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

P0DD62 (PUR5_STRP3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 22. 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:SpyM3_0022
OrganismStreptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315) [Complete proteome] [HAMAP]
Taxonomic identifier198466 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length340 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 – 340340Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000148262

Sequences

Sequence LengthMass (Da)Tools
P0DD62 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: 4E6B4A75CB1BB1A8

FASTA34036,500
        10         20         30         40         50         60 
MSEKNAYAKS GVDVEAGYEV VERIKKHVAR TERAGVMGVL GGFGGMFDLS KTGVKEPVLV 

        70         80         90        100        110        120 
SGTDGVGTKL MLAIKYDKHD TIGQDCVAMC VNDIIAAGAE PLYFLDYIAT GKNNPVKLEE 

       130        140        150        160        170        180 
VVSGVAEGCV QAGVALIGGE TAEMPGMYGE DDYDLAGFAV GVAEKSQIID GSKVKEGDIL 

       190        200        210        220        230        240 
LGLASSGIHS NGYSLVRRVF ADYTGKELLP ELEGKQLKDV LLEPTRIYVK AALPLIKEEL 

       250        260        270        280        290        300 
VNGIGHITGG GFIENVPRMF ADDLAAEIDE DKVPVLPIFK ALEKYGDIKH EEMFEIFNMG 

       310        320        330        340 
VGLMLAVSPE NVNRVKELLD EPVYEIGRII KKADASVVIK 

« Hide

References

[1]"Genome sequence of a serotype M3 strain of group A Streptococcus: phage-encoded toxins, the high-virulence phenotype, and clone emergence."
Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D., Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S., Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-595 / MGAS315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014074 Genomic DNA. Translation: AAM78629.1.
RefSeqNP_663826.1. NC_004070.1.

3D structure databases

ProteinModelPortalP0DD62.
SMRP0DD62. Positions 15-333.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM78629; AAM78629; SpyM3_0022.
GeneID1008336.
KEGGspg:SpyM3_0022.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000229090.
KOK01933.
OMAVIGKIEH.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycSPYO198466:GJDL-56-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_STRP3
AccessionPrimary (citable) accession number: P0DD62
Secondary accession number(s): Q8K8Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 27, 2011
Last modified: May 14, 2014
This is version 22 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