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P00497

- PUR1_BACSU

UniProt

P00497 - PUR1_BACSU

Protein

Amidophosphoribosyltransferase

Gene

purF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      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.
    Binds 1 4Fe-4S cluster per subunit. The 4Fe-4S cluster requires a potential lower than -600 mV for reduction.

    Enzyme regulationi

    Allosterically regulated; subject to end product regulation by purine nucleotides.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei12 – 121For GATase activity1 Publication
    Metal bindingi247 – 2471Iron-sulfur (4Fe-4S)
    Metal bindingi294 – 2941Magnesium
    Metal bindingi356 – 3561Magnesium
    Metal bindingi357 – 3571Magnesium
    Metal bindingi393 – 3931Iron-sulfur (4Fe-4S)
    Metal bindingi448 – 4481Iron-sulfur (4Fe-4S)
    Metal bindingi451 – 4511Iron-sulfur (4Fe-4S)

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. amidophosphoribosyltransferase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    4Fe-4S, Iron, Iron-sulfur, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU06490-MONOMER.
    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:BSU06490
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU06490. [Micado]

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121C → F: Loss of enzyme activity and N-terminal processing. 2 Publications
    Mutagenesisi394 – 3941F → V: Partial loss of activity. 1 Publication
    Mutagenesisi442 – 4421D → S: Partial loss of activity. 1 Publication
    Mutagenesisi448 – 4481C → S: Loss of activity. 1 Publication
    Mutagenesisi451 – 4511C → S: Loss of activity. 1 Publication
    Mutagenesisi452 – 4521F → C: Lethal. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 11111 PublicationPRO_0000029251Add
    BLAST
    Chaini12 – 476465AmidophosphoribosyltransferasePRO_0000029252Add
    BLAST

    Proteomic databases

    PaxDbiP00497.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP00497. 1 interaction.
    MINTiMINT-8365657.
    STRINGi224308.BSU06490.

    Structurei

    Secondary structure

    1
    476
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 197
    Helixi23 – 3311
    Helixi34 – 374
    Beta strandi40 – 478
    Beta strandi52 – 598
    Helixi61 – 644
    Beta strandi67 – 693
    Turni70 – 723
    Beta strandi75 – 839
    Beta strandi86 – 883
    Helixi92 – 943
    Beta strandi95 – 1017
    Turni103 – 1053
    Beta strandi108 – 1169
    Helixi119 – 12810
    Beta strandi133 – 1353
    Helixi138 – 14710
    Helixi154 – 1629
    Beta strandi167 – 1748
    Beta strandi176 – 1838
    Beta strandi192 – 1965
    Beta strandi199 – 2057
    Helixi207 – 2126
    Beta strandi215 – 2195
    Beta strandi224 – 2296
    Beta strandi232 – 2387
    Helixi248 – 2525
    Helixi266 – 28116
    Beta strandi286 – 2894
    Turni292 – 2954
    Helixi296 – 30611
    Beta strandi314 – 3163
    Helixi329 – 3346
    Beta strandi338 – 3425
    Helixi344 – 3474
    Beta strandi351 – 3577
    Beta strandi360 – 3623
    Helixi363 – 37412
    Beta strandi378 – 3869
    Turni397 – 3993
    Turni407 – 4093
    Helixi412 – 4198
    Beta strandi422 – 4265
    Helixi429 – 4368
    Turni443 – 4464
    Helixi450 – 4534
    Helixi467 – 4693

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AO0X-ray2.80A/B/C/D12-470[»]
    1GPHX-ray3.001/2/3/412-476[»]
    ProteinModelPortaliP00497.
    SMRiP00497. Positions 12-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00497.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 231220Glutamine 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.
    HOGENOMiHOG000033688.
    KOiK00764.
    OrthoDBiEOG6KT2Q1.
    PhylomeDBiP00497.

    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.

