -.
PDBsum; 3BVJ; -.
PDBsum; 3DBP; -.
PDBsum; 3EWU; -.
PDBsum; 3EWW; -.
PDBsum; 3EWX; -.
PDBsum; 3EWY; -.
PDBsum; 3EWZ; -.
PDBsum; 3EX1; -.
PDBsum; 3EX2; -.
PDBsum; 3EX3; -.
PDBsum; 3EX4; -.
PDBsum; 3EX6; -.
PDBsum; 3G3D; -.
PDBsum; 3G3M; -.
PDBsum; 3L0K; -.
PDBsum; 3L0N; -.
PDBsum; 3MI2; -.
PDBsum; 3MO7; -.
PDBsum; 3MW7; -.
PDBsum; 4HIB; -.
PDBsum; 4HKP; -.
ProteinModelPortal; P11172; -.
SMR; P11172; -.
BioGrid; 113218; 49.
DIP; DIP-29595N; -.
IntAct; P11172; 24.
MINT; P11172; -.
STRING; 9606.ENSP00000232607; -.
BindingDB; P11172; -.
ChEMBL; CHEMBL5216; -.
DrugBank; DB02890; 6-Hydroxyuridine-5'-Phosphate.
DrugBank; DB00544; Fluorouracil.
iPTMnet; P11172; -.
PhosphoSitePlus; P11172; -.
BioMuta; UMPS; -.
EPD; P11172; -.
MaxQB; P11172; -.
PaxDb; P11172; -.
PeptideAtlas; P11172; -.
PRIDE; P11172; -.
DNASU; 7372; -.
Ensembl; ENST00000232607; ENSP00000232607; ENSG00000114491. [P11172-1]
GeneID; 7372; -.
KEGG; hsa:7372; -.
UCSC; uc003ehl.5; human. [P11172-1]
CTD; 7372; -.
DisGeNET; 7372; -.
EuPathDB; HostDB:ENSG00000114491.13; -.
GeneCards; UMPS; -.
HGNC; HGNC:12563; UMPS.
HPA; HPA036178; -.
HPA; HPA036179; -.
MalaCards; UMPS; -.
MIM; 258900; phenotype.
MIM; 613891; gene.
neXtProt; NX_P11172; -.
OpenTargets; ENSG00000114491; -.
Orphanet; 30; Hereditary orotic aciduria.
PharmGKB; PA363; -.
eggNOG; KOG1377; Eukaryota.
eggNOG; COG0284; LUCA.
eggNOG; COG0461; LUCA.
GeneTree; ENSGT00390000001856; -.
HOGENOM; HOG000213905; -.
HOVERGEN; HBG000870; -.
KO; K13421; -.
OMA; RVSMKPE; -.
OrthoDB; EOG091G06JT; -.
PhylomeDB; P11172; -.
TreeFam; TF314694; -.
BRENDA; 4.1.1.23; 2681.
Reactome; R-HSA-500753; Pyrimidine biosynthesis.
SIGNOR; P11172; -.
UniPathway; UPA00070; UER00119.
UniPathway; UPA00070; UER00120.
ChiTaRS; UMPS; human.
EvolutionaryTrace; P11172; -.
GeneWiki; Uridine_monophosphate_synthetase; -.
GenomeRNAi; 7372; -.
PRO; PR:P11172; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114491; -.
CleanEx; HS_UMPS; -.
ExpressionAtlas; P11172; baseline and differential.
Genevisible; P11172; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:UniProtKB.
GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IDA:UniProtKB.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0046134; P:pyrimidine nucleoside biosynthetic process; TAS:Reactome.
GO; GO:0006222; P:UMP biosynthetic process; IDA:UniProtKB.
CDD; cd06223; PRTases_typeI; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01208; PyrE; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR014732; OMPdecase.
InterPro; IPR018089; OMPdecase_AS.
InterPro; IPR001754; OMPdeCOase_dom.
InterPro; IPR023031; OPRT.
InterPro; IPR004467; Or_phspho_trans_dom.
InterPro; IPR000836; PRibTrfase_dom.
InterPro; IPR029057; PRTase-like.
InterPro; IPR011060; RibuloseP-bd_barrel.
Pfam; PF00215; OMPdecase; 1.
Pfam; PF00156; Pribosyltran; 1.
SMART; SM00934; OMPdecase; 1.
SUPFAM; SSF51366; SSF51366; 1.
SUPFAM; SSF53271; SSF53271; 1.
TIGRFAMs; TIGR00336; pyrE; 1.
TIGRFAMs; TIGR01740; pyrF; 1.
PROSITE; PS00156; OMPDECASE; 1.
PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Decarboxylase; Disease mutation; Glycosyltransferase; Lyase;
Multifunctional enzyme; Phosphoprotein; Polymorphism;
Pyrimidine biosynthesis; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 480 Uridine 5'-monophosphate synthase.
/FTId=PRO_0000139649.
REGION 2 214 OPRTase.
REGION 215 220 Domain linker.
REGION 221 480 OMPdecase.
ACT_SITE 312 312 For OMPdecase activity.
{ECO:0000269|PubMed:18184586}.
ACT_SITE 314 314 For OMPdecase activity.
{ECO:0000269|PubMed:18184586}.
ACT_SITE 317 317 For OMPdecase activity.
{ECO:0000269|PubMed:18184586}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 37 37 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 178 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.4}.
/FTId=VSP_009273.
VAR_SEQ 1 92 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_047611.
VAR_SEQ 328 424 Missing (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_047612.
VARIANT 30 30 S -> G (in dbSNP:rs17843776).
{ECO:0000269|Ref.8}.
/FTId=VAR_020614.
VARIANT 96 96 R -> G (in ORAC1; dbSNP:rs121917890).
{ECO:0000269|PubMed:9042911}.
/FTId=VAR_006807.
VARIANT 109 109 V -> G (in ORAC1; dbSNP:rs121917892).
{ECO:0000269|PubMed:9042911}.
/FTId=VAR_006808.
VARIANT 213 213 G -> A (in dbSNP:rs1801019).
{ECO:0000269|PubMed:9042911,
ECO:0000269|Ref.8}.
/FTId=VAR_006809.
VARIANT 429 429 G -> R (in ORAC1; dbSNP:rs121917891).
{ECO:0000269|PubMed:9042911}.
/FTId=VAR_006810.
VARIANT 446 446 I -> V (in dbSNP:rs3772809).
{ECO:0000269|Ref.8}.
/FTId=VAR_020615.
MUTAGEN 312 312 D->N: Loss of OMPdecase activity.
{ECO:0000269|PubMed:18184586}.
CONFLICT 13 13 T -> G (in Ref. 11; AAA61256).
{ECO:0000305}.
CONFLICT 377 377 L -> Q (in Ref. 11; AAA61256).
{ECO:0000305}.
HELIX 8 16 {ECO:0000244|PDB:2WNS}.
TURN 17 19 {ECO:0000244|PDB:2WNS}.
STRAND 21 27 {ECO:0000244|PDB:2WNS}.
STRAND 33 38 {ECO:0000244|PDB:2WNS}.
HELIX 40 45 {ECO:0000244|PDB:2WNS}.
HELIX 47 63 {ECO:0000244|PDB:2WNS}.
STRAND 69 73 {ECO:0000244|PDB:2WNS}.
TURN 75 78 {ECO:0000244|PDB:2WNS}.
HELIX 79 89 {ECO:0000244|PDB:2WNS}.
STRAND 93 96 {ECO:0000244|PDB:2WNS}.
TURN 99 102 {ECO:0000244|PDB:2WNS}.
STRAND 103 105 {ECO:0000244|PDB:2WNS}.
STRAND 108 111 {ECO:0000244|PDB:2WNS}.
STRAND 118 129 {ECO:0000244|PDB:2WNS}.
HELIX 130 141 {ECO:0000244|PDB:2WNS}.
STRAND 148 154 {ECO:0000244|PDB:2WNS}.
HELIX 159 164 {ECO:0000244|PDB:2WNS}.
TURN 165 167 {ECO:0000244|PDB:2WNS}.
STRAND 169 175 {ECO:0000244|PDB:2WNS}.
HELIX 176 185 {ECO:0000244|PDB:2WNS}.
HELIX 191 202 {ECO:0000244|PDB:2WNS}.
HELIX 227 230 {ECO:0000244|PDB:3EWW}.
HELIX 238 250 {ECO:0000244|PDB:3EWW}.
STRAND 254 257 {ECO:0000244|PDB:3EWW}.
HELIX 263 273 {ECO:0000244|PDB:3EWW}.
HELIX 274 276 {ECO:0000244|PDB:3EWW}.
STRAND 278 282 {ECO:0000244|PDB:3EWW}.
HELIX 284 286 {ECO:0000244|PDB:3EWW}.
HELIX 292 305 {ECO:0000244|PDB:3EWW}.
STRAND 308 315 {ECO:0000244|PDB:3EWW}.
HELIX 319 327 {ECO:0000244|PDB:3EWW}.
TURN 329 331 {ECO:0000244|PDB:3EWW}.
HELIX 333 335 {ECO:0000244|PDB:3EWW}.
STRAND 338 344 {ECO:0000244|PDB:3EWW}.
HELIX 349 358 {ECO:0000244|PDB:3EWW}.
TURN 359 362 {ECO:0000244|PDB:3EWW}.
STRAND 364 368 {ECO:0000244|PDB:3EWW}.
HELIX 381 392 {ECO:0000244|PDB:3EWW}.
TURN 393 396 {ECO:0000244|PDB:3EWW}.
STRAND 397 401 {ECO:0000244|PDB:3EWW}.
STRAND 412 416 {ECO:0000244|PDB:3EWW}.
STRAND 421 425 {ECO:0000244|PDB:3EWW}.
STRAND 427 429 {ECO:0000244|PDB:4HIB}.
STRAND 431 433 {ECO:0000244|PDB:3EWW}.
HELIX 435 439 {ECO:0000244|PDB:3EWW}.
TURN 440 442 {ECO:0000244|PDB:3MI2}.
STRAND 445 450 {ECO:0000244|PDB:3EWW}.
HELIX 451 454 {ECO:0000244|PDB:3EWW}.
STRAND 456 458 {ECO:0000244|PDB:3MO7}.
HELIX 459 478 {ECO:0000244|PDB:3EWW}.
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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