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Q8F242 (PUR5_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:LA_2935
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length344 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.

Sequence caution

The sequence AAN50133.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 344344Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000148220

Sequences

Sequence LengthMass (Da)Tools
Q8F242 [UniParc].

Last modified November 28, 2003. Version 2.
Checksum: 266AF4D7F5C837EE

FASTA34437,761
        10         20         30         40         50         60 
MEEKITYKNA GVDTEKGREF IQKIKRNVES THGPRVIGGL GGFAGAYDVS VLKKYKHPIL 

        70         80         90        100        110        120 
LSGTDGVGTK IELARLLKIY NTIGIDLVAM CVNDILVCGG EPLFFLDYIA CGKLDPEKMD 

       130        140        150        160        170        180 
QIVSGIVQGC KMSNASLLGG ETAEHPGTMK EDEFDLAGFV VGAVEKDSMI DGSTIRSGDK 

       190        200        210        220        230        240 
ILGLESSGPH SNGFSLIRKL LLKEGKYLPT DPQQVKFLKD YALKPTRIYV SSILKLLQQV 

       250        260        270        280        290        300 
SVKGMVHITG GGYQENVPRI LPQGTQSKFF KEKIPSGYFF EKIKKDHKIE ELELFATFNM 

       310        320        330        340 
GIGYMVIVSE ENAELAKKIM ESSGEVVHEI GEIVSGNKEE VQFV 

« Hide

References

[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN50133.2. Different initiation.
RefSeqNP_713115.2. NC_004342.2.

3D structure databases

ProteinModelPortalQ8F242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LA2935.

Proteomic databases

PaxDbQ8F242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN50133; AAN50133; LA_2935.
GeneID1152277.
KEGGlil:LA_2935.
PATRIC22386700. VBILepInt91350_2914.

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAEFEMYRT.

Enzyme and pathway databases

BioCycLINT189518:GJBB-2372-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_LEPIN
AccessionPrimary (citable) accession number: Q8F242
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: May 14, 2014
This is version 76 of the entry and version 2 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