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

Q8G595 (PUR5_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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:BL1122
OrganismBifidobacterium longum (strain NCC 2705) [Reference proteome] [HAMAP]
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length345 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
Reference 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 – 345345Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000148198

Sequences

Sequence LengthMass (Da)Tools
Q8G595 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4A48C60D24891797

FASTA34536,002
        10         20         30         40         50         60 
MPKAYENAGV SVEAGYEVVK RIKSHVARTN RPGVVGGIGG FGGLFDLASL GYKEPVLISG 

        70         80         90        100        110        120 
TDGVGTKLMV AKLANKHDTI GIDCVAMCVN DIAAQGAEPL FFLDYIACGK NDPALLEQVV 

       130        140        150        160        170        180 
AGVADGCVQA GSALVGGETA EMPGMYDEDE YDLAGFSVGV AEKSAIVDGS TIAEGDVLIG 

       190        200        210        220        230        240 
LPSTGVHSNG FSLVRKALFE QAGYTVDTEL DELGGEKLGD VLLTPTKIYV KALSPLFKAG 

       250        260        270        280        290        300 
VVKGVAHITG GGFIENIPRM IPDGLAAEIE LGTWPVLPIF DVLEKAGNID HKEMYNIFNM 

       310        320        330        340 
GIGMVLAIDP ARKDEALKLL ADNNEPAYVL GSITADTTGT QIVLK 

« Hide

References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014295 Genomic DNA. Translation: AAN24929.1.
RefSeqNP_696293.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G595.
SMRQ8G595. Positions 13-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING206672.BL1122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN24929; AAN24929; BL1122.
GeneID1022669.
KEGGblo:BL1122.
PATRIC21118737. VBIBifLon107831_0832.

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAHCVNDIL.
OrthoDBEOG61CM1V.
ProtClustDBPRK05385.

Enzyme and pathway databases

BioCycBLON206672:GI1E-790-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_BIFLO
AccessionPrimary (citable) accession number: Q8G595
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 69 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