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B3DRY6 (PUR9_BIFLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:BLD_0459
OrganismBifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]
Taxonomic identifier205913 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length545 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 – 545545Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096041

Sequences

Sequence LengthMass (Da)Tools
B3DRY6 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: AC98E086445D7312

FASTA54558,402
        10         20         30         40         50         60 
MTNTNRPIRR ALVSVFHKEG IEVLAEAFVK AGTEVVSTGS TAKKLAELGV KVTEVSDVTG 

        70         80         90        100        110        120 
FPECLDGRVK TLHPYIHAGI LADMTNPEHA KQLEEFGIKP FDLVVVNLYP FADTVRSGAN 

       130        140        150        160        170        180 
EADTIEKIDI GGPSMVRGAA KNHATVAIVT DPADYALVAS RVADGTGFSL DERKWLAAKA 

       190        200        210        220        230        240 
FAHTAAYDAT INEWTAKHWP KPASLDAVEV DKDDQGTEVD SAKFPAQFTR TWDRAHTLRY 

       250        260        270        280        290        300 
GENSHQQAAL YIDPLNQTGF AHAEQLGGKP MSYNNYVDAD AAWRTVWDMA PAIAVAVVKH 

       310        320        330        340        350        360 
NNPCGLAIGA TAAEAHKKAH ACDPMSAYGG VIACNSKVTL EMAESVRPIF TEVIVAPDYE 

       370        380        390        400        410        420 
PAALELLQTK KKNLRILKVA EPPKGHEAIR QIDGGLLVQD TDLINAVGDD PDAWKLVAGE 

       430        440        450        460        470        480 
AADADTLKDL VFAWRAIRCV KSNAILLAHD QATVGIGMGQ VNRVDSCHLA VERANTLADG 

       490        500        510        520        530        540 
ADRATGAVAA SDAFFPFADG AQVLIDAGVK AIVQPGGSIR DEEVIEAAKK AGVTMYLTGT 


RHFFH 

« Hide

References

[1]"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth."
Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J.
BMC Genomics 9:247-247(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DJO10A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000605 Genomic DNA. Translation: ACD97905.1.
RefSeqYP_001954403.1. NC_010816.1.

3D structure databases

ProteinModelPortalB3DRY6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205913.BLD_0459.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD97905; ACD97905; BLD_0459.
GeneID6363931.
KEGGblj:BLD_0459.
PATRIC21113852. VBIBifLon134794_0475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBLON205913:GJB4-477-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_BIFLD
AccessionPrimary (citable) accession number: B3DRY6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: May 14, 2014
This is version 43 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