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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)DescriptionActionsGraphical viewLength
Binding sitei678ATP; via carbonyl oxygen1
Metal bindingi679MagnesiumUniRule annotation3 Publications1
Metal bindingi718MagnesiumUniRule annotation3 Publications1
Metal bindingi722MagnesiumUniRule annotation3 Publications1
Metal bindingi884MagnesiumUniRule annotation3 Publications1
Binding sitei886ATP1
Active sitei1135NucleophileUniRule annotation1
Active sitei1260UniRule annotation1
Active sitei1262UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi307 – 318ATPUniRule annotationAdd BLAST12
Nucleotide bindingi386 – 388ATP3

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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
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)DescriptionActionsGraphical viewLength
Mutagenesisi209F → 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 Publication1
Mutagenesisi683T → W: This mutant shows a disturbance in the secondary structure of the protein and causes a 30% loss in FGAM synthase activity. 1 Publication1
Mutagenesisi1181L → F: This mutant has a lower overall folding of the secondary structure and shows a 60% loss in FGAM synthase activity. 1 Publication1
Mutagenesisi1181L → W: This mutant has the same secondary structure content and FGAM synthetase activity as the wild-type protein and exhibits almost no destabilization. 1 Publication1
Mutagenesisi1181L → Y: This mutant is extremely deleterious to the structural integrity of the protein. 1 Publication1
Mutagenesisi1263R → A: This mutant is structurally identical to the wild-type protein. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001004181 – 1295Phosphoribosylformylglycinamidine synthaseAdd BLAST1295

Proteomic databases

PaxDbiP74881.
PRIDEiP74881.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi99287.STM2565.

Structurei

Secondary structure

11295
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 9Combined sources9
Helixi13 – 25Combined sources13
Beta strandi32 – 45Combined sources14
Helixi49 – 58Combined sources10
Beta strandi72 – 79Combined sources8
Helixi86 – 97Combined sources12
Beta strandi103 – 115Combined sources13
Helixi121 – 130Combined sources10
Turni134 – 136Combined sources3
Beta strandi137 – 142Combined sources6
Helixi143 – 150Combined sources8
Helixi163 – 166Combined sources4
Helixi169 – 178Combined sources10
Helixi184 – 197Combined sources14
Helixi203 – 212Combined sources10
Helixi215 – 218Combined sources4
Helixi220 – 223Combined sources4
Beta strandi225 – 228Combined sources4
Beta strandi231 – 235Combined sources5
Helixi237 – 247Combined sources11
Beta strandi252 – 254Combined sources3
Beta strandi256 – 273Combined sources18
Turni275 – 277Combined sources3
Beta strandi279 – 295Combined sources17
Helixi297 – 302Combined sources6
Helixi304 – 320Combined sources17
Beta strandi327 – 338Combined sources12
Beta strandi357 – 359Combined sources3
Helixi362 – 380Combined sources19
Beta strandi384 – 391Combined sources8
Beta strandi393 – 398Combined sources6
Beta strandi401 – 406Combined sources6
Beta strandi411 – 420Combined sources10
Helixi422 – 424Combined sources3
Beta strandi435 – 440Combined sources6
Helixi467 – 469Combined sources3
Helixi475 – 489Combined sources15
Helixi490 – 494Combined sources5
Beta strandi498 – 502Combined sources5
Turni505 – 507Combined sources3
Helixi508 – 518Combined sources11
Beta strandi522 – 526Combined sources5
Helixi527 – 529Combined sources3
Helixi539 – 544Combined sources6
Beta strandi548 – 555Combined sources8
Helixi557 – 559Combined sources3
Helixi560 – 570Combined sources11
Beta strandi574 – 590Combined sources17
Turni591 – 594Combined sources4
Beta strandi595 – 601Combined sources7
Helixi602 – 605Combined sources4
Beta strandi613 – 616Combined sources4
Helixi633 – 641Combined sources9
Turni644 – 646Combined sources3
Helixi650 – 653Combined sources4
Helixi660 – 662Combined sources3
Beta strandi664 – 666Combined sources3
Beta strandi668 – 670Combined sources3
Turni671 – 674Combined sources4
Beta strandi679 – 686Combined sources8
Beta strandi692 – 699Combined sources8
Helixi701 – 705Combined sources5
Helixi708 – 723Combined sources16
Helixi731 – 733Combined sources3
Beta strandi735 – 741Combined sources7
Helixi749 – 761Combined sources13
Helixi764 – 768Combined sources5
Beta strandi771 – 778Combined sources8
Beta strandi782 – 795Combined sources14
Beta strandi799 – 809Combined sources11
Helixi811 – 813Combined sources3
Beta strandi822 – 830Combined sources9
Turni831 – 834Combined sources4
Beta strandi839 – 841Combined sources3
Helixi842 – 846Combined sources5
Beta strandi852 – 854Combined sources3
Helixi860 – 875Combined sources16
Beta strandi880 – 884Combined sources5
Helixi889 – 901Combined sources13
Beta strandi903 – 908Combined sources6
Helixi910 – 912Combined sources3
Helixi916 – 921Combined sources6
Beta strandi925 – 932Combined sources8
Helixi933 – 935Combined sources3
Helixi936 – 945Combined sources10
Helixi949 – 951Combined sources3
Beta strandi952 – 968Combined sources17
Beta strandi971 – 977Combined sources7
Helixi978 – 996Combined sources19
Helixi999 – 1009Combined sources11
Helixi1031 – 1034Combined sources4
Turni1035 – 1037Combined sources3
Beta strandi1041 – 1046Combined sources6
Beta strandi1050 – 1052Combined sources3
Helixi1053 – 1062Combined sources10
Beta strandi1066 – 1071Combined sources6
Helixi1072 – 1076Combined sources5
Helixi1082 – 1084Combined sources3
Beta strandi1086 – 1090Combined sources5
Helixi1095 – 1098Combined sources4
Helixi1104 – 1111Combined sources8
Helixi1114 – 1125Combined sources12
Beta strandi1126 – 1128Combined sources3
Beta strandi1130 – 1134Combined sources5
Helixi1136 – 1143Combined sources8
Helixi1145 – 1147Combined sources3
Beta strandi1156 – 1158Combined sources3
Beta strandi1166 – 1174Combined sources9
Helixi1180 – 1182Combined sources3
Turni1183 – 1187Combined sources5
Beta strandi1189 – 1198Combined sources10
Beta strandi1200 – 1202Combined sources3
Helixi1206 – 1215Combined sources10
Beta strandi1218 – 1223Combined sources6
Beta strandi1227 – 1229Combined sources3
Turni1233 – 1235Combined sources3
Beta strandi1236 – 1238Combined sources3
Helixi1241 – 1243Combined sources3
Beta strandi1244 – 1248Combined sources5
Beta strandi1252 – 1260Combined sources9
Helixi1261 – 1263Combined sources3
Beta strandi1264 – 1266Combined sources3
Helixi1267 – 1269Combined sources3
Beta strandi1270 – 1272Combined sources3
Helixi1284 – 1294Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP74881.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP74881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1042 – 1295Glutamine amidotransferase type-1UniRule annotationAdd BLAST254

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.
OMAiKAETHNF.
PhylomeDBiP74881.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1. 1 hit.
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
PDB 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.
SMRiP74881.
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.
OMAiKAETHNF.
PhylomeDBiP74881.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
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. 1 hit.
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...

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: November 2, 2016
This is version 140 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.