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Q8NX88 (PUR9_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:MW0956
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [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.

Sequence caution

The sequence BAB94821.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 492492Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192127

Sequences

Sequence LengthMass (Da)Tools
Q8NX88 [UniParc].

Last modified December 21, 2004. Version 2.
Checksum: 39C1B60098E53467

FASTA49254,348
        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 EVLTRLRNDS 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 

« Hide

References

[1]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000033 Genomic DNA. Translation: BAB94821.1. Different initiation.
RefSeqNP_645773.1. NC_003923.1.

3D structure databases

ProteinModelPortalQ8NX88.
SMRQ8NX88. Positions 1-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196620.MW0956.

Proteomic databases

PRIDEQ8NX88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB94821; BAB94821; BAB94821.
GeneID1003068.
KEGGsam:MW0956.
PATRIC19568486. VBIStaAur44266_1002.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAGIGQADN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSAUR196620:GJ9Z-980-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_STAAW
AccessionPrimary (citable) accession number: Q8NX88
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: December 21, 2004
Last modified: May 14, 2014
This is version 74 of the entry and version 2 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