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Q67KG3 (PUR9_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:STH2850
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

Protein attributes

Sequence length540 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 – 540540Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018976

Sequences

Sequence LengthMass (Da)Tools
Q67KG3 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: B01DBC29E903F631

FASTA54057,507
        10         20         30         40         50         60 
MKRALISVYD KQGIVEFARG LADLGVEIIS TGGTYRTLQG AGIPVREVAE VAGFPEILDG 

        70         80         90        100        110        120 
RVKSLQPQIH AGILAMRANP THMAQLAEHG IGLIDLVVVN LYPFRETVAN PAVTLEEAIE 

       130        140        150        160        170        180 
KIDIGGPAMV RAAAKNYQDV GVVVNPARYP AVLAELRETG DLSLPTRFSL MLEAFQHTAA 

       190        200        210        220        230        240 
YDGAIAGWMA TRGREIVATR ALGETAPERP IGADPGPQKP AAPSPFPDVL SLTFTKVQEL 

       250        260        270        280        290        300 
RYGENPHQAA AFYSDGSDGG TVIARAKQLH GKELSFNNIN DAHAALELVK EFEEPAAVAI 

       310        320        330        340        350        360 
KHANPCGVAV APTIAEAFRK AYEADTVSIF GGIVALNRPC DRETAEALSK IFLEIVIAPA 

       370        380        390        400        410        420 
FAPEALEVLT RKKNLRLLAV GPIDRNPPSG FDMKRVGGGL LVQSWDAIAE DPVAWKPVTK 

       430        440        450        460        470        480 
AAPTPEQLRD LAFAMKVCKH VKSNAIVVAR DGQTLGVGAG QMNRIDAARF ALRQAGEKAR 

       490        500        510        520        530        540 
GAVLASDAFF PFPDVVEAAG EAGIAAIVQP GGSIRDEESI ARADELGLAM VFTGVRHFRH 

« Hide

References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD41835.1.
RefSeqYP_076679.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67KG3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292459.STH2850.

Proteomic databases

PRIDEQ67KG3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD41835; BAD41835; STH2850.
GeneID2980007.
KEGGsth:STH2850.
PATRIC23783881. VBISymThe116959_2829.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSTHE292459:GJMM-2951-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_SYMTH
AccessionPrimary (citable) accession number: Q67KG3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 70 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