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Q3BY85 (PUR9_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:XCV0547
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [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_1000018986

Sequences

Sequence LengthMass (Da)Tools
Q3BY85 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: CE12F763E04E098E

FASTA52755,788
        10         20         30         40         50         60 
MASDFLPVRR ALLSVSDKTG LIDLARALVA RNVELLSTGG TAKAIREAGL PVKDVAELTG 

        70         80         90        100        110        120 
FPEMMDGRVK TLHPLVHGGL LGRAGVDEAV MAEHGIVPID LLVLNLYPFE SVTVKADCTL 

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

       190        200        210        220        230        240 
FNRVAQYDAA ISNYLSAVAD SSEAVPTRSP 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 VLIAPDYEAG ALEYATRKAN 

       370        380        390        400        410        420 
VRVLKIPHGN GLNNYDTKRI GSGLLMQSAD NRSMSLGELS VVTQRAPNEA ELGDLLFAWR 

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

       490        500        510        520 
DGIDAAAAAG IKAVIQPGGS MRDGEVIAAA DEHGIAMVFT GVRHFRH 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ22178.1.
RefSeqYP_362278.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BY85.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV0547.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ22178; CAJ22178; XCV0547.
GeneID3732953.
KEGGxcv:XCV0547.
PATRIC24090442. VBIXanCam71633_0733.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycXCAM316273:GJF8-557-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_XANC5
AccessionPrimary (citable) accession number: Q3BY85
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 60 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