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Protein

Phosphoribosylglycinamide formyltransferase 2

Gene

purT

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

Functioni

Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP.1 Publication

Catalytic activityi

Formate + ATP + 5'-phospho-ribosylglycinamide = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate.1 Publication

Kineticsi

Kcat is 37.6 sec(-1) for transferase activity (at pH 8).1 Publication

  1. KM=10.1 µM for GAR (at pH 8)1 Publication
  2. KM=319 µM for formate (at pH 8)1 Publication

    Pathwayi: IMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route).UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Phosphoribosylglycinamide formyltransferase 2 (purT), Phosphoribosylglycinamide formyltransferase 2 (purT)
    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(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 8215'-phosphoribosylglycinamide2 Publications
    Binding sitei114 – 1141ATP2 Publications
    Binding sitei155 – 1551ATP2 Publications
    Binding sitei203 – 2031ATP2 Publications
    Metal bindingi267 – 2671Magnesium2 Publications
    Metal bindingi279 – 2791Magnesium2 Publications
    Binding sitei286 – 28615'-phosphoribosylglycinamide2 Publications
    Binding sitei355 – 35515'-phosphoribosylglycinamide2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi160 – 1656ATP2 Publications
    Nucleotide bindingi195 – 1984ATP2 Publications

    GO - Molecular functioni

    GO - Biological processi

    • 'de novo' IMP biosynthetic process Source: GO_Central
    • adenine biosynthetic process Source: GO_Central
    • phosphorylation Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:GARTRANSFORMYL2-MONOMER.
    ECOL316407:JW1838-MONOMER.
    MetaCyc:GARTRANSFORMYL2-MONOMER.
    UniPathwayiUPA00074; UER00127.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosylglycinamide formyltransferase 2UniRule annotation (EC:2.1.2.-1 Publication)
    Short name:
    GART 2UniRule annotation
    Alternative name(s):
    5'-phosphoribosylglycinamide transformylase 2UniRule annotation
    Formate-dependent GAR transformylaseUniRule annotation
    GAR transformylase 2UniRule annotation
    Gene namesi
    Name:purTUniRule annotation
    Ordered Locus Names:b1849, JW1838
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11809. purT.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 392391Phosphoribosylglycinamide formyltransferase 2PRO_0000074956Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei179 – 1791N6-acetyllysineUniRule annotation1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiP33221.
    PaxDbiP33221.
    PRIDEiP33221.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ispAP229393EBI-553029,EBI-553011

    Protein-protein interaction databases

    DIPiDIP-10618N.
    IntActiP33221. 7 interactions.
    MINTiMINT-1306001.
    STRINGi511145.b1849.

    Structurei

    Secondary structure

    1
    392
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 196Combined sources
    Helixi22 – 3211Combined sources
    Turni33 – 353Combined sources
    Beta strandi37 – 448Combined sources
    Helixi48 – 525Combined sources
    Beta strandi53 – 586Combined sources
    Helixi64 – 7411Combined sources
    Beta strandi77 – 815Combined sources
    Helixi88 – 969Combined sources
    Beta strandi100 – 1034Combined sources
    Helixi105 – 1128Combined sources
    Helixi114 – 1229Combined sources
    Beta strandi132 – 1376Combined sources
    Helixi138 – 14811Combined sources
    Beta strandi150 – 1578Combined sources
    Turni161 – 1644Combined sources
    Beta strandi166 – 1683Combined sources
    Helixi171 – 1733Combined sources
    Helixi174 – 18411Combined sources
    Helixi186 – 1883Combined sources
    Beta strandi192 – 1965Combined sources
    Beta strandi201 – 21111Combined sources
    Beta strandi214 – 2174Combined sources
    Beta strandi221 – 2266Combined sources
    Beta strandi229 – 2357Combined sources
    Helixi241 – 25818Combined sources
    Beta strandi260 – 27112Combined sources
    Beta strandi274 – 28310Combined sources
    Helixi286 – 2905Combined sources
    Helixi291 – 2944Combined sources
    Beta strandi295 – 2973Combined sources
    Helixi299 – 3079Combined sources
    Beta strandi319 – 3268Combined sources
    Beta strandi329 – 3346Combined sources
    Beta strandi336 – 3383Combined sources
    Helixi340 – 3423Combined sources
    Beta strandi348 – 3525Combined sources
    Beta strandi358 – 3614Combined sources
    Beta strandi365 – 3706Combined sources
    Helixi374 – 38714Combined sources
    Beta strandi389 – 3913Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EYZX-ray1.75A/B1-392[»]
    1EZ1X-ray1.75A/B1-392[»]
    1KJ8X-ray1.60A/B2-392[»]
    1KJ9X-ray1.60A/B2-392[»]
    1KJIX-ray1.60A/B2-392[»]
    1KJJX-ray1.75A/B2-392[»]
    1KJQX-ray1.05A/B2-392[»]
    1NFEmodel-A1-392[»]
    ProteinModelPortaliP33221.
    SMRiP33221. Positions 2-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33221.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini119 – 308190ATP-graspUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 2325'-phosphoribosylglycinamide binding2 Publications
    Regioni362 – 36325'-phosphoribosylglycinamide binding2 Publications

