Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B7HS36 (PUR9_BACC7) 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:BCAH187_A0371
OrganismBacillus cereus (strain AH187) [Complete proteome] [HAMAP]
Taxonomic identifier405534 [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_1000117867

Sequences

Sequence LengthMass (Da)Tools
B7HS36 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: CE1D240EB40D4D0A

FASTA51155,602
        10         20         30         40         50         60 
MKQRALVSVS DKTGVVEFVK GLLEQGIEVI STGGTKKLLE ENGLQVIGIS EVTGFPEIMD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLAVRDN ETHVAQMNEL GIEPIDFVVV 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 LQSKKNLRLL 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]"Genome sequence of Bacillus cereus AH187."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AH187.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001177 Genomic DNA. Translation: ACJ80890.1.
RefSeqYP_002336401.1. NC_011658.1.

3D structure databases

ProteinModelPortalB7HS36.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405534.BCAH187_A0371.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ80890; ACJ80890; BCAH187_A0371.
GeneID7078347.
KEGGbcr:BCAH187_A0371.
PATRIC18826183. VBIBacCer120511_0608.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBCER405534:GHXM-351-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_BACC7
AccessionPrimary (citable) accession number: B7HS36
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
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