    P00497-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLAEIKGLNE ECGVFGIWGH EEAPQITYYG LHSLQHRGQE GAGIVATDGE    50
    KLTAHKGQGL ITEVFQNGEL SKVKGKGAIG HVRYATAGGG GYENVQPLLF 100
    RSQNNGSLAL AHNGNLVNAT QLKQQLENQG SIFQTSSDTE VLAHLIKRSG 150
    HFTLKDQIKN SLSMLKGAYA FLIMTETEMI VALDPNGLRP LSIGMMGDAY 200
    VVASETCAFD VVGATYLREV EPGEMLIIND EGMKSERFSM NINRSICSME 250
    YIYFSRPDSN IDGINVHSAR KNLGKMLAQE SAVEADVVTG VPDSSISAAI 300
    GYAEATGIPY ELGLIKNRYV GRTFIQPSQA LREQGVRMKL SAVRGVVEGK 350
    RVVMVDDSIV RGTTSRRIVT MLREAGATEV HVKISSPPIA HPCFYGIDTS 400
    THEELIASSH SVEEIRQEIG ADTLSFLSVE GLLKGIGRKY DDSNCGQCLA 450
    CFTGKYPTEI YQDTVLPHVK EAVLTK 476
    Length:476
    Mass (Da):51,692
    Last modified:July 7, 2009 - v2
    Checksum:i6BC2FDA3288002F0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti413 – 4131E → G(PubMed:6411717)Curated
    Sequence conflicti413 – 4131E → G in AAA22680. (PubMed:3036807)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02732 Genomic DNA. Translation: AAA22680.1.
    AL009126 Genomic DNA. Translation: CAB12469.2.
    PIRiA00582. XQBS.
    RefSeqiNP_388531.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12469; CAB12469; BSU06490.
    GeneIDi936046.
    KEGGibsu:BSU06490.
    PATRICi18972940. VBIBacSub10457_0684.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02732 Genomic DNA. Translation: AAA22680.1 .
    AL009126 Genomic DNA. Translation: CAB12469.2 .
    PIRi A00582. XQBS.
    RefSeqi NP_388531.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AO0 X-ray 2.80 A/B/C/D 12-470 [» ]
    1GPH X-ray 3.00 1/2/3/4 12-476 [» ]
    ProteinModelPortali P00497.
    SMRi P00497. Positions 12-476.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00497. 1 interaction.
    MINTi MINT-8365657.
    STRINGi 224308.BSU06490.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    Protein family/group databases

    MEROPSi C44.001.

    Proteomic databases

    PaxDbi P00497.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12469 ; CAB12469 ; BSU06490 .
    GeneIDi 936046.
    KEGGi bsu:BSU06490.
    PATRICi 18972940. VBIBacSub10457_0684.

    Organism-specific databases

    GenoListi BSU06490. [Micado ]

    Phylogenomic databases

    eggNOGi COG0034.
    HOGENOMi HOG000033688.
    KOi K00764.
    OrthoDBi EOG6KT2Q1.
    PhylomeDBi P00497.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00124 .
    BioCyci BSUB:BSU06490-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P00497.

    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. "Cloning of the Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase gene in Escherichia coli. Nucleotide sequence determination and properties of the plasmid-encoded enzyme."
      Makaroff C.A., Zalkin H., Switzer R.L., Vollmer S.J.
      J. Biol. Chem. 258:10586-10593(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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].
    3. "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.
    4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 413.
    5. "The glutamine-utilizing site of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase."
      Vollmer S.J., Switzer R.L., Hermodson M.A., Bower S.G., Zalkin H.
      J. Biol. Chem. 258:10582-10585(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, PROTEIN SEQUENCE OF 12-35.
    6. "Glutamine amidotransferase function. Replacement of the active-site cysteine in glutamine phosphoribosylpyrophosphate amidotransferase by site-directed mutagenesis."
      Maentsaelae P., Zalkin H.
      J. Biol. Chem. 259:14230-14236(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-12.
    7. "Mutagenesis of ligands to the [4 Fe-4S] center of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase."
      Makaroff C.A., Paluh J.L., Zalkin H.
      J. Biol. Chem. 261:11416-11423(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    8. "Structure of the allosteric regulatory enzyme of purine biosynthesis."
      Smith J.L., Zaluzec E.J., Wery J.-P., Niu L., Switzer R.L., Zalkin H., Satow Y.
      Science 264:1427-1433(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    9. "Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides."
      Chen S., Tomchick D.R., Wolle D., Hu P., Smith J.L., Switzer R.L., Zalkin H.
      Biochemistry 36:10718-10726(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiPUR1_BACSU
    AccessioniPrimary (citable) accession number: P00497
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 135 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3