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Q73EN1 (PUR9_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:BCE_0327
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length511 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 – 511511Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018839

Sequences

Sequence LengthMass (Da)Tools
Q73EN1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F8D8A456B4774A6B

FASTA51155,643
        10         20         30         40         50         60 
MKKRALVSVS DKTGVVEFVK GLLEQGIEVI STGGTKKLLE ENGLQVIGIS EVTGFPEIMD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLAVRDN ETHVAQMNEL GIEPIDFVIV NLYPFKETIA KPDVTFADAI 

       130        140        150        160        170        180 
ENIDIGGPTM IRSAAKNHKF VSVIVDPVDY DVVLAELEEN GEVKEETKRK LAAKVFRHTA 

       190        200        210        220        230        240 
AYDALISNYL TEQMGEESPE TLTVTFEKKQ DLRYGENPHQ KATFYKAPFA ATSSVAYAEQ 

       250        260        270        280        290        300 
LHGKELSYNN INDADAALSI VKEFTEPAVV AVKHMNPCGV GVGTDIHEAY TRAYEADPVS 

       310        320        330        340        350        360 
IFGGIIAANR EIDKSTAEKL HEIFLEIIIA PSFSKEALEV LQNKKNLRLL TVNIEKSTSA 

       370        380        390        400        410        420 
SKKLTSVQGG LLVQEEDTLS LDESTISIPT KREPSEQEWK DLKLAWKVVK HVKSNAIVLA 

       430        440        450        460        470        480 
KDDMTIGVGA GQMNRVGSAK IAITQAGEKA QGSALASDAF FPMPDTLEEA AKAGITAIIQ 

       490        500        510 
PGGSIRDEDS IKVADTYGIA MVFTGVRHFK H 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS39263.1.
RefSeqNP_976655.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ73EN1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING222523.BCE_0327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS39263; AAS39263; BCE_0327.
GeneID2750147.
KEGGbca:BCE_0327.
PATRIC18849534. VBIBacCer118379_0314.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAGIGQADN.
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_BACC1
AccessionPrimary (citable) accession number: Q73EN1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 68 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