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Q5H5H7 (PUR9_XANOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:XOO0539
OrganismXanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) [Complete proteome] [HAMAP]
Taxonomic identifier291331 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length527 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 – 527527Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018989

Sequences

Sequence LengthMass (Da)Tools
Q5H5H7 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 0CD3FA8808630121

FASTA52755,747
        10         20         30         40         50         60 
MASDFLPVRR ALLSVSDKTG LIDLARALVA RNVELLSTGG TAKAIREAGL PVKDVAELTG 

        70         80         90        100        110        120 
FPEMMDGRVK TLHPLVHGGL LGRAGIDEAV MAEHGIAPID LLVLNLYPFE SVTVKTDCTL 

       130        140        150        160        170        180 
ADAVENIDIG GPAMLRSAAK NFARVAVATD PAQYADLLAE LEANNGQLSA AKRFALSVAA 

       190        200        210        220        230        240 
FNRVAQYDAA ISNYLSAVAD SAETVPTRNP FPAQINSNFV KVMDLRYGEN PHQSGAFYRD 

       250        260        270        280        290        300 
LYPVPGTLAT FQQLQGKELS YNNLADADAA WECVRQFDAP ACVIVKHANP CGVAVGAGCG 

       310        320        330        340        350        360 
DAYELAYATD PTSAFGGILA FNKTLDAATA KAILDRQFVE VLIAPDYDAG ALDYATKKAN 

       370        380        390        400        410        420 
VRVLKIPHGN GLNNYDTKRI GSGLLMQSAD NRGMSLGELS VVTQRAPSEA ELGDLLFAWR 

       430        440        450        460        470        480 
VAKYVKSNAI VYAKDSRTIG VGAGQMSRVV SAKIAALKAE EAKLTVVGSV MASDAFFPFR 

       490        500        510        520 
DGIDAAASAG IQAVIQPGGS MRDGEVIAAA DEHGIAMVFT GVRHFRH 

« Hide

References

[1]"The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice."
Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., Go S.-J.
Nucleic Acids Res. 33:577-586(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KACC10331 / KXO85.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013598 Genomic DNA. Translation: AAW73793.1.
RefSeqYP_199178.1. NC_006834.1.

3D structure databases

ProteinModelPortalQ5H5H7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING291331.XOO0539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW73793; AAW73793; XOO0539.
GeneID3263700.
KEGGxoo:XOO0539.
PATRIC24099905. VBIXanOry111333_0604.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycXORY291331:GJBV-486-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_XANOR
AccessionPrimary (citable) accession number: Q5H5H7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2005
Last modified: May 14, 2014
This is version 61 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