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Q2S567 (PURQ_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoribosylformylglycinamidine synthase 1

EC=6.3.5.3
Alternative name(s):
Phosphoribosylformylglycinamidine synthase I
Short name=FGAM synthase I
Gene names
Name:purQ
Ordered Locus Names:SRU_0521
OrganismSalinibacter ruber (strain DSM 13855 / M31) [Reference proteome] [HAMAP]
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. HAMAP-Rule MF_00421

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 1/2. HAMAP-Rule MF_00421

Subunit structure

Heterodimer of two subunits, PurQ and PurL By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00421.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   DomainGlutamine amidotransferase
   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

glutamine metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosylformylglycinamidine synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 235235Phosphoribosylformylglycinamidine synthase 1 HAMAP-Rule MF_00421
PRO_0000252729

Regions

Domain5 – 235231Glutamine amidotransferase type-1

Sites

Active site881Nucleophile By similarity
Active site2051 By similarity
Active site2071 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S567 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: D385CC7DDCB51A30

FASTA23525,198
        10         20         30         40         50         60 
MSARFGVVVF PGSNCDHDAY HAAHDVFDQE ARFIWHEEAS LGDVDVVIVP GGFSYGDYLR 

        70         80         90        100        110        120 
SGAVARFSPI MQDVVRFAED GGLVFGICNG FQVLCEAGLL PGTLMRNESL RFVCKDTPLR 

       130        140        150        160        170        180 
VENAGTPFTN ALTEGQVITI PVSHGEGRYY ADEDVLARIE ANDQVLLRYS TADGAVTDEA 

       190        200        210        220        230 
NPNGSVHGIA GLVNEAGNVC GLMPHPERCV ESLLGGDDGR LIFESLLNHV SIVAA 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC43823.1.
RefSeqYP_444664.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S567.
ModBaseSearch...

Protein-protein interaction databases

STRING309807.SRU_0521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC43823; ABC43823; SRU_0521.
GeneID3851519.
KEGGsru:SRU_0521.
PATRIC23423387. VBISalRub86502_0543.

Phylogenomic databases

eggNOGCOG0047.
HOGENOMHOG000238240.
KOK01952.
OMAFPGTNCD.
PhylomeDBQ2S567.
ProtClustDBCLSK2773662.

Enzyme and pathway databases

BioCycSRUB309807:GJJD-520-MONOMER.
UniPathwayUPA00074; UER00128.

Family and domain databases

HAMAPMF_00421. PurQ.
InterProIPR017926. GATASE.
IPR010075. PRibForGlyAmidine_synth_I.
[Graphical view]
PIRSFPIRSF001586. FGAM_synth_I. 1 hit.
TIGRFAMsTIGR01737. FGAM_synth_I. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURQ_SALRD
AccessionPrimary (citable) accession number: Q2S567
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 24, 2006
Last modified: May 29, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families