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Q27601

- PUR1_DROME

UniProt

Q27601 - PUR1_DROME

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Protein
Amidophosphoribosyltransferase
Gene
Prat, CG2867
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541For GATase activity By similarity
Metal bindingi321 – 3211Iron-sulfur (4Fe-4S) By similarity
Metal bindingi368 – 3681Magnesium By similarity
Metal bindingi430 – 4301Magnesium By similarity
Metal bindingi431 – 4311Magnesium By 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

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. amidophosphoribosyltransferase activity Source: FlyBase
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. determination of adult lifespan Source: FlyBase
  3. embryonic cleavage Source: FlyBase
  4. glutamine metabolic process Source: UniProtKB-KW
  5. nucleoside metabolic process Source: InterPro
  6. oogenesis Source: FlyBase
  7. purine nucleobase biosynthetic process Source: FlyBase
  8. 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_208157. 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: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0004901. Prat.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5353 Inferred
PRO_0000029287Add
BLAST
Chaini54 – 546493Amidophosphoribosyltransferase
PRO_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.

Structurei

3D structure databases

ProteinModelPortaliQ27601.
SMRiQ27601. Positions 54-537.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0034.
GeneTreeiENSGT00390000003428.
InParanoidiQ27601.
KOiK00764.
OMAiEMVWITE.
OrthoDBiEOG789C9W.
PhylomeDBiQ27601.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
InterProiIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[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

MSAPQQQQQS QQKQQQHVRV VEQQQVEPAE AVTSSMESES ISASKELTGL    50
THECGVFGAI ACGDWPTQMD IAHVICLGLV ALQHRGQESA GIATSEGKCS 100
KNFNVHKGMG MISTLFNDDS MKKLRGNLGI GHTRYSTAGG SGVVNCQPFE 150
VHTTHGALAL AHNGELVNNE SLRREVLARG VGLSTHSDSE LIAQSLCCAP 200
EDVSELDGPN WPARIRHFMM LAPLSYSLVI MLKDKIYAVR DTYGNRPLCI 250
GKIVPINAGH GNNLDTPADG WVVSSESCGF LSIGARYVRE VEPGEIVELS 300
RSGYRTVDIV ERPDFKRMAF CIFEYVYFAR GDSIFEGQMV YTVRLQCGRQ 350
LWREAPVEAD IVSSVPESGT AAAHGYARES GIEFAEVLCR NRYVGRTFIQ 400
PSTRLRQLGV AKKFGALSEN VAGKRLVLID DSIVRGNTIG PIIKLLRDAG 450
AREVHIRIAS PPLQYPCYMG INIPTREELI ANKLNPDQLA RHVGADSLAY 500
LSVEGLVEAV QLKHRDAGDS KSKGTGHCTA CLTGEYPGGL PDELSW 546
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501E → V in AAC39084. 1 Publication
Sequence conflicti185 – 1851T → S in AAC39084. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF017096 Genomic DNA. Translation: AAC39084.1 . Different initiation.
AE014297 Genomic DNA. Translation: AAF54163.2 .
AY069652 mRNA. Translation: AAL39797.1 .
PIRi S47860.
RefSeqi NP_001246972.1. NM_001260043.1.
NP_524271.2. NM_079547.3.
UniGenei Dm.9919.

3D structure databases

ProteinModelPortali Q27601.
SMRi Q27601. Positions 54-537.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C44.001.

Proteomic databases

PaxDbi Q27601.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0081764 ; FBpp0081261 ; FBgn0004901 .
FBtr0304705 ; FBpp0293248 ; FBgn0004901 .
GeneIDi 40935.
KEGGi dme:Dmel_CG2867.

Organism-specific databases

CTDi 40935.
FlyBasei FBgn0004901. Prat.

Phylogenomic databases

eggNOGi COG0034.
GeneTreei ENSGT00390000003428.
InParanoidi Q27601.
KOi K00764.
OMAi EMVWITE.
OrthoDBi EOG789C9W.
PhylomeDBi Q27601.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00124 .
Reactomei REACT_208157. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

GenomeRNAii 40935.
NextBioi 821362.

Gene expression databases

Bgeei Q27601.

Family and domain databases

Gene3Di 3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
InterProi IPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view ]
Pfami PF00310. GATase_2. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view ]
PIRSFi PIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMi SSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01134. purF. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 112 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