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C0QXU6 (PUR9_BRAHW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:BHWA1_02509
OrganismBrachyspira hyodysenteriae (strain ATCC 49526 / WA1) [Complete proteome] [HAMAP]
Taxonomic identifier565034 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesBrachyspiraceaeBrachyspira

Protein attributes

Sequence length509 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 – 509509Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122948

Sequences

Sequence LengthMass (Da)Tools
C0QXU6 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 8F7D8B064BA4398F

FASTA50957,057
        10         20         30         40         50         60 
MIKRALISVF YKDGILDFAK FLTSKNVEIV STGGTYKYLK ENNIPVIEVS EVTGAKEMLD 

        70         80         90        100        110        120 
GRVKTLDPKI HGAILAIRDN PTHMETIKER GITPIDMVIV NLYPFFEKVQ DDNLKFEEKI 

       130        140        150        160        170        180 
EFIDIGGPTM LRSAAKSFKD VVVISDVKDY DLVKSEMEKG EVSFETKKYL ASKVFNLTSA 

       190        200        210        220        230        240 
YDAAVSEFMF NSLESKEDKK LNYLNMSYAL QEELRYGENP HQGASYYVST TDKGSMKDFE 

       250        260        270        280        290        300 
QLNGKELSFN NIRDMDIALK IVLEFDESKK EYACSAIKHS TPCGAALGSS VLEAYNRTYE 

       310        320        330        340        350        360 
CDPTSIFGGI VAFNSTVDEA TAKELIKIFL EIVIAKDFTP EALEVLKTKK NLRVIKYKTN 

       370        380        390        400        410        420 
TNDKINLVKV DGGLLVQDED TTLIEDYKVV TEKKPTEEEM KNLIFGIKVV KYAKSNAIVV 

       430        440        450        460        470        480 
IKDFMAKGIG SGQTNRIWAC EDALERAGDG VVMASDAFFP FRDVVDACAK YNIKAIIQPG 

       490        500 
GSMRDQESID ACNEHGIAMI FTGIRHFKH 

« Hide

References

[1]"Genome sequence of the pathogenic intestinal spirochete Brachyspira hyodysenteriae reveals adaptations to its lifestyle in the porcine large intestine."
Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P., Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A., Barrero R., Phillips N.D., Hampson D.J.
PLoS ONE 4:E4641-E4641(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49526 / WA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001357 Genomic DNA. Translation: ACN84962.1.
RefSeqYP_002722666.1. NC_012225.1.

3D structure databases

ProteinModelPortalC0QXU6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING565034.BHWA1_02509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACN84962; ACN84962; BHWA1_02509.
GeneID7667597.
KEGGbhy:BHWA1_02509.
PATRIC21183062. VBIBraHyo62857_2447.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAIRASSKN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBHYO565034:GJI7-2494-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_BRAHW
AccessionPrimary (citable) accession number: C0QXU6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: May 14, 2014
This is version 42 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