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B3E7F6 (PUR9_GEOLS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Glov_2760
OrganismGeobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ) [Complete proteome] [HAMAP]
Taxonomic identifier398767 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length519 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 – 519519Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000192977

Sequences

Sequence LengthMass (Da)Tools
B3E7F6 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 14731ED400A3E798

FASTA51955,548
        10         20         30         40         50         60 
MAKITRALIS VSDKTGIVEL SKALAGYGVE ILSTGGTAKL LRESGLTVKD VSEFTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KVHGGLLGIR ANAEHQAKMK EHGIEPIDMV VVNLYPFEAT VAKPDCTLED 

       130        140        150        160        170        180 
AIENIDIGGP TMLRSAAKNN HDVTVLVDAA DYAAVLEEMA ANGGAVSAKT NFRLAVKVYQ 

       190        200        210        220        230        240 
HTAAYDGAIS NWLGARLGEN TDEYPETFTI QVKKAQDLRY GENPHQSAAF YVERGITEPC 

       250        260        270        280        290        300 
VSNAVQLQGK ELSFNNIIDL DAAIETVKEF TDKPAAVIIK HTNPCGVALG DSPISAYLKA 

       310        320        330        340        350        360 
RECDPVSAFG GIVGFNRIVD AAAARELTST FLEAVIAPGY DEEALAIFTA KKNVRVMQVP 

       370        380        390        400        410        420 
LLAGHLQTGY DLKRVVGGLL LQGRDLGMVA ATDCKVMSER QPTAQELAAL DFAWRVCKHV 

       430        440        450        460        470        480 
KSNAIVFTNA DQTVGIGAGQ MSRVDSSKIA VQKALLPIKG TVLASDAFFP FRDGVDAAAE 

       490        500        510 
AGVTAIIQPG GSVRDEEVIQ AANEHGMAMV FTNMRHFRH 

« Hide

References

[1]"Complete sequence of chromosome of Geobacter lovleyi SZ."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y., Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1151 / DSM 17278 / SZ.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001089 Genomic DNA. Translation: ACD96473.1.
RefSeqYP_001952993.1. NC_010814.1.

3D structure databases

ProteinModelPortalB3E7F6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398767.Glov_2760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD96473; ACD96473; Glov_2760.
GeneID6367669.
KEGGglo:Glov_2760.
PATRIC21997195. VBIGeoLov31523_2697.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMASDAKFAC.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycGLOV398767:GH32-2801-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_GEOLS
AccessionPrimary (citable) accession number: B3E7F6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: February 19, 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