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Protein

Uridine 5'-monophosphate synthase

Gene

r-l

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate.
Orotidine 5'-phosphate = UMP + CO2.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei320 – 3201By similarity

GO - Molecular functioni

  1. orotate phosphoribosyltransferase activity Source: FlyBase
  2. orotidine-5'-phosphate decarboxylase activity Source: FlyBase

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: FlyBase
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Glycosyltransferase, Lyase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Enzyme and pathway databases

ReactomeiREACT_310550. Pyrimidine biosynthesis.
UniPathwayiUPA00070; UER00119.
UPA00070; UER00120.

Names & Taxonomyi

Protein namesi
Recommended name:
Uridine 5'-monophosphate synthase
Short name:
UMP synthase
Alternative name(s):
Rudimentary-like protein
Including the following 2 domains:
Orotate phosphoribosyltransferase (EC:2.4.2.10)
Short name:
OPRTase
Orotidine 5'-phosphate decarboxylase (EC:4.1.1.23)
Alternative name(s):
OMPdecase
Gene namesi
Name:r-l
ORF Names:CG3593
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003257. r-l.

Subcellular locationi

GO - Cellular componenti

  1. microtubule associated complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493Uridine 5'-monophosphate synthasePRO_0000139652Add
BLAST

Proteomic databases

PaxDbiQ01637.

Expressioni

Gene expression databases

BgeeiQ01637.

Interactioni

Protein-protein interaction databases

BioGridi67464. 16 interactions.
IntActiQ01637. 1 interaction.

Structurei

3D structure databases

SMRiQ01637. Positions 12-202, 231-492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 207207OPRTaseAdd
BLAST
Regioni208 – 23326Domain linkerAdd
BLAST
Regioni234 – 493260OMPdecaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated
In the C-terminal section; belongs to the OMP decarboxylase family.Curated

Phylogenomic databases

eggNOGiCOG0284.
GeneTreeiENSGT00390000001856.
InParanoidiQ01637.
KOiK13421.
OMAiSMKPEFL.
OrthoDBiEOG754HPB.
PhylomeDBiQ01637.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE.
InterProiIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00215. OMPdecase. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
SMARTiSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
SSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00336. pyrE. 1 hit.
TIGR01740. pyrF. 1 hit.
PROSITEiPS00156. OMPDECASE. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01637-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAQNSDKMR ALALKLFEIN AFKFGDFKMK VGINSPVYFD LRVIVSYPDV
60 70 80 90 100
MQTVSDLLVE HIKDKQLSAK HVCGVPYTAL PLATIVSVQQ GTPMLVRRKE
110 120 130 140 150
AKAYGTKKLV EGIFNAGDTC LIVEDVVTSG SSILDTVRDL QGEGIVVTDA
160 170 180 190 200
VVVVDREQGG VANIAKHGVR MHSLFTLSFL LNTLHEAGRI EKSTVEAVAK
210 220 230 240 250
YIAAVQINSD GTFVGGDKGD VVRANDLQRT KLTYENRANL AKSAVAKRLF
260 270 280 290 300
NLIASKQTNL CLAADLTHAD EILDVADKCG PYICLLKTHV DIVEDFSDKF
310 320 330 340 350
IADLQALAQR HNFLLMEDRK FADIGNTVSL QYGKGIYKIS SWADLVTAHT
360 370 380 390 400
LPGRSILQGL KAGLGEGGAG KERGVFLLAE MSASGNLIDA KYKENSNKIA
410 420 430 440 450
TEGADVDFVA GVVCQSSDAF AFPGLLQLTP GVKIDEGVDQ LGQQYQSPEH
460 470 480 490
VVKERGADIG VVGRGILKAS SPKQAAQTYR DRLWAAYQDR VAK
Length:493
Mass (Da):53,419
Last modified:September 12, 2005 - v2
Checksum:i5293C47D353E45B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 515YPDVM → LGLPQ in AAA29012 (PubMed:8444350).Curated
Sequence conflicti82 – 821L → R in AAA29012 (PubMed:8444350).Curated
Sequence conflicti219 – 2235GDVVR → VTFPA in AAA29012 (PubMed:8444350).Curated
Sequence conflicti236 – 2361N → S in AAA29012 (PubMed:8444350).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00968 Genomic DNA. Translation: AAA29012.1.
AE014297 Genomic DNA. Translation: AAF55842.1.
AY058714 mRNA. Translation: AAL13943.1.
X54230 mRNA. Translation: CAA38138.1.
PIRiJU0141.
RefSeqiNP_524427.1. NM_079703.3.
UniGeneiDm.1654.

Genome annotation databases

EnsemblMetazoaiFBtr0084038; FBpp0083440; FBgn0003257.
GeneIDi42493.
KEGGidme:Dmel_CG3593.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00968 Genomic DNA. Translation: AAA29012.1.
AE014297 Genomic DNA. Translation: AAF55842.1.
AY058714 mRNA. Translation: AAL13943.1.
X54230 mRNA. Translation: CAA38138.1.
PIRiJU0141.
RefSeqiNP_524427.1. NM_079703.3.
UniGeneiDm.1654.

3D structure databases

SMRiQ01637. Positions 12-202, 231-492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67464. 16 interactions.
IntActiQ01637. 1 interaction.

Proteomic databases

PaxDbiQ01637.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084038; FBpp0083440; FBgn0003257.
GeneIDi42493.
KEGGidme:Dmel_CG3593.

Organism-specific databases

CTDi42493.
FlyBaseiFBgn0003257. r-l.

Phylogenomic databases

eggNOGiCOG0284.
GeneTreeiENSGT00390000001856.
InParanoidiQ01637.
KOiK13421.
OMAiSMKPEFL.
OrthoDBiEOG754HPB.
PhylomeDBiQ01637.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00119.
UPA00070; UER00120.
ReactomeiREACT_310550. Pyrimidine biosynthesis.

Miscellaneous databases

GenomeRNAii42493.
NextBioi829081.
PROiQ01637.

Gene expression databases

BgeeiQ01637.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE.
InterProiIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00215. OMPdecase. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
SMARTiSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
SSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00336. pyrE. 1 hit.
TIGR01740. pyrF. 1 hit.
PROSITEiPS00156. OMPDECASE. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the rudimentary-like gene and UMP synthase in Drosophila melanogaster."
    Eisenberg M., Kirkpatrick R., Rawls J.
    Gene 124:263-267(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Molecular cloning of the UMP synthase gene rudimentary-like from Drosophila melanogaster."
    Eisenberg M.T., Gathy K., Vincent T., Rawls J.
    Mol. Gen. Genet. 222:1-8(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-78.

Entry informationi

Entry nameiUMPS_DROME
AccessioniPrimary (citable) accession number: Q01637
Secondary accession number(s): Q24221, Q9VDF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1993
Last sequence update: September 12, 2005
Last modified: March 31, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.