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Protein

Phosphoribosylformylglycinamidine synthase

Gene

ade2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity).By similarity

Catalytic activityi

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 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)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei714 – 7141ATP; via carbonyl oxygenBy similarity
Metal bindingi715 – 7151MagnesiumBy similarity
Metal bindingi754 – 7541MagnesiumBy similarity
Metal bindingi758 – 7581MagnesiumBy similarity
Metal bindingi918 – 9181MagnesiumBy similarity
Binding sitei920 – 9201ATPBy similarity
Active sitei1180 – 11801NucleophileBy similarity
Active sitei1310 – 13101By similarity
Active sitei1312 – 13121By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi327 – 33812ATPSequence analysisAdd
BLAST
Nucleotide bindingi407 – 4093ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-73817. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00128.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3)
Short name:
FGAM synthase
Short name:
FGAMS
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferase
Short name:
FGAR amidotransferase
Short name:
FGAR-AT
Formylglycinamide ribotide amidotransferase
Protein adenosine-2
Gene namesi
Name:ade2
ORF Names:CG9127
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000052. ade2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13541354Phosphoribosylformylglycinamidine synthasePRO_0000100403Add
BLAST

Proteomic databases

PaxDbiP35421.

Expressioni

Gene expression databases

BgeeiP35421.
GenevisibleiP35421. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CG9961Q9VQF41EBI-89279,EBI-122086

Protein-protein interaction databases

BioGridi60012. 3 interactions.
DIPiDIP-22769N.
IntActiP35421. 2 interactions.
MINTiMINT-1579795.
STRINGi7227.FBpp0078850.

Structurei

3D structure databases

ProteinModelPortaliP35421.
SMRiP35421. Positions 1086-1313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1087 – 1337251Glutamine amidotransferase type-1Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the FGAMS family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiKOG1907. Eukaryota.
COG0046. LUCA.
COG0047. LUCA.
GeneTreeiENSGT00390000007600.
InParanoidiP35421.
KOiK01952.
OMAiLSANWMW.
OrthoDBiEOG7353X4.
PhylomeDBiP35421.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1.
InterProiIPR010918. AIR_synth_C_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM-like_N.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35421-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVILRYYDVQ AHSAAEEESV LRRLREEDGA VVSVRMERCY HLEYSAQAEH
60 70 80 90 100
SLALDELLVW LVKQPLSKGQ SLSRQPALQS TGSSQLLLEI GPRFNFSTPY
110 120 130 140 150
STNCVNIFQN LGYSEVRRME TSTRYLVTFG EGSKAPEAAR FVPLLGDRMT
160 170 180 190 200
QCLYTEENTP KASFDEQLPE RQANWHFVPV LEEGRAALER INQELGLAFN
210 220 230 240 250
DYDLDYYHDL FAKELGRNPT TVELFDCAQS NSEHSRHWFF RGRMVIDGVE
260 270 280 290 300
QPKSLIRMIM DTQAHTNPNN TIKFSDNSSA MVGFDHQTIV PSSVVAPGAV
310 320 330 340 350
RLQSVQSDLI FTAETHNMPT AVAPFSGATT GTGGRLRDVQ GVGRGGVPIA
360 370 380 390 400
GTAGYCVGAL HIPGYKQPYE PLDFKYPATF APPLQVLIEA SNGASDYGNK
410 420 430 440 450
FGEPVISGFA LSYGLNSAAD ASQRDEYVKP IMFSGGLGTM PATMREKLPP
460 470 480 490 500
ARGQLLAKIG GPVYRIGVGG GAASSVEIQG SGDAELDFNA VQRGDAEMEN
510 520 530 540 550
KLNRVVRACL DLGEQNPILA IHDQGAGGNG NVLKELVEPG FAGAVIFSKE
560 570 580 590 600
FQLGDPTITA LELWGAEYQE NNAILCNADQ RELLEKICRR ERCPISFVGV
610 620 630 640 650
VTGDGRVTLL EKPAPKDLEQ ALNASNRSEV SPFDLELKYV LGDMPKRTYD
660 670 680 690 700
LKREQTPLKE LSLPKGLLLD EALERVLSLV AVGSKRFLTN KVDRCVGGLI
710 720 730 740 750
AQQQCVGPLQ APLADYALTT VSHFSHSGIA TSIGTQPLKG LLDPAAMARM
760 770 780 790 800
CVAEALSNLV FVKISELADV KCSGNWMWAA KLPGEGARMF DACKELCQIL
810 820 830 840 850
EELHIAIDGG KDSLSMAAKV GGETIKSPGT LVISTYAPCP DVRLKVTPDL
860 870 880 890 900
KGPGAGSKTS LLWINLENSA RLGGSALAQA YAQQGKDTPN LTRSDVLGKA
910 920 930 940 950
FAVTQSLLGD GLIQAGHDVS DGGLLVCVLE MAIGGLSGLR VDLSEPLAKL
960 970 980 990 1000
KNFDKSVEKL NRPELAVLFA EECGWVVEVL DTDLERVRST YEKAGVPNYY
1010 1020 1030 1040 1050
LGVTEGFGLD SRVVLKNGKS ELLDQPLRVL YKKWERTSYE LEKLQANPEC
1060 1070 1080 1090 1100
AEAEYNSLEY RQAPQYRGPQ NVQAELTLKR SSAPVRVAVL REEGVNSERE
1110 1120 1130 1140 1150
MMACLLRANF EVHDVTMSDL LQGTASVSQY RGLIFPGGFS YADTLGSAKG
1160 1170 1180 1190 1200
WAANILHNPR LLPQFEAFKR RQDVFSLGIC NGCQLMTLIG FVGSAKSEVG
1210 1220 1230 1240 1250
ADPDVALLHN KSQRFECRWA TVKIPSNRSI MLGSMKDLVL GCWVAHGEGR
1260 1270 1280 1290 1300
FAFRDEKLIS HLQSEQLVTL QYVDDVGKPT ELYPLNPNGS PQGIAGLCSS
1310 1320 1330 1340 1350
DGRHLALMPH PERCSSMYQW PYVPSSFEVS PTQSESPWQI MFNNAYNWCV

