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B7V1R6 (PUR9_PSEA8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:PLES_52391
OrganismPseudomonas aeruginosa (strain LESB58) [Complete proteome] [HAMAP]
Taxonomic identifier557722 [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_1000192979

Sequences

Sequence LengthMass (Da)Tools
B7V1R6 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 38B912B9570E23BD

FASTA53557,666
        10         20         30         40         50         60 
MTDQTTRLPI RRALISVSDK TGVVDFAREL VALGVEILST GGTYKLLRDN GISAVEVADY 

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

       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 DNEVIAAADE ADIAMVFTGM RHFRH 

« Hide

References

[1]"Newly introduced genomic prophage islands are critical determinants of in vivo competitiveness in the Liverpool epidemic strain of Pseudomonas aeruginosa."
Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.
Genome Res. 19:12-23(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LESB58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM209186 Genomic DNA. Translation: CAW29993.1.
RefSeqYP_002442817.1. NC_011770.1.

3D structure databases

ProteinModelPortalB7V1R6.
SMRB7V1R6. Positions 7-535.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557722.PLES_52391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW29993; CAW29993; PLES_52391.
GeneID7179934.
KEGGpag:PLES_52391.
PATRIC19820378. VBIPseAer113719_5385.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPAER557722:GHJW-5326-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_PSEA8
AccessionPrimary (citable) accession number: B7V1R6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 42 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