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B2FJP9 (PUR9_STRMK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Smlt4253
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length527 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 – 527527Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096099

Sequences

Sequence LengthMass (Da)Tools
B2FJP9 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 7B28EBE61BE0A111

FASTA52755,721
        10         20         30         40         50         60 
MTADLLPVRR ALLSVSDKTG LVELATALAA RGVELLSTGG TAKAIRDAGL AVKDVADVTG 

        70         80         90        100        110        120 
FPEMMDGRVK TLHPMVHGGL LGRSGLDDAV MAEHGIGAID LLVLNLYPFE SVTAKADCTL 

       130        140        150        160        170        180 
ADAVENIDIG GPAMLRSAAK NFARVAVATD PSQYAELLAS LDANDGQLSA STRFAFSVAA 

       190        200        210        220        230        240 
FNRVAQYDAA ISNYLSAVTA TDAAVPARAE YPAQMNSTFV KVMDLRYGEN PHQSGAFYRD 

       250        260        270        280        290        300 
LYPVPGTLAT FQQLQGKELS YNNLADADAA WECVRQFDAP ACVIVKHANP CGVAVGAGNG 

       310        320        330        340        350        360 
DAYELAYATD PTSAFGGIIA FNKPLDAATA KVILDRQFVE VLIAPDYEPA ALEYAQKKAN 

       370        380        390        400        410        420 
VRVLRIPHGD GLNNFDSKRV GSGLLLQSSD NRGMTRDELK VVSKLAPTDK QFTDLLFAWK 

       430        440        450        460        470        480 
VAKFVKSNAI VYAKDNRTIG VGAGQMSRVY SARIAGIKAA DANLVVEGSV MASDAFFPFR 

       490        500        510        520 
DGIDAAAAAG IKAVIQPGGS MRDAEVIAAA DEHGLAMVFT GVRHFRH 

« Hide

References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K279a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM743169 Genomic DNA. Translation: CAQ47642.1.
RefSeqYP_001973925.1. NC_010943.1.

3D structure databases

ProteinModelPortalB2FJP9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING522373.Smlt4253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ47642; CAQ47642; Smlt4253.
GeneID6392464.
KEGGsml:Smlt4253.
PATRIC23703951. VBISteMal45202_4024.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSMAL522373:GJE8-4116-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_STRMK
AccessionPrimary (citable) accession number: B2FJP9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 45 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