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Q01637

- UMPS_DROME

UniProt

Q01637 - UMPS_DROME

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Protein

Uridine 5'-monophosphate synthase

Gene

r-l

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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_204719. 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: 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.

Structurei

3D structure databases

ProteinModelPortaliQ01637.
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 13, 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L00968 Genomic DNA. Translation: AAA29012.1 .
AE014297 Genomic DNA. Translation: AAF55842.1 .
AY058714 mRNA. Translation: AAL13943.1 .
X54230 mRNA. Translation: CAA38138.1 .
PIRi JU0141.
RefSeqi NP_524427.1. NM_079703.3.
UniGenei Dm.1654.

3D structure databases

ProteinModelPortali Q01637.
SMRi Q01637. Positions 12-202, 231-492.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 67464. 16 interactions.

Proteomic databases

PaxDbi Q01637.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0084038 ; FBpp0083440 ; FBgn0003257 .
GeneIDi 42493.
KEGGi dme:Dmel_CG3593.

Organism-specific databases

CTDi 42493.
FlyBasei FBgn0003257. r-l.

Phylogenomic databases

eggNOGi COG0284.
GeneTreei ENSGT00390000001856.
InParanoidi Q01637.
KOi K13421.
OMAi SMKPEFL.
OrthoDBi EOG754HPB.
PhylomeDBi Q01637.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00119 .
UPA00070 ; UER00120 .
Reactomei REACT_204719. Pyrimidine biosynthesis.

Miscellaneous databases

GenomeRNAii 42493.
NextBioi 829081.
PROi Q01637.

Gene expression databases

Bgeei Q01637.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
3.40.50.2020. 1 hit.
HAMAPi MF_01208. PyrE.
InterProi IPR013785. 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 ]
Pfami PF00215. OMPdecase. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view ]
SMARTi SM00934. OMPdecase. 1 hit.
[Graphical view ]
SUPFAMi SSF51366. SSF51366. 1 hit.
SSF53271. SSF53271. 1 hit.
TIGRFAMsi TIGR00336. pyrE. 1 hit.
TIGR01740. pyrF. 1 hit.
PROSITEi PS00156. OMPDECASE. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1993) [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(2000) [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(1990) [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: July 1, 1993
Last sequence update: September 13, 2005
Last modified: October 1, 2014
This is version 113 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