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B2UFL5 (PUR9_RALPJ) 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:Rpic_0380
OrganismRalstonia pickettii (strain 12J) [Complete proteome] [HAMAP]
Taxonomic identifier402626 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length524 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 – 524524Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096085

Sequences

Sequence LengthMass (Da)Tools
B2UFL5 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: FB0418EAFA7AC8C3

FASTA52456,016
        10         20         30         40         50         60 
MIQQALLSVS DKTGIVDFAR ALHERGVKLL STGGTAKLLA ESSLPVTEVA DYTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPKV HGGILARRDL PEHMAALSEH SIPTIDLLVV NLYPFQQTVA KDECSLADAI 

       130        140        150        160        170        180 
ENIDIGGPTM LRSAAKNHRD VTVIVDPADY ATVLAEMQAN NNTVGYETNF MLAKKVFAHT 

       190        200        210        220        230        240 
AQYDGAITNY LTSLGADKSH STRSAYPQTL NLAFDKVQEM RYGENPHQSA AFYRDLKAVD 

       250        260        270        280        290        300 
GALANYKQLQ GKELSYNNIA DADAAWECVK SFDAAHGAAC VIIKHANPCG VAIGGTAQEA 

       310        320        330        340        350        360 
YEKAFKTDST SAFGGIIAFN VPLDEAAAQV VAKQFVEVLI APGFSEGARA VFAAKQNVRV 

       370        380        390        400        410        420 
LEIPLGKGVN AYDFKRVGGG LLVQSPDAKN VQPSELRVVT KRHPTPKEMD DLMFAWRVAK 

       430        440        450        460        470        480 
FVKSNAIVFC GGGMTLGVGA GQMSRVDSAR IASIKAQNAG LTLAGSAVAS DAFFPFRDGL 

       490        500        510        520 
DVVVDAGASC VIQPGGSVRD DEVIAAADER NVAMIFTGTR HFRH 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia pickettii 12J."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Marsh T., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12J.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001068 Genomic DNA. Translation: ACD25538.1.
RefSeqYP_001897970.1. NC_010682.1.

3D structure databases

ProteinModelPortalB2UFL5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402626.Rpic_0380.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD25538; ACD25538; Rpic_0380.
GeneID6289677.
KEGGrpi:Rpic_0380.
PATRIC20251642. VBIRalPic63053_1589.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRPIC402626:GH94-381-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_RALPJ
AccessionPrimary (citable) accession number: B2UFL5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 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