KSNQ
Length:1,354
Mass (Da):148,085
Last modified:January 11, 2001 - v2
Checksum:i8AA167C2D2920B2C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti558 – 5581I → Y in AAC46468 (PubMed:8270203).Curated
Sequence conflicti625 – 6251S → F in AAC46468 (PubMed:8270203).Curated
Sequence conflicti766 – 7661E → V in AAR82811 (Ref. 4) Curated
Sequence conflicti910 – 9101D → E in AAR82811 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00683 Unassigned DNA. Translation: AAC46468.1.
AE014134 Genomic DNA. Translation: AAF52329.1.
AE014134 Genomic DNA. Translation: AAN10573.1.
AE014134 Genomic DNA. Translation: AAN10574.1.
BT011143 mRNA. Translation: AAR82811.1.
PIRiT13363.
RefSeqiNP_477212.1. NM_057864.4.
NP_723146.1. NM_164675.2.
NP_723147.1. NM_164676.2.

Genome annotation databases

EnsemblMetazoaiFBtr0079219; FBpp0078850; FBgn0000052.
FBtr0079220; FBpp0078851; FBgn0000052.
FBtr0079221; FBpp0078852; FBgn0000052.
GeneIDi33847.
KEGGidme:Dmel_CG9127.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00683 Unassigned DNA. Translation: AAC46468.1.
AE014134 Genomic DNA. Translation: AAF52329.1.
AE014134 Genomic DNA. Translation: AAN10573.1.
AE014134 Genomic DNA. Translation: AAN10574.1.
BT011143 mRNA. Translation: AAR82811.1.
PIRiT13363.
RefSeqiNP_477212.1. NM_057864.4.
NP_723146.1. NM_164675.2.
NP_723147.1. NM_164676.2.

3D structure databases

ProteinModelPortaliP35421.
SMRiP35421. Positions 1086-1313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60012. 3 interactions.
DIPiDIP-22769N.
IntActiP35421. 2 interactions.
MINTiMINT-1579795.
STRINGi7227.FBpp0078850.

Proteomic databases

PaxDbiP35421.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079219; FBpp0078850; FBgn0000052.
FBtr0079220; FBpp0078851; FBgn0000052.
FBtr0079221; FBpp0078852; FBgn0000052.
GeneIDi33847.
KEGGidme:Dmel_CG9127.

Organism-specific databases

CTDi33847.
FlyBaseiFBgn0000052. ade2.

Phylogenomic databases

eggNOGiKOG1907. Eukaryota.
COG0046. LUCA.
COG0047. LUCA.
GeneTreeiENSGT00390000007600.
InParanoidiP35421.
KOiK01952.
OMAiLSANWMW.
OrthoDBiEOG7353X4.
PhylomeDBiP35421.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
ReactomeiR-DME-73817. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

GenomeRNAii33847.
NextBioi785582.
PROiP35421.

Gene expression databases

BgeeiP35421.
GenevisibleiP35421. DM.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1.
InterProiIPR010918. AIR_synth_C_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM-like_N.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The adenosine2 gene of Drosophila melanogaster encodes a formylglycineamide ribotide amidotransferase."
    Tiong S.Y.K., Nash D.
    Genome 36:924-934(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Ovary.

Entry informationi

Entry nameiPUR4_DROME
AccessioniPrimary (citable) accession number: P35421
Secondary accession number(s): A4V099, Q6NNY9, Q9VMI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2001
Last modified: May 11, 2016
This is version 136 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.