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B8D8J3 (PUR9_BUCA5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:BUAP5A_030
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A) [Complete proteome] [HAMAP]
Taxonomic identifier563178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length525 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 – 525525Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122950

Sequences

Sequence LengthMass (Da)Tools
B8D8J3 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 95AE0B6FA3DF5822

FASTA52559,036
        10         20         30         40         50         60 
MPSNNLIKNA LISVSDKKNI VEVAEKLIIN KINLFSTGGT AQILKKNNIP VTEISDYTKF 

        70         80         90        100        110        120 
PEIMDGRVKT LHPKIMGGIL GQKQKDQEIM KLYNICPIDI VIVNFYPFEK IKNIKKNDID 

       130        140        150        160        170        180 
NVVNNIDIGG PTLVRASAKN YKNVIVIVDL DDFQSTIDSI NNNTMNIEKR FNLASKAFEY 

       190        200        210        220        230        240 
TSYYEQIISQ YFIEQNSLYK KTNNSLFPNE INFSFIKKQD LRYGENYHQK SSFYIEKNMC 

       250        260        270        280        290        300 
DSGTISTACQ IQGKTLSYNN ISDSDIALEC VKQFTKPACV IVKHGNPCSV AVSHNILESY 

       310        320        330        340        350        360 
LSAYNSDPIS AFGGIISFNC KLDEKTAQTI INQQFVEVII IPEISKKAVK ILQKKQNIRV 

       370        380        390        400        410        420 
LVTGKLQNNT VGLDLKKITN GLLVQEYDSH NIDYNSWSFV TKRSPTKKEL KDSIFCWQVA 

       430        440        450        460        470        480 
KFVKSNAIVY GSDEITIGIG AGQMSRIYST KLANIKVKDQ GKNIIGATMA SDAFFPFRDG 

       490        500        510        520 
IDEAASVGIS SIIQPGGSIR DEEIIRAADE HNITMIFTKK RHFKH 

« Hide

References

[1]"The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria."
Moran N.A., McLaughlin H.J., Sorek R.
Science 323:379-382(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001161 Genomic DNA. Translation: ACL30415.1.
RefSeqYP_002467802.1. NC_011833.1.

3D structure databases

ProteinModelPortalB8D8J3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING107806.BU031.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL30415; ACL30415; BUAP5A_030.
GeneID7262376.
KEGGbap:BUAP5A_030.
PATRIC21242281. VBIBucAph51993_0030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBAPH563178:GHDF-30-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_BUCA5
AccessionPrimary (citable) accession number: B8D8J3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 39 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