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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
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)DescriptionActionsGraphical viewLength
Active sitei53UniRule annotation1
Binding sitei56ATPUniRule annotation1
Binding sitei95ATPUniRule annotation1
Metal bindingi97Magnesium 1UniRule annotation1
Active sitei99Proton acceptorUniRule annotation1
Binding sitei120SubstrateUniRule annotation1
Metal bindingi121Magnesium 2UniRule annotation1
Binding sitei244SubstrateUniRule annotation1
Metal bindingi272Magnesium 2UniRule annotation1
Binding sitei523ATPUniRule annotation1
Binding sitei560ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Metal bindingi561Magnesium 1UniRule annotation1
Binding sitei563SubstrateUniRule 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:Pro_0003
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001420 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_00001004771 – 793Phosphoribosylformylglycinamidine synthase subunit PurLAdd BLAST793

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

STRINGi167539.Pro0003.

Structurei

3D structure databases

ProteinModelPortaliQ7VEK9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 101Substrate bindingUniRule annotation4
Regioni316 – 318Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the FGAMS family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108JIU. Bacteria.
COG0046. LUCA.
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.

Q7VEK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKSKDYLVD YNVELALKKE GLTKADYIEI CNRLKRSPNR TELGMFGVMW
60 70 80 90 100
SEHCCYRNSR SLLSNFPTTG KNILVGPGEN AGVVDLGEGQ RLAFKIESHN
110 120 130 140 150
HPSAIEPFQG AATGVGGILR DIFTMGARPI ALLNSLRFGP LDTPINVGLL
160 170 180 190 200
EGVVSGIAHY GNCVGVPTVG GEVAFDKSYS GNPLVNAMAL GIMETKEIVC
210 220 230 240 250
SGAKGIDFPV IYVGSTTGRD GMGGASFASS ELTQASIDDR PAVQVGDPFL
260 270 280 290 300
EKGLIEGCLE AFKTGYVVAA QDMGAAGLTC SCSEMAAKGG VGIELDLDLV
310 320 330 340 350
PAREKNMTAY EFLLSESQER MLFVVEPGKE ELIMNKFRKW GLQAKVVGKV
360 370 380 390 400
LEENIVRVIH EKQIVVNLPA DSLAEDTPVN KHELLEEPPG FIKDHWKWDE
410 420 430 440 450
TSLPKVSIKG VHFKENNTIL DWNQIILRLL DDPTIASKRW IYNQYDYQVQ
460 470 480 490 500
NNTIIAPGIG DAALIRLREI ENQNQNSNRG IAAVVDCPNR WVALDPERGA
510 520 530 540 550
IAAVAEASRN ISCVGAKPLA VTDNLNFSSP EDPIGYWQLA KACKGLSKAC
560 570 580 590 600
VVLETPVTGG NVSLYNETAL PNGLKQPIQP TPVVGMIGLI QDINSATRQG
610 620 630 640 650
WKDQGDQIYL LGTSIDPSIL NNQNISLAAT SYLENIYGLK TGRPPLIDLE
660 670 680 690 700
FEKLVQLFLR ESIANNLIKS AHDISDGGLV IGLAESCISS GLGIECNLPE
710 720 730 740 750
IDNRLDKLLF AEGGSRVLVS VSPNNIHNIK NSLNNFNIAN SEQISFNYLG
760 770 780 790
TVTDNKYFQI NINQTKIIDL SVNEITNKFE RSIPRRINST IVS
Length:793
Mass (Da):86,331
Last modified:June 7, 2005 - v2
Checksum:iDA470F1FED396B31
GO

Sequence cautioni

The sequence AAP99049 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99049.1. Different initiation.
RefSeqiNP_874397.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAP99049; AAP99049; Pro_0003.
GeneIDi1461381.
KEGGipma:Pro_0003.
PATRICi23026575. VBIProMar8617_0003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAP99049.1. Different initiation.
RefSeqiNP_874397.1. NC_005042.1.

3D structure databases

ProteinModelPortaliQ7VEK9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167539.Pro0003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP99049; AAP99049; Pro_0003.
GeneIDi1461381.
KEGGipma:Pro_0003.
PATRICi23026575. VBIProMar8617_0003.

Phylogenomic databases

eggNOGiENOG4108JIU. Bacteria.
COG0046. LUCA.
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_PROMA
AccessioniPrimary (citable) accession number: Q7VEK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 30, 2016
This is version 95 of the entry and version 2 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.