Reviewed, UniProtKB/Swiss-Prot Q9I7S8 (PUR6_DROME)

Names and origin

Protein names

Recommended name:
    Multifunctional protein ADE2
Alternative name(s):
    Protein adenosine-5
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazole-succinocarboxamide synthase
              EC=6.3.2.6
        Alternative name(s):
            SAICAR synthetase
    2- Recommended name:
            Phosphoribosylaminoimidazole carboxylase
              EC=4.1.1.21
        Alternative name(s):
            AIR carboxylase
              Short name=AIRC

Gene names

Name:	ade5
ORF Names:	CG3989

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Decarboxylase Ligase Lyase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro inter-male aggressive behavior Inferred from mutant phenotype. Source: FlyBase purine base biosynthetic process Ref.1 Inferred from genetic interaction. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct phosphoribosylaminoimidazole carboxylase activity Ref.1 Traceable author statement. Source: UniProtKB phosphoribosylaminoimidazolesuccinocarboxamide synthase activity Ref.1 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-95676,EBI-95676

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 429	429	Multifunctional protein ADE2		PRO_0000075035
Regions
	Region	7 – 264	258	SAICAR synthetase
	Region	265 – 429	165	AIR carboxylase

Sequences

	Sequence		Length	Mass (Da)
	Q9I7S8-1 [UniParc]. Last modified October 1, 2002. Version 2. Checksum: CF490A1D20CA2C7F	FASTA	429	47,281
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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: 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.
RefSeq	NP_572826.1.
3D structure databases
SMR	Q9I7S8. Positions 13-425.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9I7S8. 1 interaction.
STRING	Q9I7S8.
Genome annotation databases
Ensembl	FBtr0073705; FBpp0073538; FBgn0020513; Drosophila melanogaster. [Genome view]
GeneID	32228.
KEGG	dme:Dmel_CG3989.
NMPDR	fig|7227.3.peg.17608.
Organism-specific databases
CTD	32228.
FlyBase	FBgn0020513. ade5.
Phylogenomic databases
eggNOG	inNOG08656.
InParanoid	Q9I7S8.
OMA	ISCPPLT.
OrthoDB	EOG93XV8W.
PhylomeDB	Q9I7S8.
Enzyme and pathway databases
BRENDA	4.1.1.21. 48. 6.3.2.6. 48.
Gene expression databases
ArrayExpress	Q9I7S8.
Bgee	Q9I7S8.
GermOnline	CG3989. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000031. AIR_COase_core. IPR013816. ATP_grasp_subdomain_2. IPR001636. SAICAR_synt. IPR018236. SAICAR_synthetase_CS. [Graphical view]
Gene3D	G3DSA:3.40.50.7700. AIR_carboxyl. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
PANTHER	PTHR11609. SAICAR_synt. 1 hit.
Pfam	PF00731. AIRC. 1 hit. PF01259. SAICAR_synt. 1 hit. [Graphical view]
TIGRFAMs	TIGR01162. purE. 1 hit.
PROSITE	PS01057. SAICAR_SYNTHETASE_1. 1 hit. PS01058. SAICAR_SYNTHETASE_2. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	777492.

Entry information

Entry name

PUR6_DROME

Accession

Primary (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:	February 9, 2010
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project