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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) (ODCase) (EC 4.1.1.23)]

 UMPS_CAEEL              Reviewed;         497 AA.
G5EDZ2;
18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
05-DEC-2018, entry version 63.
RecName: Full=Uridine 5'-monophosphate synthase {ECO:0000250|UniProtKB:P11172};
Short=UMP synthase {ECO:0000250|UniProtKB:P11172};
Includes:
RecName: Full=Orotate phosphoribosyltransferase {ECO:0000303|PubMed:19645718};
Short=OPRT {ECO:0000303|PubMed:19645718};
Short=OPRTase {ECO:0000303|PubMed:19645718};
EC=2.4.2.10 {ECO:0000269|PubMed:19645718};
Includes:
RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000303|PubMed:19645718};
Short=ODC {ECO:0000303|PubMed:19645718};
Short=ODCase {ECO:0000303|PubMed:24262006};
EC=4.1.1.23 {ECO:0000269|PubMed:19645718};
Name=umps-1 {ECO:0000312|WormBase:T07C4.1};
Synonyms=rad-6 {ECO:0000303|PubMed:24262006};
ORFNames=T07C4.1 {ECO:0000312|WormBase:T07C4.1};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=19645718; DOI=10.1111/j.1742-4658.2009.07168.x;
Kim S., Park D.H., Kim T.H., Hwang M., Shim J.;
"Functional analysis of pyrimidine biosynthesis enzymes using the
anticancer drug 5-fluorouracil in Caenorhabditis elegans.";
FEBS J. 276:4715-4726(2009).
[3] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=20148972; DOI=10.1111/j.1742-4658.2010.07573.x;
Levitte S., Salesky R., King B., Coe Smith S., Depper M., Cole M.,
Hermann G.J.;
"A Caenorhabditis elegans model of orotic aciduria reveals enlarged
lysosome-related organelles in embryos lacking umps-1 function.";
FEBS J. 277:1420-1439(2010).
[4] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24262006; DOI=10.1042/BJ20131085;
Merry A., Qiao M., Hasler M., Kuwabara P.E.;
"RAD-6: pyrimidine synthesis and radiation sensitivity in
Caenorhabditis elegans.";
Biochem. J. 458:343-353(2014).
-!- FUNCTION: Bifunctional enzyme which catalyzes the formation of UMP
from orotate in the de novo pathway of pyrimidine biosynthesis
(PubMed:19645718). May also form UMP from uracil
(PubMed:19645718). Regulates the size of gut granules during
embryonic development (PubMed:20148972). Involved in resistance to
DNA damaging agents including UV-C and X-ray radiation
(PubMed:24262006). {ECO:0000269|PubMed:19645718,
ECO:0000269|PubMed:20148972, ECO:0000269|PubMed:24262006}.
-!- CATALYTIC ACTIVITY:
Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
ChEBI:CHEBI:58017; EC=2.4.2.10;
Evidence={ECO:0000269|PubMed:19645718};
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
Evidence={ECO:0000269|PubMed:19645718};
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; UMP from orotate: step 1/2.
{ECO:0000269|PubMed:19645718}.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; UMP from orotate: step 2/2.
{ECO:0000269|PubMed:19645718}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20148972}.
Note=Localizes near the apical surface of the embryonic intestine.
Appears not to localize to gut granules.
{ECO:0000269|PubMed:20148972}.
-!- TISSUE SPECIFICITY: Expressed in intestine and in neurons near the
nerve ring and rectum. {ECO:0000269|PubMed:19645718,
ECO:0000269|PubMed:20148972}.
-!- DEVELOPMENTAL STAGE: Expression starts at the early embryonic
pretzel-stage in the intestine and in a few cells in the head and
the tail, and continues throughout larval stages and adulthood.
{ECO:0000269|PubMed:20148972}.
-!- DISRUPTION PHENOTYPE: 56 percent of embryos fail to hatch and are
arrested at various stages between the bean stage and the four-
fold stage (PubMed:20148972). 30 percent of L1 larvae fail to
reach adulthood (PubMed:20148972). Embryos from the bean stage
through to hatching have abnormally enlarged gut granules which
fail to acidify (PubMed:20148972). Their size and number decreases
at the L1 larval stage (PubMed:20148972). Normal gut granules in
L2 larvae and adults (PubMed:20148972). Lysosomes in intestinal
cells are mislocalized. 7 percent of embryos lack attachment of
the anterior pharynx to the buccal cavity (PubMed:20148972).
Exposure to hypertonic conditions reduces the number of vacuoles
in mutant larvae (PubMed:20148972). Resistance to 5-fluorouracil
(5-FU)-mediated toxicity (PubMed:19645718, PubMed:24262006).
{ECO:0000269|PubMed:19645718, ECO:0000269|PubMed:20148972,
ECO:0000269|PubMed:24262006}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; BX284603; CAA82579.1; -; Genomic_DNA.
PIR; S41014; S41014.
RefSeq; NP_499291.1; NM_066890.4.
UniGene; Cel.10078; -.
ProteinModelPortal; G5EDZ2; -.
SMR; G5EDZ2; -.
IntAct; G5EDZ2; 13.
MINT; G5EDZ2; -.
STRING; 6239.T07C4.1.2; -.
EPD; G5EDZ2; -.
PaxDb; G5EDZ2; -.
PeptideAtlas; G5EDZ2; -.
EnsemblMetazoa; T07C4.1.1; T07C4.1.1; WBGene00011559.
EnsemblMetazoa; T07C4.1.2; T07C4.1.2; WBGene00011559.
GeneID; 176453; -.
KEGG; cel:CELE_T07C4.1; -.
CTD; 176453; -.
WormBase; T07C4.1; CE00638; WBGene00011559; umps-1.
eggNOG; KOG1377; Eukaryota.
eggNOG; COG0284; LUCA.
eggNOG; COG0461; LUCA.
GeneTree; ENSGT00390000001856; -.
InParanoid; G5EDZ2; -.
KO; K13421; -.
OMA; EQGGKDK; -.
OrthoDB; EOG091G06JT; -.
PhylomeDB; G5EDZ2; -.
Reactome; R-CEL-500753; Pyrimidine biosynthesis.
UniPathway; UPA00070; UER00119.
UniPathway; UPA00070; UER00120.
PRO; PR:G5EDZ2; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00011559; Expressed in 5 organ(s), highest expression level in material anatomical entity.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:WormBase.
GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IDA:WormBase.
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:0008340; P:determination of adult lifespan; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:UniProtKB.
GO; GO:0007040; P:lysosome organization; IMP:WormBase.
GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
GO; GO:0090727; P:positive regulation of brood size; IMP:UniProtKB.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IDA:WormBase.
GO; GO:0000003; P:reproduction; IMP:WormBase.
GO; GO:0010332; P:response to gamma radiation; IMP:UniProtKB.
GO; GO:0014070; P:response to organic cyclic compound; IMP:UniProtKB.
GO; GO:0009411; P:response to UV; IMP:WormBase.
GO; GO:0010225; P:response to UV-C; IMP:UniProtKB.
GO; GO:0010165; P:response to X-ray; IMP:UniProtKB.
GO; GO:0006222; P:UMP biosynthetic process; IMP:WormBase.
CDD; cd06223; PRTases_typeI; 1.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01208; PyrE; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR014732; OMPdecase.
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.
SMART; SM00934; OMPdecase; 1.
SUPFAM; SSF51366; SSF51366; 1.
SUPFAM; SSF53271; SSF53271; 1.
TIGRFAMs; TIGR00336; pyrE; 1.
TIGRFAMs; TIGR01740; pyrF; 1.
PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Decarboxylase; Glycosyltransferase;
Lyase; Multifunctional enzyme; Pyrimidine biosynthesis;
Reference proteome; Transferase.
CHAIN 1 497 Uridine 5'-monophosphate synthase.
{ECO:0000305}.
/FTId=PRO_0000438772.
REGION 8 226 OPRTase. {ECO:0000250|UniProtKB:P11172}.
REGION 227 232 Domain linker.
{ECO:0000250|UniProtKB:P11172}.
REGION 233 496 OMPdecase.
{ECO:0000250|UniProtKB:P11172}.
ACT_SITE 324 324 For OMPdecase activity.
{ECO:0000250|UniProtKB:P11172}.
ACT_SITE 326 326 For OMPdecase activity.
{ECO:0000250|UniProtKB:P11172}.
ACT_SITE 329 329 For OMPdecase activity.
{ECO:0000250|UniProtKB:P11172}.
SEQUENCE 497 AA; 54805 MW; 789AE78A9DE50233 CRC64;
MSSLTDKTRN GALKRNLLRQ MLKASVFKFG EFQLKSGQIS PIYIDLRECF GHPGLLMLIS
EAISKQVEIS EVQYAGVLGI PYAALPYASV AAGNYLKKPL LIVRKEAKSY GTKKLIEGLY
QPNDRLILIE DVVTTGGSIL DVVKVLHTEN LVASDVFCIL DREQGGRQKL QDAGVTLHSL
LDMQTVLTFL YSTGAIGDEQ WHGIVQALNL PYTSPTKLEI NSELENLSSL PYVENVRTPL
AERESLTESA LIKKILGIMR RKKSNLCLAV DYTTVEQCLQ MIELAGPFVL AIKLHADAIT
DFNEEFTRKL TTMANDMDFI IFEDRKFGDT GNTNLLQLTG AQKIANWADV VTVHAVQGSD
SIAGVFRKLA KDPTYRLSGV LLIAQLSTKG SLTALEGYTE TAVKIANENR DVISGFITQT
RVSACSDLLN WTPGVNLDAK SDSAGQQWRG VDEAIEVQQN DIIIVGRGVT SSSEPVQQLK
RYRQIAWDAL TRSDDSI


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