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Reviewed, UniProtKB/Swiss-Prot Q01637 (PYR5_DROME)

Last modified November 3, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Uridine 5'-monophosphate synthase
      Short name=UMP synthase
Alternative name(s):
    Rudimentary-like protein
Including the following 2 domains:
    1- Recommended name:
            Orotate phosphoribosyltransferase
                Short name=OPRTase
              EC=2.4.2.10
    2- Recommended name:
            Orotidine 5'-phosphate decarboxylase
              EC=4.1.1.23
        Alternative name(s):
            OMPdecase
Gene names
Name: r-l
ORF Names: CG3593
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

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

Orotidine 5'-phosphate = UMP + CO2.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.

Sequence similarities

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

In the C-terminal section; belongs to the OMP decarboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Uridine 5'-monophosphate synthase
PRO_0000139652

Regions

Region1 – 207207OPRTase
Region208 – 23326Domain linker
Region234 – 493260OMPdecase

Sites

Active site3201 By similarity

Experimental info

Sequence conflict47 – 515YPDVM → LGLPQ in AAA29012. Ref.1
Sequence conflict821L → R in AAA29012. Ref.1
Sequence conflict219 – 2235GDVVR → VTFPA in AAA29012. Ref.1
Sequence conflict2361N → S in AAA29012. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q01637-1 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: 5293C47D353E45B1

FASTA49353,419
        10         20         30         40         50         60 
MVAQNSDKMR ALALKLFEIN AFKFGDFKMK VGINSPVYFD LRVIVSYPDV MQTVSDLLVE 

        70         80         90        100        110        120 
HIKDKQLSAK HVCGVPYTAL PLATIVSVQQ GTPMLVRRKE AKAYGTKKLV EGIFNAGDTC 

       130        140        150        160        170        180 
LIVEDVVTSG SSILDTVRDL QGEGIVVTDA VVVVDREQGG VANIAKHGVR MHSLFTLSFL 

       190        200        210        220        230        240 
LNTLHEAGRI EKSTVEAVAK YIAAVQINSD GTFVGGDKGD VVRANDLQRT KLTYENRANL 

       250        260        270        280        290        300 
AKSAVAKRLF NLIASKQTNL CLAADLTHAD EILDVADKCG PYICLLKTHV DIVEDFSDKF 

       310        320        330        340        350        360 
IADLQALAQR HNFLLMEDRK FADIGNTVSL QYGKGIYKIS SWADLVTAHT LPGRSILQGL 

       370        380        390        400        410        420 
KAGLGEGGAG KERGVFLLAE MSASGNLIDA KYKENSNKIA TEGADVDFVA GVVCQSSDAF 

       430        440        450        460        470        480 
AFPGLLQLTP GVKIDEGVDQ LGQQYQSPEH VVKERGADIG VVGRGILKAS SPKQAAQTYR 

       490 
DRLWAAYQDR VAK 

« Hide

References

« Hide 'large scale' references
[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: 8444350] [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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
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: 2122228] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-78.
+Additional computationally mapped references.

Cross-references

Sequence databases

L00968 Genomic DNA. Translation: AAA29012.1.
AE014297 Genomic DNA. Translation: AAF55842.1.
AY058714 mRNA. Translation: AAL13943.1.
X54230 mRNA. Translation: CAA38138.1.
PIRJU0141.
RefSeqNP_524427.1.
UniGeneDm.1654

3D structure databases

HSSPHSSP built from PDB template 1DQW based on UniProtKB P03962.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ01637.

Genome annotation databases

EnsemblFBtr0084038; FBpp0083440; FBgn0003257; Drosophila melanogaster. [Genome view]
GeneID42493.
KEGGdme:Dmel_CG3593.
NMPDRfig|7227.3.peg.13843.

Organism-specific databases

CTD42493.
FlyBaseFBgn0003257. r-l.

Phylogenomic databases

HOGENOMQ01637.
OMAPLATVIC.

Enzyme and pathway databases

BRENDA2.4.2.10. 48.
4.1.1.23. 48.

Gene expression databases

ArrayExpressQ01637.
GermOnlineCG3593. Drosophila melanogaster.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase_1_core.
IPR018089. OMPdecase_AS.
IPR001754. OMPdecase_core.
IPR004467. Or_phspho_trans.
IPR002375. Pr/py_Pribosyl_transf_CS.
IPR000836. PRibTrfase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF00215. OMPdecase. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR00336. pyrE. 1 hit.
TIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio829081.

Entry information

Entry namePYR5_DROME
AccessionPrimary (citable) accession number: Q01637
Secondary accession number(s): Q24221, Q9VDF2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: September 13, 2005
Last modified: November 3, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents