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Q7V9S9 (PUR5_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:Pro_1745
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length345 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 – 345345Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000148230

Sequences

Sequence LengthMass (Da)Tools
Q7V9S9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 36654B43A3A8278C

FASTA34537,122
        10         20         30         40         50         60 
MDYKSAGVNV EAGRAFVNRI KASVESTSRP EVIGGIGGFG GFMRLPRGLE KPVLVSGTDG 

        70         80         90        100        110        120 
VGTKLELAQD YGSHYGVGID LVAMCVNDVI TSGAEPLFFL DYIATGKLTP EALTEVIEGI 

       130        140        150        160        170        180 
AEGCNQSKCS LLGGETAEMP GFYSDGRYDL AGFCVAVVEE NKIINGSKIK VGDQIIGIKS 

       190        200        210        220        230        240 
NGFHSNGFSL IRKVVKLAGV NEKSCFGSRK VPLIDYLLKP TQLYVHLVQA LLQANLPVKG 

       250        260        270        280        290        300 
MAHITGGGLP ENLPRCLPDG LAASIDRNNW EEPSIYKWLR NEGDIPESDL WNTFNFGIGF 

       310        320        330        340 
CLVVSPDQSK DLIDMCSANG FVAWNIGQVE EQPKQMQSRI VGLPT 

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAQ00789.1.
RefSeqNP_876136.1. NC_005042.1.

3D structure databases

ProteinModelPortalQ7V9S9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro1745.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ00789; AAQ00789; Pro_1745.
GeneID1463127.
KEGGpma:Pro_1745.
PATRIC23030331. VBIProMar8617_1843.

Phylogenomic databases

eggNOGCOG0150.
KOK01933.
OMAEFEMYRT.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-1786-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_PROMA
AccessionPrimary (citable) accession number: Q7V9S9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 69 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