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

B5ZX12 (PUR5_RHILW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:Rleg2_1095
OrganismRhizobium leguminosarum bv. trifolii (strain WSM2304) [Complete proteome] [HAMAP]
Taxonomic identifier395492 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length357 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 – 357357Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_1000193038

Sequences

Sequence LengthMass (Da)Tools
B5ZX12 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: EF62B0EB4985808E

FASTA35736,581
        10         20         30         40         50         60 
MSQSGKNGLT YSDAGVDIDA GNLLVEKIKP AVRSTRRPGA DGEIGGFGGL FDLKAAGFND 

        70         80         90        100        110        120 
PVLVAANDGV GTKLKIAIDA DYHDTVGIDL VAMCVNDLVV QGAEPLFFLD YFATGKLDPD 

       130        140        150        160        170        180 
QGAAIVGGIA AGCRQAGCAL IGGETAEMPG MYSSGDYDLA GFAVGAAERG KLLPSGDIAE 

       190        200        210        220        230        240 
GDVILGLASS GVHSNGFSLV RKIVELSGLG WDAPAPFASD KKLGEALLEP TRIYVKPLLK 

       250        260        270        280        290        300 
AIRETGAIKA LAHITGGGFP ENIPRVLPKH LAAEIDLAAV KAPPVFSWLA RTGGVETKEM 

       310        320        330        340        350 
LRTFNCGVGM IAVVASENVA AVSAALEAEG ETVVTLGRMI ARDEGAAGTV YQGTLAL 

« Hide

References

[1]"Complete sequence of chromosome of Rhizobium leguminosarum bv. trifolii WSM2304."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Yates R. expand/collapse author list , Ardley J., Tiwari R.P., O'Hara G., Howieson J., Brau L., Reeve W.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WSM2304.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001191 Genomic DNA. Translation: ACI54389.1.
RefSeqYP_002280615.1. NC_011369.1.

3D structure databases

ProteinModelPortalB5ZX12.
SMRB5ZX12. Positions 8-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395492.Rleg2_1095.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI54389; ACI54389; Rleg2_1095.
GeneID6979814.
KEGGrlt:Rleg2_1095.
PATRIC23126128. VBIRhiLeg95088_2906.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAEFEMYRT.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycRLEG395492:GJB3-1105-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_RHILW
AccessionPrimary (citable) accession number: B5ZX12
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: May 14, 2014
This is version 42 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