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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Corynebacterium glutamicum (strain R)
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 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581UniRule annotation
Binding sitei61 – 611ATPUniRule annotation
Binding sitei105 – 1051ATPUniRule annotation
Metal bindingi107 – 1071Magnesium 1UniRule annotation
Active sitei109 – 1091Proton acceptorUniRule annotation
Binding sitei130 – 1301SubstrateUniRule annotation
Metal bindingi131 – 1311Magnesium 2UniRule annotation
Binding sitei255 – 2551SubstrateUniRule annotation
Metal bindingi283 – 2831Magnesium 2UniRule annotation
Binding sitei513 – 5131ATPUniRule annotation
Binding sitei550 – 5501ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
Metal bindingi551 – 5511Magnesium 1UniRule annotation
Binding sitei553 – 5531SubstrateUniRule annotation

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

BioCyciCGLU340322:GJBE-2612-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:cgR_2491
OrganismiCorynebacterium glutamicum (strain R)
Taxonomic identifieri340322 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000006698 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 762762Phosphoribosylformylglycinamidine synthase subunit PurLPRO_1000050306Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliA4QGY6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni108 – 1114Substrate bindingUniRule annotation
Regioni327 – 3293Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the FGAMS family.UniRule annotation

Phylogenomic databases

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.

A4QGY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFVNDTVE DAIKTPELDQ PFEALGLKDD EYARIKEILG RRPTDAELTV
60 70 80 90 100
YSVMWSEHCS YKSSKVHLRY FGETTTEEMA SKILAGIGEN AGVVDIGDGN
110 120 130 140 150
AVTFRVESHN HPSFVEPHQG AATGIGGIVR DIMAMGARPI AVMDQLRFGA
160 170 180 190 200
LDNPDTQRVL PGVVDGISHY GNCLGLPNIG GETVFDDSYA GNPLVNALCV
210 220 230 240 250
GTLKVEDLKL AFASGTGNKV ILFGSRTGLD GIGGVSVLGS ASFEEGEERK
260 270 280 290 300
LPAVQVGDPF AEKVLIECCL ELYKAGVVVG IQDLGGGGLA CATSELAAAG
310 320 330 340 350
DGGMRVNLDN VPLRAENMSA AEILASESQE RMCAVVTPEN VERFLEICAK
360 370 380 390 400
WDVTCAEIGE VTDEKDRYVV VHNGEVVIDA PPSTIDEGPV YNRPVARPEN
410 420 430 440 450
QDELQLEGEI ARPVDVEDIK AAWLKLVASP ALASRAFITE QYDRYVRGNT
460 470 480 490 500
VQAKNANAGV LRIDEETNRG VAISADASGR YTKLEPNTGA QLALAEAYRN
510 520 530 540 550
VVSTGARPVA VTNCLNFGSP ENAGVMWQFK EAVHGLADGS KLLGIPVSGG
560 570 580 590 600
NVSFYNQTGD EPILPTPVVG VLGVLDNVEQ SIGNVLPSED NDLYLLGETF
610 620 630 640 650
DEFGGSIWQQ VSGAGLNGLP PVVDLLNEQR LADLFVGSDL FAASHDLSEG
660 670 680 690 700
GLGQTLAELA IHADKGMDVD LSQIHPSLFT SLFAESASRI VVATNRGEEL
710 720 730 740 750
EKRAAELGVP VFKLGRTNDS AVIAVKGADV EFNISVEELR EAWTNTLPEA
760
FGHAVGANAV VG
Length:762
Mass (Da):80,908
Last modified:May 15, 2007 - v1
Checksum:i496F1EDA2FBF4CEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF55502.1.
RefSeqiWP_003854014.1. NC_009342.1.

Genome annotation databases

EnsemblBacteriaiBAF55502; BAF55502; cgR_2491.
KEGGicgt:cgR_2491.
PATRICi21509662. VBICorGlu58097_2554.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF55502.1.
RefSeqiWP_003854014.1. NC_009342.1.

3D structure databases

ProteinModelPortaliA4QGY6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF55502; BAF55502; cgR_2491.
KEGGicgt:cgR_2491.
PATRICi21509662. VBICorGlu58097_2554.

Phylogenomic databases

HOGENOMiHOG000238227.
KOiK01952.
OMAiVMWQFAE.
OrthoDBiPOG091H009J.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
BioCyciCGLU340322:GJBE-2612-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_CORGB
AccessioniPrimary (citable) accession number: A4QGY6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: September 7, 2016
This is version 60 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

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.