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Protein

Phosphoribosylformylglycinamidine synthase

Gene

purL

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

Functioni

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.UniRule annotation1 Publication

Catalytic activityi

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.UniRule annotation1 Publication

Kineticsi

  1. KM=64 µM for glutamine (at pH 7.25 and 37 degrees Celsius)1 Publication
  2. KM=51 µM for ATP (at pH 7.25 and 37 degrees Celsius)1 Publication
  3. KM=30 µM for FGAR (formylglycinamide ribonucleotide at pH 7.25 and 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.2 with only 50% of this activity retains at pH 6.2 or 8.0.1 Publication

    Pathwayi: IMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Phosphoribosylformylglycinamidine synthase (purL)
    2. Phosphoribosylformylglycinamidine cyclo-ligase (purM)
    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 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei678 – 6781ATP; via carbonyl oxygenUniRule annotation
    Metal bindingi718 – 7181MagnesiumUniRule annotation
    Metal bindingi722 – 7221MagnesiumUniRule annotation
    Metal bindingi884 – 8841MagnesiumUniRule annotation
    Binding sitei886 – 8861ATPUniRule annotation
    Active sitei1135 – 11351NucleophileUniRule annotation
    Active sitei1260 – 12601UniRule annotation
    Active sitei1262 – 12621UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi307 – 31812ATPUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    • ATPase activity, coupled Source: EcoliWiki
    • ATP binding Source: EcoliWiki
    • metal ion binding Source: UniProtKB-KW
    • phosphoribosylformylglycinamidine synthase activity Source: EcoCyc

    GO - Biological processi

    • 'de novo' IMP biosynthetic process Source: EcoliWiki
    • glutamine metabolic process Source: EcoliWiki
    • purine nucleotide biosynthetic process Source: GO_Central
    • ribonucleoside monophosphate biosynthetic process Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:FGAMSYN-MONOMER.
    ECOL316407:JW2541-MONOMER.
    MetaCyc:FGAMSYN-MONOMER.
    UniPathwayiUPA00074; UER00128.

    Protein family/group databases

    MEROPSiC56.972.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosylformylglycinamidine synthaseUniRule annotation (EC:6.3.5.3UniRule annotation)
    Short name:
    FGAM synthaseUniRule annotation
    Short name:
    FGAMSUniRule annotation
    Alternative name(s):
    Formylglycinamide ribonucleotide amidotransferaseUniRule annotation
    Short name:
    FGAR amidotransferaseUniRule annotation
    Short name:
    FGAR-ATUniRule annotation
    Gene namesi
    Name:purLUniRule annotation
    Synonyms:purI
    Ordered Locus Names:b2557, JW2541
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10797. purL.

    Subcellular locationi

    • Cytoplasm UniRule annotation1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12951295Phosphoribosylformylglycinamidine synthasePRO_0000100406Add
    BLAST

    Post-translational modificationi

    Both N-terminus methionine truncation and retention have been observed for this protein.1 Publication

    Proteomic databases

    PaxDbiP15254.
    PRIDEiP15254.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation1 Publication

    Protein-protein interaction databases

    BioGridi4259206. 41 interactions.
    DIPiDIP-10614N.
    IntActiP15254. 8 interactions.
    MINTiMINT-1262623.
    STRINGi511145.b2557.

    Structurei

    3D structure databases

    ProteinModelPortaliP15254.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1042 – 1295254Glutamine amidotransferase type-1UniRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the FGAMS family.UniRule annotation
    Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4107QIK. Bacteria.
    COG0046. LUCA.
    COG0047. LUCA.
    HOGENOMiHOG000261359.
    InParanoidiP15254.
    KOiK01952.
    OMAiKAETHNF.
    PhylomeDBiP15254.

