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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Synechococcus sp. (strain WH7803)
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 PurS (purS), 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)DescriptionActionsGraphical viewLength
Active sitei41UniRule annotation1
Binding sitei44ATPUniRule annotation1
Binding sitei83ATPUniRule annotation1
Metal bindingi85Magnesium 1UniRule annotation1
Active sitei87Proton acceptorUniRule annotation1
Binding sitei108SubstrateUniRule annotation1
Metal bindingi109Magnesium 2UniRule annotation1
Binding sitei232SubstrateUniRule annotation1
Metal bindingi260Magnesium 2UniRule annotation1
Binding sitei503ATPUniRule annotation1
Binding sitei540ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Metal bindingi541Magnesium 1UniRule annotation1
Binding sitei543SubstrateUniRule 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:SynWH7803_0003
OrganismiSynechococcus sp. (strain WH7803)
Taxonomic identifieri32051 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001566 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_10000805581 – 765Phosphoribosylformylglycinamidine synthase subunit PurLAdd BLAST765

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

STRINGi32051.SynWH7803_0003.

Structurei

3D structure databases

ProteinModelPortaliA5GHL4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni86 – 89Substrate bindingUniRule annotation4
Regioni304 – 306Substrate 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.

A5GHL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASALRQEGL TQEDYIEIQR RLGRDPNRAE LGMFGVMWSE HCCYRNSRPL
60 70 80 90 100
LRGFPTDGPR ILVGPGENAG VVDLGEGHRL AFKIESHNHP SAVEPFQGAA
110 120 130 140 150
TGVGGILRDI FTMGARPIAL LNALRFGPLD EPATQGLVEG VVAGISHYGN
160 170 180 190 200
CVGVPTVGGE VAFDPAYRGN PLVNAMALGL METDDIVKSG ASGVGNPVVY
210 220 230 240 250
VGSTTGRDGM GGASFASAEL SADSLDDRPA VQVGDPFLEK GLIEACLEAF
260 270 280 290 300
QSGDVVAAQD MGAAGLTCSC SEMAAKGNVG VELDLDRVPA REQGMTAYEF
310 320 330 340 350
LLSESQERML FVVQAGREEA LMQRFRRWGL QAAVVGQVLE EPVVRVLQHG
360 370 380 390 400
SVAAEVPARA LAEDTPINQH TLISEPPEDI QEHWRWSETD LPSVSRDHDW
410 420 430 440 450
GADLLALLDD PTIASKRWVY RQYDQQVLAN TVVPAGGADA AVVRLRPQQG
460 470 480 490 500
DASLRGANRG VAATVDCPNR WVALDPERGA MAAVAEAARN LSCVGAVPVA
510 520 530 540 550
VTDNLNFPSP ETPKGYWQLA MACRGLSEGC RVLGTPVTGG NVSLYNETRA
560 570 580 590 600
DDGSLQPIHP TPVVGMVGLV EDLGRVGGLA WRQAGDAVVL LGVSSDERQD
610 620 630 640 650
DRVGLAGSSY QGVIHGLLTG RPPRVDLDLE QRVQALVRQA WEQGLLASAH
660 670 680 690 700
DSSDGGLAVA LAECSIASGL GVDGALPGDG VAPERRLFAE GGARIVVSVR
710 720 730 740 750
AECMDAWTSL LADEAHAAVP VTILGAVADH GRFRLSLGSQ PVLDQAVQTL
760
TERFDQALPR RLGTA
Length:765
Mass (Da):80,875
Last modified:June 12, 2007 - v1
Checksum:iC9F91BCA5B018514
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT971583 Genomic DNA. Translation: CAK22429.1.

Genome annotation databases

EnsemblBacteriaiCAK22429; CAK22429; SynWH7803_0003.
KEGGisyx:SynWH7803_0003.
PATRICi23826036. VBISynSp43824_0004.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT971583 Genomic DNA. Translation: CAK22429.1.

3D structure databases

ProteinModelPortaliA5GHL4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi32051.SynWH7803_0003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAK22429; CAK22429; SynWH7803_0003.
KEGGisyx:SynWH7803_0003.
PATRICi23826036. VBISynSp43824_0004.

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_SYNPW
AccessioniPrimary (citable) accession number: A5GHL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: November 2, 2016
This is version 62 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.