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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Status
Unreviewed-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

Pathway:iIMP 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 PurL (purL), Phosphoribosylformylglycinamidine synthase subunit PurQ (purQ), Phosphoribosylformylglycinamidine synthase subunit PurL (purL), Phosphoribosylformylglycinamidine synthase subunit PurQ (purQ), Phosphoribosylformylglycinamidine synthase subunit PurS (purS)
  2. Phosphoribosylformylglycinamidine cyclo-ligase (purM), 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 sitei51 – 511UniRule annotation
Binding sitei54 – 541ATPUniRule annotation
Binding sitei93 – 931ATPUniRule annotation
Metal bindingi95 – 951Magnesium 1UniRule annotation
Active sitei97 – 971Proton acceptorUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation
Metal bindingi119 – 1191Magnesium 2UniRule annotation
Binding sitei242 – 2421SubstrateUniRule annotation
Metal bindingi270 – 2701Magnesium 2UniRule annotation
Binding sitei494 – 4941ATPUniRule annotation
Binding sitei531 – 5311ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
Metal bindingi532 – 5321Magnesium 1UniRule annotation
Binding sitei534 – 5341SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotation

Keywords - Biological processi

Purine biosynthesisUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciGDIA272568:GJPS-1997-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
Glutamine amidotransferase PurLUniRule annotation
Phosphoribosylformylglycinamidine synthase subunit IIUniRule annotation
Gene namesi
Name:purLUniRule annotationImported
Ordered Locus Names:GDI1960Imported
OrganismiGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)Imported
Taxonomic identifieri272568 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter
ProteomesiUP000001176 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

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

STRINGi272568.GDI_1960.

Structurei

3D structure databases

ProteinModelPortaliA9HJG3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 994Substrate bindingUniRule annotation
Regioni314 – 3163Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the FGAMS family.UniRule annotation

Phylogenomic databases

KOiK01952.
OMAiHYGNCVG.
OrthoDBiEOG6FNHHR.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.90.650.10. 1 hit.
HAMAPiMF_00420. PurL_2.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR010074. PRibForGlyAmidine_synth_PurL.
IPR016188. PurM_N-like.
[Graphical view]
PfamiPF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
[Graphical view]
PIRSFiPIRSF001587. FGAM_synthase_II. 1 hit.
SUPFAMiSSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01736. FGAM_synth_II. 1 hit.

Sequencei

Sequence statusi: Complete.

A9HJG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEKGQRPV DQDLAKEFGL TAEEYGNVLS IMGRTPSLTE LGIFSVMWSE
60 70 80 90 100
HCSYKSSRVW LKTLPTTAPW VIHGPGENAG VVDIGQGLAA IFKMESHNHP
110 120 130 140 150
SFIEPYQGAA TGVGGILRDV FTMGARPVAN LNALRFGSPE NPQTRRIVDG
160 170 180 190 200
VVRGVGGYGN CVGVPTVGGE INFHPSYDGN PLVNAMTVGI ARQDRIFLSA
210 220 230 240 250
AAGVGNPVIY VGSKTGRDGI HGATMSSSEF DEDALAKRPT VQVGDPFVEK
260 270 280 290 300
LLIEACLELM ATDAIVAIQD MGAAGLTSSS VEMAGKGGVG IDLDLDAVPQ
310 320 330 340 350
RERGMTAYEM MLSESQERML IVIRPDRTDV ARAIFEKWEL DFAVIGHLTE
360 370 380 390 400
TGHIVVRHQG RVEADIPLDP LADQAPIYRR PTAPAPVPAP LGPLTDPVGI
410 420 430 440 450
EQALIRLIGC PDLASRAWVW NQYDSTVGGQ TVKRPGGADA AIVKIEDTSL
460 470 480 490 500
GLALTTDCTP RYCRADARLG GAQAVAEAWR NIVATGARPL AVTDNLNFGS
510 520 530 540 550
PEKPEVMGQF VAAIEGMGEA CRALDFPVVS GNVSLYNETR APDGSSVSIL
560 570 580 590 600
PTPAIGGLGV LEDVAKAVGL AMPADCTLVL VGATRGEMGQ SLWLREIHGR
610 620 630 640 650
EDGPPPALDL AAERRNGDFV RGQIQDGHVV ACHDVADGGL LVTLAEMVMA
660 670 680 690 700
GDVGCVLSAP QSGIRPEAFW FGEDQSRYVV AVRDADAFTL AATGAGVETR
710 720 730
VLGRSGGDGL TLPSGATIST ARLNAVNSAF FPALMDR
Length:737
Mass (Da):77,704
Last modified:February 5, 2008 - v1
Checksum:iB2AC151E0A665F73
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM889285 Genomic DNA. Translation: CAP55903.1.
RefSeqiWP_012225618.1. NC_010125.1.

Genome annotation databases

EnsemblBacteriaiCAP55903; CAP55903; GDI1960.
KEGGigdi:GDI_1960.
PATRICi22059468. VBIGluDia122154_1893.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM889285 Genomic DNA. Translation: CAP55903.1.
RefSeqiWP_012225618.1. NC_010125.1.

3D structure databases

ProteinModelPortaliA9HJG3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272568.GDI_1960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAP55903; CAP55903; GDI1960.
KEGGigdi:GDI_1960.
PATRICi22059468. VBIGluDia122154_1893.

Phylogenomic databases

KOiK01952.
OMAiHYGNCVG.
OrthoDBiEOG6FNHHR.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
BioCyciGDIA272568:GJPS-1997-MONOMER.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.90.650.10. 1 hit.
HAMAPiMF_00420. PurL_2.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR010074. PRibForGlyAmidine_synth_PurL.
IPR016188. PurM_N-like.
[Graphical view]
PfamiPF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
[Graphical view]
PIRSFiPIRSF001587. FGAM_synthase_II. 1 hit.
SUPFAMiSSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01736. FGAM_synth_II. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5."
    Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A., Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.
    , Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B., Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.
    BMC Genomics 10:450-450(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49037 / DSM 5601 / PAl5Imported.

Entry informationi

Entry nameiA9HJG3_GLUDA
AccessioniPrimary (citable) accession number: A9HJG3
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 22, 2015
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.