Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A9I602 (PUR5_BORPD)

Last modified November 3, 2009. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoribosylformylglycinamidine cyclo-ligase
    EC=6.3.3.1
Alternative name(s):
    AIRS
    Phosphoribosyl-aminoimidazole synthetase
    AIR synthase
Gene names
Name: purM
Ordered Locus Names: Bpet0825
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 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 MF_00741

Subcellular location

Cytoplasm By similarity.

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: InterPro

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 349349Phosphoribosylformylglycinamidine cyclo-ligase HAMAP MF_00741
PRO_1000192999

Sequences

Sequence LengthMass (Da)Tools
A9I602-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 2F64D7F655C13247

FASTA34936,336
        10         20         30         40         50         60 
MTTQPSAPLT YRDAGVDIDA GDALVDRIKP LAARTMRPGV LAGIGGFGAL FQVPGKYREP 

        70         80         90        100        110        120 
VLVSGTDGVG TKLRLAFEWN RHDTVGVDLV AMSVNDILVQ GAEPLFFLDY FACGKLSVDT 

       130        140        150        160        170        180 
AAAVVGGIAR GCELAGCALI GGETAEMPGM YPDGEYDLAG FAVGAVEKSA ILDGKSIQPG 

       190        200        210        220        230        240 
DVVLGLASSG AHSNGYSLVR KILDRAGARP DQDFHGQPLA DVVMAPTRIY VKQVLAALAA 

       250        260        270        280        290        300 
HTGGIKGLAH ITGGGLLDNV PRILQPGLSA RLHRDAWQMP QLFQWLQQQG GVADTEMHRV 

       310        320        330        340 
FNCGIGMVIV VDAAQADAVA ATLAAQGETV SRIGEIVAQK DGEAQTVVV 

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM902716 Genomic DNA. Translation: CAP41157.1.
RefSeqYP_001629428.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5819047.
GenomeReviewsGene locus Bpet0825 in contig AM902716_GR.
KEGGbpt:Bpet0825.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAVHGLAHI.

Family and domain databases

HAMAPMF_00741.
[Tree]
InterProIPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR004733. PurM_cligase.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00878. purM. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR5_BORPD
AccessionPrimary (citable) accession number: A9I602
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: November 3, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents