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Q27601

- PUR1_DROME

UniProt

Q27601 - PUR1_DROME

Protein

Amidophosphoribosyltransferase

Gene

Prat

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (13 Sep 2005)
      Previous versions | rss
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    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 activityBy similarity
    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

    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

    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 – 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.

    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 113 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