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Protein

Phosphoribosylformylglycinamidine synthase

Gene

purL

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.UniRule annotation1 Publication

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 (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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei678 – 6781ATP; via carbonyl oxygen
Metal bindingi679 – 6791MagnesiumUniRule annotation3 Publications
Metal bindingi718 – 7181MagnesiumUniRule annotation3 Publications
Metal bindingi722 – 7221MagnesiumUniRule annotation3 Publications
Metal bindingi884 – 8841MagnesiumUniRule annotation3 Publications
Binding sitei886 – 8861ATP
Active sitei1135 – 11351NucleophileUniRule annotation
Active sitei1260 – 12601UniRule annotation
Active sitei1262 – 12621UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi307 – 31812ATPUniRule annotationAdd
BLAST
Nucleotide bindingi386 – 3883ATP

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

BioCyciSENT99287:GCTI-2579-MONOMER.
BRENDAi6.3.5.3. 5542.
UniPathwayiUPA00074; UER00128.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthaseUniRule annotation (EC:6.3.5.3UniRule annotation)
Short name:
FGAM synthaseUniRule annotation
Short name:
FGAMSUniRule annotation
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferaseUniRule annotation
Short name:
FGAR amidotransferaseUniRule annotation
Short name:
FGAR-ATUniRule annotation
Gene namesi
Name:purLUniRule annotation
Ordered Locus Names:STM2565
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091F → W: This mutant shows a perturbation of the local environment, however has a secondary structure content and a FGAM synthase activity very similar to the wild-type protein. 1 Publication
Mutagenesisi683 – 6831T → W: This mutant shows a disturbance in the secondary structure of the protein and causes a 30% loss in FGAM synthase activity. 1 Publication
Mutagenesisi1181 – 11811L → F: This mutant has a lower overall folding of the secondary structure and shows a 60% loss in FGAM synthase activity. 1 Publication
Mutagenesisi1181 – 11811L → W: This mutant has the same secondary structure content and FGAM synthetase activity as the wild-type protein and exhibits almost no destabilization. 1 Publication
Mutagenesisi1181 – 11811L → Y: This mutant is extremely deleterious to the structural integrity of the protein. 1 Publication
Mutagenesisi1263 – 12631R → A: This mutant is structurally identical to the wild-type protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12951295Phosphoribosylformylglycinamidine synthasePRO_0000100418Add
BLAST

Proteomic databases

PaxDbiP74881.
PRIDEiP74881.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi99287.STM2565.

