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P00497

- PUR1_BACSU

UniProt

P00497 - PUR1_BACSU

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Protein

Amidophosphoribosyltransferase

Gene

purF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

Binds 1 magnesium ion per subunit.1 PublicationUniRule annotation
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 – 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-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.
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:
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.

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.
InParanoidi P00497.
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.
HAMAPi MF_01931. PurF.
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

« 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: October 29, 2014
This is version 136 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