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Reviewed, UniProtKB/Swiss-Prot Q5HH14 (PUR1_STAAC)

Last modified November 3, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: SACOL1079
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length494 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.

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.

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

Propeptide1 – 1010 By similarity
PRO_0000045298
Chain11 – 494484Amidophosphoribosyltransferase
PRO_0000045299

Regions

Domain11 – 231221Glutamine amidotransferase type-2

Sites

Active site111For GATase activity By similarity
Metal binding3561Magnesium By similarity
Metal binding3571Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HH14-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: FED58A366B36AD8A

FASTA49454,397
        10         20         30         40         50         60 
MFNYSGLNEE CGVFGIWNHP EAAQLTYMGL HSLQHRGQEG AGIVVSDQNE LKGERGLGLL 

        70         80         90        100        110        120 
TEAIKDDQME RLKGYQHAIG HVRYATSGNK GIENIQPFLY HFYDMSVGIC HNGNLINAKS 

       130        140        150        160        170        180 
LRQNLEKQGA IFHSSSDTEV IMHLIRRSKA PTFEEALKES LRKVKGGFTF AILTKDALYG 

       190        200        210        220        230        240 
AVDPNAIRPL VVGKMKDGTY ILASETCAID VLGAEFVQDI HAGEYVVIND KGITVKSYTH 

       250        260        270        280        290        300 
HTTTAISAME YIYFARPDST IAGKNVHAVR KASGKKLAQE SPVNADMVIG VPNSSLSAAS 

       310        320        330        340        350        360 
GYAEEIGLPY EMGLVKNQYV ARTFIQPTQE LREQGVRVKL SAVKDIVDGK NIILVDDSIV 

       370        380        390        400        410        420 
RGTTIRRIVK MLKDSGANKV HVRIASPEFM FPSFYGIDVS TTAELISASK SPEEIKDYIG 

       430        440        450        460        470        480 
ADSLAYLSVD GLIESIGLDY DAPYSGLCVE SFTGDYPAGL YDYEANYKAH LSHRQKQYIS 

       490 
KNKHFFDSEG NLNV 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000046 Genomic DNA. Translation: AAW37959.1.
RefSeqYP_185943.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HH14.

Genome annotation databases

GeneID3236103.
GenomeReviewsGene locus SACOL1079 in contig CP000046_GR.
KEGGsac:SACOL1079.
TIGRSACOL1079.

Phylogenomic databases

HOGENOMQ5HH14.
OMAGIPFELG.

Enzyme and pathway databases

BioCycSAUR93062:SACOL1079-MON.

Family and domain databases

InterProIPR005854. Amd_phspho_trans.
IPR000583. GATase_2.
IPR017932. GATase_II.
IPR002375. Pr/py_Pribosyl_transf_CS.
IPR000836. PRibTrfase.
[Graphical view]
PANTHERPTHR11907. Amd_phspho_trans. 1 hit.
PfamPF00310. GATase_2. 1 hit.
PF00156. Pribosyltran. 1 hit.
[Graphical view]
PIRSFPIRSF000485. Amd_phspho_trans. 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_STAAC
AccessionPrimary (citable) accession number: Q5HH14
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: November 3, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents