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A6QFT1 (PUR9_STAAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:NWMN_0941
OrganismStaphylococcus aureus (strain Newman) [Complete proteome] [HAMAP]
Taxonomic identifier426430 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length492 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 – 492492Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000071452

Sequences

Sequence LengthMass (Da)Tools
A6QFT1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 7D1B3ADA1C6C4FCE

FASTA49254,305
        10         20         30         40         50         60 
MKKAILSVSN KTGIVEFAKA LTQLNYELYS TGGTKRILDE ANVPVRSVSD LTHFPEIMDG 

        70         80         90        100        110        120 
RVKTLHPAVH GGILADRNKP QHLNELSEQH IDLIDMVVVN LYPFQQTVAN PDVTMDEAIE 

       130        140        150        160        170        180 
NIDIGGPTML RAAAKNYKHV TTIVHPADYQ EVLTLLRNDS LDESYRQSLM IKVFEHTAEY 

       190        200        210        220        230        240 
DEAIVRFFKG DKETLRYGEN PQQSAYFVRT SNAKHTIAGA KQLHGKQLSY NNIKDADATL 

       250        260        270        280        290        300 
ALVKKFDTPA TVAVKHMNPC GVGIGDTIEQ AFQHAYEADS QSIFGGIVAL NRAVTPELAE 

       310        320        330        340        350        360 
QLHSIFLEVI IAPKFTDEAL DILKQKKNVR LLEIDMTIDS NEEEFVSVSG GYLVQDKDNY 

       370        380        390        400        410        420 
VVPKEEMKVV TEVAPTDEQW EAMLLGWKVV PSVKSNAIIL SNNKQTVGIG AGQMNRVGAA 

       430        440        450        460        470        480 
KIALERAIEI NDHVALVSDG FFPMGDTVEL AAQHGIKAII QPGGSIKDQD SIDMANKHGI 

       490 
AMVVTGTRHF KH 

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References

[1]"Genome sequence of Staphylococcus aureus strain Newman and comparative analysis of staphylococcal genomes: polymorphism and evolution of two major pathogenicity islands."
Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.
J. Bacteriol. 190:300-310(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Newman.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009351 Genomic DNA. Translation: BAF67213.1.
RefSeqYP_001331975.1. NC_009641.1.

3D structure databases

ProteinModelPortalA6QFT1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING426430.NWMN_0941.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF67213; BAF67213; NWMN_0941.
GeneID5332310.
KEGGsae:NWMN_0941.
PATRIC19585379. VBIStaAur133992_1016.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAGIGQADN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSAUR426430:GIXC-963-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_STAAE
AccessionPrimary (citable) accession number: A6QFT1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 51 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