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B0TEC5 (PUR9_HELMI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Helmi_29820
ORF Names:HM1_3106
OrganismHeliobacterium modesticaldum (strain ATCC 51547 / Ice1) [Complete proteome] [HAMAP]
Taxonomic identifier498761 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacterium

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_1000096066

Sequences

Sequence LengthMass (Da)Tools
B0TEC5 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: E6823292C8E00394

FASTA52756,109
        10         20         30         40         50         60 
MNRRALISVS DKTGVVDFAR GLADLGFEIV STGGTYQTIK AAGVPVTYVT EITGFPEILD 

        70         80         90        100        110        120 
GRVKTLHPKV HGGILARRTP EHLAQLEAHA IVPIDVVAVN LYPFRETVAK PGVTREEAVE 

       130        140        150        160        170        180 
NIDIGGPAMV RASAKNHESV AIIVNPDRYA TVLAELQQNG VVSEATRRAL AREAFAHTAE 

       190        200        210        220        230        240 
YDAAIAAYLA AEAGDDDPFA GIFAPGKVEK VQDLRYGENP HQKAAFYRER GYRGAGAGTA 

       250        260        270        280        290        300 
KQRWGKELSF NNLLDLNAAL ELVREFDRPA AAIIKHNNPC GVAVAATLKE AYEKAFAADP 

       310        320        330        340        350        360 
VSAFGGIIAF NVAVDADTAN EVVKTFMEAV IAPSFDEAAL EILQQKKGLR IMETGPLADS 

       370        380        390        400        410        420 
APATADVKKI RGGFLVQEAD LGDVTAEQIQ VVTERAPEEG ELADLLFAWK VVKHVKSNAI 

       430        440        450        460        470        480 
VIAKDGVAIG VGAGQMNRVG SAQIALEQAK ASRAFGGDSV DHNNPAQGAV LASDAFLPFK 

       490        500        510        520 
DTVETAARYG IRAIIQPGGS VRDAESIEAC NRLGVAMVFT GMRHFKH 

« Hide

References

[1]"The genome of Heliobacterium modesticaldum, a phototrophic representative of the Firmicutes containing the simplest photosynthetic apparatus."
Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M., Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.
J. Bacteriol. 190:4687-4696(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51547 / Ice1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000930 Genomic DNA. Translation: ABZ85607.1.
RefSeqYP_001681618.1. NC_010337.2.

3D structure databases

ProteinModelPortalB0TEC5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING498761.HM1_3106.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ85607; ABZ85607; HM1_3106.
GeneID5909556.
KEGGhmo:HM1_3106.
PATRIC22110165. VBIHelMod36755_2762.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycHMOD498761:GI46-3119-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_HELMI
AccessionPrimary (citable) accession number: B0TEC5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 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