    Sequence similaritiesi

    Belongs to the PurK/PurT family.UniRule annotation
    Contains 1 ATP-grasp domain.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4108HH9. Bacteria.
    COG0027. LUCA.
    HOGENOMiHOG000072820.
    InParanoidiP33221.
    KOiK08289.
    OMAiIFGVEFF.
    OrthoDBiEOG6GJBVD.
    PhylomeDBiP33221.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    HAMAPiMF_01643. PurT.
    InterProiIPR011761. ATP-grasp.
    IPR003135. ATP-grasp_carboxylate-amine.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR016185. PreATP-grasp_dom.
    IPR005862. PurT.
    IPR011054. Rudment_hybrid_motif.
    [Graphical view]
    PfamiPF02222. ATP-grasp. 1 hit.
    [Graphical view]
    SUPFAMiSSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    TIGRFAMsiTIGR01142. purT. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P33221-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM
    60 70 80 90 100
    HVAHRSHVIN MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN
    110 120 130 140 150
    VVPCARATKL TMNREGIRRL AAEELQLPTS TYRFADSESL FREAVADIGY
    160 170 180 190 200
    PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY AQQGGRAGAG RVIVEGVVKF
    210 220 230 240 250
    DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS PLALERAQEI
    260 270 280 290 300
    ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
    310 320 330 340 350
    ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI
    360 370 380 390
    RLFGKPEIDG SRRLGVALAT AESVVDAIER AKHAAGQVKV QG
    Length:392
    Mass (Da):42,434
    Last modified:January 23, 2007 - v3
    Checksum:i276B3883E7403EA9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L20897 Genomic DNA. Translation: AAA23861.1.
    U00096 Genomic DNA. Translation: AAC74919.1.
    AP009048 Genomic DNA. Translation: BAA15657.1.
    PIRiA54227.
    RefSeqiNP_416363.1. NC_000913.3.
    WP_000173484.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74919; AAC74919; b1849.
    BAA15657; BAA15657; BAA15657.
    GeneIDi946368.
    KEGGiecj:JW1838.
    eco:b1849.
    PATRICi32119019. VBIEscCol129921_1927.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L20897 Genomic DNA. Translation: AAA23861.1.
    U00096 Genomic DNA. Translation: AAC74919.1.
    AP009048 Genomic DNA. Translation: BAA15657.1.
    PIRiA54227.
    RefSeqiNP_416363.1. NC_000913.3.
    WP_000173484.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EYZX-ray1.75A/B1-392[»]
    1EZ1X-ray1.75A/B1-392[»]
    1KJ8X-ray1.60A/B2-392[»]
    1KJ9X-ray1.60A/B2-392[»]
    1KJIX-ray1.60A/B2-392[»]
    1KJJX-ray1.75A/B2-392[»]
    1KJQX-ray1.05A/B2-392[»]
    1NFEmodel-A1-392[»]
    ProteinModelPortaliP33221.
    SMRiP33221. Positions 2-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10618N.
    IntActiP33221. 7 interactions.
    MINTiMINT-1306001.
    STRINGi511145.b1849.

    Proteomic databases

    EPDiP33221.
    PaxDbiP33221.
    PRIDEiP33221.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74919; AAC74919; b1849.
    BAA15657; BAA15657; BAA15657.
    GeneIDi946368.
    KEGGiecj:JW1838.
    eco:b1849.
    PATRICi32119019. VBIEscCol129921_1927.

    Organism-specific databases

    EchoBASEiEB1757.
    EcoGeneiEG11809. purT.

    Phylogenomic databases

    eggNOGiENOG4108HH9. Bacteria.
    COG0027. LUCA.
    HOGENOMiHOG000072820.
    InParanoidiP33221.
    KOiK08289.
    OMAiIFGVEFF.
    OrthoDBiEOG6GJBVD.
    PhylomeDBiP33221.

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00127.
    BioCyciEcoCyc:GARTRANSFORMYL2-MONOMER.
    ECOL316407:JW1838-MONOMER.
    MetaCyc:GARTRANSFORMYL2-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP33221.
    PROiP33221.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    HAMAPiMF_01643. PurT.
    InterProiIPR011761. ATP-grasp.
    IPR003135. ATP-grasp_carboxylate-amine.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR016185. PreATP-grasp_dom.
    IPR005862. PurT.
    IPR011054. Rudment_hybrid_motif.
    [Graphical view]
    PfamiPF02222. ATP-grasp. 1 hit.
    [Graphical view]
    SUPFAMiSSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    TIGRFAMsiTIGR01142. purT. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and characterization of a new purine biosynthetic enzyme: a non-folate glycinamide ribonucleotide transformylase from E. coli."
      Marolewski A., Smith J.M., Benkovic S.J.
      Biochemistry 33:2531-2537(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    5. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    6. "Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase."
      Thoden J.B., Firestine S., Nixon A., Benkovic S.J., Holden H.M.
      Biochemistry 39:8791-8802(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ATP ANALOG; BETA-FORMYL GLYCINAMIDE RIBONUCLEOTIDE AND MAGNESIUM ION, SUBUNIT.
    7. "PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of adenosine nucleotide analogs within the active site."
      Thoden J.B., Firestine S.M., Benkovic S.J., Holden H.M.
      J. Biol. Chem. 277:23898-23908(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH BETA-FORMYL GLYCINAMIDE RIBONUCLEOTIDE; ATP AND MAGNESIUM ION, SUBUNIT.

    Entry informationi

    Entry nameiPURT_ECOLI
    AccessioniPrimary (citable) accession number: P33221
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: March 16, 2016
    This is version 157 of the entry and version 3 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.