Reviewed, UniProtKB/Swiss-Prot P00967 (PUR2_DROME)

Names and origin

Protein names

Recommended name:
    Trifunctional purine biosynthetic protein adenosine-3
Including 3 domains:
  Recommended name:
      Phosphoribosylamine--glycine ligase
      EC=6.3.4.13
  Alternative name(s):
      Glycinamide ribonucleotide synthetase
        Short name(s)=GARS
      Phosphoribosylglycinamide synthetase
  Recommended name:
      Phosphoribosylformylglycinamidine cyclo-ligase
      EC=6.3.3.1
  Alternative name(s):
      Phosphoribosyl-aminoimidazole synthetase
      AIR synthase
        Short name(s)=AIRS
  Recommended name:
      Phosphoribosylglycinamide formyltransferase
      EC=2.1.2.2
  Alternative name(s):
      5'-phosphoribosylglycinamide transformylase
      GAR transformylase
        Short name(s)=GART

Gene names

Name:	ade3
Synonyms:	Gart
ORF Names:	CG31628

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	1353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. 10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5. Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Sequence similarities	In the N-terminal section; belongs to the GARS family. In the central section; belongs to the AIR synthase family. In the C-terminal section; belongs to the GART family. Contains 1 ATP-grasp domain.

Ontologies

Keywords
Biological process	Purine biosynthesis
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
None. [Check GOA]

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P00967-1)

Also known as: A; 4.7 kb;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P00967-2)

Also known as: 1.7 kb;

