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B5XYD2 (PUR9_KLEP3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:KPK_5286
OrganismKlebsiella pneumoniae (strain 342) [Complete proteome] [HAMAP]
Taxonomic identifier507522 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length529 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 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096067

Sequences

Sequence LengthMass (Da)Tools
B5XYD2 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 63A80A54BCB71C7A

FASTA52957,203
        10         20         30         40         50         60 
MQQRRPVRRA LLSVSDKAGI VEFAQALTAR GVELLSTGGT ARLLADKGLP VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRGQDDGIM QQHGIAPIDM VVVNLYPFAQ TVAREGCSLE 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYDAIINEM DANEGSLTLN TRFDLAIKAF 

       190        200        210        220        230        240 
EHTAAYDSMI ANYFGSMVPA YHGESQEAAG RFPRTLNLNF IKKQDMRYGE NSHQQAAFYI 

       250        260        270        280        290        300 
EENVKEASVA TATQLQGKAL SYNNIADTDA ALECVKEFNE PACVIVKHAN PCGVAVSNSI 

       310        320        330        340        350        360 
LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE EALKITAAKQ 

       370        380        390        400        410        420 
NVRVLTCGQW DARVAGLDFK RVNGGLLVQD RDLGMVTAGE LRVVSKRQPS EQELRDALFC 

       430        440        450        460        470        480 
WKVAKFVKSN AIVYAKDNMT IGIGAGQMSR VYSAKIAGIK AGDEGLEVKG SAMASDAFFP 

       490        500        510        520 
FRDGIDAAAA VGITCVIQPG GSIRDDEVIA AADEHGIAMI FTDMRHFRH 

« Hide

References

[1]"Complete genome sequence of the N2-fixing broad host range endophyte Klebsiella pneumoniae 342 and virulence predictions verified in mice."
Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., Methe B.A.
PLoS Genet. 4:E1000141-E1000141(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 342.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000964 Genomic DNA. Translation: ACI06763.1.
RefSeqYP_002241053.1. NC_011283.1.

3D structure databases

ProteinModelPortalB5XYD2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING507522.KPK_5286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI06763; ACI06763; KPK_5286.
GeneID6940236.
KEGGkpe:KPK_5286.
PATRIC20443670. VBIKlePne121904_5159.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycKPNE507522:GI0B-5287-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_KLEP3
AccessionPrimary (citable) accession number: B5XYD2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: February 19, 2014
This is version 43 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