Structurei

Secondary structure

1295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 99Combined sources
Helixi13 – 2513Combined sources
Beta strandi32 – 4514Combined sources
Helixi49 – 5810Combined sources
Beta strandi72 – 798Combined sources
Helixi86 – 9712Combined sources
Beta strandi103 – 11513Combined sources
Helixi121 – 13010Combined sources
Turni134 – 1363Combined sources
Beta strandi137 – 1426Combined sources
Helixi143 – 1508Combined sources
Helixi163 – 1664Combined sources
Helixi169 – 17810Combined sources
Helixi184 – 19714Combined sources
Helixi203 – 21210Combined sources
Helixi215 – 2184Combined sources
Helixi220 – 2234Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi231 – 2355Combined sources
Helixi237 – 24711Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi256 – 27318Combined sources
Turni275 – 2773Combined sources
Beta strandi279 – 29517Combined sources
Helixi297 – 3026Combined sources
Helixi304 – 32017Combined sources
Beta strandi327 – 33812Combined sources
Beta strandi357 – 3593Combined sources
Helixi362 – 38019Combined sources
Beta strandi384 – 3918Combined sources
Beta strandi393 – 3986Combined sources
Beta strandi401 – 4066Combined sources
Beta strandi411 – 42010Combined sources
Helixi422 – 4243Combined sources
Beta strandi435 – 4406Combined sources
Helixi467 – 4693Combined sources
Helixi475 – 48915Combined sources
Helixi490 – 4945Combined sources
Beta strandi498 – 5025Combined sources
Turni505 – 5073Combined sources
Helixi508 – 51811Combined sources
Beta strandi522 – 5265Combined sources
Helixi527 – 5293Combined sources
Helixi539 – 5446Combined sources
Beta strandi548 – 5558Combined sources
Helixi557 – 5593Combined sources
Helixi560 – 57011Combined sources
Beta strandi574 – 59017Combined sources
Turni591 – 5944Combined sources
Beta strandi595 – 6017Combined sources
Helixi602 – 6054Combined sources
Beta strandi613 – 6164Combined sources
Helixi633 – 6419Combined sources
Turni644 – 6463Combined sources
Helixi650 – 6534Combined sources
Helixi660 – 6623Combined sources
Beta strandi664 – 6663Combined sources
Beta strandi668 – 6703Combined sources
Turni671 – 6744Combined sources
Beta strandi679 – 6868Combined sources
Beta strandi692 – 6998Combined sources
Helixi701 – 7055Combined sources
Helixi708 – 72316Combined sources
Helixi731 – 7333Combined sources
Beta strandi735 – 7417Combined sources
Helixi749 – 76113Combined sources
Helixi764 – 7685Combined sources
Beta strandi771 – 7788Combined sources
Beta strandi782 – 79514Combined sources
Beta strandi799 – 80911Combined sources
Helixi811 – 8133Combined sources
Beta strandi822 – 8309Combined sources
Turni831 – 8344Combined sources
Beta strandi839 – 8413Combined sources
Helixi842 – 8465Combined sources
Beta strandi852 – 8543Combined sources
Helixi860 – 87516Combined sources
Beta strandi880 – 8845Combined sources
Helixi889 – 90113Combined sources
Beta strandi903 – 9086Combined sources
Helixi910 – 9123Combined sources
Helixi916 – 9216Combined sources
Beta strandi925 – 9328Combined sources
Helixi933 – 9353Combined sources
Helixi936 – 94510Combined sources
Helixi949 – 9513Combined sources
Beta strandi952 – 96817Combined sources
Beta strandi971 – 9777Combined sources
Helixi978 – 99619Combined sources
Helixi999 – 100911Combined sources
Helixi1031 – 10344Combined sources
Turni1035 – 10373Combined sources
Beta strandi1041 – 10466Combined sources
Beta strandi1050 – 10523Combined sources
Helixi1053 – 106210Combined sources
Beta strandi1066 – 10716Combined sources
Helixi1072 – 10765Combined sources
Helixi1082 – 10843Combined sources
Beta strandi1086 – 10905Combined sources
Helixi1095 – 10984Combined sources
Helixi1104 – 11118Combined sources
Helixi1114 – 112512Combined sources
Beta strandi1126 – 11283Combined sources
Beta strandi1130 – 11345Combined sources
Helixi1136 – 11438Combined sources
Helixi1145 – 11473Combined sources
Beta strandi1156 – 11583Combined sources
Beta strandi1166 – 11749Combined sources
Helixi1180 – 11823Combined sources
Turni1183 – 11875Combined sources
Beta strandi1189 – 119810Combined sources
Beta strandi1200 – 12023Combined sources
Helixi1206 – 121510Combined sources
Beta strandi1218 – 12236Combined sources
Beta strandi1227 – 12293Combined sources
Turni1233 – 12353Combined sources
