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Q1I4C1 (PUR9_PSEE4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:PSEEN4863
OrganismPseudomonas entomophila (strain L48) [Complete proteome] [HAMAP]
Taxonomic identifier384676 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length535 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 – 535535Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018937

Sequences

Sequence LengthMass (Da)Tools
Q1I4C1 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 6470ED72B5823497

FASTA53557,784
        10         20         30         40         50         60 
MTDQTTRLPI RRALISVSDK TGILEFAREL QQLGVEILST GGTYKLLKDN GVNAVEVADY 

        70         80         90        100        110        120 
TGFAEMMDGR VKTLHPKIHG GILGRRGTDD AIMNEHGIKP IDLVAVNLYP FEATISKPGC 

       130        140        150        160        170        180 
DLPTAIENID IGGPTMVRSA AKNHKDVAIV VNASDYAGVV EGLKAGGLTY AQRFDLMLKA 

       190        200        210        220        230        240 
FEHTAAYDGM IANYMGTIDQ SKESLSTEDR SEFPRTFNSQ FVKAQEMRYG ENPHQSAAFY 

       250        260        270        280        290        300 
VEAKKGEASI STAIQLQGKE LSFNNVADTD AALECVKSFV KPACVIVKHA NPCGVAVVPE 

       310        320        330        340        350        360 
DEGGIRKAYD LAYATDTESA FGGIIAFNRE LDGETAKAIV ERQFVEVIIA PKISQAAREV 

       370        380        390        400        410        420 
VAAKQNVRLL ECGEWPAERA AGWDFKRVNG GLLVQSRDIG MITADDLKIV TKRAPTEQEI 

       430        440        450        460        470        480 
HDLVFAWKVA KFVKSNAIVY AKNRQTIGVG AGQMSRVNSA RIAAIKAEHA GLQVQGAVMA 

       490        500        510        520        530 
SDAFFPFRDG IDNAAKVGIS AVIQPGGSMR DAEVIAAADE AGIAMVFTGM RHFRH 

« Hide

References

[1]"Complete genome sequence of the entomopathogenic and metabolically versatile soil bacterium Pseudomonas entomophila."
Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C., Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P., Weissenbach J., Lemaitre B., Medigue C., Boccard F.
Nat. Biotechnol. 24:673-679(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L48.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT573326 Genomic DNA. Translation: CAK17515.1.
RefSeqYP_610298.1. NC_008027.1.

3D structure databases

ProteinModelPortalQ1I4C1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING384676.PSEEN4863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK17515; CAK17515; PSEEN4863.
GeneID4087545.
KEGGpen:PSEEN4863.
PATRIC19867730. VBIPseEnt83862_4662.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycPENT384676:GJB8-4621-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_PSEE4
AccessionPrimary (citable) accession number: Q1I4C1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 55 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