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P0AG16 (PUR1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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:b2312, JW2309
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length505 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.

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

Initiator methionine11Removed Ref.8
Chain2 – 505504Amidophosphoribosyltransferase
PRO_0000139638

Regions

Domain2 – 236235Glutamine amidotransferase type-2

Sites

Active site21For GATase activity
Metal binding3671Magnesium
Metal binding3681Magnesium

Experimental info

Sequence conflict45 – 462LR → SL Ref.2
Sequence conflict45 – 462LR → SL Ref.3
Sequence conflict501G → A Ref.2
Sequence conflict501G → A Ref.3
Sequence conflict213 – 23018ALDTL…APGEA → GSIRWALISCVTSRRAR Ref.2
Sequence conflict213 – 23018ALDTL…APGEA → GSIRWALISCVTSRRAR Ref.3
Sequence conflict2771V → A Ref.2
Sequence conflict2771V → A Ref.3
Sequence conflict2831L → V Ref.2
Sequence conflict2831L → V Ref.3
Sequence conflict3371M → I in AAA24453. Ref.2
Sequence conflict3861A → R in CAA30971. Ref.1
Sequence conflict4941N → S Ref.2
Sequence conflict4941N → S Ref.3

Secondary structure

................................................................................................. 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AG16 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 50FD08EA85E6F2A8

FASTA50556,488
        10         20         30         40         50         60 
MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG LVSDVFEARH 

        70         80         90        100        110        120 
MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA HNGNLTNAHE LRKKLFEEKR 

       130        140        150        160        170        180 
RHINTTSDSE ILLNIFASEL DNFRHYPLEA DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV 

       190        200        210        220        230        240 
AFRDPNGIRP LVLGKRDIDE NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF 

       250        260        270        280        290        300 
TRQCADNPVS NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI 

       310        320        330        340        350        360 
PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK LNANRAEFRD 

       370        380        390        400        410        420 
KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI RFPNVYGIDM PSATELIAHG 

       430        440        450        460        470        480 
REVDEIRQII GADGLIFQDL NDLIDAVRAE NPDIQQFECS VFNGVYVTKD VDQGYLDFLD 

       490        500 
TLRNDDAKAV QRQNEVENLE MHNEG 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Escherichia coli purF gene encoding amidophosphoribosyltransferase for de novo purine nucleotide synthesis."
Sampei G., Mizobuchi K.
Nucleic Acids Res. 16:8717-8717(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes."
Zalkin H.
Adv. Enzyme Regul. 21:225-237(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase."
Tso J.Y., Zalkin H., van Cleemput M., Yanofsky C., Smith J.M.
J. Biol. Chem. 257:3525-3531(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons."
Nonet M.L., Marvel C.C., Tolan D.R.
J. Biol. Chem. 262:12209-12217(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31 AND 483-505.
Strain: K12.
[8]"Glutamine phosphoribosylpyrophosphate amidotransferase from cloned Escherichia coli purF. NH2-terminal amino acid sequence, identification of the glutamine site, and trace metal analysis."
Tso J.Y., Hermodson M.A., Zalkin H.
J. Biol. Chem. 257:3532-3536(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-24.
[9]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[10]"Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site."
Krahn J.M., Kim J.H., Burns M.R., Parry R.J., Zalkin H., Smith J.L.
Biochemistry 36:11061-11068(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[11]"Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli."
Muchmore C.R.A., Krahn J.M., Kim J.H., Zalkin H., Smith J.L.
Protein Sci. 7:39-51(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12423 Genomic DNA. Translation: CAA30971.1.
V00322 Genomic DNA. Translation: CAA23613.1.
M26893 Genomic DNA. Translation: AAA24453.1.
J01666 Genomic DNA. Translation: AAA24452.1.
U00096 Genomic DNA. Translation: AAC75372.1.
AP009048 Genomic DNA. Translation: BAA16158.1.
M68935, M68934 Genomic DNA. Translation: AAA23969.1. Sequence problems.
PIRXQEC. F65003.
RefSeqNP_416815.1. NC_000913.3.
YP_490554.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ECBX-ray2.70A/B/C/D2-505[»]
1ECCX-ray2.40A/B2-505[»]
1ECFX-ray2.00A/B2-505[»]
1ECGX-ray2.30A/B2-505[»]
1ECJX-ray2.50A/B/C/D2-505[»]
DisProtDP00578.
ProteinModelPortalP0AG16.
SMRP0AG16. Positions 2-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b2312.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Protein family/group databases

MEROPSC44.001.

Proteomic databases

PaxDbP0AG16.
PRIDEP0AG16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75372; AAC75372; b2312.
BAA16158; BAA16158; BAA16158.
GeneID12932081.
946794.
KEGGecj:Y75_p2278.
eco:b2312.
PATRIC32119995. VBIEscCol129921_2407.

Organism-specific databases

EchoBASEEB0787.
EcoGeneEG10794. purF.

Phylogenomic databases

eggNOGCOG0034.
KOK00764.
OMAAARVHMG.
OrthoDBEOG6KT2Q1.
PhylomeDBP0AG16.

Enzyme and pathway databases

BioCycEcoCyc:PRPPAMIDOTRANS-MONOMER.
ECOL316407:JW2309-MONOMER.
MetaCyc:PRPPAMIDOTRANS-MONOMER.
SABIO-RKP0AG16.
UniPathwayUPA00074; UER00124.

Gene expression databases

GenevestigatorP0AG16.

Family and domain databases

Gene3D3.40.50.2020. 1 hit.
3.60.20.10. 1 hit.
InterProIPR005854. Amd_phspho_trans.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamPF00310. GATase_2. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 1 hit.
SUPFAMSSF53271. SSF53271. 1 hit.
SSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR01134. purF. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AG16.
PROP0AG16.

Entry information

Entry namePUR1_ECOLI
AccessionPrimary (citable) accession number: P0AG16
Secondary accession number(s): P00496 expand/collapse secondary AC list , P78092, P78191, P78192, Q47255, Q59425
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 85 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene