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Protein

Phosphoribosylformylglycinamidine synthase subunit PurQ

Gene

purQ

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.UniRule annotation

Catalytic activityi

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.UniRule annotation
L-glutamine + H2O = L-glutamate + NH3.UniRule annotation

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoribosylformylglycinamidine synthase subunit PurS (purS), Phosphoribosylformylglycinamidine synthase subunit PurQ (purQ), Phosphoribosylformylglycinamidine synthase subunit PurL (purL)
  2. Phosphoribosylformylglycinamidine cyclo-ligase (purM)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei85NucleophileUniRule annotation1
Active sitei193UniRule annotation1
Active sitei195UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthase subunit PurQUniRule annotation (EC:6.3.5.3UniRule annotation)
Short name:
FGAM synthaseUniRule annotation
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferase subunit IUniRule annotation
Short name:
FGAR amidotransferase IUniRule annotation
Short name:
FGAR-AT IUniRule annotation
Glutaminase PurQUniRule annotation (EC:3.5.1.2UniRule annotation)
Phosphoribosylformylglycinamidine synthase subunit IUniRule annotation
Gene namesi
Name:purQUniRule annotation
Ordered Locus Names:SH1889
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000543 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002527351 – 223Phosphoribosylformylglycinamidine synthase subunit PurQAdd BLAST223

Interactioni

Subunit structurei

Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.UniRule annotation

Protein-protein interaction databases

STRINGi279808.SH1889.

Structurei

3D structure databases

ProteinModelPortaliQ4L577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 223Glutamine amidotransferase type-1UniRule annotationAdd BLAST221

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105D21. Bacteria.
COG0047. LUCA.
HOGENOMiHOG000238240.
KOiK01952.
OMAiHAEGRFY.
OrthoDBiPOG091H0A3G.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00421. PurQ. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010075. PRibForGlyAmidine_synth_PurQ.
[Graphical view]
PIRSFiPIRSF001586. FGAM_synth_I. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01737. FGAM_synth_I. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4L577-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFAVLVFPG SNCDRDMYNA AIKSGAQADY VDYRETSLDG YDGVLIPGGF
60 70 80 90 100
SFGDYLRSGA MASVAPIINE VKRLANDGKP VLGVCNGFQI LTEIGLLPGA
110 120 130 140 150
LLHNDSHLFI SRNENLKIAN NQTPFTNLYG ENEIVVYPVA HGEGHYYCTD
160 170 180 190 200
DIYNELVENN QIILTYEDNP NGSHENIAGI VNKAGNVCGM MPHPERALEK
210 220
ILGTDSGVKL FEAMVNSWRE QNV
Length:223
Mass (Da):24,464
Last modified:August 2, 2005 - v1
Checksum:i2B9D79985DB7B1EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05198.1.
RefSeqiWP_011276162.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05198; BAE05198; SH1889.
GeneIDi24246221.
KEGGisha:SH1889.
PATRICi19619885. VBIStaHae67511_1865.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05198.1.
RefSeqiWP_011276162.1. NC_007168.1.

3D structure databases

ProteinModelPortaliQ4L577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279808.SH1889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE05198; BAE05198; SH1889.
GeneIDi24246221.
KEGGisha:SH1889.
PATRICi19619885. VBIStaHae67511_1865.

Phylogenomic databases

eggNOGiENOG4105D21. Bacteria.
COG0047. LUCA.
HOGENOMiHOG000238240.
KOiK01952.
OMAiHAEGRFY.
OrthoDBiPOG091H0A3G.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00421. PurQ. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010075. PRibForGlyAmidine_synth_PurQ.
[Graphical view]
PIRSFiPIRSF001586. FGAM_synth_I. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01737. FGAM_synth_I. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPURQ_STAHJ
AccessioniPrimary (citable) accession number: Q4L577
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: August 2, 2005
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.