    Family and domain databases

    Gene3Di3.30.1330.10. 2 hits.
    3.40.50.880. 1 hit.
    HAMAPiMF_00419. PurL_1. 1 hit.
    InterProiIPR010918. AIR_synth_C_dom.
    IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR010073. PRibForGlyAmidine_synth.
    IPR016188. PurM-like_N.
    [Graphical view]
    PfamiPF02769. AIRS_C. 2 hits.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    SSF56042. SSF56042. 2 hits.
    TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P15254-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMEILRGSPA LSAFRINKLL ARFQAARLPV HNIYAEYVHF ADLNAPLNDD
    60 70 80 90 100
    EHAQLERLLK YGPALASHAP QGKLLLVTPR PGTISPWSSK ATDIAHNCGL
    110 120 130 140 150
    QQVNRLERGV AYYIEAGTLT NEQWQQVTAE LHDRMMETVF FALDDAEQLF
    160 170 180 190 200
    AHHQPTPVTS VDLLGQGRQA LIDANLRLGL ALAEDEIDYL QDAFTKLGRN
    210 220 230 240 250
    PNDIELYMFA QANSEHCRHK IFNADWVIDG EQQPKSLFKM IKNTFETTPD
    260 270 280 290 300
    HVLSAYKDNA AVMEGSEVGR YFADHETGRY DFHQEPAHIL MKVETHNHPT
    310 320 330 340 350
    AISPWPGAAT GSGGEIRDEG ATGRGAKPKA GLVGFSVSNL RIPGFEQPWE
    360 370 380 390 400
    EDFGKPERIV TALDIMTEGP LGGAAFNNEF GRPALNGYFR TYEEKVNSHN
    410 420 430 440 450
    GEELRGYHKP IMLAGGIGNI RADHVQKGEI NVGAKLVVLG GPAMNIGLGG
    460 470 480 490 500
    GAASSMASGQ SDADLDFASV QRDNPEMERR CQEVIDRCWQ LGDANPILFI
    510 520 530 540 550
    HDVGAGGLSN AMPELVSDGG RGGKFELREI LSDEPGMSPL EIWCNESQER
    560 570 580 590 600
    YVLAVAADQL PLFDELCKRE RAPYAVIGEA TEELHLSLHD RHFDNQPIDL
    610 620 630 640 650
    PLDVLLGKTP KMTRDVQTLK AKGDALAREG ITIADAVKRV LHLPTVAEKT
    660 670 680 690 700
    FLVTIGDRSV TGMVARDQMV GPWQVPVANC AVTTASLDSY YGEAMAIGER
    710 720 730 740 750
    APVALLDFAA SARLAVGEAL TNIAATQIGD IKRIKLSANW MAAAGHPGED
    760 770 780 790 800
    AGLYEAVKAV GEELCPALGL TIPVGKDSMS MKTRWQEGNE EREMTSPLSL
    810 820 830 840 850
    VISAFARVED VRHTITPQLS TEDNALLLID LGKGNNALGA TALAQVYRQL
    860 870 880 890 900
    GDKPADVRDV AQLKGFYDAI QALVAQRKLL AYHDRSDGGL LVTLAEMAFA
    910 920 930 940 950
    GHCGIDADIA TLGDDRLAAL FNEELGAVIQ VRAADREAVE SVLAQHGLAD
    960 970 980 990 1000
    CVHYVGQAVS GDRFVITANG QTVFSESRTT LRVWWAETTW QMQRLRDNPE
    1010 1020 1030 1040 1050
    CADQEHQAKS NDADPGLNVK LSFDINEDVA APYIATGARP KVAVLREQGV
    1060 1070 1080 1090 1100
    NSHVEMAAAF HRAGFDAIDV HMSDLLTGRT GLEDFHALVA CGGFSYGDVL
    1110 1120 1130 1140 1150
    GAGEGWAKSI LFNDRVRDEF ATFFHRPQTL ALGVCNGCQM MSNLRELIPG
    1160 1170 1180 1190 1200
    SELWPRFVRN TSDRFEARFS LVEVTQSPSL LLQGMVGSQM PIAVSHGEGR
    1210 1220 1230 1240 1250
    VEVRDAAHLA ALESKGLVAL RYVDNFGKVT ETYPANPNGS PNGITAVTTE
    1260 1270 1280 1290
    SGRVTIMMPH PERVFRTVSN SWHPENWGED GPWMRIFRNA RKQLG
    Length:1,295
    Mass (Da):141,403
    Last modified:December 4, 2007 - v3
    Checksum:i30943AA218D758FE
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M19501 Genomic DNA. Translation: AAA24456.1.
    U36841 Genomic DNA. Translation: AAA79819.1.
    U00096 Genomic DNA. Translation: AAT48143.1.
    AP009048 Genomic DNA. Translation: BAE76733.1.
    PIRiD65033. SYECPG.
    RefSeqiWP_000970102.1. NZ_LN832404.1.
    YP_026170.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAT48143; AAT48143; b2557.
    BAE76733; BAE76733; BAE76733.
    GeneIDi947032.
    KEGGiecj:JW2541.
    eco:b2557.
    PATRICi32120513. VBIEscCol129921_2659.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M19501 Genomic DNA. Translation: AAA24456.1.
    U36841 Genomic DNA. Translation: AAA79819.1.
    U00096 Genomic DNA. Translation: AAT48143.1.
    AP009048 Genomic DNA. Translation: BAE76733.1.
    PIRiD65033. SYECPG.
    RefSeqiWP_000970102.1. NZ_LN832404.1.
    YP_026170.1. NC_000913.3.

    3D structure databases

    ProteinModelPortaliP15254.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259206. 41 interactions.
    DIPiDIP-10614N.
    IntActiP15254. 8 interactions.
    MINTiMINT-1262623.
    STRINGi511145.b2557.

    Protein family/group databases

    MEROPSiC56.972.

    Proteomic databases

    PaxDbiP15254.
    PRIDEiP15254.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAT48143; AAT48143; b2557.
    BAE76733; BAE76733; BAE76733.
    GeneIDi947032.
    KEGGiecj:JW2541.
    eco:b2557.
    PATRICi32120513. VBIEscCol129921_2659.

    Organism-specific databases

    EchoBASEiEB0790.
    EcoGeneiEG10797. purL.

    Phylogenomic databases

    eggNOGiENOG4107QIK. Bacteria.
    COG0046. LUCA.
    COG0047. LUCA.
    HOGENOMiHOG000261359.
    InParanoidiP15254.
    KOiK01952.
    OMAiKAETHNF.
    PhylomeDBiP15254.

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00128.
    BioCyciEcoCyc:FGAMSYN-MONOMER.
    ECOL316407:JW2541-MONOMER.
    MetaCyc:FGAMSYN-MONOMER.

    Miscellaneous databases

    PROiP15254.

    Family and domain databases

    Gene3Di3.30.1330.10. 2 hits.
    3.40.50.880. 1 hit.
    HAMAPiMF_00419. PurL_1. 1 hit.
    InterProiIPR010918. AIR_synth_C_dom.
    IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR010073. PRibForGlyAmidine_synth.
    IPR016188. PurM-like_N.
    [Graphical view]
    PfamiPF02769. AIRS_C. 2 hits.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    SSF56042. SSF56042. 2 hits.
    TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPUR4_ECOLI
    AccessioniPrimary (citable) accession number: P15254
    Secondary accession number(s): P78097, Q2MAH3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: December 4, 2007
    Last modified: September 7, 2016
    This is version 159 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

    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. 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.