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Q6FZK1 (PUR5_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. 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:BQ07380
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length361 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 – 361361Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000258334

Sequences

Sequence LengthMass (Da)Tools
Q6FZK1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 2C6FCAB9B2630DF7

FASTA36138,139
        10         20         30         40         50         60 
MSNQDLINCK SNSGLTYAKA GVDIDVGNAM VEKIKPFIRS TKRAGADVEI GGFGGLFDLK 

        70         80         90        100        110        120 
AAGFTDPILV AANDGVGTKL KIAIEVGIHD TVGIDLVAMC INDLLVQGAE PLFFLDYFAT 

       130        140        150        160        170        180 
GKLDPEQGAA IVSGIAVGCQ QAGAALIGGE TAEMPGMYAK GDYDLAGFAV GATERSALLP 

       190        200        210        220        230        240 
SKDLAEGDII LGLSSSGIHS NGFSLVRRIV QQSGLKWGDY APFNPQMNLG TALLTPTRIY 

       250        260        270        280        290        300 
VKSLLPIIKT YKGIKALAHI TGGGLPENIP RVLPSSLCAE INLSAIHVPP VFSWIAKQGK 

       310        320        330        340        350        360 
IEETEMLRTF NCGIGMVIIV AQHAVETITQ ILEMQGEIVT LLGILTKHPT KKILYKGVLH 


L 

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References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF26222.1.
RefSeqYP_032367.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6FZK1.
SMRQ6FZK1. Positions 55-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283165.BQ07380.

Proteomic databases

PRIDEQ6FZK1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAF26222; CAF26222; BQ07380.
GeneID2866350.
KEGGbqu:BQ07380.
PATRIC31952777. VBIBarQui58630_0809.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBQUI283165:GHZA-737-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_BARQU
AccessionPrimary (citable) accession number: Q6FZK1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 65 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