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P00497 (PUR1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amidophosphoribosyltransferase

Short name=ATase
EC=2.4.2.14
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase
Short name=GPATase
Gene names
Name:purF
Ordered Locus Names:BSU06490
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.

Cofactor

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 regulation

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

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.

Subunit structure

Homotetramer.

Sequence similarities

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.

Contains 1 glutamine amidotransferase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 1111
PRO_0000029251
Chain12 – 476465Amidophosphoribosyltransferase
PRO_0000029252

Regions

Domain12 – 231220Glutamine amidotransferase type-2

Sites

Active site121For GATase activity Ref.5
Metal binding2471Iron-sulfur (4Fe-4S)
Metal binding2941Magnesium
Metal binding3561Magnesium
Metal binding3571Magnesium
Metal binding3931Iron-sulfur (4Fe-4S)
Metal binding4481Iron-sulfur (4Fe-4S)
Metal binding4511Iron-sulfur (4Fe-4S)

Experimental info

Mutagenesis121C → F: Loss of enzyme activity and N-terminal processing. Ref.6
Mutagenesis3941F → V: Partial loss of activity.
Mutagenesis4421D → S: Partial loss of activity.
Mutagenesis4481C → S: Loss of activity.
Mutagenesis4511C → S: Loss of activity.
Mutagenesis4521F → C: Lethal.
Sequence conflict4131E → G Ref.1
Sequence conflict4131E → G in AAA22680. Ref.2

Secondary structure

.......................................................................................... 476
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00497 [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: 6BC2FDA3288002F0

FASTA47651,692
        10         20         30         40         50         60 
MLAEIKGLNE ECGVFGIWGH EEAPQITYYG LHSLQHRGQE GAGIVATDGE KLTAHKGQGL 

        70         80         90        100        110        120 
ITEVFQNGEL SKVKGKGAIG HVRYATAGGG GYENVQPLLF RSQNNGSLAL AHNGNLVNAT 

       130        140        150        160        170        180 
QLKQQLENQG SIFQTSSDTE VLAHLIKRSG HFTLKDQIKN SLSMLKGAYA FLIMTETEMI 

       190        200        210        220        230        240 
VALDPNGLRP LSIGMMGDAY VVASETCAFD VVGATYLREV EPGEMLIIND EGMKSERFSM 

       250        260        270        280        290        300 
NINRSICSME YIYFSRPDSN IDGINVHSAR KNLGKMLAQE SAVEADVVTG VPDSSISAAI 

       310        320        330        340        350        360 
GYAEATGIPY ELGLIKNRYV GRTFIQPSQA LREQGVRMKL SAVRGVVEGK RVVMVDDSIV 

       370        380        390        400        410        420 
RGTTSRRIVT MLREAGATEV HVKISSPPIA HPCFYGIDTS THEELIASSH SVEEIRQEIG 

       430        440        450        460        470 
ADTLSFLSVE GLLKGIGRKY DDSNCGQCLA CFTGKYPTEI YQDTVLPHVK EAVLTK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02732 Genomic DNA. Translation: AAA22680.1.
AL009126 Genomic DNA. Translation: CAB12469.2.
PIRXQBS. A00582.
RefSeqNP_388531.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AO0X-ray2.80A/B/C/D12-470[»]
1GPHX-ray3.001/2/3/412-476[»]
ProteinModelPortalP00497.
SMRP00497. Positions 12-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00497. 1 interaction.
MINTMINT-8365657.
STRING224308.BSU06490.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Protein family/group databases

MEROPSC44.001.

Proteomic databases

PaxDbP00497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12469; CAB12469; BSU06490.
GeneID936046.
KEGGbsu:BSU06490.
PATRIC18972940. VBIBacSub10457_0684.

Organism-specific databases

GenoListBSU06490. [Micado]

Phylogenomic databases

eggNOGCOG0034.
HOGENOMHOG000033688.
KOK00764.
OrthoDBEOG6KT2Q1.
ProtClustDBPRK07631.

Enzyme and pathway databases

BioCycBSUB:BSU06490-MONOMER.
UniPathwayUPA00074; UER00124.

Family and domain databases

InterProIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF00310. GATase_2. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 1 hit.
TIGRFAMsTIGR01134. purF. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00497.

Entry information

Entry namePUR1_BACSU
AccessionPrimary (citable) accession number: P00497
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 7, 2009
Last modified: December 11, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

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