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Protein

Phosphoribosylformylglycinamidine synthase subunit PurQ

Gene

purQ

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Status
Reviewed-Annotation score: -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 + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(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 PurL (purL), 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 sitei87NucleophileUniRule annotation1
Active sitei195UniRule annotation1
Active sitei197UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Ligase
Biological processPurine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZMOB264203:G1FZK-1384-MONOMER
UniPathwayi
UPA00074;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:ZMO1532
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001006041 – 221Phosphoribosylformylglycinamidine synthase subunit PurQAdd BLAST221

Proteomic databases

PRIDEiQ5NMA4

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ5NMA4
SMRiQ5NMA4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 221Glutamine amidotransferase type-1UniRule annotationAdd BLAST219

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

HOGENOMiHOG000238240
KOiK01952
OMAiNCDRDVA

Family and domain databases

Gene3Di3.40.50.880, 1 hit
HAMAPiMF_00421 PurQ, 1 hit
InterProiView protein in InterPro
IPR029062 Class_I_gatase-like
IPR017926 GATASE
IPR010075 PRibForGlyAmidine_synth_PurQ
PIRSFiPIRSF001586 FGAM_synth_I, 1 hit
SUPFAMiSSF52317 SSF52317, 1 hit
TIGRFAMsiTIGR01737 FGAM_synth_I, 1 hit
PROSITEiView protein in PROSITE
PS51273 GATASE_TYPE_1, 1 hit

Sequencei

Sequence statusi: Complete.

Q5NMA4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKAAVLVFPG SNCDRDLAVA IEKICGTKPL MVWHQESELP DDLDLIAVPG
60 70 80 90 100
GFSYGDYLRS GAMAARSAVM PAVIKQAERG VPVLGICNGF QILTEAGLLP
110 120 130 140 150
GALMRNAGLS FICRNVGLEI QNTTSPFLRL YKKNQKIHLP VAHHDGNYTA
160 170 180 190 200
DEATLDQLED EDRVALRYTE SVNGSARNIA GVLNKKGNVL GLMPHPERMI
210 220
EDAHGGKDGY NMFASLMQVM A
Length:221
Mass (Da):23,952
Last modified:February 1, 2005 - v1
Checksum:i68CEC688EC270603
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008692 Genomic DNA Translation: AAV90156.1
RefSeqiWP_011241302.1, NZ_CP023715.1

Genome annotation databases

EnsemblBacteriaiAAV90156; AAV90156; ZMO1532
KEGGizmo:ZMO1532

Similar proteinsi

Entry informationi

Entry nameiPURQ_ZYMMO
AccessioniPrimary (citable) accession number: Q5NMA4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 1, 2005
Last modified: July 18, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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