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Q3J517 (PUR5_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. 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:RHOS4_05490
ORF Names:RSP_1969
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length348 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
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 – 348348Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000258393

Sequences

Sequence LengthMass (Da)Tools
Q3J517 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: E43B6EC870FF8225

FASTA34835,762
        10         20         30         40         50         60 
MAEQQKGLTY ADAGVDIDAG NALVERIKPA AKRTARPGTV SGLGGFGALF DLKAAGYQDP 

        70         80         90        100        110        120 
VLVAATDGVG TKLRIAIDTG EVDTIGIDLV AMCVNDLVCQ GAEPLFFLDY FATGKLEVAQ 

       130        140        150        160        170        180 
AARIIEGIAE GCAASGCALI GGETAEMPGM YHKGDFDLAG FAVGAMERGA DLPQGVAEGD 

       190        200        210        220        230        240 
LLLGLGSNGV HSNGYSFVRK VVELSGLGWD APAPFGGDSL GRALLAPTRL YVKQALAAVR 

       250        260        270        280        290        300 
AGGVHALAHI TGGGLTENLP RVLPKGLGAR IDLSAWELPP VFRWLAETAS MAEPELLKTF 

       310        320        330        340 
NCGIGMIVVV AADRADEIAA LLAAEGETVT RIGEVIAGEG VSYDGRLL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000143 Genomic DNA. Translation: ABA78117.1.
RefSeqYP_352018.1. NC_007493.2.

3D structure databases

ProteinModelPortalQ3J517.
SMRQ3J517. Positions 7-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272943.RSP_1969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA78117; ABA78117; RSP_1969.
GeneID3719300.
KEGGrsp:RSP_1969.
PATRIC23150920. VBIRhoSph57909_0857.

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229091.
KOK01933.
OMAGEATCEV.
OrthoDBEOG61CM1V.
PhylomeDBQ3J517.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-568-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_RHOS4
AccessionPrimary (citable) accession number: Q3J517
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 8, 2005
Last modified: July 9, 2014
This is version 60 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