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Q8FR29 (PUR9_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:CE0937
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length521 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 – 521521Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192088

Sequences

Sequence LengthMass (Da)Tools
Q8FR29 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 1FC6B7425B53936E

FASTA52155,454
        10         20         30         40         50         60 
MSEDRKAIKR ALISVYDKTG LEDLAQALHR AGVEIVSTGS TAAKIADLGI PVTPVEELTG 

        70         80         90        100        110        120 
FPECLEGRVK TLHPKVHAGI LADTRKDDHL RQLDELGVTP FQLVVVNLYP FAETVASGAD 

       130        140        150        160        170        180 
FDDCVEQIDI GGPSMVRAAA KNHPSVAVVT SPGQYEDVVS VLNTGGFSRA ERTKLAAEAF 

       190        200        210        220        230        240 
RHTATYDVTV ATWISEQLSA ADTELEFPGW IGSTSTLARS LRYGENPHQS AALYVSHGAS 

       250        260        270        280        290        300 
GLAQATQLHG KEMSYNNYTD SDAAWRAAWD HERPCVAIIK HANPCGIAVS DESIAAAHRQ 

       310        320        330        340        350        360 
AHACDSVSAF GGVIASNREV SVEMAEQVAE IFTEVIIAPS YEEGAVEVLS QKKNIRILQA 

       370        380        390        400        410        420 
EAPVREGFET REISGGLLVQ ERDLIHAEGD NPANWTLAAG EAVSAEVLKD LEFAWTAVRS 

       430        440        450        460        470        480 
VKSNAILLAK DGATVGVGMG QVNRVDSARL AVDRAGEERA TGSVAASDAF FPFADGFEVL 

       490        500        510        520 
AQAGITAVVQ PGGSIRDDEV IEAANKAGVT MYLTGARHFS H 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC17747.1.
RefSeqNP_737547.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FR29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE0937.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC17747; BAC17747; BAC17747.
GeneID1031951.
KEGGcef:CE0937.
PATRIC21488014. VBICorEff9312_0943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230373.
KOK00602.
OMAHRRAHAC.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

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_COREF
AccessionPrimary (citable) accession number: Q8FR29
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 73 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