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B1XS23 (PUR9_POLNS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:Pnec_1581
OrganismPolynucleobacter necessarius subsp. necessarius (strain STIR1) [Complete proteome] [HAMAP]
Taxonomic identifier452638 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaePolynucleobacter

Protein attributes

Sequence length526 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 – 526526Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096080

Sequences

Sequence LengthMass (Da)Tools
B1XS23 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 8C3ACFF62C9A2910

FASTA52656,412
        10         20         30         40         50         60 
MIRTALLSVS DKNGIVPFAK SLHEQGIKLI STGGTAKLLA ENGLPVVEIS SLTKFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPMV HGGLLARRDF PEHMAALKEY GINTIDMLVI NLYPFNETVA KENCSFEDAV 

       130        140        150        160        170        180 
ENIDIGGPAM LRAAAKNHQD VTVLISPEDY APVLAEMKAN QNSVSYKTNL ALAKKVFAHT 

       190        200        210        220        230        240 
AQYDGAIANY LSALGDDLDH KARSAYPETL HLAFEKVQEM RYGENPHQAA AFYKDIYPVD 

       250        260        270        280        290        300 
GALANYKQLQ GKELSYNNIA DADSAWECVK SFTGNAGGAA ACVIIKHANP CGVAVGASAL 

       310        320        330        340        350        360 
EAYQKAFKTD PSSAFGGIIA FNVSCDGAAA EAISKQFVEV LIAPSFSDEA KTIFAAKQNM 

       370        380        390        400        410        420 
RLLEIPLGTA FNTFDFKRVG GGLLVQSPDA KNVLENEMCV VSKRLPTPSE MHDMMFAWRV 

       430        440        450        460        470        480 
AKFVKSNAII YCANGMTLGI GAGQMSRVDS ARMASIKAKN AGLSLKGSAV ASDAFFPFRD 

       490        500        510        520 
GLDVVVNGGA SCAIQPGGSM RDDEIIAAAD EHGIAMIFTG TRHFRH 

« Hide

References

[1]"Complete sequence of Polynucleobacter necessarius STIR1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Hahn M., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: STIR1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001010 Genomic DNA. Translation: ACB44658.1.
RefSeqYP_001798272.1. NC_010531.1.

3D structure databases

ProteinModelPortalB1XS23.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING452638.Pnec_1581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB44658; ACB44658; Pnec_1581.
GeneID6183700.
KEGGpne:Pnec_1581.
PATRIC22972447. VBIPolNec8289_1820.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMACGVATGP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPNEC452638:GI4T-1580-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_POLNS
AccessionPrimary (citable) accession number: B1XS23
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 44 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