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A0Q1J0 (PUR9_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:NT01CX_2419
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length500 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 – 500500Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018879

Sequences

Sequence LengthMass (Da)Tools
A0Q1J0 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: FCF54E3C946C5F3C

FASTA50055,650
        10         20         30         40         50         60 
MLKRALISVF NKEGIVDFAK FLVNKGVEII STGGTYKHLK ENNIPVTEVN EVTGFDEILD 

        70         80         90        100        110        120 
GRVKTLHPAI HGGILAIRDN KEHMSIIENK GIKPIDMVVV NLYPFFEKVK EDLEFQEKIE 

       130        140        150        160        170        180 
FIDIGGPTMI RAAAKNFKDV VVLTDTKDYS DVMDQIEKNN EVNYDTRKRL AGKVFNLMAS 

       190        200        210        220        230        240 
YDAAISNFLL EDTEYPENLA LSYTKSMDLR YGENSHQSAA CYTANNGKGI MNNIEILNGK 

       250        260        270        280        290        300 
QLSYNNIKDM DIAWKVVWEF DDIACCGLKH NTPCGVALGE NVHDAYLKAY SCDPVSIFGG 

       310        320        330        340        350        360 
IVAFNRKVDK KTAEEMVKIF LEIVIAPDFD SDALEVLKTK KNLRVIKCNT KPEDNFNIAK 

       370        380        390        400        410        420 
VDGAILVQSE DKLFAEKMEV VTDKKPTEEE LKELTFAMKV CKYTKSNAIV VSKGCVAVGI 

       430        440        450        460        470        480 
GGGQVNRIWA AEEALERGEG ATVLASDAFF PFDDVVKTAA KHGIKAIIQP GGSIRDKDSI 

       490        500 
KACNENDISM VFTGIRHFKH 

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000382 Genomic DNA. Translation: ABK61189.1.
RefSeqYP_878492.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0Q1J0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386415.NT01CX_2419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK61189; ABK61189; NT01CX_2419.
GeneID4540229.
KEGGcno:NT01CX_2419.
PATRIC19480504. VBICloNov112828_1522.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCNOV386415:GH98-1551-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_CLONN
AccessionPrimary (citable) accession number: A0Q1J0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: May 14, 2014
This is version 52 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