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Protein

Amidophosphoribosyltransferase

Gene

purF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. Can also use NH3 in place of glutamine.1 Publication

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Enzyme regulationi

Inhibited by iodoacetamide and by the glutamine analogs chloroketone and DON.1 Publication

Kineticsi

  1. KM=0.067 mM for phosphoribosylpyrophosphate1 Publication
  2. KM=1.7 mM for glutamine1 Publication
  3. KM=8.8 mM for NH31 Publication

    Pathwayi: IMP 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.UniRule annotation1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Amidophosphoribosyltransferase (purF)
    2. Phosphoribosylamine--glycine ligase (purD)
    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)DescriptionActionsGraphical viewLength
    Active sitei2NucleophileUniRule annotation1 Publication1
    Metal bindingi305MagnesiumUniRule annotation1
    Metal bindingi367MagnesiumUniRule annotation1
    Metal bindingi368MagnesiumUniRule annotation1

    GO - Molecular functioni

    • amidophosphoribosyltransferase activity Source: EcoliWiki
    • identical protein binding Source: EcoCyc
    • magnesium ion binding Source: UniProtKB-HAMAP
    • transferase activity, transferring glycosyl groups Source: EcoliWiki

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PRPPAMIDOTRANS-MONOMER.
    ECOL316407:JW2309-MONOMER.
    MetaCyc:PRPPAMIDOTRANS-MONOMER.
    BRENDAi2.4.2.14. 2026.
    SABIO-RKP0AG16.
    UniPathwayiUPA00074; UER00124.

    Protein family/group databases

    MEROPSiC44.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amidophosphoribosyltransferase1 PublicationUniRule annotation (EC:2.4.2.14UniRule annotation1 Publication)
    Short name:
    ATaseUniRule annotation
    Alternative name(s):
    Glutamine phosphoribosylpyrophosphate amidotransferase1 PublicationUniRule annotation
    Short name:
    GPATase1 PublicationUniRule annotation
    Gene namesi
    Name:purFUniRule annotation
    Ordered Locus Names:b2312, JW2309
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10794. purF.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    • cytosol Source: UniProtKB
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001396382 – 505AmidophosphoribosyltransferaseAdd BLAST504

    Proteomic databases

    PaxDbiP0AG16.
    PRIDEiP0AG16.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    STRINGi511145.b2312.

    Structurei

    Secondary structure

    1505
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 8Combined sources6
    Helixi14 – 23Combined sources10
    Helixi24 – 27Combined sources4
    Beta strandi30 – 37Combined sources8
    Beta strandi43 – 50Combined sources8
    Helixi52 – 55Combined sources4
    Helixi58 – 63Combined sources6
    Beta strandi66 – 74Combined sources9
    Beta strandi78 – 80Combined sources3
    Helixi83 – 85Combined sources3
    Beta strandi89 – 91Combined sources3
    Beta strandi93 – 95Combined sources3
    Beta strandi97 – 105Combined sources9
    Helixi108 – 119Combined sources12
    Helixi128 – 140Combined sources13
    Beta strandi145 – 147Combined sources3
    Helixi150 – 163Combined sources14
    Beta strandi166 – 174Combined sources9
    Turni175 – 177Combined sources3
    Beta strandi178 – 183Combined sources6
    Beta strandi192 – 197Combined sources6
    Beta strandi199 – 201Combined sources3
    Beta strandi203 – 210Combined sources8
    Helixi212 – 217Combined sources6
    Beta strandi220 – 224Combined sources5
    Beta strandi229 – 234Combined sources6
    Beta strandi239 – 243Combined sources5
    Beta strandi245 – 247Combined sources3
    Helixi254 – 258Combined sources5
    Helixi272 – 290Combined sources19
    Turni291 – 293Combined sources3
    Beta strandi298 – 301Combined sources4
    Turni303 – 306Combined sources4
    Helixi307 – 317Combined sources11
    Beta strandi325 – 327Combined sources3
    Beta strandi338 – 340Combined sources3
    Turni348 – 350Combined sources3
    Beta strandi351 – 353Combined sources3
    Helixi355 – 357Combined sources3
    Turni358 – 360Combined sources3
    Beta strandi363 – 368Combined sources6
    Beta strandi371 – 373Combined sources3
    Helixi374 – 385Combined sources12
    Beta strandi389 – 397Combined sources9
    Beta strandi406 – 410Combined sources5
    Helixi413 – 415Combined sources3
    Turni417 – 420Combined sources4
    Helixi423 – 430Combined sources8
    Beta strandi433 – 437Combined sources5
    Helixi440 – 448Combined sources9
    Helixi460 – 463Combined sources4
    Helixi473 – 492Combined sources20
    Helixi494 – 499Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ECBX-ray2.70A/B/C/D2-505[»]
    1ECCX-ray2.40A/B2-505[»]
    1ECFX-ray2.00A/B2-505[»]
    1ECGX-ray2.30A/B2-505[»]
    1ECJX-ray2.50A/B/C/D2-505[»]
    DisProtiDP00578.
    ProteinModelPortaliP0AG16.
    SMRiP0AG16.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG16.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini2 – 236Glutamine amidotransferase type-2UniRule annotationAdd BLAST235

