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C1CWJ7 (PUR9_DEIDV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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:Deide_16000
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length510 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 – 510510Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000203248

Sequences

Sequence LengthMass (Da)Tools
C1CWJ7 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: C7AD9AE095FA73B6

FASTA51054,521
        10         20         30         40         50         60 
MTKRALISVS DKTGVVEFAR SLTARGWEVL STGGTFQALQ EAGVSVTQVS DVTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPAV HGGILARREP QHLSQLEAQG FGTIDLVCVN LYPFRETVAR GAPDPEVIEN 

       130        140        150        160        170        180 
IDIGGPAMIR SAAKNHSGVL VLVDPADYPV ALQDEVSGSE RRRLAAKAYR HTSEYDAAIT 

       190        200        210        220        230        240 
AYLEGASEEL PTRLPERLTV DLHRVAQVRY GENPHQPGAV YRWGQARGPV MDAQVVAGKP 

       250        260        270        280        290        300 
MSFNNYADAD AAWSLCQELA AQEDGAVCVA VKHANPCGVA VADDVRAAWE RARDADTLSV 

       310        320        330        340        350        360 
FGGVVAVSRP VDFQAAQAMR GTFLEVLIAP EVTPDAVEWF AEKKPDLRVL VAAQASGVSV 

       370        380        390        400        410        420 
LDVRPLTGGF AVQERDTRPW DDLCPEVVTA RQPTDQEWAD LRFAWATVKH ARSNAVVLAR 

       430        440        450        460        470        480 
GGVTVGLGAG AVSRIWAAER AVANAGDKAQ GAVLASEAFF PFDDVVRLAA QSGVTAILQP 

       490        500        510 
GGAKRDPEVI AAANELGVSM VFTGSRHFRH 

« Hide

References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001114 Genomic DNA. Translation: ACO46564.1.
RefSeqYP_002786318.1. NC_012526.1.

3D structure databases

ProteinModelPortalC1CWJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING546414.Deide_16000.

Proteomic databases

PaxDbC1CWJ7.
PRIDEC1CWJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO46564; ACO46564; Deide_16000.
GeneID7737271.
KEGGddr:Deide_16000.
PATRIC21617126. VBIDeiDes121019_1841.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycDDES546414:GHOM-1819-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_DEIDV
AccessionPrimary (citable) accession number: C1CWJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 39 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