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P35433

- PUR1_RAT

UniProt

P35433 - PUR1_RAT

Protein

Amidophosphoribosyltransferase

Gene

Ppat

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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

    Enzyme regulationi

    Activated by the substrate 5-phospho-alpha-D-ribosyl-1-pyrophosphate and inhibited by the purine ribonucleotides, the end products of purine biosynthesis.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei12 – 121For GATase activityBy similarity
    Metal bindingi280 – 2801Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi327 – 3271MagnesiumBy similarity
    Metal bindingi389 – 3891MagnesiumBy similarity
    Metal bindingi390 – 3901MagnesiumBy similarity
    Metal bindingi426 – 4261Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi503 – 5031Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi506 – 5061Iron-sulfur (4Fe-4S)By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    2. cellular response to drug Source: RGD
    3. cellular response to insulin stimulus Source: RGD
    4. G1/S transition of mitotic cell cycle Source: RGD
    5. glutamine catabolic process Source: RGD
    6. kidney development Source: RGD
    7. lactation Source: RGD
    8. maternal process involved in female pregnancy Source: RGD
    9. nucleoside metabolic process Source: InterPro
    10. organ regeneration Source: RGD
    11. protein homotetramerization Source: RGD
    12. purine nucleobase biosynthetic process Source: InterPro
    13. purine ribonucleoside monophosphate biosynthetic process Source: RGD
    14. response to drug Source: RGD
    15. ribose phosphate metabolic process Source: RGD

    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_217264. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RKP35433.
    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:Ppat
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 14

    Organism-specific databases

    RGDi620237. Ppat.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 11111 PublicationPRO_0000029285Add
    BLAST
    Chaini12 – 517506AmidophosphoribosyltransferasePRO_0000029286Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP35433.
    PRIDEiP35433.

    PTM databases

    PhosphoSiteiP35433.

    Expressioni

    Tissue specificityi

    Expressed at a high level in brain, heart, liver and stomach.

    Gene expression databases

    GenevestigatoriP35433.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000002905.

    Structurei

    3D structure databases

    ProteinModelPortaliP35433.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 261250Glutamine 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.
    HOGENOMiHOG000033688.
    HOVERGENiHBG002589.
    InParanoidiP35433.
    KOiK00764.
    OMAiIPVGDMN.
    OrthoDBiEOG789C9W.
    PhylomeDBiP35433.
    TreeFamiTF106370.

    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. 2 hits.
    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.

    P35433-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELEESGIRE ECGVFGCIAS GDWPTQLDVP HVITLGLVGL QHRGQESAGI    50
    VTSDGSSVPK FRVHKGMGLV NHVFTEDNLK KLYVSNLGIG HTRYATTGKC 100
    ELENCQPFVV ETLHGKIAVA HNGELVNAAR LRKKLLRHGI GLSTSSDSEM 150
    ITQLLAYTPP QEQDDTPDWV ARIKNLMKEA PAAYSLVIMH RDVIYAVRDP 200
    YGNRPLCIGR LMPVSDINDK EKKSSETEGW VVSSESCSFL SIGARYCHEV 250
    KPGEIVEISR HGVRTLDIIP RSNGDPVAFC IFEYVYFARP DSMFEDQMVY 300
    TVRYRCGQQL AVEAPVEADL VSTVPESATP AALGYATKCG LPYVEVLCKN 350
    RYVGRTFIQP NMRLRQLGVA KKFGVLSDNF KGKRIVLIDD SIVRGNTISP 400
    IIKLLKESGA KEVHIRVASP PIKHPCFMGI NIPTKEELIA NKPEFEYLAE 450
    YLGANSVVYL SVEGLVSSVQ QEIKFKKQKV KKRDITIQEN GNGLEYFEKT 500
    GHCTACLTGQ YPVDLEW 517
    Length:517
    Mass (Da):57,437
    Last modified:June 1, 1994 - v1
    Checksum:i8AD3D05A380C120F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10853 mRNA. Translation: BAA01626.1.
    BC086999 mRNA. Translation: AAH86999.1.
    D37978 Genomic DNA. Translation: BAA21036.1.
    PIRiA46088.
    RefSeqiNP_476546.1. NM_057198.2.
    UniGeneiRn.18690.

    Genome annotation databases

    EnsembliENSRNOT00000002905; ENSRNOP00000002905; ENSRNOG00000002128.
    GeneIDi117544.
    KEGGirno:117544.
    UCSCiRGD:620237. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10853 mRNA. Translation: BAA01626.1 .
    BC086999 mRNA. Translation: AAH86999.1 .
    D37978 Genomic DNA. Translation: BAA21036.1 .
    PIRi A46088.
    RefSeqi NP_476546.1. NM_057198.2.
    UniGenei Rn.18690.

    3D structure databases

    ProteinModelPortali P35433.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000002905.

    Protein family/group databases

    MEROPSi C44.001.

    PTM databases

    PhosphoSitei P35433.

    Proteomic databases

    PaxDbi P35433.
    PRIDEi P35433.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000002905 ; ENSRNOP00000002905 ; ENSRNOG00000002128 .
    GeneIDi 117544.
    KEGGi rno:117544.
    UCSCi RGD:620237. rat.

    Organism-specific databases

    CTDi 5471.
    RGDi 620237. Ppat.

    Phylogenomic databases

    eggNOGi COG0034.
    GeneTreei ENSGT00390000003428.
    HOGENOMi HOG000033688.
    HOVERGENi HBG002589.
    InParanoidi P35433.
    KOi K00764.
    OMAi IPVGDMN.
    OrthoDBi EOG789C9W.
    PhylomeDBi P35433.
    TreeFami TF106370.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00124 .
    Reactomei REACT_217264. Purine ribonucleoside monophosphate biosynthesis.
    SABIO-RK P35433.

    Miscellaneous databases

    NextBioi 620369.
    PROi P35433.

    Gene expression databases

    Genevestigatori P35433.

    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. 2 hits.
    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 cloning of rat amidophosphoribosyltransferase."
      Iwahana H., Yamaoka T., Mizutani M., Mizusawa N., Ii S., Yoshimoto K., Itakura M.
      J. Biol. Chem. 268:7225-7237(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-29.
      Strain: Wistar.
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Heart.
    3. "Rat genomic structure of amidophosphoribosyltransferase, cDNA sequence of aminoimidazole ribonucleotide carboxylase, and cell cycle-dependent expression of these two physically linked genes."
      Iwahana H., Honda S., Tsujisawa T., Takahashi Y., Adzuma K., Katashima R., Yamaoka T., Moritani M., Yoshimoto K., Itakura M.
      Biochim. Biophys. Acta 1261:369-380(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
      Strain: Wistar.
      Tissue: Liver.

    Entry informationi

    Entry nameiPUR1_RAT
    AccessioniPrimary (citable) accession number: P35433
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3