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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.UniRule annotation1 Publication

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.UniRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation1 PublicationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation1 Publication
  • [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: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Amidophosphoribosyltransferase (purF)
  2. Phosphoribosylamine--glycine ligase (purD)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei12NucleophileUniRule annotation1 Publication1
Metal bindingi247Iron-sulfur (4Fe-4S)UniRule annotation2 Publications1
Metal bindingi294MagnesiumUniRule annotation1 Publication1
Metal bindingi356MagnesiumUniRule annotation1 Publication1
Metal bindingi357MagnesiumUniRule annotation1 Publication1
Metal bindingi393Iron-sulfur (4Fe-4S)UniRule annotation2 Publications1
Metal bindingi448Iron-sulfur (4Fe-4S)UniRule annotation2 Publications1
Metal bindingi451Iron-sulfur (4Fe-4S)UniRule annotation2 Publications1

GO - Molecular functioni

GO - Biological processi

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.
BRENDAi2.4.2.14. 658.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.001.

Names & Taxonomyi

Protein namesi
Recommended name:
AmidophosphoribosyltransferaseUniRule annotation (EC:2.4.2.14UniRule annotation1 Publication)
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
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12C → F: Loss of enzyme activity and N-terminal processing. 1 Publication1
Mutagenesisi394F → V: Partial loss of activity. 1 Publication1
Mutagenesisi442D → S: Partial loss of activity. 1 Publication1
Mutagenesisi448C → S: Loss of activity. 1 Publication1
Mutagenesisi451C → S: Loss of activity. 1 Publication1
Mutagenesisi452F → C: Lethal. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000292511 – 111 PublicationAdd BLAST11
ChainiPRO_000002925212 – 476AmidophosphoribosyltransferaseAdd BLAST465

Proteomic databases

PaxDbiP00497.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP00497. 1 interactor.
MINTiMINT-8365657.
STRINGi224308.Bsubs1_010100003668.

Structurei

Secondary structure

1476
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 19Combined sources7
Helixi23 – 33Combined sources11
Helixi34 – 37Combined sources4
Beta strandi40 – 47Combined sources8
Beta strandi52 – 59Combined sources8
Helixi61 – 64Combined sources4
Beta strandi67 – 69Combined sources3
Turni70 – 72Combined sources3
Beta strandi75 – 83Combined sources9
Beta strandi86 – 88Combined sources3
Helixi92 – 94Combined sources3
Beta strandi95 – 101Combined sources7
Turni103 – 105Combined sources3
Beta strandi108 – 116Combined sources9
Helixi119 – 128Combined sources10
Beta strandi133 – 135Combined sources3
Helixi138 – 147Combined sources10
Helixi154 – 162Combined sources9
Beta strandi167 – 174Combined sources8
Beta strandi176 – 183Combined sources8
Beta strandi192 – 196Combined sources5
Beta strandi199 – 205Combined sources7
Helixi207 – 212Combined sources6
Beta strandi215 – 219Combined sources5
Beta strandi224 – 229Combined sources6
Beta strandi232 – 238Combined sources7
Helixi248 – 252Combined sources5
Helixi266 – 281Combined sources16
Beta strandi286 – 289Combined sources4
Turni292 – 295Combined sources4
Helixi296 – 306Combined sources11
Beta strandi314 – 316Combined sources3
Helixi329 – 334Combined sources6
Beta strandi338 – 342Combined sources5
Helixi344 – 347Combined sources4
Beta strandi351 – 357Combined sources7
Beta strandi360 – 362Combined sources3
Helixi363 – 374Combined sources12
Beta strandi378 – 386Combined sources9
Turni397 – 399Combined sources3
Turni407 – 409Combined sources3
Helixi412 – 419Combined sources8
Beta strandi422 – 426Combined sources5
Helixi429 – 436Combined sources8
Turni443 – 446Combined sources4
Helixi450 – 453Combined sources4
Helixi467 – 469Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00497.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 231Glutamine amidotransferase type-2UniRule annotationAdd BLAST220

Sequence similaritiesi

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

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0034. LUCA.
HOGENOMiHOG000033688.
InParanoidiP00497.
KOiK00764.
OMAiAARVHMG.
PhylomeDBiP00497.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF. 1 hit.
InterProiIPR017932. GATase_2_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00156. 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)DescriptionActionsGraphical viewLength
Sequence conflicti413E → G (PubMed:6411717).Curated1
Sequence conflicti413E → G in AAA22680 (PubMed:3036807).Curated1

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.
WP_003233947.1. NZ_JNCM01000032.1.

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.
WP_003233947.1. NZ_JNCM01000032.1.

3D structure databases

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

Protein-protein interaction databases

IntActiP00497. 1 interactor.
MINTiMINT-8365657.
STRINGi224308.Bsubs1_010100003668.

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.

Phylogenomic databases

eggNOGiCOG0034. LUCA.
HOGENOMiHOG000033688.
InParanoidiP00497.
KOiK00764.
OMAiAARVHMG.
PhylomeDBiP00497.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00124.
BioCyciBSUB:BSU06490-MONOMER.
BRENDAi2.4.2.14. 658.

Miscellaneous databases

EvolutionaryTraceiP00497.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
HAMAPiMF_01931. PurF. 1 hit.
InterProiIPR017932. GATase_2_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
IPR005854. PurF.
[Graphical view]
PfamiPF00156. 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...

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: November 2, 2016
This is version 149 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

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 one 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.