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Q4L582 (PUR9_STAHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:
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:SH1884
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [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_1000018964

Sequences

Sequence LengthMass (Da)Tools
Q4L582 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 03C0512577303EC7

FASTA49254,216
        10         20         30         40         50         60 
MKKAILSVSN KSGIVEFAKS LIKLDYELYS TGGTKGALED ASVPVKSVSE LTQFPEIMDG 

        70         80         90        100        110        120 
RVKTLHPAVH GGILADRDKP EHLEQLSEQH IDLIDMVVVN LYPFQKTVAK PDVTEAEAIE 

       130        140        150        160        170        180 
NIDIGGPTML RAAAKNFKHV TTIVHPADYN EVIERIKEDR LDEDFRKELM IKVFAHTNEY 

       190        200        210        220        230        240 
DHAIVSFFKG DSEQLRYGEN PQQSARFVRT SNSKHTIAGA KQLHGKALSF NNIKDADSAL 

       250        260        270        280        290        300 
SLVKKFKESA AVAVKHMNPC GVGIGDNIET AFKHAYDADN QSIFGGIIAL NRTVTSDLAE 

       310        320        330        340        350        360 
TLHAIFLEVV IAPRFTDEAL DILTKKKNIR LLEIDMTIDN REEEFVSVSG GYLVQDKDNF 

       370        380        390        400        410        420 
EVAKEDMKVV TDKAPTDDQW DAMLLGWKVI PSVKSNAVIL SNTKQTVGIG AGQMNRVGSA 

       430        440        450        460        470        480 
KIALERAIEI NDNVALVSDG FFPMDDTVEL AAQHGIKAII QPGGSIKDQD SIDMANKYGI 

       490 
AMVTTGMRHF KH 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC1435.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006716 Genomic DNA. Translation: BAE05193.1.
RefSeqYP_253799.1. NC_007168.1.

3D structure databases

ProteinModelPortalQ4L582.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279808.SH1884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE05193; BAE05193; SH1884.
GeneID3481920.
KEGGsha:SH1884.
PATRIC19619875. VBIStaHae67511_1860.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSHAE279808:GJX7-1939-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_STAHJ
AccessionPrimary (citable) accession number: Q4L582
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 2, 2005
Last modified: May 14, 2014
This is version 65 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