Beta strandi1236 – 12383Combined sources
Helixi1241 – 12433Combined sources
Beta strandi1244 – 12485Combined sources
Beta strandi1252 – 12609Combined sources
Helixi1261 – 12633Combined sources
Beta strandi1264 – 12663Combined sources
Helixi1267 – 12693Combined sources
Beta strandi1270 – 12723Combined sources
Helixi1284 – 129411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3TX-ray1.90A1-1295[»]
3UGJX-ray1.78A1-1295[»]
3UJNX-ray2.98A1-1295[»]
3UMMX-ray3.20A1-1295[»]
4L78X-ray2.18A1-1295[»]
4LGYX-ray1.48A1-1295[»]
4MGHX-ray2.65A1-1295[»]
4R7GX-ray2.90A1-1295[»]
ProteinModelPortaliP74881.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP74881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1042 – 1295254Glutamine amidotransferase type-1UniRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the FGAMS family.UniRule annotation
Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4108ETH. Bacteria.
COG0046. LUCA.
COG0047. LUCA.
HOGENOMiHOG000261359.
KOiK01952.
OMAiLSANWMW.
OrthoDBiEOG6FNHHR.
PhylomeDBiP74881.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1.
InterProiIPR010918. AIR_synth_C_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM-like_N.
[Graphical view]
PfamiPF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P74881-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMEILRGSPA LSAFRINKLL ARFQAANLQV HNIYAEYVHF ADLNAPLNDS
60 70 80 90 100
EQAQLTRLLQ YGPALSSHTP AGKLLLVTPR PGTISPWSSK ATDIAHNCGL
110 120 130 140 150
QQVDRLERGV AYYIEASTLT AEQWRQVAAE LHDRMMETVF SSLTDAEKLF
160 170 180 190 200
IHHQPAPVSS VDLLGEGRQA LIDANLRLGL ALAEDEIDYL QEAFTKLGRN
210 220 230 240 250
PNDIELYMFA QANSEHCRHK IFNADWIIDG KPQPKSLFKM IKNTFETTPD
260 270 280 290 300
YVLSAYKDNA AVMEGSAVGR YFADHNTGRY DFHQEPAHIL MKVETHNHPT
310 320 330 340 350
AISPWPGAAT GSGGEIRDEG ATGRGAKPKA GLVGFSVSNL RIPGFEQPWE
360 370 380 390 400
EDFGKPERIV TALDIMTEGP LGGAAFNNEF GRPALTGYFR TYEEKVNSHN
410 420 430 440 450
GEELRGYHKP IMLAGGIGNI RADHVQKGEI VVGAKLIVLG GPAMNIGLGG
460 470 480 490 500
GAASSMASGQ SDADLDFASV QRDNPEMERR CQEVIDRCWQ LGDANPILFI
510 520 530 540 550
HDVGAGGLSN AMPELVSDGG RGGKFELRDI LSDEPGMSPL EIWCNESQER
560 570 580 590 600
YVLAVAADQL PLFDELCKRE RAPYAVIGDA TEEQHLSLHD NHFDNQPIDL
610 620 630 640 650
PLDVLLGKTP KMTRDVQTLK AKGDALNRAD ITIADAVKRV LHLPTVAEKT
660 670 680 690 700
FLVTIGDRTV TGMVARDQMV GPWQVPVADC AVTTASLDSY YGEAMSIGER
710 720 730 740 750
APVALLDFAA SARLAVGEAL TNIAATQIGD IKRIKLSANW MAAAGHPGED
760 770 780 790 800
AGLYDAVKAV GEELCPQLGL TIPVGKDSMS MKTRWQEGNE QREMTSPLSL
810 820 830 840 850
VISAFARVED VRHTLTPQLS TEDNALLLID LGKGHNALGA TALAQVYRQL
860 870 880 890 900
GDKPADVRDV AQLKGFYDAM QALVAARKLL AWHDRSDGGL LVTLAEMAFA
910 920 930 940 950
GHCGVQVDIA ALGDDHLAAL FNEELGGVIQ VRAEDRDAVE ALLAQYGLAD
960 970 980 990 1000
CVHYLGQALA GDRFVITAND QTVFSESRTT LRVWWAETTW QMQRLRDNPQ
1010 1020 1030 1040 1050
CADQEHEAKA NDTDPGLNVK LSFDINEDIA APYIATGARP KVAVLREQGV
1060 1070 1080 1090 1100
NSHVEMAAAF HRAGFDAIDV HMSDLLGGRI GLGNFHALVA CGGFSYGDVL
1110 1120 1130 1140 1150
GAGEGWAKSI LFNHRVRDEF ETFFHRPQTL ALGVCNGCQM MSNLRELIPG
1160 1170 1180 1190 1200
SELWPRFVRN HSDRFEARFS LVEVTQSPSL LLQGMVGSQM PIAVSHGEGR
1210 1220 1230 1240 1250
VEVRDDAHLA ALESKGLVAL RYVDNFGKVT ETYPANPNGS PNGITAVTTE
1260 1270 1280 1290
NGRVTIMMPH PERVFRTVAN SWHPENWGED SPWMRIFRNA RKQLG
Length:1,295
Mass (Da):141,472
Last modified:December 4, 2007 - v3
Checksum:i55072EAD8712040D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68728 Genomic DNA. Translation: AAB08888.1.
AE006468 Genomic DNA. Translation: AAL21459.1.
RefSeqiNP_461500.1. NC_003197.1.
WP_000970045.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21459; AAL21459; STM2565.
GeneIDi1254087.
KEGGistm:STM2565.
PATRICi32383767. VBISalEnt20916_2706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U68728 Genomic DNA. Translation: AAB08888.1.
AE006468 Genomic DNA. Translation: AAL21459.1.
RefSeqiNP_461500.1. NC_003197.1.
WP_000970045.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3TX-ray1.90A1-1295[»]
3UGJX-ray1.78A1-1295[»]
3UJNX-ray2.98A1-1295[»]
3UMMX-ray3.20A1-1295[»]
4L78X-ray2.18A1-1295[»]
4LGYX-ray1.48A1-1295[»]
4MGHX-ray2.65A1-1295[»]
4R7GX-ray2.90A1-1295[»]
ProteinModelPortaliP74881.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2565.

