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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
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 sitei50UniRule annotation1
Binding sitei53ATPUniRule annotation1
Binding sitei92ATPUniRule annotation1
Metal bindingi94Magnesium 1UniRule annotation1
Active sitei96Proton acceptorUniRule annotation1
Binding sitei117SubstrateUniRule annotation1
Metal bindingi118Magnesium 2UniRule annotation1
Binding sitei241SubstrateUniRule annotation1
Metal bindingi269Magnesium 2UniRule annotation1
Binding sitei495ATPUniRule annotation1
Binding sitei532ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Metal bindingi533Magnesium 1UniRule annotation1
Binding sitei535SubstrateUniRule 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:BMEI1127
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000419 Componenti: Chromosome I

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_00001004441 – 740Phosphoribosylformylglycinamidine synthase subunit PurLAdd BLAST740

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

STRINGi224914.BAWG_1082.

Structurei

3D structure databases

ProteinModelPortaliQ8YGN1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni95 – 98Substrate bindingUniRule annotation4
Regioni313 – 315Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the FGAMS family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QIK. 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.

Q8YGN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTISNTRDIT PELIEAHGLK PDEYQRILEL IGREPTFTEL GIFSAMWNEH
60 70 80 90 100
CSYKSSKKWL RTLPTSGPRV IQGPGENAGV VDIGDGDCVV FKMESHNHPS
110 120 130 140 150
YIEPYQGAAT GVGGILRDVF TMGARPVAAM NALRFGEPDH PKTRHLVSGV
160 170 180 190 200
VSGVGGYGNA FGVPTVGGEV NFDKRYNGNI LVNAFAAGLA RHDGIFLSEA
210 220 230 240 250
EGVGLPVVYL GAKTSRDGVG GATMASAEFD ESIEEKRPTV QVGDPFTEKC
260 270 280 290 300
LLEACLELMA SGAVIAIQDM GAAGLTCSAV EMGAKGDLGI ELILDHVPVR
310 320 330 340 350
EENMTAYEMM LSESQERMLM VLKPEKEAEA QAIFRKWGLD FAIVGKTTDD
360 370 380 390 400
LRFRVIHQGE EVANLPIKDL GDEAPEYDRP WMEPGKHAPL PASNVPQVED
410 420 430 440 450
YSAALLKLIG SPDLSSRRWV YEQYDTLIQG NSLQVPGGDA GVIRVEGHET
460 470 480 490 500
KALAFSSDVT PRYCEADPFE GGKQAVAECW RNITATGAEP LASTDNLNFG
510 520 530 540 550
NPEKPEIMGQ LVKAIEGIGE ACRALDFPIV SGNVSLYNET NGQAILPTPT
560 570 580 590 600
IAGVGLLPDW SQMAKIGGMQ DGDTLVLLGG DGTHLGQSVY LRDLFDRADG
610 620 630 640 650
PAPFVDLALE KRNGEFVRSA IRNGQVTACH DLSDGGLAIA VAEMAIKSGK
660 670 680 690 700
GATLDAGDGL PHALLFGEDQ ARYVISATPE MAKLIALNAE GAGVPFRILG
710 720 730 740
TVGGDRLKIS KNVDVSVADL TQAYEGWFPN FMNGELTGNN
Length:740
Mass (Da):79,148
Last modified:March 5, 2002 - v1
Checksum:iC59E25D61D763D78
GO

Sequence cautioni

The sequence AAL52308 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52308.1. Different initiation.
PIRiAI3392.
RefSeqiWP_002966777.1. NZ_GG703778.1.

Genome annotation databases

EnsemblBacteriaiAAL52308; AAL52308; BMEI1127.
GeneIDi3787541.
KEGGibme:BMEI1127.
bmel:DK63_287.
PATRICi17852535. VBIBruMel92729_1262.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52308.1. Different initiation.
PIRiAI3392.
RefSeqiWP_002966777.1. NZ_GG703778.1.

3D structure databases

ProteinModelPortaliQ8YGN1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224914.BAWG_1082.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL52308; AAL52308; BMEI1127.
GeneIDi3787541.
KEGGibme:BMEI1127.
bmel:DK63_287.
PATRICi17852535. VBIBruMel92729_1262.

Phylogenomic databases

eggNOGiENOG4107QIK. Bacteria.
COG0046. LUCA.
HOGENOMiHOG000238227.
KOiK01952.
OMAiVMWQFAE.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.

Miscellaneous databases

PROiQ8YGN1.

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_BRUME
AccessioniPrimary (citable) accession number: Q8YGN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: November 30, 2016
This is version 97 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. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.