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Reviewed, UniProtKB/Swiss-Prot P35421 (PUR4_DROME)

Last modified November 3, 2009. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoribosylformylglycinamidine synthase
      Short name=FGAM synthase
      Short name=FGAMS
    EC=6.3.5.3
Alternative name(s):
    Formylglycinamide ribotide amidotransferase
      Short name=FGARAT
    Formylglycinamide ribotide synthetase
    Protein adenosine-2
Gene names
Name: ade2
ORF Names: CG9127
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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.

Pathway

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

Sequence similarities

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

Contains 1 glutamine amidotransferase type-1 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9VQF41EBI-89279,EBI-122086

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13541354Phosphoribosylformylglycinamidine synthase
PRO_0000100403

Regions

Domain1087 – 1337251Glutamine amidotransferase type-1
Nucleotide binding327 – 33812ATP Potential

Sites

Active site11801For GATase activity By similarity

Experimental info

Sequence conflict5581I → Y in AAC46468. Ref.1
Sequence conflict6251S → F in AAC46468. Ref.1
Sequence conflict7661E → V in AAR82811. Ref.4
Sequence conflict9101D → E in AAR82811. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P35421-1 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 8AA167C2D2920B2C

FASTA1,354148,085
        10         20         30         40         50         60 
MVILRYYDVQ AHSAAEEESV LRRLREEDGA VVSVRMERCY HLEYSAQAEH SLALDELLVW 

        70         80         90        100        110        120 
LVKQPLSKGQ SLSRQPALQS TGSSQLLLEI GPRFNFSTPY STNCVNIFQN LGYSEVRRME 

       130        140        150        160        170        180 
TSTRYLVTFG EGSKAPEAAR FVPLLGDRMT QCLYTEENTP KASFDEQLPE RQANWHFVPV 

       190        200        210        220        230        240 
LEEGRAALER INQELGLAFN DYDLDYYHDL FAKELGRNPT TVELFDCAQS NSEHSRHWFF 

       250        260        270        280        290        300 
RGRMVIDGVE QPKSLIRMIM DTQAHTNPNN TIKFSDNSSA MVGFDHQTIV PSSVVAPGAV 

       310        320        330        340        350        360 
RLQSVQSDLI FTAETHNMPT AVAPFSGATT GTGGRLRDVQ GVGRGGVPIA GTAGYCVGAL 

       370        380        390        400        410        420 
HIPGYKQPYE PLDFKYPATF APPLQVLIEA SNGASDYGNK FGEPVISGFA LSYGLNSAAD 

       430        440        450        460        470        480 
ASQRDEYVKP IMFSGGLGTM PATMREKLPP ARGQLLAKIG GPVYRIGVGG GAASSVEIQG 

       490        500        510        520        530        540 
SGDAELDFNA VQRGDAEMEN KLNRVVRACL DLGEQNPILA IHDQGAGGNG NVLKELVEPG 

       550        560        570        580        590        600 
FAGAVIFSKE FQLGDPTITA LELWGAEYQE NNAILCNADQ RELLEKICRR ERCPISFVGV 

       610        620        630        640        650        660 
VTGDGRVTLL EKPAPKDLEQ ALNASNRSEV SPFDLELKYV LGDMPKRTYD LKREQTPLKE 

       670        680        690        700        710        720 
LSLPKGLLLD EALERVLSLV AVGSKRFLTN KVDRCVGGLI AQQQCVGPLQ APLADYALTT 

       730        740        750        760        770        780 
VSHFSHSGIA TSIGTQPLKG LLDPAAMARM CVAEALSNLV FVKISELADV KCSGNWMWAA 

       790        800        810        820        830        840 
KLPGEGARMF DACKELCQIL EELHIAIDGG KDSLSMAAKV GGETIKSPGT LVISTYAPCP 

       850        860        870        880        890        900 
DVRLKVTPDL KGPGAGSKTS LLWINLENSA RLGGSALAQA YAQQGKDTPN LTRSDVLGKA 

       910        920        930        940        950        960 
FAVTQSLLGD GLIQAGHDVS DGGLLVCVLE MAIGGLSGLR VDLSEPLAKL KNFDKSVEKL 

       970        980        990       1000       1010       1020 
NRPELAVLFA EECGWVVEVL DTDLERVRST YEKAGVPNYY LGVTEGFGLD SRVVLKNGKS 

      1030       1040       1050       1060       1070       1080 
ELLDQPLRVL YKKWERTSYE LEKLQANPEC AEAEYNSLEY RQAPQYRGPQ NVQAELTLKR 

      1090       1100       1110       1120       1130       1140 
SSAPVRVAVL REEGVNSERE MMACLLRANF EVHDVTMSDL LQGTASVSQY RGLIFPGGFS 

      1150       1160       1170       1180       1190       1200 
YADTLGSAKG WAANILHNPR LLPQFEAFKR RQDVFSLGIC NGCQLMTLIG FVGSAKSEVG 

      1210       1220       1230       1240       1250       1260 
ADPDVALLHN KSQRFECRWA TVKIPSNRSI MLGSMKDLVL GCWVAHGEGR FAFRDEKLIS 

      1270       1280       1290       1300       1310       1320 
HLQSEQLVTL QYVDDVGKPT ELYPLNPNGS PQGIAGLCSS DGRHLALMPH PERCSSMYQW 

      1330       1340       1350 
PYVPSSFEVS PTQSESPWQI MFNNAYNWCV KSNQ 

« Hide

References

« Hide 'large scale' references
[1]"The adenosine2 gene of Drosophila melanogaster encodes a formylglycineamide ribotide amidotransferase."
Tiong S.Y.K., Nash D.
Genome 36:924-934(1993) [PubMed: 8270203] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
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. 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.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
PIRT13363.
RefSeqNP_477212.1.
NP_723146.1.
NP_723147.1.
UniGeneDm.4474

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:22769N.
IntActP35421. 3 interactions.
STRINGP35421.

Genome annotation databases

EnsemblFBtr0079220; FBpp0078851; FBgn0000052; Drosophila melanogaster. [Genome view]
GeneID33847.
KEGGdme:Dmel_CG9127.

Organism-specific databases

CTD33847.
FlyBaseFBgn0000052. ade2.

Phylogenomic databases

OMAERGIAYY.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-007589-MON.
DMEL-XXX-02:DMEL-XXX-02-007590-MON.
DMEL-XXX-02:DMEL-XXX-02-007591-MON.
BRENDA6.3.5.3. 48.

Gene expression databases

ArrayExpressP35421.
GermOnlineCG9127. Drosophila melanogaster.

Family and domain databases

InterProIPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR017926. GATASE_1.
IPR010073. PRibForGlyAmidine_synth.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view]
TIGRFAMsTIGR01735. FGAM_synt. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio785582.

Entry information

Entry namePUR4_DROME
AccessionPrimary (citable) accession number: P35421
Secondary accession number(s): A4V099, Q6NNY9, Q9VMI7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2001
Last modified: November 3, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents