UMPS_ARATH
ID UMPS_ARATH Reviewed; 476 AA.
AC Q42586; Q9M1I0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Uridine 5'-monophosphate synthase;
DE Short=UMP synthase;
DE Includes:
DE RecName: Full=Orotate phosphoribosyltransferase;
DE Short=OPRTase;
DE EC=2.4.2.10;
DE Includes:
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMPdecase;
GN Name=PYRE-F; Synonyms=UMPS; OrderedLocusNames=At3g54470;
GN ORFNames=T14E10.40;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8041358; DOI=10.1007/bf00280183;
RA Nasr F., Bertauche N., Dufour M.E., Minet M., Lacroute F.;
RT "Heterospecific cloning of Arabidopsis thaliana cDNAs by direct
RT complementation of pyrimidine auxotrophic mutants of Saccharomyces
RT cerevisiae. I. Cloning and sequence analysis of two cDNAs catalysing the
RT second, fifth and sixth steps of the de novo pyrimidine biosynthesis
RT pathway.";
RL Mol. Gen. Genet. 244:23-32(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Columbia;
RA Kafer C.W., Thornburg R.W.;
RT "Transcriptional analysis of the Arabidopsis thaliana UMP synthase locus.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC ChEBI:CHEBI:58017; EC=2.4.2.10;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2.
CC -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the OMP decarboxylase
CC family. {ECO:0000305}.
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DR EMBL; X71842; CAA50686.1; -; mRNA.
DR EMBL; AF276887; AAK69440.1; -; Genomic_DNA.
DR EMBL; AL138656; CAB77567.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79235.1; -; Genomic_DNA.
DR EMBL; AY140098; AAM98239.1; -; mRNA.
DR EMBL; BT006612; AAP31956.1; -; mRNA.
DR PIR; S46440; S46440.
DR PIR; T47606; T47606.
DR RefSeq; NP_680130.1; NM_148875.5.
DR AlphaFoldDB; Q42586; -.
DR SMR; Q42586; -.
DR BioGRID; 9928; 3.
DR IntAct; Q42586; 1.
DR STRING; 3702.AT3G54470.1; -.
DR PaxDb; Q42586; -.
DR PRIDE; Q42586; -.
DR ProteomicsDB; 245270; -.
DR EnsemblPlants; AT3G54470.1; AT3G54470.1; AT3G54470.
DR GeneID; 824612; -.
DR Gramene; AT3G54470.1; AT3G54470.1; AT3G54470.
DR KEGG; ath:AT3G54470; -.
DR Araport; AT3G54470; -.
DR TAIR; locus:504955714; AT3G54470.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_049275_1_0_1; -.
DR OMA; DHLGQQY; -.
DR OrthoDB; 1303452at2759; -.
DR PhylomeDB; Q42586; -.
DR BioCyc; ARA:AT3G54470-MON; -.
DR BioCyc; MetaCyc:AT3G54470-MON; -.
DR UniPathway; UPA00070; UER00119.
DR UniPathway; UPA00070; UER00120.
DR PRO; PR:Q42586; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42586; baseline and differential.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
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:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006222; P:UMP biosynthetic process; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW Decarboxylase; Glycosyltransferase; Lyase; Multifunctional enzyme;
KW Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..476
FT /note="Uridine 5'-monophosphate synthase"
FT /id="PRO_0000139653"
FT ACT_SITE 305
FT /evidence="ECO:0000250"
FT CONFLICT 186
FT /note="V -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 51850 MW; F79AE7992503D928 CRC64;
MSAMEALILQ LHEIGAVKFG NFKLKSGIFS PVYIDLRLIV SYPSLLTQIS QTLISSLPPS
ATFDVVCGVP YTALPIATVV SVSNGIPMLM RRKEIKDYGT SKAIEGIFEK DQTCLIIEDL
VTSGASVLET AAPLRAVGLK VSDAVVLIDR QQGGRENLAE NGIKLHSMIM LTDMVRVLKE
KGKIEVEVEV NLLKFLEENR RVSVPSVEKP KPKPRVLGFK ERSELSKNPT GKKLFDIMLK
KETNLCLAAD VGTAAELLDI ADKVGPEICL LKTHVDILPD FTPDFGSKLR AIADKHKFLI
FEDRKFADIG NTVTMQYEGG IFKILEWADI INAHVISGPG IVDGLKLKGM PRGRGLLLLA
EMSSAGNLAT GDYTAAAVKI ADAHSDFVMG FISVNPASWK CGYVYPSMIH ATPGVQMVKG
GDALGQQYNT PHSVITERGS DIIIVGRGII KAENPAETAH EYRVQGWNAY LEKCSQ
