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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Mycobacterium leprae (strain TN)
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

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 (ML2219.1)
  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 sitei54UniRule annotation1
Binding sitei57ATPUniRule annotation1
Binding sitei101ATPUniRule annotation1
Metal bindingi103Magnesium 1UniRule annotation1
Active sitei105Proton acceptorUniRule annotation1
Binding sitei126SubstrateUniRule annotation1
Metal bindingi127Magnesium 2UniRule annotation1
Binding sitei252SubstrateUniRule annotation1
Metal bindingi280Magnesium 2UniRule annotation1
Binding sitei512ATPUniRule annotation1
Binding sitei549ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Metal bindingi550Magnesium 1UniRule annotation1
Binding sitei552SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00074; 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:ML2211
ORF Names:MLCB5.30
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML2211.

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_00001004711 – 754Phosphoribosylformylglycinamidine synthase subunit PurLAdd BLAST754

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

STRINGi272631.ML2211.

Structurei

3D structure databases

ProteinModelPortaliQ50023.
SMRiQ50023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni104 – 107Substrate bindingUniRule annotation4
Regioni324 – 326Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the FGAMS family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108JIU. Bacteria.
COG0046. LUCA.
HOGENOMiHOG000238227.
KOiK01952.
OMAiVMWQFAE.
OrthoDBiPOG091H009J.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.90.650.10. 1 hit.
HAMAPiMF_00420. PurL_2. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR010074. PRibForGlyAmidine_synth_PurL.
IPR016188. PurM-like_N.
[Graphical view]
PfamiPF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
[Graphical view]
PIRSFiPIRSF001587. FGAM_synthase_II. 1 hit.
SUPFAMiSSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01736. FGAM_synth_II. 1 hit.

Sequencei

Sequence statusi: Complete.

Q50023-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDTVEYAAT TPDQPQPFAE LGLREDEYQR VREILGRRPT DTELAMYSVM
60 70 80 90 100
WSEHCSYKSS KVHLRYFGET TTEEMRTGML AGIGENAGVV DIGDGWAVTF
110 120 130 140 150
KVESHNHPSY VEPYQGAATG VGGIVRDIMA MGARPVAVMD QLRFGAADAL
160 170 180 190 200
DTRRVLDGVV RGIGGYGNSL GLPNIGGETV FDSCYDGNPL VNALCVGVLR
210 220 230 240 250
QEDLHLAFAS GAGNKIILFG ACTGLDGIGG VSVLASDTFD AEGARKKLPS
260 270 280 290 300
VQVGDPFMEK VLIECCLELY AGGLVIGIQD LGGAGLSCAT SELASAGDVG
310 320 330 340 350
MAIQLDTVPR RAKDMTPAEV FCSESQERMC AVVAPENVDA FLAVCRKWEV
360 370 380 390 400
LATVIGEVTD GDRLRITWHG ETVVDVPPRT VAHEGPVYQR PVSRPESQEA
410 420 430 440 450
LNADSSKGLP RPVSGDELRA TLLALLGSPH LCSRAFITEQ YDRYVRGNTV
460 470 480 490 500
LAEHADAGVL RIDESTGRGI ALSTDASGRY TRLDPYAGAQ LALAEAYRNV
510 520 530 540 550
AVTGATPVAV TNCLNFGSPE DPGVMWQFAQ AVRGLADGCA ALKIPVTGGN
560 570 580 590 600
VSFYNQTGAV AILPTPVVGV LGVLDNVARR IHTSLGTEPG EILMLLGDTY
610 620 630 640 650
DEFDGSVWAQ VMAGHLGGLP PMVDLAREKL LAEVLSSASR DELVSAAHDL
660 670 680 690 700
SEGGLAQAIV ESALAGETGC RIALPEDADP FVMLFSESAG RVLVAVPRPE
710 720 730 740 750
ESRFRSMCEA RGLPAMRIGV VDQGSDSIEV RGQFTVSLAE LRMTFEAVLP

RFFG
Length:754
Mass (Da):80,131
Last modified:November 1, 1996 - v1
Checksum:iAEC969914F0C9ECB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15182 Genomic DNA. Translation: AAA62986.1.
Z95151 Genomic DNA. Translation: CAB08431.1.
AL583924 Genomic DNA. Translation: CAC31166.1.
PIRiF87185.
RefSeqiNP_302451.1. NC_002677.1.
WP_010908771.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31166; CAC31166; CAC31166.
GeneIDi908524.
KEGGimle:ML2211.
PATRICi18058535. VBIMycLep78757_4186.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15182 Genomic DNA. Translation: AAA62986.1.
Z95151 Genomic DNA. Translation: CAB08431.1.
AL583924 Genomic DNA. Translation: CAC31166.1.
PIRiF87185.
RefSeqiNP_302451.1. NC_002677.1.
WP_010908771.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ50023.
SMRiQ50023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML2211.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC31166; CAC31166; CAC31166.
GeneIDi908524.
KEGGimle:ML2211.
PATRICi18058535. VBIMycLep78757_4186.

Organism-specific databases

LepromaiML2211.

Phylogenomic databases

eggNOGiENOG4108JIU. Bacteria.
COG0046. LUCA.
HOGENOMiHOG000238227.
KOiK01952.
OMAiVMWQFAE.
OrthoDBiPOG091H009J.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.90.650.10. 1 hit.
HAMAPiMF_00420. PurL_2. 1 hit.
InterProiIPR010918. AIR_synth_C_dom.
IPR010074. PRibForGlyAmidine_synth_PurL.
IPR016188. PurM-like_N.
[Graphical view]
PfamiPF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
[Graphical view]
PIRSFiPIRSF001587. FGAM_synthase_II. 1 hit.
SUPFAMiSSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01736. FGAM_synth_II. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPURL_MYCLE
AccessioniPrimary (citable) accession number: Q50023
Secondary accession number(s): O05759
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 110 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.