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Q8G6B1 (PUR9_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 72. 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:BL0735
OrganismBifidobacterium longum (strain NCC 2705) [Reference proteome] [HAMAP]
Taxonomic identifier206672 [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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 545545Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192072

Sequences

Sequence LengthMass (Da)Tools
Q8G6B1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 45EC500131DFA331

FASTA54558,413
        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 PAKFPAQFTR 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 KKNLRILEVA 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]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN24552.1.
RefSeqNP_695916.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G6B1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING206672.BL0735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN24552; AAN24552; BL0735.
GeneID1021781.
KEGGblo:BL0735.
PATRIC21117917. VBIBifLon107831_0432.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAHRRAHAC.
OrthoDBEOG6QCDFF.
PhylomeDBQ8G6B1.

Enzyme and pathway databases

BioCycBLON206672:GI1E-402-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_BIFLO
AccessionPrimary (citable) accession number: Q8G6B1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 72 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