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P0AG16

- PUR1_ECOLI

UniProt

P0AG16 - PUR1_ECOLI

Protein

Amidophosphoribosyltransferase

Gene

purF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei2 – 21For GATase activity
    Metal bindingi367 – 3671Magnesium
    Metal bindingi368 – 3681Magnesium

    GO - Molecular functioni

    1. amidophosphoribosyltransferase activity Source: EcoliWiki
    2. identical protein binding Source: EcoCyc
    3. metal ion binding Source: UniProtKB-KW
    4. transferase activity, transferring glycosyl groups Source: EcoliWiki

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    2. glutamine metabolic process Source: EcoliWiki
    3. nucleoside metabolic process Source: InterPro
    4. purine nucleobase biosynthetic process Source: InterPro
    5. purine nucleotide biosynthetic process Source: EcoliWiki

    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.
    SABIO-RKP0AG16.
    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:
    GPATase
    Gene namesi
    Name:purF
    Ordered Locus Names:b2312, JW2309
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10794. purF.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoliWiki
    2. cytosol Source: UniProtKB

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 505504AmidophosphoribosyltransferasePRO_0000139638Add
    BLAST

    Proteomic databases

    PaxDbiP0AG16.
    PRIDEiP0AG16.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AG16.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi511145.b2312.

    Structurei

    Secondary structure

    1
    505
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi14 – 2310
    Helixi24 – 274
    Beta strandi30 – 378
    Beta strandi43 – 508
    Helixi52 – 554
    Helixi58 – 636
    Beta strandi66 – 749
    Beta strandi78 – 803
    Helixi83 – 853
    Beta strandi89 – 913
    Beta strandi93 – 953
    Beta strandi97 – 1059
    Helixi108 – 11912
    Helixi128 – 14013
    Beta strandi145 – 1473
    Helixi150 – 16314
    Beta strandi166 – 1749
    Turni175 – 1773
    Beta strandi178 – 1836
    Beta strandi192 – 1976
    Beta strandi199 – 2013
    Beta strandi203 – 2108
    Helixi212 – 2176
    Beta strandi220 – 2245
    Beta strandi229 – 2346
    Beta strandi239 – 2435
    Beta strandi245 – 2473
    Helixi254 – 2585
    Helixi272 – 29019
    Turni291 – 2933
    Beta strandi298 – 3014
    Turni303 – 3064
    Helixi307 – 31711
    Beta strandi325 – 3273
    Beta strandi338 – 3403
    Turni348 – 3503
    Beta strandi351 – 3533
    Helixi355 – 3573
    Turni358 – 3603
    Beta strandi363 – 3686
    Beta strandi371 – 3733
    Helixi374 – 38512
    Beta strandi389 – 3979
    Beta strandi406 – 4105
    Helixi413 – 4153
    Turni417 – 4204
    Helixi423 – 4308
    Beta strandi433 – 4375
    Helixi440 – 4489
    Helixi460 – 4634
    Helixi473 – 49220

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG16.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 236235Glutamine 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.
    KOiK00764.
    OMAiAARVHMG.
    OrthoDBiEOG6KT2Q1.
    PhylomeDBiP0AG16.

    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.

