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A2S554 (PUR5_BURM9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:BMA10229_A1088
OrganismBurkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP]
Taxonomic identifier412022 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

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_1000046427

Sequences

Sequence LengthMass (Da)Tools
A2S554 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: BB25FAB317BCFFFA

FASTA35136,913
        10         20         30         40         50         60 
MNPPKSAPDA QGLSYRDAGV DIDAGDALVD KIKPFAKKTL RDGVLGGIGG FGALFEVPKK 

        70         80         90        100        110        120 
YREPVLVSGT DGVGTKLKLA FHLNKHDTVG QDLVAMSVND ILVQGAEPLF FLDYFACGKL 

       130        140        150        160        170        180 
DVETAATVVK GIATGCELAG CALIGGETAE MPGMYPDGEY DLAGFAVGAV EKSKIIDGST 

       190        200        210        220        230        240 
IAEGDVVLGL ASSGIHSNGF SLVRKIIERA NPDLSADFHG RSLADALMAP TRIYVKPLLA 

       250        260        270        280        290        300 
LMEKIAVKGM AHITGGGLVE NIPRVLRDGL TAELDQHAWP LPPLFQWLQQ HGGVADAEMH 

       310        320        330        340        350 
RVFNCGIGMA VIVSAADADD ALRQLADAGE QVWKIGTVRA SREGEAQTVV V 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000546 Genomic DNA. Translation: ABN03748.1.
RefSeqYP_001027073.1. NC_008836.1.

3D structure databases

ProteinModelPortalA2S554.
SMRA2S554. Positions 13-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING412022.BMA10229_A1088.

Proteomic databases

PRIDEA2S554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN03748; ABN03748; BMA10229_A1088.
GeneID4791130.
KEGGbml:BMA10229_A1088.
PATRIC19133128. VBIBurMal46188_3284.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAGEATCEV.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycBMAL412022:GJI8-1088-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_BURM9
AccessionPrimary (citable) accession number: A2S554
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: May 14, 2014
This is version 54 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