UMPS_DROME
ID UMPS_DROME Reviewed; 493 AA.
AC Q01637; Q24221; Q9VDF2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Uridine 5'-monophosphate synthase;
DE Short=UMP synthase;
DE AltName: Full=Rudimentary-like protein;
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=r-l; ORFNames=CG3593;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8444350; DOI=10.1016/0378-1119(93)90403-p;
RA Eisenberg M., Kirkpatrick R., Rawls J.;
RT "Structure of the rudimentary-like gene and UMP synthase in Drosophila
RT melanogaster.";
RL Gene 124:263-267(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-78.
RX PubMed=2122228; DOI=10.1007/bf00283015;
RA Eisenberg M.T., Gathy K., Vincent T., Rawls J.;
RT "Molecular cloning of the UMP synthase gene rudimentary-like from
RT Drosophila melanogaster.";
RL Mol. Gen. Genet. 222:1-8(1990).
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; L00968; AAA29012.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55842.1; -; Genomic_DNA.
DR EMBL; AY058714; AAL13943.1; -; mRNA.
DR EMBL; X54230; CAA38138.1; -; mRNA.
DR PIR; JU0141; JU0141.
DR RefSeq; NP_524427.1; NM_079703.3.
DR AlphaFoldDB; Q01637; -.
DR SMR; Q01637; -.
DR BioGRID; 67464; 17.
DR IntAct; Q01637; 1.
DR STRING; 7227.FBpp0083440; -.
DR PaxDb; Q01637; -.
DR PRIDE; Q01637; -.
DR DNASU; 42493; -.
DR EnsemblMetazoa; FBtr0084038; FBpp0083440; FBgn0003257.
DR GeneID; 42493; -.
DR KEGG; dme:Dmel_CG3593; -.
DR CTD; 42493; -.
DR FlyBase; FBgn0003257; r-l.
DR VEuPathDB; VectorBase:FBgn0003257; -.
DR eggNOG; KOG1377; Eukaryota.
DR GeneTree; ENSGT00390000001856; -.
DR HOGENOM; CLU_049275_1_0_1; -.
DR InParanoid; Q01637; -.
DR OMA; DHLGQQY; -.
DR OrthoDB; 1303452at2759; -.
DR PhylomeDB; Q01637; -.
DR Reactome; R-DME-500753; Pyrimidine biosynthesis.
DR SignaLink; Q01637; -.
DR UniPathway; UPA00070; UER00119.
DR UniPathway; UPA00070; UER00120.
DR BioGRID-ORCS; 42493; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42493; -.
DR PRO; PR:Q01637; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003257; Expressed in mouthpart and 43 other tissues.
DR Genevisible; Q01637; DM.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IMP:FlyBase.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IMP:FlyBase.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IC:FlyBase.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
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..493
FT /note="Uridine 5'-monophosphate synthase"
FT /id="PRO_0000139652"
FT REGION 1..207
FT /note="OPRTase"
FT REGION 208..233
FT /note="Domain linker"
FT REGION 234..493
FT /note="OMPdecase"
FT ACT_SITE 320
FT /evidence="ECO:0000250"
FT CONFLICT 47..51
FT /note="YPDVM -> LGLPQ (in Ref. 1; AAA29012)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="L -> R (in Ref. 1; AAA29012)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..223
FT /note="GDVVR -> VTFPA (in Ref. 1; AAA29012)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="N -> S (in Ref. 1; AAA29012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 53419 MW; 5293C47D353E45B1 CRC64;
MVAQNSDKMR ALALKLFEIN AFKFGDFKMK VGINSPVYFD LRVIVSYPDV MQTVSDLLVE
HIKDKQLSAK HVCGVPYTAL PLATIVSVQQ GTPMLVRRKE AKAYGTKKLV EGIFNAGDTC
LIVEDVVTSG SSILDTVRDL QGEGIVVTDA VVVVDREQGG VANIAKHGVR MHSLFTLSFL
LNTLHEAGRI EKSTVEAVAK YIAAVQINSD GTFVGGDKGD VVRANDLQRT KLTYENRANL
AKSAVAKRLF NLIASKQTNL CLAADLTHAD EILDVADKCG PYICLLKTHV DIVEDFSDKF
IADLQALAQR HNFLLMEDRK FADIGNTVSL QYGKGIYKIS SWADLVTAHT LPGRSILQGL
KAGLGEGGAG KERGVFLLAE MSASGNLIDA KYKENSNKIA TEGADVDFVA GVVCQSSDAF
AFPGLLQLTP GVKIDEGVDQ LGQQYQSPEH VVKERGADIG VVGRGILKAS SPKQAAQTYR
DRLWAAYQDR VAK
