SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q01637

- UMPS_DROME

UniProt

Q01637 - UMPS_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Uridine 5'-monophosphate synthase
Gene
r-l, CG3593
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.UniRule annotation
Orotidine 5'-phosphate = UMP + CO2.UniRule annotation

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 207207OPRTaseUniRule annotation
Add
BLAST
Regioni208 – 23326Domain linkerUniRule annotation
Add
BLAST
Regioni234 – 493260OMPdecaseUniRule annotation
Add
BLAST

Sequence similaritiesi

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

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

MVAQNSDKMR ALALKLFEIN AFKFGDFKMK VGINSPVYFD LRVIVSYPDV    50
MQTVSDLLVE HIKDKQLSAK HVCGVPYTAL PLATIVSVQQ GTPMLVRRKE 100
AKAYGTKKLV EGIFNAGDTC LIVEDVVTSG SSILDTVRDL QGEGIVVTDA 150
VVVVDREQGG VANIAKHGVR MHSLFTLSFL LNTLHEAGRI EKSTVEAVAK 200
YIAAVQINSD GTFVGGDKGD VVRANDLQRT KLTYENRANL AKSAVAKRLF 250
NLIASKQTNL CLAADLTHAD EILDVADKCG PYICLLKTHV DIVEDFSDKF 300
IADLQALAQR HNFLLMEDRK FADIGNTVSL QYGKGIYKIS SWADLVTAHT 350
LPGRSILQGL KAGLGEGGAG KERGVFLLAE MSASGNLIDA KYKENSNKIA 400
TEGADVDFVA GVVCQSSDAF AFPGLLQLTP GVKIDEGVDQ LGQQYQSPEH 450
VVKERGADIG VVGRGILKAS SPKQAAQTYR DRLWAAYQDR VAK 493
Length:493
Mass (Da):53,419
Last modified:September 13, 2005 - v2
Checksum:i5293C47D353E45B1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 515YPDVM → LGLPQ in AAA29012. 1 Publication
Sequence conflicti82 – 821L → R in AAA29012. 1 Publication
Sequence conflicti219 – 2235GDVVR → VTFPA in AAA29012. 1 Publication
Sequence conflicti236 – 2361N → S in AAA29012. 1 Publication

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: September 3, 2014
This is version 112 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