Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed-Annotation score: -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 + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(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

Keywordsi

Molecular functionLigase
Biological processPurine biosynthesis
LigandATP-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

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
SMRiQ8YGN1
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
OMAiFIEPYQG

Family and domain databases

Gene3Di3.30.1330.10, 2 hits
3.90.650.10, 3 hits
HAMAPiMF_00420 PurL_2, 1 hit
InterProiView protein in InterPro
IPR010074 PRibForGlyAmidine_synth_PurL
IPR010918 PurM-like_C_dom
IPR036676 PurM-like_C_sf
IPR016188 PurM-like_N
IPR036921 PurM-like_N_sf
PANTHERiPTHR43555 PTHR43555, 1 hit
PfamiView protein in Pfam
PF00586 AIRS, 2 hits
PF02769 AIRS_C, 2 hits
PIRSFiPIRSF001587 FGAM_synthase_II, 1 hit
SUPFAMiSSF55326 SSF55326, 2 hits
SSF56042 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
GeneIDi29593962
KEGGibme:BMEI1127
bmel:DK63_287
PATRICifig|224914.52.peg.296

Similar proteinsi

Entry informationi

Entry nameiPURL_BRUME
AccessioniPrimary (citable) accession number: Q8YGN1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: February 28, 2018
This is version 104 of the entry and version 1 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health