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Q39RK1 (PUR9_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Gmet_2905
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [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_1000057896

Sequences

Sequence LengthMass (Da)Tools
Q39RK1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 4545BC83ABDCD382

FASTA52155,783
        10         20         30         40         50         60 
MAKITRALIS LSDKTGIVEF ARELAGYGVE ILSTGGTAKL LRDAGLTVKD VSEHTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KVHGGLLGMR SNPEHVATMK EHGILPIDMV VVNLYPFEAT VANPACTLED 

       130        140        150        160        170        180 
AIENIDIGGP TMLRSAAKNN ADVTVVVDPA DYRTVLDEMK ASGGSVAKET NFRLAVKVYQ 

       190        200        210        220        230        240 
HTAAYDGAIS NWLGARTGEG VATYSDTITL QFKKAQEMRY GENPHQSAAF YVERQVQEAS 

       250        260        270        280        290        300 
VSTARQLQGK ELSYNNIGDT DAALECVKQF SEGPACVIVK HANPCGVAIG KNLLEAYDRA 

       310        320        330        340        350        360 
YATDPESAFG GIIAFNGELD AETAKAICDR QFVEVIIAPS VSKAAVEVVA AKKNVRLLEC 

       370        380        390        400        410        420 
GIWPAQPAQR LDFKRVNGGL LVQDTDLALS AELKVVSKRQ PTAQEMIDLQ FAWRVAKFVK 

       430        440        450        460        470        480 
SNAIVYGKDG MTIGVGAGQM SRVNSARIAA IKAEHAGLEV QGAVMASDAF FPFRDGIDNA 

       490        500        510        520 
AAVGITAVIQ PGGSMRDAEV IAAADEHGMA MVFTGMRHFR H 

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000148 Genomic DNA. Translation: ABB33123.1.
RefSeqYP_006721862.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39RK1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269799.Gmet_2905.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB33123; ABB33123; Gmet_2905.
GeneID3740855.
KEGGgme:Gmet_2905.
PATRIC22005064. VBIGeoMet55070_2939.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGMET269799:GHNY-2949-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_GEOMG
AccessionPrimary (citable) accession number: Q39RK1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 60 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