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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
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 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 sitei81UniRule annotation1
Binding sitei84ATPUniRule annotation1
Binding sitei123ATPUniRule annotation1
Metal bindingi125Magnesium 1UniRule annotation1
Active sitei127Proton acceptorUniRule annotation1
Binding sitei148SubstrateUniRule annotation1
Metal bindingi149Magnesium 2UniRule annotation1
Binding sitei272SubstrateUniRule annotation1
Metal bindingi300Magnesium 2UniRule annotation1
Binding sitei525ATPUniRule annotation1
Binding sitei562ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Metal bindingi563Magnesium 1UniRule annotation1
Binding sitei565SubstrateUniRule 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

BioCyciAGRO:ATU1850-MONOMER.
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:Atu1850
ORF Names:AGR_C_3393
OrganismiAgrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Taxonomic identifieri176299 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
Proteomesi
  • UP000000813 Componenti: Chromosome circular

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_00001004291 – 775Phosphoribosylformylglycinamidine synthase subunit PurLAdd BLAST775

Proteomic databases

PRIDEiQ8UEB0.

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

STRINGi176299.Atu1850.

Structurei

3D structure databases

ProteinModelPortaliQ8UEB0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 129Substrate bindingUniRule annotation4
Regioni344 – 346Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the FGAMS family.UniRule annotation

Phylogenomic databases

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

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.

Q8UEB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVKLRIFLS HGEASCAKEP ETFLGSNRVR PMSISNSIKI TPELVASHGL
60 70 80 90 100
KPDEYQRILD LIGREPSFTE LGIFSAMWNE HCSYKSSKKW LKTLPTTGPR
110 120 130 140 150
VIQGPGENAG VVDIDDGDCV VFKMESHNHP SYIEPYQGAA TGVGGILRDV
160 170 180 190 200
FTMGARPIAA MNALRFGAPD HPKTRHLVAG VVAGVGGYGN SFGVPTVGGE
210 220 230 240 250
VEFDPRYNGN ILVNAFAAGL AKSNAIFLSE AKGVGLPVVY LGAKTGRDGV
260 270 280 290 300
GGATMASAEF DESIEEKRPT VQVGDPFTEK CLLEACLELM KTGAVIAIQD
310 320 330 340 350
MGAAGLTCSA VEMGAKGDLG IELDLNAVPV REERMTAYEM MLSESQERML
360 370 380 390 400
MVLEPSKEEV AKAIFVKWGL DFAIVGKTTD DLRFRVLHNG EEVANLPIKE
410 420 430 440 450
LGDEAPEYDR PWTPAKVPAA LSETDIPEAD IADALVSLVG SANNSSRRWV
460 470 480 490 500
YEQYDTLIQG NSLQLPGGDA GVVRVEGHDK KALAFSSDVT PRYVEADAFE
510 520 530 540 550
GGKQAVAECW RNITATGALP LAATDNLNFG NPEKPEIMSQ LVHAIKGIGE
560 570 580 590 600
ACRVLEFPIV SGNVSLYNET NGQAILPTPT IGGVGLLKDW GRMARIRFAA
610 620 630 640 650
ADEVVLLVGA PAGLGTHIAQ SVYMRDVHGR TDGPAPHVDL IAEKKNGDFV
660 670 680 690 700
RGLITEGLTT AVHDCSSGGL ALAVAEMAIS SGIGATIDAV EGHNPILTFY
710 720 730 740 750
GEDQARYVLT VKKSDLDKVR AAAKAAGVSC PLIGTTGGST VKLGTARAVE
760 770
IKELHLAYES WFPQFMDGET LIAAE
Length:775
Mass (Da):82,517
Last modified:June 1, 2002 - v1
Checksum:i2737EECB6D2699BE
GO

Sequence cautioni

The sequence AAK87617 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007869 Genomic DNA. Translation: AAK87617.2. Different initiation.
PIRiAH2803.
H97582.
RefSeqiNP_354832.2. NC_003062.2.

Genome annotation databases

EnsemblBacteriaiAAK87617; AAK87617; Atu1850.
GeneIDi1133888.
KEGGiatu:Atu1850.
PATRICi20813477. VBIAgrTum91616_1863.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007869 Genomic DNA. Translation: AAK87617.2. Different initiation.
PIRiAH2803.
H97582.
RefSeqiNP_354832.2. NC_003062.2.

3D structure databases

ProteinModelPortaliQ8UEB0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi176299.Atu1850.

Proteomic databases

PRIDEiQ8UEB0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK87617; AAK87617; Atu1850.
GeneIDi1133888.
KEGGiatu:Atu1850.
PATRICi20813477. VBIAgrTum91616_1863.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
BioCyciAGRO:ATU1850-MONOMER.

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_AGRFC
AccessioniPrimary (citable) accession number: Q8UEB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 2002
Last modified: November 30, 2016
This is version 92 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.