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B0U7A0 (PUR9_XYLFM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Xfasm12_0998
OrganismXylella fastidiosa (strain M12) [Complete proteome] [HAMAP]
Taxonomic identifier405440 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length530 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 – 530530Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096110

Sequences

Sequence LengthMass (Da)Tools
B0U7A0 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: D2C73AE7348AB03E

FASTA53057,304
        10         20         30         40         50         60 
MASDFLPVHR ALLSVSDKTG LVELARVLLA YNIELLSTGG TATIIREAGL PVQDVADLTG 

        70         80         90        100        110        120 
FPEMMDGRVK TLHPVVHGGL LGRAGIDDAV MAKHGIAPID LLILNLYPFE QITAKKDCTL 

       130        140        150        160        170        180 
ADAVDTIDIG GPAMLRSAAK NFARVAVATS PDQYPDLLAE LQEHHGQLSA EKRFALAVAA 

       190        200        210        220        230        240 
FNHVAQYDAA ISNYLSSVSD MHTTLPLRHE FPAQLNNTFV KMTELRYGEN PHQTGAFYRD 

       250        260        270        280        290        300 
VHPQPGTLAT FQQLQGKRLS YNNLVDADAA WECVRQFEAP ACVIVKHANP CGVAVGMACS 

       310        320        330        340        350        360 
DAYEAAYATD PTSAFGGIIA FNRTLDAVTM KSILDRQFVE VFIAPYYDAD ALAYAAKKAN 

       370        380        390        400        410        420 
VRVLRIPSSA AMKATNQYDF KRIGSGLLVQ SADTMHIHSD VLRTVTTLAP TDKQRRDLMF 

       430        440        450        460        470        480 
AWRVVKYVKS NAIVYAKDNR TIGIGAGQMS RVYSARIAGI KAADAHLAVT GSVMASDAFF 

       490        500        510        520        530 
PFRDGIDAAA ATGIKAVIQP GGSMRDNEVI AAADEHGIAM LFTGIRHFRH 

« Hide

References

[1]"Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) causing almond leaf scorch disease in California."
Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.
J. Bacteriol. 192:4534-4534(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000941 Genomic DNA. Translation: ACA11966.1.
RefSeqYP_001775596.1. NC_010513.1.

3D structure databases

ProteinModelPortalB0U7A0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405440.Xfasm12_0998.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA11966; ACA11966; Xfasm12_0998.
GeneID6121482.
KEGGxfm:Xfasm12_0998.
PATRIC24138453. VBIXylFas124301_1182.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycXFAS405440:GH0D-1026-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_XYLFM
AccessionPrimary (citable) accession number: B0U7A0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 46 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