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P00497

- PUR1_BACSU

UniProt

P00497 - PUR1_BACSU

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Protein
Amidophosphoribosyltransferase
Gene
purF, BSU06490
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
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:
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. 1 Publication
Mutagenesisi394 – 3941F → V: Partial loss of activity.
Mutagenesisi442 – 4421D → S: Partial loss of activity.
Mutagenesisi448 – 4481C → S: Loss of activity.
Mutagenesisi451 – 4511C → S: Loss of activity.
Mutagenesisi452 – 4521F → C: Lethal.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1111
PRO_0000029251Add
BLAST
Chaini12 – 476465Amidophosphoribosyltransferase
PRO_0000029252Add
BLAST

Proteomic databases

PaxDbiP00497.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP00497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 231220Glutamine amidotransferase type-2
Add
BLAST

Sequence similaritiesi

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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti413 – 4131E → G1 Publication
Sequence conflicti413 – 4131E → G in AAA22680. 1 Publication

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

« 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. "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: July 9, 2014
This is version 134 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

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