Proteomic databases

PaxDbiP74881.
PRIDEiP74881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21459; AAL21459; STM2565.
GeneIDi1254087.
KEGGistm:STM2565.
PATRICi32383767. VBISalEnt20916_2706.

Phylogenomic databases

eggNOGiENOG4108ETH. Bacteria.
COG0046. LUCA.
COG0047. LUCA.
HOGENOMiHOG000261359.
KOiK01952.
OMAiLSANWMW.
OrthoDBiEOG6FNHHR.
PhylomeDBiP74881.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
BioCyciSENT99287:GCTI-2579-MONOMER.
BRENDAi6.3.5.3. 5542.

Miscellaneous databases

EvolutionaryTraceiP74881.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1.
InterProiIPR010918. AIR_synth_C_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM-like_N.
[Graphical view]
PfamiPF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Zilles J.L., Downs D.M.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography."
    Anand R., Hoskins A.A., Stubbe J., Ealick S.E.
    Biochemistry 43:10328-10342(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ATP ANALOG; ADP AND MAGNESIUM.
  4. "Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: role of ATP complexation and the glutaminase domain in catalytic coupling."
    Tanwar A.S., Morar M., Panjikar S., Anand R.
    Acta Crystallogr. D 68:627-636(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH ADP AND MAGNESIUM.
  5. "Importance of hydrophobic cavities in allosteric regulation of formylglycinamide synthetase: insight from xenon trapping and statistical coupling analysis."
    Tanwar A.S., Goyal V.D., Choudhary D., Panjikar S., Anand R.
    PLoS ONE 8:E77781-E77781(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF WILD-TYPE; MUTANTS TRP-209 AND ALA-1263 IN COMPLEX WITH ADP AND MAGNESIUM, FUNCTION, MUTAGENESIS OF PHE-209; THR-683; LEU-1181 AND ARG-1263.

Entry informationi

Entry nameiPUR4_SALTY
AccessioniPrimary (citable) accession number: P74881
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: December 4, 2007
Last modified: February 17, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.