The sequence of this isoform differs from the canonical sequence as follows:
     434-434: I → M
     435-1353: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 1353	1353	Trifunctional purine biosynthetic protein adenosine-3
Regions
	Domain	114 – 321	208	ATP-grasp
	Nucleotide binding	140 – 202	63	ATP By similarity
	Region	434 – 1152	719	AIRS
	Region	1153 – 1353	201	GART
	Region	1164 – 1166	3	5'-phosphoribosylglycinamide binding By similarity
	Region	1244 – 1247	4	10-formyltetrahydrofolate binding By similarity
	Region	1295 – 1299	5	10-formyltetrahydrofolate binding By similarity
	Region	1325 – 1328	4	5'-phosphoribosylglycinamide binding By similarity
Sites
	Active site	1263	1	Proton donor By similarity
	Metal binding	291	1	Manganese By similarity
	Metal binding	293	1	Manganese By similarity
	Binding site	1219	1	10-formyltetrahydrofolate By similarity
	Binding site	1261	1	10-formyltetrahydrofolate By similarity
	Site	1299	1	Raises pKa of active site His By similarity
Amino acid modifications
	Modified residue	814	1	Phosphoserine
	Modified residue	816	1	Phosphoserine
Natural variations
	Alternative sequence	434	1	I → M in isoform Short.
	Alternative sequence	435 – 1353	919	Missing in isoform Short.
Experimental info
	Sequence conflict	515	1	F → L in AAF52474. Ref.2
	Sequence conflict	602	1	H → Q in AAF52474. Ref.2
	Sequence conflict	907	1	G → E in AAF52474. Ref.2
	Sequence conflict	960	1	A → D in AAF52474. Ref.2
	Sequence conflict	1193	1	P → T in AAF52474. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long (A) (4.7 kb) [UniParc]. Last modified April 1, 1990. Version 2. Checksum: A68DAB61A02DFD4F	FASTA	1,353	144,448
	10 20 30 40 50 60 MSHRVLVIGS GGREHAICWK LSQSPKVAQI YALPGSHGIQ LVEKCRNLDA KTLDPKDFEA 70 80 90 100 110 120 IAKWSKENQI ALVVVGPEDP LALGLGDVLQ SAGIPCFGPG KQGAQIEADK KWAKDFMLRH 130 140 150 160 170 180 GIPTARYESF TDTEKAKAFI RSAPYPALVV KAAGLAAGKG VVVAANAKEA CQAVDEILGD 190 200 210 220 230 240 LKYGQAGATL VVEELLEGEE VSVLAFTDGK SVRAMLPAQD HKRLGNGDTG PNTGGMGAYC 250 260 270 280 290 300 PCPLISQPAL ELVQKAVLER AVQGLIKERI NYQGVLYAGL MLTRDGPRVL EFNCRFGDPE 310 320 330 340 350 360 TQVILPLLES DLFDVMEACC SGKLDKIPLQ WRNGVSAVGV ILASAGYPET STKGCIISGL 370 380 390 400 410 420 PAANTPTQLV FHSGLAVNAQ KEALTNGGRV LIAIALDGSL KEAAAKATKL AGSISFSGSG 430 440 450 460 470 480 AQYRTDIAQK AFKIASASTP GLSYKDSGVD IDAGDALVQR IKPLSRGTQR PGVIGGLGGF 490 500 510 520 530 540 GGLFRLKELT YKEPVIAEAT QGVGAKIHLA LTHEFYENVG YDLFALAAND VLEVGAEPVA 550 560 570 580 590 600 FLDYIACGKL QVPLAAQLVK GMADGCRDAR CALVGGETAE MPSLYAPGQH DMAGYCVGIV 610 620 630 640 650 660 EHSRILPRFD LYQPGDLLIG LPSSGLHCAG FNEILTQLAA SKVNLRERSP VDGGDDGLTL 670 680 690 700 710 720 AHVLATPTQL YVQQLLPHLQ KGDEIKSVAH VTHGLLNDIL RLLPDGFETT LDFGAVPVPK 730 740 750 760 770 780 IFGWLAGKLK LSAQTILERH NCGIGMVLIL PQSSQLWRTS LPGAKVLGVL QRRSKVSGSP 790 800 810 820 830 840 VQVRNFVEQL EKVASPFGGL GDRELPEELK KLPSNSDLSA PREECFENAA GRRLTRIPTH 850 860 870 880 890 900 YKDPILILGT DGVGTKLKIA QQTNRNTSVG IDLVAMCVND ILCNGAEPIS FSSYYACGHW 910 920 930 940 950 960 QEQLAKGVHS GVQEGARQAN SSFIDSHSAA LPLLYEPQVY DLAGFALGIA EHTGILPLLA 970 980 990 1000 1010 1020 EIQPGDVLIG LPSSGVHSNG FSLVHAVLKR VGLGLHDKAP FSDKTLGEEL LVPTKIYVKA 1030 1040 1050 1060 1070 1080 LSTLLSRGKH GIKALAHITG GGLSENIPRV LRKDLAVRLD ANKFQLPPVF AWLAAAGNIS 1090 1100 1110 1120 1130 1140 STELQRTYNC GLGMVLVVAP TEVEDVLKEL RYPQRAAVVG EVVARKDPKK SQVVVQNFEA 1150 1160 1170 1180 1190 1200 SLARTQKMLS QRRKRVAVLI SGTGSNLQAL IDATRDSAQG IHADVVLVIS NKPGVLGLQR 1210 1220 1230 1240 1250 1260 ATQAGIPSLV ISHKDFASRE VYDAELTRNL KAARVDLICL AGFMRVLSAP FVREWRGRLV 1270 1280 1290 1300 1310 1320 NIHPSLLPKY PGLHVQKQAL EAGEKESGCT VHFVDEGVDT GAIIVQAAVP ILPDDDEDSL 1330 1340 1350 TQRIHKAEHW AFPRALAMLV NGTALISPEV SSQ
