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Q3YZ53 (PUR5_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:SSON_2581
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Initiator methionine11Removed By similarity
Chain2 – 345344Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000258404

Sequences

Sequence LengthMass (Da)Tools
Q3YZ53 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2DBC0975E81815D7

FASTA34536,873
        10         20         30         40         50         60 
MTDKTSLSYK DAGVDIDAGN ALVGRIKGVV KKTRRPEVMG GLGGFGALCA LPQKYREPVL 

        70         80         90        100        110        120 
VSGTDGVGTK LRLAMDLKRH DTIGIDLVAM CVNDLVVQGA EPLFFLDYYA TGKLDVDTAS 

       130        140        150        160        170        180 
AVISGIAEGC LQSGCSLVGG ETAEMPGMYH GEDYDVAGFC VGVVEKSEII DGSKVSDGDV 

       190        200        210        220        230        240 
LIALGSSGPH SNGYSLVRKI LEVSGCDPQT TELDGKPLAD HLLAPTRIYV KSVLELIEKV 

       250        260        270        280        290        300 
DVHAIAHLTG GGFWENIPRV LPDNTQAVID ESSWQWPEVF NWLQTAGNVE RHEMYRTFNC 

       310        320        330        340 
GVGMIIALPA PEVDKALALL NANGENAWKI GIIKASDSEQ RVVIE 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ss046.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000038 Genomic DNA. Translation: AAZ89209.1.
RefSeqYP_311444.1. NC_007384.1.

3D structure databases

ProteinModelPortalQ3YZ53.
SMRQ3YZ53. Positions 5-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300269.SSON_2581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ89209; AAZ89209; SSON_2581.
GeneID3668036.
KEGGssn:SSON_2581.
PATRIC18739543. VBIShiSon107113_3096.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229091.
KOK01933.
OMAIDMIAMN.
OrthoDBEOG61CM1V.
ProtClustDBPRK05385.

Enzyme and pathway databases

BioCycSSON300269:GJJF-2576-MONOMER.
UniPathwayUPA00074; UER00129.

Family and domain databases

Gene3D3.90.650.10. 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_SHISS
AccessionPrimary (citable) accession number: Q3YZ53
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 65 of the entry and version 3 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