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Q9I7S8 (PUR6_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multifunctional protein ADE2
Alternative name(s):
Protein adenosine-5

Including the following 2 domains:

  1. Phosphoribosylaminoimidazole-succinocarboxamide synthase
    EC=6.3.2.6
    Alternative name(s):
    SAICAR synthetase
  2. Phosphoribosylaminoimidazole carboxylase
    EC=4.1.1.21
    Alternative name(s):
    AIR carboxylase
    Short name=AIRC
Gene names
Name:ade5
ORF Names:CG3989
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate. UniProtKB P22234

5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2. UniProtKB P22234

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.

Sequence similarities

In the N-terminal section; belongs to the SAICAR synthetase family.

In the C-terminal section; belongs to the AIR carboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Multifunctional protein ADE2
PRO_0000075035

Regions

Region7 – 264258SAICAR synthetase
Region265 – 429165AIR carboxylase

Sequences

Sequence LengthMass (Da)Tools
Q9I7S8 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: CF490A1D20CA2C7F

FASTA42947,281
        10         20         30         40         50         60 
MSTTTTASIE GYKLGKVIIE GKTKQVYDLP EQPGLCLLLS KDRITAGDGV KAHDLAGKAE 

        70         80         90        100        110        120 
ISNTTNGQVF RLLNEAGIRT AYVKQCGAKA FIARKCQMIP IEWVTRRLAT GSFLKRNVGV 

       130        140        150        160        170        180 
PEGYRFSPPK QETFFKDDAN HDPQWSEEQI VSAKFELNGL VIGQDEVDIM RRTTLLVFEI 

       190        200        210        220        230        240 
LERAWQTKNC ALIDMKVEFG ICDDGNIVLA DIIDSDSWRL WPAGDKRLMV DKQVYRNLAS 

       250        260        270        280        290        300 
VTASDLDTVK RNFIWVAEQL ADIVPKKDHL VVILMGSASD ISHSEKIATS CRSLGLNVEL 

       310        320        330        340        350        360 
RVSSAHKGPE ETLRIVREYE SVMSNLIFVA VAGRSNGLGP VVSGSTNYPV INCPPVKSDN 

       370        380        390        400        410        420 
MQVDVWSSLN LPSGLGCATV LYPEAAALHA ATILGLGNFM VWSKLRVKAL NNFITLKKAD 


KELRGVRNA

« Hide

References

« Hide 'large scale' references
[1]"The Drosophila melanogaster ade5 gene encodes a bifunctional enzyme for two steps in the de novo purine synthesis pathway."
O'Donnell A.F., Tiong S., Nash D., Clark D.V.
Genetics 154:1239-1253(2000) [PubMed: 10757766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: Canton-S.
[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.
Strain: Berkeley.
[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: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF102579 mRNA. Translation: AAF06355.1.
AF102580 Genomic DNA. Translation: AAF06356.1.
AE014298 Genomic DNA. Translation: AAG22346.2.
AY095520 mRNA. Translation: AAM12252.1.
RefSeqNP_572826.1. NM_132598.3.
UniGeneDm.3315.

3D structure databases

ProteinModelPortalQ9I7S8.
SMRQ9I7S8. Positions 12-426.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9I7S8. 1 interaction.
MINTMINT-317742.
STRINGQ9I7S8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0073705; FBpp0073538; FBgn0020513.
GeneID32228.
KEGGdme:Dmel_CG3989.
NMPDRfig|7227.3.peg.17608.

Organism-specific databases

CTD32228.
FlyBaseFBgn0020513. ade5.

Phylogenomic databases

eggNOGinNOG08656.
GeneTreeEMGT00050000017964.
InParanoidQ9I7S8.
OMAQCRVVVL.
OrthoDBEOG43FFC5.
PhylomeDBQ9I7S8.

Gene expression databases

ArrayExpressQ9I7S8.
BgeeQ9I7S8.
GermOnlineCG3989. Drosophila melanogaster.

Family and domain databases

InterProIPR013816. ATP_grasp_subdomain_2.
IPR000031. N5-CAIR_Mutase_PurE_dom.
IPR001636. SAICAR_synth.
IPR018236. SAICAR_synthetase_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.7700. AIR_carboxyl. 1 hit.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
KOK01587.
PANTHERPTHR11609. SAICAR_synt. 1 hit.
PfamPF00731. AIRC. 1 hit.
PF01259. SAICAR_synt. 1 hit.
[Graphical view]
SMARTSM01001. AIRC. 1 hit.
[Graphical view]
SUPFAMSSF52255. AIR_carboxyl. 1 hit.
TIGRFAMsTIGR01162. PurE. 1 hit.
PROSITEPS01057. SAICAR_SYNTHETASE_1. 1 hit.
PS01058. SAICAR_SYNTHETASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio777492.

Entry information

Entry namePUR6_DROME
AccessionPrimary (citable) accession number: Q9I7S8
Secondary accession number(s): Q9TVK1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents