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Q9PNY0 (PURL_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoribosylformylglycinamidine synthase 2

EC=6.3.5.3
Alternative name(s):
Phosphoribosylformylglycinamidine synthase II
Short name=FGAM synthase II
Gene names
Name:purL
Ordered Locus Names:Cj0955
OrganismCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]
Taxonomic identifier192222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length728 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. HAMAP-Rule MF_00420

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. HAMAP-Rule MF_00420

Subunit structure

Heterodimer of two subunits, PurQ and PurL By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the FGAMS family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

phosphoribosylformylglycinamidine synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

flaGQ0PAW91EBI-1192636,EBI-1191365

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 728728Phosphoribosylformylglycinamidine synthase 2 HAMAP-Rule MF_00420
PRO_0000100446

Regions

Nucleotide binding99 – 11012ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q9PNY0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A7CAD4432EDF678A

FASTA72879,310
        10         20         30         40         50         60 
MDKETIKAHK ISDEEYAQIL EILGREPNLL ELGVISAMWS EHCSYKSSKK YLNGFPTKAP 

        70         80         90        100        110        120 
WVIQGPGENA GVIDIGQGMA AVFKVESHNH PSFIEPFAGA ATGVGGILRD VFTMGARVVA 

       130        140        150        160        170        180 
GLNSLKFGDI HDEKCGKHQK YLVKGVVNGI SHYGNCMGVP TIGGECAFDE CFNGNILVNA 

       190        200        210        220        230        240 
FALGVCKSED IFYAKAEGVG NPVIYVGSKT GRDGLGGAVM ASDSFNEESK SLRPTVQIGD 

       250        260        270        280        290        300 
PFSEKLLMEA CLELFKTDYI VGIQDMGAAG LTSSSFEMAG RSGSGMKLYL DKTPMRESGM 

       310        320        330        340        350        360 
TPYELMLSES QERMLICAKK GYEDKVIEIF KKWDLDAVVM GEVTNTGKME LFWHDELVGL 

       370        380        390        400        410        420 
IPIEPLSEKA PILSRPTSEP KYLSEIKNYK FELKSSVQEL FIQMLQNENI NNKAFIYDQF 

       430        440        450        460        470        480 
DSSVQTNTIK ADGRLGASVI RIKENGASVA MAIECNSRLN YVNSKIGAAL AVASAGRKVA 

       490        500        510        520        530        540 
CTGAKPLAIS DCLNYGNPQN PEVMWQFAQG CEGIKEACKE LNTPVVSGNV SLYNETEGVS 

       550        560        570        580        590        600 
IYPSPTIVSV GVLEDANKTL KASFEKENLS VYLLGESLGE FSGSMVMKIQ DKKVSGSLKE 

       610        620        630        640        650        660 
LDYKAELALW DLLYKANQNS LLECANSVGI GGIAMTLAKM FAISSVGANL TSDFDDEKMI 

       670        680        690        700        710        720 
FDESASRAII GLSKENEEAF LNLAKEFGVK AYKLGVSTSQ KHFKLDSIEL SKAELDKLYF 


ESFKEQIQ 

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References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL35075.1.
PIRB81370.
RefSeqYP_002344353.1. NC_002163.1.

3D structure databases

ProteinModelPortalQ9PNY0.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PNY0. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL35075; CAL35075; Cj0955c.
GeneID904957.
KEGGcje:Cj0955c.
PATRIC20058870. VBICamJej33762_0939.

Phylogenomic databases

eggNOGCOG0046.
HOGENOMHOG000238227.
KOK01952.
OMAWSEHCCY.
ProtClustDBPRK01213.

Enzyme and pathway databases

BioCycCJEJ192222:GJTS-930-MONOMER.
UniPathwayUPA00074; UER00128.

Family and domain databases

HAMAPMF_00420. PurL_2.
InterProIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR010074. PRibForGlyAmidine_synth_II.
IPR016188. PurM_N-like.
[Graphical view]
PfamPF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMSSF56042. AIR_synth_C. 2 hits.
SSF55326. PurM_N-like. 2 hits.
TIGRFAMsTIGR01736. FGAM_synth_II. 1 hit.
ProtoNetSearch...

Entry information

Entry namePURL_CAMJE
AccessionPrimary (citable) accession number: Q9PNY0
Secondary accession number(s): Q0P9U4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families