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Q5QUP9 (PUR5_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. 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:IL1661
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length351 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 – 351351Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000258361

Sequences

Sequence LengthMass (Da)Tools
Q5QUP9 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 2C0488856A4F362C

FASTA35137,425
        10         20         30         40         50         60 
MSDKKPSLSY KDAGVDIDAG NALVERIKGV TKRTHRPEVM GNIGGFGALC EIPAGYKQPV 

        70         80         90        100        110        120 
LVSGTDGVGT KLRLAIDLKR HRGVGIDLVA MCVNDLIVQG AEPLFFLDYY ATGKLDVDVA 

       130        140        150        160        170        180 
ADVVAGIGDG CEQSGCALIG GETAEMPGMY EGGDYDLAGF CTGVVEKSEI IDGTKVADGD 

       190        200        210        220        230        240 
ALIALASSGP HSNGYSLIRK IIEVSGADLE SHLQGKTLAD HLLEPTRIYV KPVLELIKHV 

       250        260        270        280        290        300 
PVHALSHITG GGFWENIPRV LPKGSKAVID GNSWDWPVIF DWLKENGNIS MKEMYRTFNC 

       310        320        330        340        350 
GVGMVIAVPN EQADKAIQIL TDAGEDAWKI GRIANAAEGE EQVDILADET H 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV82494.1.
RefSeqYP_156043.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QUP9.
SMRQ5QUP9. Positions 7-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL1661.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV82494; AAV82494; IL1661.
GeneID3172382.
KEGGilo:IL1661.
PATRIC22141410. VBIIdiLoi21852_1667.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229091.
KOK01933.
OMAVIGKIEH.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycILOI283942:GI0U-1669-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_IDILO
AccessionPrimary (citable) accession number: Q5QUP9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 63 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