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Protein

Phosphoribosylformylglycinamidine synthase subunit PurQ

Gene

purQ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.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
L-glutamine + H2O = L-glutamate + NH3.UniRule annotation1 Publication

Kineticsi

Kcat is 2.49 sec(-1) for FGAM synthase activity (at pH 7.2 and 37 degrees Celsius). Kcat is 0.002 sec(-1) for glutaminase activity (at pH 7.2 and 37 degrees Celsius).

  1. KM=181 µM for ATP (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)1 Publication
  2. KM=507 µM for FGAR (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)1 Publication
  3. KM=1.3 mM for glutamine (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)1 Publication
  4. KM=2.5 mM for glutamine (Glutaminase activity at pH 7.2 and 37 degrees Celsius)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 subunit PurL (purL), Phosphoribosylformylglycinamidine synthase subunit PurQ (purQ), Phosphoribosylformylglycinamidine synthase subunit PurS (purS)
    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
    Active sitei86 – 861NucleophileUniRule annotation
    Active sitei194 – 1941UniRule annotation
    Active sitei196 – 1961UniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Ligase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU06470-MONOMER.
    UniPathwayiUPA00074; UER00128.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoribosylformylglycinamidine synthase subunit PurQUniRule annotation (EC:6.3.5.3UniRule annotation)
    Short name:
    FGAM synthaseUniRule annotation
    Alternative name(s):
    Formylglycinamide ribonucleotide amidotransferase subunit IUniRule annotation
    Short name:
    FGAR amidotransferase IUniRule annotation
    Short name:
    FGAR-AT IUniRule annotation
    Glutaminase PurQUniRule annotation (EC:3.5.1.2UniRule annotation)
    Phosphoribosylformylglycinamidine synthase subunit IUniRule annotation
    Gene namesi
    Name:purQUniRule annotation
    Ordered Locus Names:BSU06470
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 227227Phosphoribosylformylglycinamidine synthase subunit PurQPRO_0000100539Add
    BLAST

    Proteomic databases

    PaxDbiP12041.

    Interactioni

    Subunit structurei

    Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.UniRule annotation1 Publication

    Protein-protein interaction databases

    IntActiP12041. 5 interactions.
    STRINGi224308.Bsubs1_010100003653.

    Structurei

    3D structure databases

    ProteinModelPortaliP12041.
    SMRiP12041. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 225223Glutamine amidotransferase type-1UniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiENOG4105D21. Bacteria.
    COG0047. LUCA.
    HOGENOMiHOG000238240.
    InParanoidiP12041.
    KOiK01952.
    OMAiHAEGRFY.
    OrthoDBiEOG6P5ZJP.
    PhylomeDBiP12041.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    HAMAPiMF_00421. PurQ.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR010075. PRibForGlyAmidine_synth_PurQ.
    [Graphical view]
    PIRSFiPIRSF001586. FGAM_synth_I. 1 hit.
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR01737. FGAM_synth_I. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P12041-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKFAVIVLPG SNCDIDMYHA VKDELGHEVE YVWHEETSLD GFDGVLIPGG
    60 70 80 90 100
    FSYGDYLRCG AIARFANIMP AVKQAAAEGK PVLGVCNGFQ ILQELGLLPG
    110 120 130 140 150
    AMRRNKDLKF ICRPVELIVQ NDETLFTASY EKGESITIPV AHGEGNFYCD
    160 170 180 190 200
    DETLATLKEN NQIAFTYGSN INGSVSDIAG VVNEKGNVLG MMPHPERAVD
    210 220
    ELLGSADGLK LFQSIVKNWR ETHVTTA
    Length:227
    Mass (Da):24,784
    Last modified:October 1, 1989 - v1
    Checksum:iEBD8A20EF679FC5B
    GO

    Mass spectrometryi

    Molecular mass is 24816 Da from positions 1 - 227. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02732 Genomic DNA. Translation: AAA22678.1.
    AL009126 Genomic DNA. Translation: CAB12467.1.
    PIRiF29326. SYBS1G.
    RefSeqiNP_388529.1. NC_000964.3.
    WP_003243954.1. NZ_JNCM01000032.1.

    Genome annotation databases

    EnsemblBacteriaiCAB12467; CAB12467; BSU06470.
    GeneIDi938760.
    KEGGibsu:BSU06470.
    PATRICi18972936. VBIBacSub10457_0682.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02732 Genomic DNA. Translation: AAA22678.1.
    AL009126 Genomic DNA. Translation: CAB12467.1.
    PIRiF29326. SYBS1G.
    RefSeqiNP_388529.1. NC_000964.3.
    WP_003243954.1. NZ_JNCM01000032.1.

    3D structure databases

    ProteinModelPortaliP12041.
    SMRiP12041. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP12041. 5 interactions.
    STRINGi224308.Bsubs1_010100003653.

    Proteomic databases

    PaxDbiP12041.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB12467; CAB12467; BSU06470.
    GeneIDi938760.
    KEGGibsu:BSU06470.
    PATRICi18972936. VBIBacSub10457_0682.

    Phylogenomic databases

    eggNOGiENOG4105D21. Bacteria.
    COG0047. LUCA.
    HOGENOMiHOG000238240.
    InParanoidiP12041.
    KOiK01952.
    OMAiHAEGRFY.
    OrthoDBiEOG6P5ZJP.
    PhylomeDBiP12041.

    Enzyme and pathway databases

    UniPathwayiUPA00074; UER00128.
    BioCyciBSUB:BSU06470-MONOMER.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    HAMAPiMF_00421. PurQ.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR010075. PRibForGlyAmidine_synth_PurQ.
    [Graphical view]
    PIRSFiPIRSF001586. FGAM_synth_I. 1 hit.
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR01737. FGAM_synth_I. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis."
      Ebbole D.J., Zalkin H.
      J. Biol. Chem. 262:8274-8287(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formation."
      Hoskins A.A., Anand R., Ealick S.E., Stubbe J.
      Biochemistry 43:10314-10327(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, SUBUNIT.

    Entry informationi

    Entry nameiPURQ_BACSU
    AccessioniPrimary (citable) accession number: P12041
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: February 17, 2016
    This is version 142 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

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    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.