    P0AG16-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG    50
    LVSDVFEARH MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA 100
    HNGNLTNAHE LRKKLFEEKR RHINTTSDSE ILLNIFASEL DNFRHYPLEA 150
    DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV AFRDPNGIRP LVLGKRDIDE 200
    NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF TRQCADNPVS 250
    NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI 300
    PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK 350
    LNANRAEFRD KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI 400
    RFPNVYGIDM PSATELIAHG REVDEIRQII GADGLIFQDL NDLIDAVRAE 450
    NPDIQQFECS VFNGVYVTKD VDQGYLDFLD TLRNDDAKAV QRQNEVENLE 500
    MHNEG 505
    Length:505
    Mass (Da):56,488
    Last modified:January 23, 2007 - v2
    Checksum:i50FD08EA85E6F2A8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 462LR → SL(PubMed:6443594)Curated
    Sequence conflicti45 – 462LR → SL(PubMed:6277938)Curated
    Sequence conflicti50 – 501G → A(PubMed:6443594)Curated
    Sequence conflicti50 – 501G → A(PubMed:6277938)Curated
    Sequence conflicti213 – 23018ALDTL…APGEA → GSIRWALISCVTSRRAR(PubMed:6443594)CuratedAdd
    BLAST
    Sequence conflicti213 – 23018ALDTL…APGEA → GSIRWALISCVTSRRAR(PubMed:6277938)CuratedAdd
    BLAST
    Sequence conflicti277 – 2771V → A(PubMed:6443594)Curated
    Sequence conflicti277 – 2771V → A(PubMed:6277938)Curated
    Sequence conflicti283 – 2831L → V(PubMed:6443594)Curated
    Sequence conflicti283 – 2831L → V(PubMed:6277938)Curated
    Sequence conflicti337 – 3371M → I in AAA24453. (PubMed:6443594)Curated
    Sequence conflicti386 – 3861A → R in CAA30971. (PubMed:3047685)Curated
    Sequence conflicti494 – 4941N → S(PubMed:6443594)Curated
    Sequence conflicti494 – 4941N → S(PubMed:6277938)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490554.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75372; AAC75372; b2312.
    BAA16158; BAA16158; BAA16158.
    GeneIDi12932081.
    946794.
    KEGGiecj:Y75_p2278.
    eco:b2312.
    PATRICi32119995. VBIEscCol129921_2407.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi F65003. XQEC.
    RefSeqi NP_416815.1. NC_000913.3.
    YP_490554.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ECB X-ray 2.70 A/B/C/D 2-505 [» ]
    1ECC X-ray 2.40 A/B 2-505 [» ]
    1ECF X-ray 2.00 A/B 2-505 [» ]
    1ECG X-ray 2.30 A/B 2-505 [» ]
    1ECJ X-ray 2.50 A/B/C/D 2-505 [» ]
    DisProti DP00578.
    ProteinModelPortali P0AG16.
    SMRi P0AG16. Positions 2-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 511145.b2312.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    Protein family/group databases

    MEROPSi C44.001.

    Proteomic databases

    PaxDbi P0AG16.
    PRIDEi P0AG16.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75372 ; AAC75372 ; b2312 .
    BAA16158 ; BAA16158 ; BAA16158 .
    GeneIDi 12932081.
    946794.
    KEGGi ecj:Y75_p2278.
    eco:b2312.
    PATRICi 32119995. VBIEscCol129921_2407.

    Organism-specific databases

    EchoBASEi EB0787.
    EcoGenei EG10794. purF.

    Phylogenomic databases

    eggNOGi COG0034.
    KOi K00764.
    OMAi AARVHMG.
    OrthoDBi EOG6KT2Q1.
    PhylomeDBi P0AG16.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00124 .
    BioCyci EcoCyc:PRPPAMIDOTRANS-MONOMER.
    ECOL316407:JW2309-MONOMER.
    MetaCyc:PRPPAMIDOTRANS-MONOMER.
    SABIO-RK P0AG16.

    Miscellaneous databases

    EvolutionaryTracei P0AG16.
    PROi P0AG16.

    Gene expression databases

    Genevestigatori P0AG16.

    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. "Nucleotide sequence of the Escherichia coli purF gene encoding amidophosphoribosyltransferase for de novo purine nucleotide synthesis."
      Sampei G., Mizobuchi K.
      Nucleic Acids Res. 16:8717-8717(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes."
      Zalkin H.
      Adv. Enzyme Regul. 21:225-237(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase."
      Tso J.Y., Zalkin H., van Cleemput M., Yanofsky C., Smith J.M.
      J. Biol. Chem. 257:3525-3531(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons."
      Nonet M.L., Marvel C.C., Tolan D.R.
      J. Biol. Chem. 262:12209-12217(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31 AND 483-505.
      Strain: K12.
    8. "Glutamine phosphoribosylpyrophosphate amidotransferase from cloned Escherichia coli purF. NH2-terminal amino acid sequence, identification of the glutamine site, and trace metal analysis."
      Tso J.Y., Hermodson M.A., Zalkin H.
      J. Biol. Chem. 257:3532-3536(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-24.
    9. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    10. "Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site."
      Krahn J.M., Kim J.H., Burns M.R., Parry R.J., Zalkin H., Smith J.L.
      Biochemistry 36:11061-11068(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    11. "Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli."
      Muchmore C.R.A., Krahn J.M., Kim J.H., Zalkin H., Smith J.L.
      Protein Sci. 7:39-51(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    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: October 1, 2014
    This is version 86 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

    External Data

    Dasty 3