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Protein

Phosphoribosylformylglycinamidine synthase subunit PurQ

Gene

purQ

Organism
Geobacillus kaustophilus (strain HTA426)
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 PurQ (purQ), Phosphoribosylformylglycinamidine synthase subunit PurS (purS), 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861NucleophileUniRule annotation
Active sitei195 – 1951UniRule annotation
Active sitei197 – 1971UniRule annotation

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

BioCyciGKAU235909:GJO7-313-MONOMER.
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:GK0262
OrganismiGeobacillus kaustophilus (strain HTA426)
Taxonomic identifieri235909 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
Proteomesi
  • UP000001172 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228228Phosphoribosylformylglycinamidine synthase subunit PurQPRO_0000100554Add
BLAST

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

STRINGi235909.GK0262.

Structurei

3D structure databases

ProteinModelPortaliQ5L3D3.
SMRiQ5L3D3. Positions 1-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 226223Glutamine amidotransferase type-1UniRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105D21. Bacteria.
COG0047. LUCA.
HOGENOMiHOG000238240.
KOiK01952.
OMAiHAEGRFY.
OrthoDBiEOG6P5ZJP.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00421. PurQ.
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.

Q5L3D3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFAVVVFPG SNCDVDMYHA IADELGEEVE YVWHDEDNLD RFDAVLLPGG
60 70 80 90 100
FSYGDYLRSG AIARFSKVMA AVKKAAEAGK PVLGVCNGFQ ILLEAGLLPG
110 120 130 140 150
AMRRNQGLKF ICRPVQLTVE NHETMFTSAY EKGEVITIPI AHGEGNYYCD
160 170 180 190 200
EQTLERLVEN RQIVFRYHGE NPNGSLADIA GIVNEQGNVL GMMPHPERAV
210 220
DALLGSADGL KLFRSIVNYW RETHVVTA
Length:228
Mass (Da):25,209
Last modified:February 1, 2005 - v1
Checksum:i5B67F86E9A0DF4B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD74547.1.
RefSeqiWP_011229771.1. NC_006510.1.

Genome annotation databases

EnsemblBacteriaiBAD74547; BAD74547; GK0262.
GeneIDi3186489.
KEGGigka:GK0262.
PATRICi21961668. VBIGeoKau81518_0330.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD74547.1.
RefSeqiWP_011229771.1. NC_006510.1.

3D structure databases

ProteinModelPortaliQ5L3D3.
SMRiQ5L3D3. Positions 1-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi235909.GK0262.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD74547; BAD74547; GK0262.
GeneIDi3186489.
KEGGigka:GK0262.
PATRICi21961668. VBIGeoKau81518_0330.

Phylogenomic databases

eggNOGiENOG4105D21. Bacteria.
COG0047. LUCA.
HOGENOMiHOG000238240.
KOiK01952.
OMAiHAEGRFY.
OrthoDBiEOG6P5ZJP.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
BioCyciGKAU235909:GJO7-313-MONOMER.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00421. PurQ.
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...

Publicationsi

  1. "Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
    Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
    Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HTA426.

Entry informationi

Entry nameiPURQ_GEOKA
AccessioniPrimary (citable) accession number: Q5L3D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 1, 2005
Last modified: November 11, 2015
This is version 83 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, Reference 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.