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Q0IDE8 (PUR9_SYNS3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:sync_0289
OrganismSynechococcus sp. (strain CC9311) [Complete proteome] [HAMAP]
Taxonomic identifier64471 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length529 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 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018980

Sequences

Sequence LengthMass (Da)Tools
Q0IDE8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 01579B74B08DD49E

FASTA52955,772
        10         20         30         40         50         60 
MAPTALLSVS DKRGVVPLAE ALHRLHGYQL LSSGGTAKVL QEAGLPVTRV ADHTGAPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR IHGGILARRG DPAHEADLLE QQIDPIDVVV VNLYPFRETV ATPDVSWDAA 

       130        140        150        160        170        180 
IENIDIGGPT MVRSAAKNHA HVAVLTSPEQ YDRFLKALSG SAGGVNANVR RQLALEAFAH 

       190        200        210        220        230        240 
TAAYDVAISR WMQSRPELQP DVEAAAPAEA LPWLEALPLR QTLRYGENPH QKAAWFSSPM 

       250        260        270        280        290        300 
GWGGAKQLQG KALSTNNLLD LEAALATVRE FGYGSSGLHP AQQAAAVVVK HTNPCGVAVG 

       310        320        330        340        350        360 
DGVGIALTRA LDGDRISAFG GIVALNAVVD GPAAKELTSL FLECVVAPGY SSEALEILAA 

       370        380        390        400        410        420 
KGNLRLLELP PEAIDAAPKD HVRSILGGVL VQDLDDQPID PSAWTVASQR QPTTAETADL 

       430        440        450        460        470        480 
RFAWQLVRHV RSNAILVARD GQSLGVGAGQ MNRVGSARIA LEAAGEQAVG AVLASDGFFP 

       490        500        510        520 
FDDTVRLAAS HGIKAVIHPG GSLRDADSIK ACDELGLAMV LTGRRHFLH 

« Hide

References

[1]"Genome sequence of Synechococcus CC9311: insights into adaptation to a coastal environment."
Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R., Paulsen I.T.
Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000435 Genomic DNA. Translation: ABI46591.1.
RefSeqYP_729524.1. NC_008319.1.

3D structure databases

ProteinModelPortalQ0IDE8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64471.sync_0289.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI46591; ABI46591; sync_0289.
GeneID4259254.
KEGGsyg:sync_0289.
PATRIC23791432. VBISynSp88089_0299.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSSP64471:GIVP-289-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_SYNS3
AccessionPrimary (citable) accession number: Q0IDE8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 59 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