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Q31R91 (PUR9_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:Synpcc7942_0396
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length513 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 – 513513Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018977

Sequences

Sequence LengthMass (Da)Tools
Q31R91 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 07F6334DA28E34D7

FASTA51354,414
        10         20         30         40         50         60 
MPRFALLSVS DKTGLVDFAR QLVDRFQFQI VSSGGTAKQL LEAGIPVTKV AEHTGSPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR IHGGILARRD REEDQADLAA NNIQPFDLVV VNLYPFEATI ARPEVTLADA 

       130        140        150        160        170        180 
IEQIDIGGPA MVRASAKNHA HLTILTNPSQ YEPYLTALAD GEGQIPLAFR QQCALAAFQH 

       190        200        210        220        230        240 
TAAYDAAIAT YLAEQFEATS DRLQLSAQPV QVLRYGENPH QAATWYQTGA TASGWAAAQQ 

       250        260        270        280        290        300 
LQGKELSYNN LVDLEAARQI IAEFPADGPA AAAILKHNNP CGVATAEALS DAYQKAFDAD 

       310        320        330        340        350        360 
SVSAFGGIVA LNRAIDAATA TAMTGTFLEC IVAPSVEPAA AEILAAKKNL RVLTLADFNS 

       370        380        390        400        410        420 
GPQQTVRSIA GGFLVQDSDD QLETVDAWQV VTEQQPSEAD WQELLFAWKV VKHVKSNAIA 

       430        440        450        460        470        480 
VTANGVTLGI GAGQMNRVGS VKIALEQAGD RAQGAILASD GFFPFDDSVR TAAAAGIRAI 

       490        500        510 
VQPGGSLRDA DSIAAANELG LVMVFTGTRH FLH 

« Hide

References

[1]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000100 Genomic DNA. Translation: ABB56428.1.
RefSeqYP_399415.1. NC_007604.1.

3D structure databases

ProteinModelPortalQ31R91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_0396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB56428; ABB56428; Synpcc7942_0396.
GeneID3774917.
KEGGsyf:Synpcc7942_0396.
PATRIC23785887. VBISynElo51371_0488.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSYNEL:SYNPCC7942_0396-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_SYNE7
AccessionPrimary (citable) accession number: Q31R91
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 56 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