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P0AG16

- PUR1_ECOLI

UniProt

P0AG16 - PUR1_ECOLI

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Protein

Amidophosphoribosyltransferase

Gene

purF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. Can also use NH3 in place of glutamine.1 Publication

Catalytic activityi

5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O.1 PublicationUniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg(2+) ion per subunit.UniRule annotation

Enzyme regulationi

Inhibited by iodoacetamide and by the glutamine analogs chloroketone and DON.1 Publication

Kineticsi

  1. KM=0.067 mM for phosphoribosylpyrophosphate1 Publication
  2. KM=1.7 mM for glutamine1 Publication
  3. KM=8.8 mM for NH31 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21Nucleophile1 PublicationUniRule annotation
Metal bindingi305 – 3051MagnesiumUniRule annotation
Metal bindingi367 – 3671MagnesiumUniRule annotation
Metal bindingi368 – 3681MagnesiumUniRule annotation

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

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-RKP0AG16.
UniPathwayiUPA00074; UER00124.

Protein family/group databases

MEROPSiC44.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Amidophosphoribosyltransferase1 PublicationUniRule annotation (EC:2.4.2.141 PublicationUniRule annotation)
Short name:
ATaseUniRule annotation
Alternative name(s):
Glutamine phosphoribosylpyrophosphate amidotransferase1 PublicationUniRule annotation
Short name:
GPATase1 PublicationUniRule annotation
Gene namesi
Name:purFUniRule annotation
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...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 505504AmidophosphoribosyltransferasePRO_0000139638Add
BLAST

Proteomic databases

PaxDbiP0AG16.
PRIDEiP0AG16.

Expressioni

Gene expression databases

GenevestigatoriP0AG16.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi511145.b2312.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi14 – 2310Combined sources
Helixi24 – 274Combined sources
Beta strandi30 – 378Combined sources
Beta strandi43 – 508Combined sources
Helixi52 – 554Combined sources
Helixi58 – 636Combined sources
Beta strandi66 – 749Combined sources
Beta strandi78 – 803Combined sources
Helixi83 – 853Combined sources
Beta strandi89 – 913Combined sources
Beta strandi93 – 953Combined sources
Beta strandi97 – 1059Combined sources
Helixi108 – 11912Combined sources
Helixi128 – 14013Combined sources
Beta strandi145 – 1473Combined sources
Helixi150 – 16314Combined sources
Beta strandi166 – 1749Combined sources
Turni175 – 1773Combined sources
Beta strandi178 – 1836Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi203 – 2108Combined sources
Helixi212 – 2176Combined sources
Beta strandi220 – 2245Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi239 – 2435Combined sources
Beta strandi245 – 2473Combined sources
Helixi254 – 2585Combined sources
Helixi272 – 29019Combined sources
Turni291 – 2933Combined sources
Beta strandi298 – 3014Combined sources
Turni303 – 3064Combined sources
Helixi307 – 31711Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi338 – 3403Combined sources
Turni348 – 3503Combined sources
Beta strandi351 – 3533Combined sources
Helixi355 – 3573Combined sources
Turni358 – 3603Combined sources
Beta strandi363 – 3686Combined sources
Beta strandi371 – 3733Combined sources
Helixi374 – 38512Combined sources
Beta strandi389 – 3979Combined sources
Beta strandi406 – 4105Combined sources
Helixi413 – 4153Combined sources
Turni417 – 4204Combined sources
Helixi423 – 4308Combined sources
Beta strandi433 – 4375Combined sources
Helixi440 – 4489Combined sources
Helixi460 – 4634Combined sources
Helixi473 – 49220Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG16.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 236235Glutamine 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.
InParanoidiP0AG16.
KOiK00764.
OMAiAARVHMG.
OrthoDBiEOG6KT2Q1.
PhylomeDBiP0AG16.

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.

P0AG16-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG
60 70 80 90 100
LVSDVFEARH MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA
110 120 130 140 150
HNGNLTNAHE LRKKLFEEKR RHINTTSDSE ILLNIFASEL DNFRHYPLEA
160 170 180 190 200
DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV AFRDPNGIRP LVLGKRDIDE
210 220 230 240 250
NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF TRQCADNPVS
260 270 280 290 300
NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI
310 320 330 340 350
PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK
360 370 380 390 400
LNANRAEFRD KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI
410 420 430 440 450
RFPNVYGIDM PSATELIAHG REVDEIRQII GADGLIFQDL NDLIDAVRAE
460 470 480 490 500
NPDIQQFECS VFNGVYVTKD VDQGYLDFLD TLRNDDAKAV QRQNEVENLE

MHNEG
Length:505
Mass (Da):56,488
Last modified:January 23, 2007 - v2
Checksum:i50FD08EA85E6F2A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462LR → SL(PubMed:6443594)Curated
Sequence conflicti45 – 462LR → SL(PubMed:6277938)Curated
Sequence conflicti50 – 501G → A(PubMed:6443594)Curated
Sequence conflicti50 – 501G → A(PubMed:6277938)Curated
Sequence conflicti213 – 23018ALDTL…APGEA → GSIRWALISCVTSRRAR(PubMed:6443594)CuratedAdd
BLAST
Sequence conflicti213 – 23018ALDTL…APGEA → GSIRWALISCVTSRRAR(PubMed:6277938)CuratedAdd
BLAST
Sequence conflicti277 – 2771V → A(PubMed:6443594)Curated
Sequence conflicti277 – 2771V → A(PubMed:6277938)Curated
Sequence conflicti283 – 2831L → V(PubMed:6443594)Curated
Sequence conflicti283 – 2831L → V(PubMed:6277938)Curated
Sequence conflicti337 – 3371M → I in AAA24453. (PubMed:6443594)Curated
Sequence conflicti386 – 3861A → R in CAA30971. (PubMed:3047685)Curated
Sequence conflicti494 – 4941N → S(PubMed:6443594)Curated
Sequence conflicti494 – 4941N → S(PubMed:6277938)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 511145.b2312.

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.
InParanoidi P0AG16.
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-RK 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.
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. "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, ACTIVE SITE.
  9. "Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties."
    Messenger L.J., Zalkin H.
    J. Biol. Chem. 254:3382-3392(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
  10. "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.
  11. "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).
  12. "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), SUBUNIT.

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: November 26, 2014
This is version 88 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