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Protein

Phosphoribosylglycinamide formyltransferase

Gene

purN

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

Functioni

Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.UniRule annotation2 Publications

Catalytic activityi

10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation2 Publications

Enzyme regulationi

Inhibited by N10-(bromoacetyl)-5,8-dideazafolate.1 Publication

Kineticsi

kcat is 20.7 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 8.5). kcat is 13.5 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 7.5).1 Publication

Manual assertion based on experiment ini

  1. KM=77.5 µM for (6R)-N10-formyltetrahydrofolate (at pH 8.5)1 Publication
  2. KM=84.8 µM for (6R)-N10-formyltetrahydrofolate (at pH 7.5)1 Publication

    pH dependencei

    Optimum pH is 8.5.1 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 (10-formyl THF route).UniRule annotation1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Phosphoribosylglycinamide formyltransferase (purN)
    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 (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei6410-formyltetrahydrofolateUniRule annotation1 Publication1
    Binding sitei10610-formyltetrahydrofolateUniRule annotation1 Publication1
    Active sitei108Proton donorUniRule annotation1 Publication1
    Sitei144Raises pKa of active site HisUniRule annotation1 Publication1

    GO - Molecular functioni

    • phosphoribosylglycinamide formyltransferase activity Source: EcoCyc

    GO - Biological processi

    • 'de novo' IMP biosynthetic process Source: UniProtKB-HAMAP
    • cellular response to DNA damage stimulus Source: EcoliWiki
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Enzyme and pathway databases

    BioCyciEcoCyc:GART-MONOMER.
    ECOL316407:JW2485-MONOMER.
    MetaCyc:GART-MONOMER.
    UniPathwayiUPA00074; UER00126.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosylglycinamide formyltransferaseUniRule annotation (EC:2.1.2.2UniRule annotation2 Publications)
    Alternative name(s):
    5'-phosphoribosylglycinamide transformylaseUniRule annotation
    GAR transformylaseUniRule annotation
    Short name:
    GARTUniRule annotation
    Gene namesi
    Name:purN1 PublicationUniRule annotation
    Ordered Locus Names:b2500, JW2485
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10799. purN.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi70E → A: Loss of homodimerization. No effect on activity. 1 Publication1
    Mutagenesisi106N → A, D, G or S: Reduces activity about 2000-fold. 1 Publication1
    Mutagenesisi106N → E, H, I, K, L or Y: Loss of activity. 1 Publication1
    Mutagenesisi108H → A, G, M, N, Q or R: Loss of activity. 2 Publications1
    Mutagenesisi108H → E, S or T: Reduces activity about 1000-fold. 1 Publication1
    Mutagenesisi119H → A: No effect. 1 Publication1
    Mutagenesisi121H → Q: Increases Km for 5'-phosphoribosylglycinamide 4-fold. 1 Publication1
    Mutagenesisi135S → A or L: Reduces activity about 1000-fold. 1 Publication1
    Mutagenesisi137H → F or Q: No effect. 1 Publication1
    Mutagenesisi144D → A, E, S or Y: Reduces activity about 1000-fold. 2 Publications1
    Mutagenesisi144D → C, F, H, K, L, N, P, Q, R, T or V: Loss of activity. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000749431 – 212Phosphoribosylglycinamide formyltransferaseAdd BLAST212

    Proteomic databases

    PaxDbiP08179.
    PRIDEiP08179.

    Interactioni

    Subunit structurei

    Monomer. Homodimer below pH 6.8.5 Publications

    Protein-protein interaction databases

    BioGridi4261440. 10 interactors.
    IntActiP08179. 1 interactor.
    STRINGi511145.b2500.

    Chemistry databases

    BindingDBiP08179.

    Structurei

    Secondary structure

    1212
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 9Combined sources8
    Helixi12 – 22Combined sources11
    Beta strandi25 – 36Combined sources12
    Helixi41 – 48Combined sources8
    Beta strandi52 – 55Combined sources4
    Helixi58 – 60Combined sources3
    Beta strandi61 – 63Combined sources3
    Helixi64 – 75Combined sources12
    Helixi76 – 78Combined sources3
    Beta strandi81 – 87Combined sources7
    Helixi94 – 99Combined sources6
    Turni100 – 102Combined sources3
    Beta strandi103 – 110Combined sources8
    Beta strandi112 – 114Combined sources3
    Helixi120 – 126Combined sources7
    Beta strandi130 – 138Combined sources9
    Beta strandi141 – 146Combined sources6
    Beta strandi148 – 155Combined sources8
    Helixi162 – 185Combined sources24
    Beta strandi189 – 192Combined sources4
    Beta strandi195 – 198Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1C2TX-ray2.10A/B1-212[»]
    1C3EX-ray2.10A/B1-209[»]
    1CDDX-ray2.80A/B1-212[»]
    1CDEX-ray2.50A/B/C/D1-212[»]
    1GARX-ray1.96A/B1-212[»]
    1GRCX-ray3.00A/B1-212[»]
    1JKXX-ray1.60A/B/C/D1-212[»]
    2GARX-ray1.80A1-212[»]
    3GARX-ray1.90A1-212[»]
    ProteinModelPortaliP08179.
    SMRiP08179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08179.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni11 – 135'-phosphoribosylglycinamide bindingUniRule annotation2 Publications3
    Regioni89 – 9210-formyltetrahydrofolate bindingUniRule annotation2 Publications4
    Regioni140 – 14410-formyltetrahydrofolate binding2 Publications5
    Regioni170 – 1735'-phosphoribosylglycinamide binding2 Publications4

    Sequence similaritiesi

    Belongs to the GART family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4108V3E. Bacteria.
    COG0299. LUCA.
    HOGENOMiHOG000033575.
    InParanoidiP08179.
    KOiK11175.
    OMAiFKGTHTH.
    PhylomeDBiP08179.

