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Q27601 (PUR1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amidophosphoribosyltransferase

Short name=ATase
EC=2.4.2.14
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name=GPAT
Gene names
Name:Prat
ORF Names:CG2867
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Binds 1 4Fe-4S cluster per subunit By similarity.

Pathway

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

Sequence similarities

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Contains 1 glutamine amidotransferase type-2 domain.

Sequence caution

The sequence AAC39084.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 5353 Probable
PRO_0000029287
Chain54 – 546493Amidophosphoribosyltransferase
PRO_0000029288

Regions

Domain54 – 302249Glutamine amidotransferase type-2

Sites

Active site541For GATase activity By similarity
Metal binding3211Iron-sulfur (4Fe-4S) By similarity
Metal binding3681Magnesium By similarity
Metal binding4301Magnesium By similarity
Metal binding4311Magnesium By similarity
Metal binding4671Iron-sulfur (4Fe-4S) By similarity
Metal binding5281Iron-sulfur (4Fe-4S) By similarity
Metal binding5311Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Modified residue1131Phosphoserine Ref.5
Modified residue1141Phosphothreonine Ref.5
Modified residue1201Phosphoserine Ref.5

Experimental info

Sequence conflict1501E → V in AAC39084. Ref.1
Sequence conflict1851T → S in AAC39084. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q27601 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: 4CA4D981EF2C34CC

FASTA54659,520
        10         20         30         40         50         60 
MSAPQQQQQS QQKQQQHVRV VEQQQVEPAE AVTSSMESES ISASKELTGL THECGVFGAI 

        70         80         90        100        110        120 
ACGDWPTQMD IAHVICLGLV ALQHRGQESA GIATSEGKCS KNFNVHKGMG MISTLFNDDS 

       130        140        150        160        170        180 
MKKLRGNLGI GHTRYSTAGG SGVVNCQPFE VHTTHGALAL AHNGELVNNE SLRREVLARG 

       190        200        210        220        230        240 
VGLSTHSDSE LIAQSLCCAP EDVSELDGPN WPARIRHFMM LAPLSYSLVI MLKDKIYAVR 

       250        260        270        280        290        300 
DTYGNRPLCI GKIVPINAGH GNNLDTPADG WVVSSESCGF LSIGARYVRE VEPGEIVELS 

       310        320        330        340        350        360 
RSGYRTVDIV ERPDFKRMAF CIFEYVYFAR GDSIFEGQMV YTVRLQCGRQ LWREAPVEAD 

       370        380        390        400        410        420 
IVSSVPESGT AAAHGYARES GIEFAEVLCR NRYVGRTFIQ PSTRLRQLGV AKKFGALSEN 

       430        440        450        460        470        480 
VAGKRLVLID DSIVRGNTIG PIIKLLRDAG AREVHIRIAS PPLQYPCYMG INIPTREELI 

       490        500        510        520        530        540 
ANKLNPDQLA RHVGADSLAY LSVEGLVEAV QLKHRDAGDS KSKGTGHCTA CLTGEYPGGL 


PDELSW 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and genetic analyses of Drosophila Prat, which encodes the first enzyme of de novo purine biosynthesis."
Clark D.V.
Genetics 136:547-557(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-114 AND SER-120, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF017096 Genomic DNA. Translation: AAC39084.1. Different initiation.
AE014297 Genomic DNA. Translation: AAF54163.2.
AY069652 mRNA. Translation: AAL39797.1.
PIRS47860.
RefSeqNP_001246972.1. NM_001260043.1.
NP_524271.2. NM_079547.3.
UniGeneDm.9919.

3D structure databases

ProteinModelPortalQ27601.
SMRQ27601. Positions 54-537.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC44.001.

Proteomic databases

PaxDbQ27601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0081764; FBpp0081261; FBgn0004901.
FBtr0304705; FBpp0293248; FBgn0004901.
GeneID40935.
KEGGdme:Dmel_CG2867.

Organism-specific databases

CTD40935.
FlyBaseFBgn0004901. Prat.

Phylogenomic databases

eggNOGCOG0034.
GeneTreeENSGT00390000003428.
InParanoidQ27601.
KOK00764.
OMAEMVWITE.
OrthoDBEOG789C9W.
PhylomeDBQ27601.

Enzyme and pathway databases

UniPathwayUPA00074; UER00124.

Gene expression databases

BgeeQ27601.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
InterProIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00310. GATase_2. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR01134. purF. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi40935.
NextBio821362.

Entry information

Entry namePUR1_DROME
AccessionPrimary (citable) accession number: Q27601
Secondary accession number(s): Q8T009, Q9VHY4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase