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B2TN76 (PUR9_CLOBB) 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:CLL_A1108
OrganismClostridium botulinum (strain Eklund 17B / Type B) [Complete proteome] [HAMAP]
Taxonomic identifier508765 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length501 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 – 501501Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096054

Sequences

Sequence LengthMass (Da)Tools
B2TN76 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 25FF64FD340B0EE9

FASTA50156,031
        10         20         30         40         50         60 
MKKRALISVF NKDGVLDFAK FLVSKDIEIV STGGTYKYLK ENGIDVIEIN EVTNFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPLV HAGILAIRDN KEHMKVLEER EIHTIDYVVV NLYPFFEKVK EDLTFEEKVE 

       130        140        150        160        170        180 
FIDIGGPTML RAAAKNFQDV VVISNINDYE VVKSEIKNDG QVSLKTKKKL SGKVFNLMSA 

       190        200        210        220        230        240 
YDGAIANFML GDEEEYPEYL SVSYKKMQNL RYGENSHQSA AVYSSTMVDG AMNTFETLNG 

       250        260        270        280        290        300 
KELSYNNFKD VDIAWKCANE FDEPACCALK HNTPCGVATG ENSYEAYMKA YEVDPTSIFG 

       310        320        330        340        350        360 
GIIGFNRKVD KKTAQEMVKI FLEVIAAPDY DEDALEVLKT KKNLRVLKFH NTPKAEKCMV 

       370        380        390        400        410        420 
TVDGAILVQD EDNKLIDEIK VVTEKKPSDE EMKDLLFGMK VVKYVKSNAI VVAHNGIALG 

       430        440        450        460        470        480 
IGGGQVNRIW PTEDALRRGK GATILASDAF FPFRDVVDKA AEGGIKAIIQ PGGSMRDQES 

       490        500 
IDACNEHGIA MVFTGFRHFK H 

« Hide

References

[1]"Complete sequence of Clostridium botulinum strain Eklund."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Eklund 17B / Type B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001056 Genomic DNA. Translation: ACD23710.1.
RefSeqYP_001885306.1. NC_010674.1.

3D structure databases

ProteinModelPortalB2TN76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING508765.CLL_A1108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD23710; ACD23710; CLL_A1108.
GeneID6293713.
KEGGcbk:CLL_A1108.
PATRIC19395060. VBICloBot123574_1040.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAGIGQADN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCBOT508765:GJ4H-1102-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_CLOBB
AccessionPrimary (citable) accession number: B2TN76
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 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