    Sequence similaritiesi

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

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4105CBA. Bacteria.
    COG0034. LUCA.
    InParanoidiP0AG16.
    KOiK00764.
    OMAiAARVHMG.
    PhylomeDBiP0AG16.

    Family and domain databases

    CDDicd06223. PRTases_typeI. 1 hit.
    Gene3Di3.40.50.2020. 1 hit.
    3.60.20.10. 1 hit.
    HAMAPiMF_01931. PurF. 1 hit.
    InterProiIPR017932. GATase_2_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR005854. PurF.
    [Graphical view]
    PfamiPF00156. 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.

    P0AG16-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG
    60 70 80 90 100
    LVSDVFEARH MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA
    110 120 130 140 150
    HNGNLTNAHE LRKKLFEEKR RHINTTSDSE ILLNIFASEL DNFRHYPLEA
    160 170 180 190 200
    DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV AFRDPNGIRP LVLGKRDIDE
    210 220 230 240 250
    NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF TRQCADNPVS
    260 270 280 290 300
    NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI
    310 320 330 340 350
    PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK
    360 370 380 390 400
    LNANRAEFRD KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI
    410 420 430 440 450
    RFPNVYGIDM PSATELIAHG REVDEIRQII GADGLIFQDL NDLIDAVRAE
    460 470 480 490 500
    NPDIQQFECS VFNGVYVTKD VDQGYLDFLD TLRNDDAKAV QRQNEVENLE