	Isoform Short (1.7 kb) [UniParc]. Checksum: 0EF3BD499D8B8495		434	45,864
	10 20 30 40 50 60 MSHRVLVIGS GGREHAICWK LSQSPKVAQI YALPGSHGIQ LVEKCRNLDA KTLDPKDFEA 70 80 90 100 110 120 IAKWSKENQI ALVVVGPEDP LALGLGDVLQ SAGIPCFGPG KQGAQIEADK KWAKDFMLRH 130 140 150 160 170 180 GIPTARYESF TDTEKAKAFI RSAPYPALVV KAAGLAAGKG VVVAANAKEA CQAVDEILGD 190 200 210 220 230 240 LKYGQAGATL VVEELLEGEE VSVLAFTDGK SVRAMLPAQD HKRLGNGDTG PNTGGMGAYC 250 260 270 280 290 300 PCPLISQPAL ELVQKAVLER AVQGLIKERI NYQGVLYAGL MLTRDGPRVL EFNCRFGDPE 310 320 330 340 350 360 TQVILPLLES DLFDVMEACC SGKLDKIPLQ WRNGVSAVGV ILASAGYPET STKGCIISGL 370 380 390 400 410 420 PAANTPTQLV FHSGLAVNAQ KEALTNGGRV LIAIALDGSL KEAAAKATKL AGSISFSGSG 430 AQYRTDIAQK AFKM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conserved arrangement of nested genes at the Drosophila Gart locus." Henikoff S., Eghtedarzadeh M.K. Genetics 117:711-725(1987) [PubMed: 3123310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT). Strain: Canton-S. Tissue: Embryo.
[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 metabolic gene transcript is alternatively processed." Henikoff S., Sloan J.S., Kelly J.D. Cell 34:405-414(1983) [PubMed: 6413075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-1353, ALTERNATIVE SPLICING. Strain: Canton-S and Oregon-R. Tissue: Embryo.
[5]	"Sequence of a Drosophila DNA segment that functions in Saccharomyces cerevisiae and its regulation by a yeast promoter." Henikoff S., Furlong C.E. Nucleic Acids Res. 11:789-800(1983) [PubMed: 6300768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1147-1353 (ISOFORM LONG). Strain: Oregon-R. Tissue: Embryo.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-814 AND SER-816, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J02527 Genomic DNA. Translation: AAA28562.1. J02527 Genomic DNA. Translation: AAA28563.1. AE014134 Genomic DNA. Translation: AAF52474.2. X00041 Genomic DNA. Translation: CAA24923.1.
PIR	AJFFPM. S01206.
RefSeq	NP_523497.2.
UniGene	Dm.21459
3D structure databases
HSSP	HSSP built from PDB template 1GAR based on UniProtKB P08179.
ModBase	Search...
Genome annotation databases
Ensembl	CG31628. Drosophila melanogaster. [Contig view]
GeneID	33986.
Organism-specific databases
FlyBase	FBgn0000053. ade3.
Phylogenomic databases
HOGENOM	P00967.
Gene expression databases
ArrayExpress	P00967.
GermOnline	CG31628. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000728. AIR_synth. IPR010918. AIR_synth_C. IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR002376. Formyl_transf_N. IPR000115. Gars. IPR001555. GART_AS. IPR013817. Pre-ATP_grasp. IPR004733. PurM_cligase. IPR004607. PurN_trans. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit. G3DSA:3.40.50.170. Formyl_transf_N. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
Pfam	PF00586. AIRS. 2 hits. PF02769. AIRS_C. 2 hits. PF00551. Formyl_trans_N. 1 hit. PF01071. GARS_A. 1 hit. PF02843. GARS_C. 1 hit. PF02844. GARS_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00877. purD. 1 hit. TIGR00878. purM. 2 hits. TIGR00639. PurN. 1 hit.
PROSITE	PS50975. ATP_GRASP. 1 hit. PS00184. GARS. 1 hit. PS00373. GART. 1 hit. [Graphical view]
ProDom	P00967. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

PUR2_DROME

Accession

Primary (citable) accession number: P00967
Secondary accession number(s): Q9VM53

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1990
Last modified:	July 22, 2008
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project