Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q24QH4 (PUR5_DESHY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:
Phosphoribosylformylglycinamidine cyclo-ligase

EC=6.3.3.1
Alternative name(s):
AIR synthase
AIRS
Phosphoribosyl-aminoimidazole synthetase
Gene names
Name:purM
Ordered Locus Names:DSY3929
OrganismDesulfitobacterium hafniense (strain Y51) [Complete proteome] [HAMAP]
Taxonomic identifier138119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. HAMAP-Rule MF_00741

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. HAMAP-Rule MF_00741

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00741.

Sequence similarities

Belongs to the AIR synthase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosylformylglycinamidine cyclo-ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000258350

Sequences

Sequence LengthMass (Da)Tools
Q24QH4 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: C8C584C7B542E497

FASTA33936,329
        10         20         30         40         50         60 
MGYSYRQAGV DIDAGNQAVE LMKPAVKRTV RPEVMGGLGG FGGLFALDLK KYPEPVLVSG 

        70         80         90        100        110        120 
TDGVGTKLKL AFQMNRHDTI GQDAVAMCVN DILVQGAEPL FFLDYLAVGK LVPERVAQVV 

       130        140        150        160        170        180 
GGIAKGCELA GCALIGGETA EMPGFYDEGE YDIAGFAVGA VNRPDLIDGS QIQAGDVLIG 

       190        200        210        220        230        240 
LPSSGFHSNG YSLVRKIFTP DLWEKNYPEL GETLGEALIR PTRIYVKTVL PLIESRKVLG 

       250        260        270        280        290        300 
MAHITGGGLT ENIPRILPEG LGIKIARSAW QVPALFTLLQ RLGEVEEAEM LRTFNMGIGF 

       310        320        330 
VLIVHPEDVD FIQTQLQAAG EKCFVLGEVS GQSEGVSYL 

« Hide

References

[1]"Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195."
Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., Inatomi K., Furukawa K., Inui M., Yukawa H.
J. Bacteriol. 188:2262-2274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y51.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008230 Genomic DNA. Translation: BAE85718.1.
RefSeqYP_520162.1. NC_007907.1.

3D structure databases

ProteinModelPortalQ24QH4.
SMRQ24QH4. Positions 3-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING138119.DSY3929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE85718; BAE85718; DSY3929.
GeneID3956418.
KEGGdsy:DSY3929.
PATRIC21676926. VBIDesHaf65307_4393.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAVIGKIEH.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycDHAF138119:GHT5-4001-MONOMER.
UniPathwayUPA00074; UER00129.

Family and domain databases

Gene3D3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPMF_00741_B. AIRS_B.
InterProIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMSSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsTIGR00878. purM. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR5_DESHY
AccessionPrimary (citable) accession number: Q24QH4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 18, 2006
Last modified: May 14, 2014
This is version 60 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