Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A6U0N9 (PUR5_STAA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:
Phosphoribosylformylglycinamidine cyclo-ligase

EC=6.3.3.1
Alternative name(s):
AIR synthase
AIRS
Phosphoribosyl-aminoimidazole synthetase
Gene names
Name:purM
Ordered Locus Names:SaurJH1_1153
OrganismStaphylococcus aureus (strain JH1) [Complete proteome] [HAMAP]
Taxonomic identifier359787 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. HAMAP-Rule MF_00741

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 2/2. HAMAP-Rule MF_00741

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00741.

Sequence similarities

Belongs to the AIR synthase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete 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: UniProtKB-KW

phosphoribosylformylglycinamidine cyclo-ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_1000083467

Sequences

Sequence LengthMass (Da)Tools
A6U0N9 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 64574C39FB36508D

FASTA34236,989
        10         20         30         40         50         60 
MSKAYEQSGV NIHAGYEAVE RMSSHVKRTM RKEVIGGLGG FGATFDLSQL NMTAPVLVSG 

        70         80         90        100        110        120 
TDGVGTKLKL AIDYGKHDSI GIDAVAMCVN DILTTGAEPL YFLDYIATNK VVPEVIEQIV 

       130        140        150        160        170        180 
KGISDACVET NTALIGGETA EMGEMYHEGE YDVAGFAVGA VEKDDYVDGS EVKEGQVVIG 

       190        200        210        220        230        240 
LASSGIHSNG YSLVRKLINE SGIDLASNFD NRPFIDVFLE PTKLYVKPVL ALKKEVSIKA 

       250        260        270        280        290        300 
MNHITGGGFY ENIPRALPAG YAARIDTTSF PTPKIFDWLQ QQGNIDTNEM YNIFNMGIGY 

       310        320        330        340 
TVIVDEKDAS RALKILAEQN VEAYQIGHIV KNESTAIELL GV 

« Hide

References

[1]"Complete sequence of chromosome of Staphylococcus aureus subsp. aureus JH1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000736 Genomic DNA. Translation: ABR52007.1.
RefSeqYP_001316294.1. NC_009632.1.

3D structure databases

ProteinModelPortalA6U0N9.
SMRA6U0N9. Positions 17-331.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359787.SaurJH1_1153.

Proteomic databases

PRIDEA6U0N9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR52007; ABR52007; SaurJH1_1153.
GeneID5316419.
KEGGsah:SaurJH1_1153.
PATRIC19534147. VBIStaAur98826_1184.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAVIGKIEH.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycSAUR359787:GCG4-1179-MONOMER.
UniPathwayUPA00074; UER00129.

Family and domain databases

Gene3D3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPMF_00741_B. AIRS_B.
InterProIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMSSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsTIGR00878. purM. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR5_STAA2
AccessionPrimary (citable) accession number: A6U0N9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 48 of the entry and version 1 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