    Family and domain databases

    CDDicd08645. FMT_core_GART. 1 hit.
    Gene3Di3.40.50.170. 1 hit.
    HAMAPiMF_01930. PurN. 1 hit.
    InterProiIPR002376. Formyl_transf_N.
    IPR001555. GART_AS.
    IPR004607. PurN.
    [Graphical view]
    PfamiPF00551. Formyl_trans_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53328. SSF53328. 1 hit.
    TIGRFAMsiTIGR00639. PurN. 1 hit.
    PROSITEiPS00373. GART. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08179-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNIVVLISGN GSNLQAIIDA CKTNKIKGTV RAVFSNKADA FGLERARQAG
    60 70 80 90 100
    IATHTLIASA FDSREAYDRE LIHEIDMYAP DVVVLAGFMR ILSPAFVSHY
    110 120 130 140 150
    AGRLLNIHPS LLPKYPGLHT HRQALENGDE EHGTSVHFVT DELDGGPVIL
    160 170 180 190 200
    QAKVPVFAGD SEDDITARVQ TQEHAIYPLV ISWFADGRLK MHENAAWLDG
    210
    QRLPPQGYAA DE
    Length:212
    Mass (Da):23,238
    Last modified:August 1, 1988 - v1
    Checksum:iD38F326BCBA103FB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M13747 Genomic DNA. Translation: AAA83899.1.
    U00096 Genomic DNA. Translation: AAC75553.1.
    AP009048 Genomic DNA. Translation: BAA16388.1.
    AF293167 Genomic DNA. Translation: AAG14584.1.
    PIRiA28486. XYECGF.
    RefSeqiNP_416995.1. NC_000913.3.
    WP_001028612.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75553; AAC75553; b2500.
    BAA16388; BAA16388; BAA16388.
    GeneIDi946973.
    KEGGiecj:JW2485.
    eco:b2500.
    PATRICi32120389. VBIEscCol129921_2597.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M13747 Genomic DNA. Translation: AAA83899.1.
    U00096 Genomic DNA. Translation: AAC75553.1.
    AP009048 Genomic DNA. Translation: BAA16388.1.
    AF293167 Genomic DNA. Translation: AAG14584.1.
    PIRiA28486. XYECGF.
    RefSeqiNP_416995.1. NC_000913.3.
    WP_001028612.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1C2TX-ray2.10A/B1-212[»]
    1C3EX-ray2.10A/B1-209[»]
    1CDDX-ray2.80A/B1-212[»]
    1CDEX-ray2.50A/B/C/D1-212[»]
    1GARX-ray1.96A/B1-212[»]
    1GRCX-ray3.00A/B1-212[»]
    1JKXX-ray1.60A/B/C/D1-212[»]
    2GARX-ray1.80A1-212[»]
    3GARX-ray1.90A1-212[»]
    ProteinModelPortaliP08179.
    SMRiP08179.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261440. 10 interactors.
    IntActiP08179. 1 interactor.
    STRINGi511145.b2500.

    Chemistry databases

    BindingDBiP08179.

    Proteomic databases

    PaxDbiP08179.
    PRIDEiP08179.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75553; AAC75553; b2500.
    BAA16388; BAA16388; BAA16388.
    GeneIDi946973.
    KEGGiecj:JW2485.
    eco:b2500.
    PATRICi32120389. VBIEscCol129921_2597.

    Organism-specific databases

    EchoBASEiEB0792.
    EcoGeneiEG10799. purN.

    Phylogenomic databases

    eggNOGiENOG4108V3E. Bacteria.
    COG0299. LUCA.
    HOGENOMiHOG000033575.
    InParanoidiP08179.
    KOiK11175.
    OMAiFKGTHTH.
    PhylomeDBiP08179.

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00126.
    BioCyciEcoCyc:GART-MONOMER.
    ECOL316407:JW2485-MONOMER.
    MetaCyc:GART-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP08179.
    PROiP08179.

    Family and domain databases

    CDDicd08645. FMT_core_GART. 1 hit.
    Gene3Di3.40.50.170. 1 hit.
    HAMAPiMF_01930. PurN. 1 hit.
    InterProiIPR002376. Formyl_transf_N.
    IPR001555. GART_AS.
    IPR004607. PurN.
    [Graphical view]
    PfamiPF00551. Formyl_trans_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53328. SSF53328. 1 hit.
    TIGRFAMsiTIGR00639. PurN. 1 hit.
    PROSITEiPS00373. GART. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPUR3_ECOLI
    AccessioniPrimary (citable) accession number: P08179
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: November 2, 2016
    This is version 153 of the entry and version 1 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.