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P0AG16

- PUR1_ECOLI

UniProt

P0AG16 - PUR1_ECOLI

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Protein
Amidophosphoribosyltransferase
Gene
purF, b2312, JW2309
Organism
Escherichia coli (strain K12)
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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activity
Metal bindingi367 – 3671Magnesium
Metal bindingi368 – 3681Magnesium

GO - Molecular functioni

  1. amidophosphoribosyltransferase activity Source: EcoliWiki
  2. identical protein binding Source: EcoCyc
  3. metal ion binding Source: UniProtKB-KW
  4. transferase activity, transferring glycosyl groups Source: EcoliWiki
Complete GO annotation...

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. glutamine metabolic process Source: EcoliWiki
  3. nucleoside metabolic process Source: InterPro
  4. purine nucleobase biosynthetic process Source: InterPro
  5. purine nucleotide biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:PRPPAMIDOTRANS-MONOMER.
ECOL316407:JW2309-MONOMER.
MetaCyc:PRPPAMIDOTRANS-MONOMER.
SABIO-RKiP0AG16.
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:b2312, JW2309
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10794. purF.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
  2. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 505504Amidophosphoribosyltransferase
PRO_0000139638Add
BLAST

Proteomic databases

PaxDbiP0AG16.
PRIDEiP0AG16.

Expressioni

Gene expression databases

GenevestigatoriP0AG16.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi511145.b2312.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Helixi14 – 2310
Helixi24 – 274
Beta strandi30 – 378
Beta strandi43 – 508
Helixi52 – 554
Helixi58 – 636
Beta strandi66 – 749
Beta strandi78 – 803
Helixi83 – 853
Beta strandi89 – 913
Beta strandi93 – 953
Beta strandi97 – 1059
Helixi108 – 11912
Helixi128 – 14013
Beta strandi145 – 1473
Helixi150 – 16314
Beta strandi166 – 1749
Turni175 – 1773
Beta strandi178 – 1836
Beta strandi192 – 1976
Beta strandi199 – 2013
Beta strandi203 – 2108
Helixi212 – 2176
Beta strandi220 – 2245
Beta strandi229 – 2346
Beta strandi239 – 2435
Beta strandi245 – 2473
Helixi254 – 2585
Helixi272 – 29019
Turni291 – 2933
Beta strandi298 – 3014
Turni303 – 3064
Helixi307 – 31711
Beta strandi325 – 3273
Beta strandi338 – 3403
Turni348 – 3503
Beta strandi351 – 3533
Helixi355 – 3573
Turni358 – 3603
Beta strandi363 – 3686
Beta strandi371 – 3733
Helixi374 – 38512
Beta strandi389 – 3979
Beta strandi406 – 4105
Helixi413 – 4153
Turni417 – 4204
Helixi423 – 4308
Beta strandi433 – 4375
Helixi440 – 4489
Helixi460 – 4634
Helixi473 – 49220

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00578.
ProteinModelPortaliP0AG16.
SMRiP0AG16. Positions 2-501.

Miscellaneous databases

EvolutionaryTraceiP0AG16.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 236235Glutamine 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.
KOiK00764.
OMAiAARVHMG.
OrthoDBiEOG6KT2Q1.
PhylomeDBiP0AG16.

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.

P0AG16-1 [UniParc]FASTAAdd to Basket

« Hide

MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG    50
LVSDVFEARH MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA 100
HNGNLTNAHE LRKKLFEEKR RHINTTSDSE ILLNIFASEL DNFRHYPLEA 150
DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV AFRDPNGIRP LVLGKRDIDE 200
NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF TRQCADNPVS 250
NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI 300
PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK 350
LNANRAEFRD KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI 400
RFPNVYGIDM PSATELIAHG REVDEIRQII GADGLIFQDL NDLIDAVRAE 450
NPDIQQFECS VFNGVYVTKD VDQGYLDFLD TLRNDDAKAV QRQNEVENLE 500
MHNEG 505
Length:505
Mass (Da):56,488
Last modified:January 23, 2007 - v2
Checksum:i50FD08EA85E6F2A8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462LR → SL1 Publication
Sequence conflicti45 – 462LR → SL1 Publication
Sequence conflicti50 – 501G → A1 Publication
Sequence conflicti50 – 501G → A1 Publication
Sequence conflicti213 – 23018ALDTL…APGEA → GSIRWALISCVTSRRAR1 Publication
Add
BLAST
Sequence conflicti213 – 23018ALDTL…APGEA → GSIRWALISCVTSRRAR1 Publication
Add
BLAST
Sequence conflicti277 – 2771V → A1 Publication
Sequence conflicti277 – 2771V → A1 Publication
Sequence conflicti283 – 2831L → V1 Publication
Sequence conflicti283 – 2831L → V1 Publication
Sequence conflicti337 – 3371M → I in AAA24453. 1 Publication
Sequence conflicti386 – 3861A → R in CAA30971. 1 Publication
Sequence conflicti494 – 4941N → S1 Publication
Sequence conflicti494 – 4941N → S1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiF65003. XQEC.
RefSeqiNP_416815.1. NC_000913.3.
YP_490554.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75372; AAC75372; b2312.
BAA16158; BAA16158; BAA16158.
GeneIDi12932081.
946794.
KEGGiecj:Y75_p2278.
eco:b2312.
PATRICi32119995. VBIEscCol129921_2407.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi F65003. XQEC.
RefSeqi NP_416815.1. NC_000913.3.
YP_490554.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ECB X-ray 2.70 A/B/C/D 2-505 [» ]
1ECC X-ray 2.40 A/B 2-505 [» ]
1ECF X-ray 2.00 A/B 2-505 [» ]
1ECG X-ray 2.30 A/B 2-505 [» ]
1ECJ X-ray 2.50 A/B/C/D 2-505 [» ]
DisProti DP00578.
ProteinModelPortali P0AG16.
SMRi P0AG16. Positions 2-501.
ModBasei Search...

Protein-protein interaction databases

STRINGi 511145.b2312.

Chemistry

DrugBanki DB00131. Adenosine monophosphate.

Protein family/group databases

MEROPSi C44.001.

Proteomic databases

PaxDbi P0AG16.
PRIDEi P0AG16.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75372 ; AAC75372 ; b2312 .
BAA16158 ; BAA16158 ; BAA16158 .
GeneIDi 12932081.
946794.
KEGGi ecj:Y75_p2278.
eco:b2312.
PATRICi 32119995. VBIEscCol129921_2407.

Organism-specific databases

EchoBASEi EB0787.
EcoGenei EG10794. purF.

Phylogenomic databases

eggNOGi COG0034.
KOi K00764.
OMAi AARVHMG.
OrthoDBi EOG6KT2Q1.
PhylomeDBi P0AG16.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00124 .
BioCyci EcoCyc:PRPPAMIDOTRANS-MONOMER.
ECOL316407:JW2309-MONOMER.
MetaCyc:PRPPAMIDOTRANS-MONOMER.
SABIO-RKi P0AG16.

Miscellaneous databases

EvolutionaryTracei P0AG16.
PROi P0AG16.

Gene expression databases

Genevestigatori P0AG16.

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. "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.
    , 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. 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).

Entry informationi

Entry nameiPUR1_ECOLI
AccessioniPrimary (citable) accession number: P0AG16
Secondary accession number(s): P00496
, P78092, P78191, P78192, Q47255, Q59425
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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