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A5G879 (PUR9_GEOUR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Gura_3847
OrganismGeobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens) [Complete proteome] [HAMAP]
Taxonomic identifier351605 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length521 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 – 521521Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076482

Sequences

Sequence LengthMass (Da)Tools
A5G879 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 70476ADFD8902271

FASTA52156,027
        10         20         30         40         50         60 
MAKITRALIS VSDKTGIVEF SRELAGYGVE ILSTGGTAKL LREAGLKVKD VSEFTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KVHGGLLGMR GNPEHVATMK AHGIEPIDMV VVNLYPFEAT VAKPDCTLED 

       130        140        150        160        170        180 
AIENIDIGGP TMLRSAAKNN ADVTVVVDHN DYRLVLDEMK AAGGGVSKET NFRLAVKVYQ 

       190        200        210        220        230        240 
HTAAYDGAIS NWLGARTGEG VAAYPDTLTL QFKKAQGMRY GENPHQSAAF YVERDVKEAS 

       250        260        270        280        290        300 
VATARQLQGK ELSYNNIGDT DAALECVKQF AEGPGCVIVK HANPCGVAIG DTLLDAYDRA 

       310        320        330        340        350        360 
YKTDPESAFG GIIAFNGELD EATAKAIVER QFVEVIIAPK VSAKASEVVA AKKNVRLLEC 

       370        380        390        400        410        420 
GTWQKEPMPR LDFKRVNGGL LVQYTDLALH GELKVVTKRA PTEKEMIDLL FTWRVAKFVK 

       430        440        450        460        470        480 
SNAIVYGKDG MTIGVGAGQM SRVNSARIAA IKAEHAGLPV AGSVMASDAF FPFRDGLDNA 

       490        500        510        520 
AAVGITAVIQ PGGSMRDEEV IAAADEHGMA MVFTSMRHFR H 

« Hide

References

[1]"Complete sequence of Geobacter uraniireducens Rf4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M., Lovley D., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Rf4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000698 Genomic DNA. Translation: ABQ27997.1.
RefSeqYP_001232570.1. NC_009483.1.

3D structure databases

ProteinModelPortalA5G879.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351605.Gura_3847.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ27997; ABQ27997; Gura_3847.
GeneID5166435.
KEGGgur:Gura_3847.
PATRIC22038113. VBIGeoUra13052_4105.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycGURA351605:GI6A-3899-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_GEOUR
AccessionPrimary (citable) accession number: A5G879
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 53 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