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Q02FG6 (PUR9_PSEAB) 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:PA14_64200
OrganismPseudomonas aeruginosa (strain UCBPP-PA14) [Complete proteome] [HAMAP]
Taxonomic identifier208963 [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_1000018936

Sequences

Sequence LengthMass (Da)Tools
Q02FG6 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 05A0141BEA969F8C

FASTA53557,667
        10         20         30         40         50         60 
MTDQTTRLPI RRALISVSDK TGVVDFAREL VALGVEILST GGTYKLLRDN GISAVEVADY 

        70         80         90        100        110        120 
TGFPEMMDGR VKTLHPKVHG GILGRRDLDG AVMEQHGIKP IDLVAVNLYP FEATVVRPDC 

       130        140        150        160        170        180 
DLPTAIENID IGGPTMVRSA AKNHKDVAIV VNAGDYAAVI ESLKAGGLTY AQRFDLALKA 

       190        200        210        220        230        240 
FEHTSAYDGM IANYLGTIDQ TRDTLGTADR GAFPRTFNSQ FVKAQEMRYG ENPHQSAAFY 

       250        260        270        280        290        300 
VEAKKGEASV STAIQLQGKE LSFNNVADTD AALECVKSFL KPACVIVKHA NPCGVAVVPE 

       310        320        330        340        350        360 
DEGGIRKAYD LAYATDSESA FGGIIAFNRE LDGETAKAIV ERQFVEVIIA PKISAAAREV 

       370        380        390        400        410        420 
VAAKANVRLL ECGEWPAERA PGWDFKRVNG GLLVQSRDIG MIKAEDLKIV TRRAPTEQEI 

       430        440        450        460        470        480 
HDLIFAWKVA KFVKSNAIVY ARNRQTVGVG AGQMSRVNSA RIAAIKAEHA GLEVKGAVMA 

       490        500        510        520        530 
SDAFFPFRDG IDNAAKAGIT AVIQPGGSMR DSEVIAAADE ADIAMVFTGM RHFRH 

« Hide

References

[1]"Genomic analysis reveals that Pseudomonas aeruginosa virulence is combinatorial."
Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.
Genome Biol. 7:R90.1-R90.14(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCBPP-PA14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000438 Genomic DNA. Translation: ABJ14238.1.
RefSeqYP_793320.1. NC_008463.1.

3D structure databases

ProteinModelPortalQ02FG6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208963.PA14_64200.

Proteomic databases

PRIDEQ02FG6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ14238; ABJ14238; PA14_64200.
GeneID4383323.
KEGGpau:PA14_64200.
PATRIC19856704. VBIPseAer79785_5266.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPAER208963:GI5K-5239-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_PSEAB
AccessionPrimary (citable) accession number: Q02FG6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
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