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Protein

Amidophosphoribosyltransferase

Gene

purF

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

Functioni

Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.1 PublicationUniRule annotation

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 PublicationUniRule annotationNote: Binds 1 Mg2+ ion per subunit.1 PublicationUniRule annotation
  • [4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster per subunit. The [4Fe-4S] cluster requires a potential lower than -600 mV for reduction.1 Publication

Enzyme regulationi

Allosterically regulated; subject to end product regulation by purine nucleotides.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121Nucleophile1 PublicationUniRule annotation
Metal bindingi247 – 2471Iron-sulfur (4Fe-4S)2 PublicationsUniRule annotation
Metal bindingi294 – 2941Magnesium1 PublicationUniRule annotation
Metal bindingi356 – 3561Magnesium1 PublicationUniRule annotation
Metal bindingi357 – 3571Magnesium1 PublicationUniRule annotation
Metal bindingi393 – 3931Iron-sulfur (4Fe-4S)2 PublicationsUniRule annotation
Metal bindingi448 – 4481Iron-sulfur (4Fe-4S)2 PublicationsUniRule annotation
Metal bindingi451 – 4511Iron-sulfur (4Fe-4S)2 PublicationsUniRule annotation

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
Complete GO annotation...

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:
AmidophosphoribosyltransferaseUniRule annotation (EC:2.4.2.141 PublicationUniRule annotation)
Short name:
ATaseUniRule annotation
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferaseUniRule annotation
Short name:
GPATaseUniRule annotation
Gene namesi
Name:purF1 PublicationUniRule annotation
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. 1 Publication
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.1 Publication

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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-2UniRule annotationAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.CuratedUniRule annotation
Contains 1 glutamine amidotransferase type-2 domain.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0034.
HOGENOMiHOG000033688.
InParanoidiP00497.
KOiK00764.
OMAiAARVHMG.
OrthoDBiEOG6KT2Q1.
PhylomeDBiP00497.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
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

        10         20         30         40         50
MLAEIKGLNE ECGVFGIWGH EEAPQITYYG LHSLQHRGQE GAGIVATDGE
60 70 80 90 100
KLTAHKGQGL ITEVFQNGEL SKVKGKGAIG HVRYATAGGG GYENVQPLLF
110 120 130 140 150
RSQNNGSLAL AHNGNLVNAT QLKQQLENQG SIFQTSSDTE VLAHLIKRSG
160 170 180 190 200
HFTLKDQIKN SLSMLKGAYA FLIMTETEMI VALDPNGLRP LSIGMMGDAY
210 220 230 240 250
VVASETCAFD VVGATYLREV EPGEMLIIND EGMKSERFSM NINRSICSME
260 270 280 290 300
YIYFSRPDSN IDGINVHSAR KNLGKMLAQE SAVEADVVTG VPDSSISAAI
310 320 330 340 350
GYAEATGIPY ELGLIKNRYV GRTFIQPSQA LREQGVRMKL SAVRGVVEGK
360 370 380 390 400
RVVMVDDSIV RGTTSRRIVT MLREAGATEV HVKISSPPIA HPCFYGIDTS
410 420 430 440 450
THEELIASSH SVEEIRQEIG ADTLSFLSVE GLLKGIGRKY DDSNCGQCLA
460 470
CFTGKYPTEI YQDTVLPHVK EAVLTK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
J02732 Genomic DNA. Translation: AAA22680.1.
AL009126 Genomic DNA. Translation: CAB12469.2.
PIRiA00582. XQBS.
RefSeqiNP_388531.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiC44.001.

Proteomic databases

PaxDbiP00497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

GenoListiBSU06490. [Micado]

Phylogenomic databases

eggNOGiCOG0034.
HOGENOMiHOG000033688.
InParanoidiP00497.
KOiK00764.
OMAiAARVHMG.
OrthoDBiEOG6KT2Q1.
PhylomeDBiP00497.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
BioCyciBSUB:BSU06490-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00497.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis."
    Wong J.Y., Bernlohr D.A., Turnbough C.L., Switzer R.L.
    Biochemistry 20:5669-5674(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  6. "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.
  7. "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.
  8. "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.
  9. "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) IN COMPLEX WITH IRON-SULFUR (4FE-4S), ENZYME REGULATION, SUBUNIT.
  10. "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) IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND MAGNESIUM.

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: January 7, 2015
This is version 138 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

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 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.