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P0AG17 (PUR1_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:SF2388, S2523
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

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 By similarity.

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 By similarity
Chain2 – 505504Amidophosphoribosyltransferase
PRO_0000139642

Regions

Domain2 – 236235Glutamine amidotransferase type-2

Sites

Active site21For GATase activity By similarity
Metal binding3671Magnesium By similarity
Metal binding3681Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AG17 [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

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN43901.1.
AE014073 Genomic DNA. Translation: AAP17719.1.
RefSeqNP_708194.1. NC_004337.2.
NP_837909.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0AG17.
SMRP0AG17. Positions 2-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF2388.

Protein family/group databases

MEROPSC44.001.

Proteomic databases

PaxDbP0AG17.
PRIDEP0AG17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN43901; AAN43901; SF2388.
AAP17719; AAP17719; S2523.
GeneID1025528.
1078808.
KEGGsfl:SF2388.
sfx:S2523.
PATRIC18706641. VBIShiFle31049_2796.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0034.
KOK00764.
OMAAARVHMG.
OrthoDBEOG6KT2Q1.

Enzyme and pathway databases

UniPathwayUPA00074; UER00124.

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...

Entry information

Entry namePUR1_SHIFL
AccessionPrimary (citable) accession number: P0AG17
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 66 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

PATHWAY comments

Index of metabolic and biosynthesis pathways