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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 PurL (purL), Phosphoribosylformylglycinamidine synthase subunit PurQ (purQ), Phosphoribosylformylglycinamidine synthase subunit PurS (purS)
  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 sitei41UniRule annotation1
Active sitei87Proton acceptorUniRule annotation1
Binding sitei108SubstrateUniRule annotation1
Binding sitei109ATP1
Binding sitei211Substrate; via carbonyl oxygenUniRule annotation1
Binding sitei231SubstrateUniRule annotation1
Metal bindingi430Magnesium1 Publication1
Metal bindingi472Magnesium1 Publication1
Binding sitei485ATP1
Binding sitei525SubstrateCurated1
Metal bindingi620Magnesium1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 67ATP2
Nucleotide bindingi83 – 85ATP3
Nucleotide bindingi522 – 523ATP2

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:TTHA1519
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 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_00001005031 – 725Phosphoribosylformylglycinamidine synthase subunit PurLAdd BLAST725

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

STRINGi300852.TTHA1519.

Structurei

Secondary structure

1725
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 7Combined sources6
Helixi12 – 22Combined sources11
Helixi28 – 37Combined sources10
Helixi40 – 43Combined sources4
Turni45 – 47Combined sources3
Helixi48 – 51Combined sources4
Beta strandi61 – 63Combined sources3
Beta strandi67 – 75Combined sources9
Beta strandi78 – 86Combined sources9
Helixi88 – 93Combined sources6
Helixi95 – 112Combined sources18
Beta strandi116 – 127Combined sources12
Helixi132 – 152Combined sources21
Beta strandi156 – 163Combined sources8
Helixi165 – 167Combined sources3
Beta strandi168 – 170Combined sources3
Beta strandi172 – 182Combined sources11
Helixi183 – 185Combined sources3
Beta strandi196 – 202Combined sources7
Helixi235 – 250Combined sources16
Beta strandi254 – 259Combined sources6
Helixi264 – 275Combined sources12
Beta strandi278 – 283Combined sources6
Helixi284 – 286Combined sources3
Beta strandi289 – 293Combined sources5
Helixi296 – 301Combined sources6
Beta strandi305 – 312Combined sources8
Helixi317 – 326Combined sources10
Beta strandi331 – 347Combined sources17
Beta strandi350 – 356Combined sources7
Helixi357 – 361Combined sources5
Helixi374 – 380Combined sources7
Helixi391 – 399Combined sources9
Turni402 – 404Combined sources3
Helixi408 – 411Combined sources4
Beta strandi420 – 424Combined sources5
Beta strandi430 – 436Combined sources7
Beta strandi439 – 448Combined sources10
Helixi451 – 456Combined sources6
Helixi458 – 475Combined sources18
Beta strandi479 – 488Combined sources10
Beta strandi492 – 494Combined sources3
Helixi495 – 515Combined sources21
Beta strandi519 – 525Combined sources7
Beta strandi538 – 548Combined sources11
Beta strandi554 – 556Combined sources3
Beta strandi563 – 568Combined sources6
Helixi578 – 584Combined sources7
Helixi596 – 611Combined sources16
Beta strandi616 – 620Combined sources5
Helixi625 – 634Combined sources10
Turni635 – 637Combined sources3
Beta strandi641 – 644Combined sources4
Helixi650 – 653Combined sources4
Beta strandi661 – 665Combined sources5
Helixi667 – 669Combined sources3
Helixi670 – 679Combined sources10
Beta strandi684 – 690Combined sources7
Beta strandi692 – 699Combined sources8
Beta strandi702 – 707Combined sources6
Helixi708 – 723Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VIUX-ray2.35A1-725[»]
ProteinModelPortaliQ5SMH8.
SMRiQ5SMH8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SMH8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni86 – 89Substrate bindingCurated4
Regioni303 – 305Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the FGAMS family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108JIU. Bacteria.
COG0046. LUCA.
HOGENOMiHOG000238227.
KOiK01952.
OMAiVMWQFAE.
PhylomeDBiQ5SMH8.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
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.

Q5SMH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEALAKEIGI PEGEYREIVQ RLGREPNRVE LLLFKVMWSE HCAYKNSRPL
60 70 80 90 100
LKALPKEGEA VLQGPGENAG VVRVGEGWAV AFKIESHNHP SAVEPFQGAA
110 120 130 140 150
TGVGGILRDI MSMGARPIAL LDSLRFGPPE EARSRYLLKG VVSGIAFYGN
160 170 180 190 200
AIGVPTVGGD LYFHEGYREN PLVNAMCLGL LREEHLKRSR ASLGRPIYYA
210 220 230 240 250
GAKTGRDGIG GAAFASRELK EEKAEDRPAV QVGDPFLGKL LMEATLEAIE
260 270 280 290 300
LDLVEGVQDM GAAGLTSSLS ELAHKSGLGV ELHLDLVPTR EEGMTPEELL
310 320 330 340 350
LSESQERMVL VPKEGKEKAL EEVFGRWGLD CVPVARTIPE RVFRVLFRGE
360 370 380 390 400
VVAEVPTEAL AEAPTYVRVG REDPEVRRLR ETPIPPLEAD PQEVLRRLLA
410 420 430 440 450
SPNLASREAV YERYDHQVGT RTALLPGKGD AAVLWIKGTR LGVAAKVDQN
460 470 480 490 500
PRYSRLHPRL GAMHALAEAC RNVSVVGAKP LAYTDGLNLG SPETPEGYHE
510 520 530 540 550
LAETIAGLKE ASEALGVPVV SGNVSLYNES GGKRIPPTAM VGVVGVLEVD
560 570 580 590 600
KRAEMGFRRP GEVLLLIGEE RGELGASEVL YLLTGKEFGH PPRLDLGREK
610 620 630 640 650
AVQEAIRDLI QRGLTRTAHD VAEGGLLLAL AEMTFPYGVG ATVEVREEGL
660 670 680 690 700
EALFGEAPSR VLFTVEKTRL QEATLLLEER GLPYRVLGET GGKSLTVLTP
710 720
GGVLEWSLEE LLSAWKAPLR EVLDG
Length:725
Mass (Da):78,643
Last modified:December 21, 2004 - v1
Checksum:iC5CC5FAE833F0199
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71342.1.
RefSeqiWP_011173566.1. NC_006461.1.
YP_144785.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71342; BAD71342; BAD71342.
GeneIDi3168862.
KEGGittj:TTHA1519.
PATRICi23957999. VBITheThe93045_1494.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71342.1.
RefSeqiWP_011173566.1. NC_006461.1.
YP_144785.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VIUX-ray2.35A1-725[»]
ProteinModelPortaliQ5SMH8.
SMRiQ5SMH8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1519.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71342; BAD71342; BAD71342.
GeneIDi3168862.
KEGGittj:TTHA1519.
PATRICi23957999. VBITheThe93045_1494.

Phylogenomic databases

eggNOGiENOG4108JIU. Bacteria.
COG0046. LUCA.
HOGENOMiHOG000238227.
KOiK01952.
OMAiVMWQFAE.
PhylomeDBiQ5SMH8.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.

Miscellaneous databases

EvolutionaryTraceiQ5SMH8.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
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_THET8
AccessioniPrimary (citable) accession number: Q5SMH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 87 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.