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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Thermosynechococcus elongatus (strain BP-1)
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

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 PurL (purL), Phosphoribosylformylglycinamidine synthase subunit PurQ (purQ)
  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 sitei48UniRule annotation1
Binding sitei51ATPUniRule annotation1
Binding sitei90ATPUniRule annotation1
Metal bindingi92Magnesium 1UniRule annotation1
Active sitei94Proton acceptorUniRule annotation1
Binding sitei115SubstrateUniRule annotation1
Metal bindingi116Magnesium 2UniRule annotation1
Binding sitei239SubstrateUniRule annotation1
Metal bindingi267Magnesium 2UniRule annotation1
Binding sitei499ATPUniRule annotation1
Binding sitei536ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Metal bindingi537Magnesium 1UniRule annotation1
Binding sitei539SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processPurine biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTELO197221:G1G3I-1711-MONOMER
UniPathwayi
UPA00074;UER00128

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthase subunit PurLUniRule annotation (EC:6.3.5.3UniRule annotation)
Short name:
FGAM synthaseUniRule annotation
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferase subunit IIUniRule annotation
Short name:
FGAR amidotransferase IIUniRule annotation
Short name:
FGAR-AT IIUniRule annotation
Glutamine amidotransferase PurLUniRule annotation
Phosphoribosylformylglycinamidine synthase subunit IIUniRule annotation
Gene namesi
Name:purLUniRule annotation
Ordered Locus Names:tlr1683
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001004961 – 761Phosphoribosylformylglycinamidine synthase subunit PurLAdd BLAST761

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi197221.tlr1683

Structurei

3D structure databases

ProteinModelPortaliQ8DIA7
SMRiQ8DIA7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni93 – 96Substrate bindingUniRule annotation4
Regioni311 – 313Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the FGAMS family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QIK Bacteria
COG0046 LUCA
HOGENOMiHOG000238227
KOiK01952
OMAiFIEPYQG
OrthoDBiPOG091H009J

Family and domain databases

Gene3Di3.30.1330.10, 2 hits
3.90.650.10, 4 hits
HAMAPiMF_00420 PurL_2, 1 hit
InterProiView protein in InterPro
IPR010074 PRibForGlyAmidine_synth_PurL
IPR010918 PurM-like_C_dom
IPR036676 PurM-like_C_sf
IPR016188 PurM-like_N
IPR036921 PurM-like_N_sf
PANTHERiPTHR43555 PTHR43555, 1 hit
PfamiView protein in Pfam
PF00586 AIRS, 2 hits
PF02769 AIRS_C, 2 hits
PIRSFiPIRSF001587 FGAM_synthase_II, 1 hit
SUPFAMiSSF55326 SSF55326, 2 hits
SSF56042 SSF56042, 2 hits
TIGRFAMsiTIGR01736 FGAM_synth_II, 1 hit

Sequencei

Sequence statusi: Complete.

Q8DIA7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQTPLVTEA EITAEGLKPQ EYTEIVRRLG RHPNRAELGM FGVMWSEHCC
60 70 80 90 100
YKNSRLLLKQ FPTQGPRVLV GPGENAGVVD LGDGLRLAFK IESHNHPSAI
110 120 130 140 150
EPFQGAATGV GGILRDIFTM GARPIALLNA LRFGDLKEAK TQQLVKGVVA
160 170 180 190 200
GIAHYGNCVG VPTVGGEVYF DPCYAGNPLV NAMALGLMET PEIVKSAASG
210 220 230 240 250
IGNPVLYVGS TTGRDGMGGA SFASAELTDE SMSDRPAVQV GDPFVEKCLI
260 270 280 290 300
EACLEAFQTG AVVAAQDMGA AGLTCSTSEM AAKGGVGIEL DLDKVPVREQ
310 320 330 340 350
GMVPYEFLLS ESQERMLFVA AQGREAELIE IFQRWGLQAV VVGRVIAEPL
360 370 380 390 400
VRVLYRGEVA AEVPARALAE ETPLYERECP KEPPAYVQQA RQWSVDQLPL
410 420 430 440 450
PARSPAEILL TLLATPSIAS KAWVYRQYDH EVQNNTLVFP GDGDAAVIRL
460 470 480 490 500
RGTAKGIAAT VDCPSRYVYL DPYEGGKAAV AEAARNLSCV GAEPLAVTDN
510 520 530 540 550
LNFGSPETPV GYWQLANACR GLAEACRALQ TPVTGGNVSL YNETIDSNGQ
560 570 580 590 600
PQPIYPTPVV GMVGLIADLQ RVVGQGWRAT GDAIYLLGLP LTTPLSDPRL
610 620 630 640 650
SLGGSEYLAQ IHGLVAGCPP QIDLDLEQRV QAVCRYGIQQ GWIASAHDLS
660 670 680 690 700
EGGLAVALAE SCLSGQRGAT IQLPEGTYPR WDALLFAEGG ARILVSVPPR
710 720 730 740 750
EQVAWEAYAQ AQLPNAWTRL GVVNGEDTEL CIDSCNNSPL IRVTIKELDL
760
AWRSPLPKYL D
Length:761
Mass (Da):81,412
Last modified:March 1, 2003 - v1
Checksum:iCA1224C86FF8CE64
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA Translation: BAC09235.1
RefSeqiNP_682473.1, NC_004113.1
WP_011057520.1, NC_004113.1

Genome annotation databases

EnsemblBacteriaiBAC09235; BAC09235; BAC09235
GeneIDi1010851
KEGGitel:tlr1683
PATRICifig|197221.4.peg.1764

Similar proteinsi

Entry informationi

Entry nameiPURL_THEEB
AccessioniPrimary (citable) accession number: Q8DIA7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: February 28, 2018
This is version 98 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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