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Protein

Amidophosphoribosyltransferase

Gene

Prat

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

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathway:iIMP biosynthesis via de novo pathway

This protein is involved in step 1 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)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541NucleophilePROSITE-ProRule annotation
Metal bindingi321 – 3211Iron-sulfur (4Fe-4S)By similarity
Metal bindingi368 – 3681MagnesiumBy similarity
Metal bindingi430 – 4301MagnesiumBy similarity
Metal bindingi431 – 4311MagnesiumBy similarity
Metal bindingi467 – 4671Iron-sulfur (4Fe-4S)By similarity
Metal bindingi528 – 5281Iron-sulfur (4Fe-4S)By similarity
Metal bindingi531 – 5311Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • amidophosphoribosyltransferase activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  • determination of adult lifespan Source: FlyBase
  • embryonic cleavage Source: FlyBase
  • glutamine metabolic process Source: UniProtKB-KW
  • nucleoside metabolic process Source: InterPro
  • oogenesis Source: FlyBase
  • purine nucleobase biosynthetic process Source: FlyBase
  • purine nucleotide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_283178. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Amidophosphoribosyltransferase (EC:2.4.2.14)
Short name:
ATase
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name:
GPAT
Gene namesi
Name:Prat
ORF Names:CG2867
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0004901. Prat.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5353CuratedPRO_0000029287Add
BLAST
Chaini54 – 546493AmidophosphoribosyltransferasePRO_0000029288Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131Phosphoserine1 Publication
Modified residuei114 – 1141Phosphothreonine1 Publication
Modified residuei120 – 1201Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ27601.

Expressioni

Gene expression databases

BgeeiQ27601.
ExpressionAtlasiQ27601. differential.
GenevisibleiQ27601. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0081261.

Structurei

3D structure databases

ProteinModelPortaliQ27601.
SMRiQ27601. Positions 54-537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 302249Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0034.
GeneTreeiENSGT00390000003428.
InParanoidiQ27601.
KOiK00764.
OMAiQLWREAP.
OrthoDBiEOG789C9W.
PhylomeDBiQ27601.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00310. GATase_2. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q27601-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAPQQQQQS QQKQQQHVRV VEQQQVEPAE AVTSSMESES ISASKELTGL
60 70 80 90 100
THECGVFGAI ACGDWPTQMD IAHVICLGLV ALQHRGQESA GIATSEGKCS
110 120 130 140 150
KNFNVHKGMG MISTLFNDDS MKKLRGNLGI GHTRYSTAGG SGVVNCQPFE
160 170 180 190 200
VHTTHGALAL AHNGELVNNE SLRREVLARG VGLSTHSDSE LIAQSLCCAP
210 220 230 240 250
EDVSELDGPN WPARIRHFMM LAPLSYSLVI MLKDKIYAVR DTYGNRPLCI
260 270 280 290 300
GKIVPINAGH GNNLDTPADG WVVSSESCGF LSIGARYVRE VEPGEIVELS
310 320 330 340 350
RSGYRTVDIV ERPDFKRMAF CIFEYVYFAR GDSIFEGQMV YTVRLQCGRQ
360 370 380 390 400
LWREAPVEAD IVSSVPESGT AAAHGYARES GIEFAEVLCR NRYVGRTFIQ
410 420 430 440 450
PSTRLRQLGV AKKFGALSEN VAGKRLVLID DSIVRGNTIG PIIKLLRDAG
460 470 480 490 500
AREVHIRIAS PPLQYPCYMG INIPTREELI ANKLNPDQLA RHVGADSLAY
510 520 530 540
LSVEGLVEAV QLKHRDAGDS KSKGTGHCTA CLTGEYPGGL PDELSW
Length:546
Mass (Da):59,520
Last modified:September 13, 2005 - v2
Checksum:i4CA4D981EF2C34CC
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501E → V in AAC39084 (PubMed:8150282).Curated
Sequence conflicti185 – 1851T → S in AAC39084 (PubMed:8150282).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017096 Genomic DNA. Translation: AAC39084.1. Different initiation.
AE014297 Genomic DNA. Translation: AAF54163.2.
AY069652 mRNA. Translation: AAL39797.1.
PIRiS47860.
RefSeqiNP_001246972.1. NM_001260043.1.
NP_524271.2. NM_079547.3.
UniGeneiDm.9919.

Genome annotation databases

EnsemblMetazoaiFBtr0081764; FBpp0081261; FBgn0004901.
FBtr0304705; FBpp0293248; FBgn0004901.
GeneIDi40935.
KEGGidme:Dmel_CG2867.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017096 Genomic DNA. Translation: AAC39084.1. Different initiation.
AE014297 Genomic DNA. Translation: AAF54163.2.
AY069652 mRNA. Translation: AAL39797.1.
PIRiS47860.
RefSeqiNP_001246972.1. NM_001260043.1.
NP_524271.2. NM_079547.3.
UniGeneiDm.9919.

3D structure databases

ProteinModelPortaliQ27601.
SMRiQ27601. Positions 54-537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0081261.

Protein family/group databases

MEROPSiC44.001.

Proteomic databases

PaxDbiQ27601.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081764; FBpp0081261; FBgn0004901.
FBtr0304705; FBpp0293248; FBgn0004901.
GeneIDi40935.
KEGGidme:Dmel_CG2867.

Organism-specific databases

CTDi40935.
FlyBaseiFBgn0004901. Prat.

Phylogenomic databases

eggNOGiCOG0034.
GeneTreeiENSGT00390000003428.
InParanoidiQ27601.
KOiK00764.
OMAiQLWREAP.
OrthoDBiEOG789C9W.
PhylomeDBiQ27601.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
ReactomeiREACT_283178. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

GenomeRNAii40935.
NextBioi821362.
PROiQ27601.

Gene expression databases

BgeeiQ27601.
ExpressionAtlasiQ27601. differential.
GenevisibleiQ27601. DM.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00310. GATase_2. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFiPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01134. purF. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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: 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.

Entry informationi

Entry nameiPUR1_DROME
AccessioniPrimary (citable) accession number: Q27601
Secondary accession number(s): Q8T009, Q9VHY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 13, 2005
Last modified: July 22, 2015
This is version 120 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

External Data

Dasty 3

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 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.