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Protein

Trifunctional purine biosynthetic protein adenosine-3

Gene

ade3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide.
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.
10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoribosylformylglycinamidine synthase (ade2)
  2. Trifunctional purine biosynthetic protein adenosine-3 (ade3), Trifunctional purine biosynthetic protein adenosine-3 (Gart), Trifunctional purine biosynthetic protein adenosine-3 (ade3-RA)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Amidophosphoribosyltransferase (Prat), Amidophosphoribosyltransferase (Prat), Amidophosphoribosyltransferase (Prat2), Amidophosphoribosyltransferase (CG2867), Amidophosphoribosyltransferase (CG2867), Amidophosphoribosyltransferase (Prat2)
  2. Trifunctional purine biosynthetic protein adenosine-3 (ade3), Trifunctional purine biosynthetic protein adenosine-3 (Gart), Trifunctional purine biosynthetic protein adenosine-3 (ade3-RA)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route).
Proteins known to be involved in this subpathway in this organism are:
  1. Trifunctional purine biosynthetic protein adenosine-3 (ade3), Trifunctional purine biosynthetic protein adenosine-3 (Gart), Trifunctional purine biosynthetic protein adenosine-3 (ade3-RA)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi291ManganeseBy similarity1
Metal bindingi293ManganeseBy similarity1
Binding sitei121910-formyltetrahydrofolateBy similarity1
Binding sitei126110-formyltetrahydrofolateBy similarity1
Active sitei1263Proton donorBy similarity1
Sitei1299Raises pKa of active site HisBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 202ATPBy similarityAdd BLAST63

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • phosphoribosylamine-glycine ligase activity Source: FlyBase
  • phosphoribosylformylglycinamidine cyclo-ligase activity Source: FlyBase
  • phosphoribosylglycinamide formyltransferase activity Source: FlyBase

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  • purine nucleobase biosynthetic process Source: FlyBase

Keywordsi

Molecular functionLigase, Multifunctional enzyme, Transferase
Biological processPurine biosynthesis
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-73817 Purine ribonucleoside monophosphate biosynthesis
UniPathwayiUPA00074; UER00125
UPA00074; UER00126
UPA00074; UER00129

Names & Taxonomyi

Protein namesi
Recommended name:
Trifunctional purine biosynthetic protein adenosine-3
Including the following 3 domains:
Phosphoribosylamine--glycine ligase (EC:6.3.4.13)
Alternative name(s):
Glycinamide ribonucleotide synthetase
Short name:
GARS
Phosphoribosylglycinamide synthetase
Phosphoribosylformylglycinamidine cyclo-ligase (EC:6.3.3.1)
Alternative name(s):
AIR synthase
Short name:
AIRS
Phosphoribosyl-aminoimidazole synthetase
Phosphoribosylglycinamide formyltransferase (EC:2.1.2.2)
Alternative name(s):
5'-phosphoribosylglycinamide transformylase
GAR transformylase
Short name:
GART
Gene namesi
Name:ade3
Synonyms:Gart
ORF Names:CG31628
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000053 ade3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000749341 – 1353Trifunctional purine biosynthetic protein adenosine-3Add BLAST1353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei814Phosphoserine1 Publication1
Modified residuei816Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00967
PRIDEiP00967

PTM databases

iPTMnetiP00967

Expressioni

Gene expression databases

BgeeiFBgn0000053
ExpressionAtlasiP00967 baseline and differential
GenevisibleiP00967 DM

Interactioni

Protein-protein interaction databases

BioGridi60135, 1 interactor
IntActiP00967, 20 interactors
STRINGi7227.FBpp0079059

Structurei

3D structure databases

ProteinModelPortaliP00967
SMRiP00967
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini114 – 321ATP-graspAdd BLAST208

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni434 – 1152AIRSAdd BLAST719
Regioni1153 – 1353GARTAdd BLAST201
Regioni1164 – 11665'-phosphoribosylglycinamide bindingBy similarity3
Regioni1244 – 124710-formyltetrahydrofolate bindingBy similarity4
Regioni1295 – 129910-formyltetrahydrofolate bindingBy similarity5
Regioni1325 – 13285'-phosphoribosylglycinamide bindingBy similarity4

Sequence similaritiesi

In the N-terminal section; belongs to the GARS family.Curated
In the central section; belongs to the AIR synthase family.Curated
In the C-terminal section; belongs to the GART family.Curated

Phylogenomic databases

eggNOGiKOG0237 Eukaryota
KOG3076 Eukaryota
COG0150 LUCA
COG0151 LUCA
COG0299 LUCA
InParanoidiP00967
KOiK11787
OMAiKATVCKY
OrthoDBiEOG091G026D
PhylomeDBiP00967

Family and domain databases

CDDicd08645 FMT_core_GART, 1 hit
cd02196 PurM, 2 hits
Gene3Di3.30.1330.10, 2 hits
3.30.1490.20, 1 hit
3.90.600.10, 1 hit
3.90.650.10, 2 hits
HAMAPiMF_00741 AIRS, 1 hit
MF_00138 GARS, 1 hit
MF_01930 PurN, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR002376 Formyl_transf_N
IPR036477 Formyl_transf_N_sf
IPR004607 GART
IPR001555 GART_AS
IPR016185 PreATP-grasp_dom_sf
IPR020561 PRibGlycinamid_synth_ATP-grasp
IPR000115 PRibGlycinamide_synth
IPR020560 PRibGlycinamide_synth_C-dom
IPR037123 PRibGlycinamide_synth_C_sf
IPR020559 PRibGlycinamide_synth_CS
IPR020562 PRibGlycinamide_synth_N
IPR010918 PurM-like_C_dom
IPR036676 PurM-like_C_sf
IPR016188 PurM-like_N
IPR036921 PurM-like_N_sf
IPR004733 PurM_cligase
IPR011054 Rudment_hybrid_motif
PANTHERiPTHR10520 PTHR10520, 2 hits
PfamiView protein in 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
SMARTiView protein in SMART
SM01210 GARS_C, 1 hit
SUPFAMiSSF51246 SSF51246, 1 hit
SSF52440 SSF52440, 1 hit
SSF53328 SSF53328, 1 hit
SSF55326 SSF55326, 2 hits
SSF56042 SSF56042, 2 hits
TIGRFAMsiTIGR00877 purD, 1 hit
TIGR00878 purM, 2 hits
TIGR00639 PurN, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS00184 GARS, 1 hit
PS00373 GART, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P00967-1) [UniParc]FASTAAdd to basket
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.

« Hide

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

SSQ
Length:1,353
Mass (Da):144,448
Last modified:April 1, 1990 - v2
Checksum:iA68DAB61A02DFD4F
GO
Isoform Short (identifier: P00967-2) [UniParc]FASTAAdd to basket
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.

Show »
Length:434
Mass (Da):45,864
Checksum:i0EF3BD499D8B8495
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti515F → L in AAF52474 (PubMed:10731132).Curated1
Sequence conflicti602H → Q in AAF52474 (PubMed:10731132).Curated1
Sequence conflicti907G → E in AAF52474 (PubMed:10731132).Curated1
Sequence conflicti960A → D in AAF52474 (PubMed:10731132).Curated1
Sequence conflicti1193P → T in AAF52474 (PubMed:10731132).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005512434I → M in isoform Short. Curated1
Alternative sequenceiVSP_005513435 – 1353Missing in isoform Short. CuratedAdd BLAST919

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02527 Genomic DNA Translation: AAA28562.1
J02527 Genomic DNA Translation: AAA28563.1
AE014134 Genomic DNA Translation: AAF52474.2
X00041 Genomic DNA Translation: CAA24923.1
PIRiS01206 AJFFPM
RefSeqiNP_001014477.1, NM_001014477.2 [P00967-2]
NP_001285698.1, NM_001298769.1
NP_523497.2, NM_078773.3
UniGeneiDm.21459

Genome annotation databases

EnsemblMetazoaiFBtr0100353; FBpp0099760; FBgn0000053 [P00967-2]
GeneIDi33986
KEGGidme:Dmel_CG31628

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiPUR2_DROME
AccessioniPrimary (citable) accession number: P00967
Secondary accession number(s): Q9VM53
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: July 18, 2018
This is version 174 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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