    MHNEG
    Length:505
    Mass (Da):56,488
    Last modified:January 23, 2007 - v2
    Checksum:i50FD08EA85E6F2A8
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti45 – 46LR → SL (PubMed:6443594).Curated2
    Sequence conflicti45 – 46LR → SL (PubMed:6277938).Curated2
    Sequence conflicti50G → A (PubMed:6443594).Curated1
    Sequence conflicti50G → A (PubMed:6277938).Curated1
    Sequence conflicti213 – 230ALDTL…APGEA → GSIRWALISCVTSRRAR (PubMed:6443594).CuratedAdd BLAST18
    Sequence conflicti213 – 230ALDTL…APGEA → GSIRWALISCVTSRRAR (PubMed:6277938).CuratedAdd BLAST18
    Sequence conflicti277V → A (PubMed:6443594).Curated1
    Sequence conflicti277V → A (PubMed:6277938).Curated1
    Sequence conflicti283L → V (PubMed:6443594).Curated1
    Sequence conflicti283L → V (PubMed:6277938).Curated1
    Sequence conflicti337M → I in AAA24453 (PubMed:6443594).Curated1
    Sequence conflicti386A → R in CAA30971 (PubMed:3047685).Curated1
    Sequence conflicti494N → S (PubMed:6443594).Curated1
    Sequence conflicti494N → S (PubMed:6277938).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X12423 Genomic DNA. Translation: CAA30971.1.
    V00322 Genomic DNA. Translation: CAA23613.1.
    M26893 Genomic DNA. Translation: AAA24453.1.
    J01666 Genomic DNA. Translation: AAA24452.1.
    U00096 Genomic DNA. Translation: AAC75372.1.
    AP009048 Genomic DNA. Translation: BAA16158.1.
    M68935, M68934 Genomic DNA. Translation: AAA23969.1. Sequence problems.
    PIRiF65003. XQEC.
    RefSeqiNP_416815.1. NC_000913.3.
    WP_000334220.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75372; AAC75372; b2312.
    BAA16158; BAA16158; BAA16158.
    GeneIDi946794.
    KEGGiecj:JW2309.
    eco:b2312.
    PATRICi32119995. VBIEscCol129921_2407.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X12423 Genomic DNA. Translation: CAA30971.1.
    V00322 Genomic DNA. Translation: CAA23613.1.
    M26893 Genomic DNA. Translation: AAA24453.1.
    J01666 Genomic DNA. Translation: AAA24452.1.
    U00096 Genomic DNA. Translation: AAC75372.1.
    AP009048 Genomic DNA. Translation: BAA16158.1.
    M68935, M68934 Genomic DNA. Translation: AAA23969.1. Sequence problems.
    PIRiF65003. XQEC.
    RefSeqiNP_416815.1. NC_000913.3.
    WP_000334220.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ECBX-ray2.70A/B/C/D2-505[»]
    1ECCX-ray2.40A/B2-505[»]
    1ECFX-ray2.00A/B2-505[»]
    1ECGX-ray2.30A/B2-505[»]
    1ECJX-ray2.50A/B/C/D2-505[»]
    DisProtiDP00578.
    ProteinModelPortaliP0AG16.
    SMRiP0AG16.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi511145.b2312.

    Protein family/group databases

    MEROPSiC44.001.

    Proteomic databases

    PaxDbiP0AG16.
    PRIDEiP0AG16.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75372; AAC75372; b2312.
    BAA16158; BAA16158; BAA16158.
    GeneIDi946794.
    KEGGiecj:JW2309.
    eco:b2312.
    PATRICi32119995. VBIEscCol129921_2407.

    Organism-specific databases

    EchoBASEiEB0787.
    EcoGeneiEG10794. purF.

    Phylogenomic databases

    eggNOGiENOG4105CBA. Bacteria.
    COG0034. LUCA.
    InParanoidiP0AG16.
    KOiK00764.
    OMAiAARVHMG.
    PhylomeDBiP0AG16.

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00124.
    BioCyciEcoCyc:PRPPAMIDOTRANS-MONOMER.
    ECOL316407:JW2309-MONOMER.
    MetaCyc:PRPPAMIDOTRANS-MONOMER.
    BRENDAi2.4.2.14. 2026.
    SABIO-RKP0AG16.

    Miscellaneous databases

    EvolutionaryTraceiP0AG16.
    PROiP0AG16.

    Family and domain databases

    CDDicd06223. PRTases_typeI. 1 hit.
    Gene3Di3.40.50.2020. 1 hit.
    3.60.20.10. 1 hit.
    HAMAPiMF_01931. PurF. 1 hit.
    InterProiIPR017932. GATase_2_dom.
    IPR029055. Ntn_hydrolases_N.
    IPR000836. PRibTrfase_dom.
    IPR029057. PRTase-like.
    IPR005854. PurF.
    [Graphical view]
    PfamiPF00156. 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...

    Entry informationi

    Entry nameiPUR1_ECOLI
    AccessioniPrimary (citable) accession number: P0AG16
    Secondary accession number(s): P00496
    , P78092, P78191, P78192, Q47255, Q59425
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 100 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    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 one 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.