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Q5WJ82 (PUR9_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:ABC1034
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length511 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 – 511511Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018843

Sequences

Sequence LengthMass (Da)Tools
Q5WJ82 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 6A59A64216026DF9

FASTA51154,665
        10         20         30         40         50         60 
MTKRALVSVS NKTGLIPFVK GLAEAGVEIL STGGGTKRAL EEAGIAVVNV SDVTGFPEIL 

        70         80         90        100        110        120 
DGRVKTLHPN IHGGLLAMRT NDEHIKQIEE LGIEPIDYVV VNLYPFAETI ANPDASFADA 

       130        140        150        160        170        180 
IENIDIGGPS MLRSAAKNHA DVTVVVDPAD YDAVLASLDA SKEEQLALRQ KLAAKVFRHT 

       190        200        210        220        230        240 
AAYDAMIGSY LTDAVGEENP ESLTVTYTHK QTLRYGENPH QKAAFYESRT SSPSSIAQAK 

       250        260        270        280        290        300 
QLHGKELSYN NINDANAALE IVKEFSEPAA VAVKHMNPCG VGTGATVGEA YTRAYEADPK 

       310        320        330        340        350        360 
SIFGGIVALN REVDRATAEK MAAIFLEVIL APSFSEEAKA ILQQKKNIRL LEVAVTKGEL 

       370        380        390        400        410        420 
EKKLASVHGG LLIQEEDHLG FDDGDIRIPT KREPTEEEWT ALKLGWKVVK HVKSNAIVLT 

       430        440        450        460        470        480 
NGEMTVGIGA GQMNRVGAAA IAIEQAGERA QGAALASDAF FPYGDTVEAA AKAGITAIIQ 

       490        500        510 
PGGSVRDNES IEKADEYGIA MVFTGVRHFK H 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD63573.1.
RefSeqYP_174534.1. NC_006582.1.

3D structure databases

ProteinModelPortalQ5WJ82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING66692.ABC1034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD63573; BAD63573; ABC1034.
GeneID3202811.
KEGGbcl:ABC1034.
PATRIC18921434. VBIBacCla58185_1105.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBCLA66692:GHMP-1081-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_BACSK
AccessionPrimary (citable) accession number: Q5WJ82
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 64 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