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P0DD60 (PUR9_STRP3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 19. 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:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:SpyM3_0024
OrganismStreptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315) [Complete proteome] [HAMAP]
Taxonomic identifier198466 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192136

Sequences

Sequence LengthMass (Da)Tools
P0DD60 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: 58C11340BBB97049

FASTA51556,217
        10         20         30         40         50         60 
MTKRALISVS DKSGIVDFAK ELKNLGWDII STGGTKVALD NAGVETIAID DVTGFPEMMD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLARRDA DSHLQAAKDN NIELIDLVVV NLYPFKETIL RPDITYDLAV 

       130        140        150        160        170        180 
ENIDIGGPSM LRSAAKNHAS VTVVVDPADY ATVLGELADA GQTTFETRQR LAAKVFRHTA 

       190        200        210        220        230        240 
AYDALIAEYF TTQVGEAKPE KLTITYDLKQ AMRYGENPQQ DADFYQKALP IDYSIASAKQ 

       250        260        270        280        290        300 
LNGKELSFNN IRDADAAIRI IRDFKDRPTV VVLKHMNPCG IGQADDIETA WDYAYEADPV 

       310        320        330        340        350        360 
SIFGGIVVLN REVDAATAKK MHPIFLEIII APSYSEEALA ILTNKKKNLR ILELPFDAQA 

       370        380        390        400        410        420 
ASEVEAEYTG VVGGLLVQNQ DVVAENPSDW QVVTDRQPTE QEATALEFAW KAIKYVKSNG 

       430        440        450        460        470        480 
IIITNDHMTL GLGAGQTNRV GSVKIAIEQA KDHLDGAVLA SDAFFPFADN IEEIAAAGIK 

       490        500        510 
AIIQPGGSVR DQDSIDAANK HGLTMIFTGV RHFRH 

« 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: AAM78631.1.
RefSeqNP_663828.1. NC_004070.1.

3D structure databases

ProteinModelPortalP0DD60.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM78631; AAM78631; SpyM3_0024.
GeneID1008338.
KEGGspg:SpyM3_0024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSPYO198466:GJDL-58-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_STRP3
AccessionPrimary (citable) accession number: P0DD60
Secondary accession number(s): Q8K8Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 27, 2011
Last modified: February 19, 2014
This is version 19 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