UniProtKB - P50384 (TRPD_SACS2)
Protein
Anthranilate phosphoribosyltransferase
Gene
trpD
Organism
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Status
Functioni
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).UniRule annotation2 Publications
Catalytic activityi
- diphosphate + N-(5-phospho-β-D-ribosyl)anthranilate = 5-phospho-α-D-ribose 1-diphosphate + anthranilateUniRule annotation1 PublicationEC:2.4.2.18UniRule annotation1 Publication
Cofactori
Mg2+Note: Binds 2 magnesium ions per monomer.
Kineticsi
- KM=50 µM for magnesium (at 60 degrees Celsius and at pH 7.5)2 Publications
- KM=40 nM for anthranilate (at 60 degrees Celsius and at pH 7.5)2 Publications
- KM=160 µM for phosphoribosylpyrophosphate (at 60 degrees Celsius and at pH 7.5)2 Publications
- KM=20 nM for anthranilate (at 25 degrees Celsius and at pH 7.5)2 Publications
- KM=26 nM for anthranilate (at 40 degrees Celsius and at pH 7.5)2 Publications
- KM=32 nM for anthranilate (at 50 degrees Celsius and at pH 7.5)2 Publications
- KM=35 nM for anthranilate (at 60 degrees Celsius and at pH 7.5)2 Publications
- KM=500 nM for anthranilate (at 87 degrees Celsius and at pH 7.52 Publications
: L-tryptophan biosynthesis Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes L-tryptophan from chorismate.UniRule annotationProteins known to be involved in the 5 steps of the subpathway in this organism are:
- Anthranilate synthase component 1 (trpE), Anthranilate synthase component 2 (trpG)
- Anthranilate phosphoribosyltransferase (trpD)
- N-(5'-phosphoribosyl)anthranilate isomerase (trpF)
- Indole-3-glycerol phosphate synthase (trpC)
- Tryptophan synthase beta chain 2 (trpB2), Tryptophan synthase beta chain 1 (trpB1), Tryptophan synthase alpha chain (trpA)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 79 | Anthranilate 1; via carbonyl oxygen | 1 | |
Binding sitei | 87 | PhosphoribosylpyrophosphateUniRule annotation2 Publications | 1 | |
Metal bindingi | 91 | Magnesium 1 | 1 | |
Binding sitei | 109 | Anthranilate 1 | 1 | |
Binding sitei | 118 | Phosphoribosylpyrophosphate; via amide nitrogenUniRule annotation2 Publications | 1 | |
Binding sitei | 164 | Anthranilate 2 | 1 | |
Metal bindingi | 223 | Magnesium 2 | 1 | |
Metal bindingi | 224 | Magnesium 1 | 1 | |
Metal bindingi | 224 | Magnesium 2 | 1 |
GO - Molecular functioni
- anthranilate phosphoribosyltransferase activity Source: UniProtKB-UniRule
- magnesium ion binding Source: UniProtKB-UniRule
GO - Biological processi
- tryptophan biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Biological process | Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | SSOL273057:G1FZF-929-MONOMER |
BRENDAi | 2.4.2.18, 6163 |
SABIO-RKi | P50384 |
UniPathwayi | UPA00035;UER00041 |
Names & Taxonomyi
Protein namesi | Recommended name: Anthranilate phosphoribosyltransferaseUniRule annotation (EC:2.4.2.18UniRule annotation) |
Gene namesi | Name:trpDUniRule annotation Ordered Locus Names:SSO0890 |
Organismi | Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) |
Taxonomic identifieri | 273057 [NCBI] |
Taxonomic lineagei | Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Saccharolobus › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 106 | K → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency dedreases only 10-fold. 1 Publication | 1 | |
Mutagenesisi | 107 | H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-178. 1 Publication | 1 | |
Mutagenesisi | 154 | H → A: Limited effect on either affinity for anthranilate and catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 164 | R → A: Strong decrease of the affinity for anthranilate, although only a moderate 7-fold decrease in catalytic efficiency. 1 Publication | 1 | |
Mutagenesisi | 178 | P → A: 300-fold decrease of the affinity for anthranilate, whereas catalytic efficiency remains nearly unchanged; when associated with A-107. | 1 | |
Mutagenesisi | 223 | D → N: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication | 1 | |
Mutagenesisi | 224 | E → Q: Affinity for phosphoribosylpyrophosphate is similar to that of the wild-type enzyme and catalytic efficiency is unchanged. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000154523 | 1 – 345 | Anthranilate phosphoribosyltransferaseAdd BLAST | 345 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotation4 PublicationsProtein-protein interaction databases
STRINGi | 273057.SSO0890 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P50384 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P50384 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 77 – 79 | Phosphoribosylpyrophosphate binding | 3 | |
Regioni | 82 – 83 | Phosphoribosylpyrophosphate binding | 2 | |
Regioni | 89 – 92 | Phosphoribosylpyrophosphate binding | 4 | |
Regioni | 106 – 114 | Phosphoribosylpyrophosphate binding | 9 |
Sequence similaritiesi
Belongs to the anthranilate phosphoribosyltransferase family.UniRule annotation
Phylogenomic databases
eggNOGi | arCOG02012, Archaea |
HOGENOMi | CLU_034315_2_1_2 |
InParanoidi | P50384 |
OMAi | LYHQSFK |
Family and domain databases
Gene3Di | 1.20.970.10, 1 hit 3.40.1030.10, 1 hit |
HAMAPi | MF_00211, TrpD, 1 hit |
InterProi | View protein in InterPro IPR005940, Anthranilate_Pribosyl_Tfrase IPR000312, Glycosyl_Trfase_fam3 IPR017459, Glycosyl_Trfase_fam3_N_dom IPR036320, Glycosyl_Trfase_fam3_N_dom)sf IPR035902, Nuc_phospho_transferase |
Pfami | View protein in Pfam PF02885, Glycos_trans_3N, 1 hit PF00591, Glycos_transf_3, 1 hit |
SUPFAMi | SSF47648, SSF47648, 1 hit SSF52418, SSF52418, 1 hit |
TIGRFAMsi | TIGR01245, trpD, 1 hit |
i Sequence
Sequence statusi: Complete.
P50384-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNINEILKKL INKSDLEINE AEELAKAIIR GEVPEILVSA ILVALRMKGE
60 70 80 90 100
SKNEIVGFAR AMRELAIKID VPNAIDTAGT GGDGLGTVNV STASAILLSL
110 120 130 140 150
VNPVAKHGNR AVSGKSGSAD VLEALGYNII VPPERAKELV NKTNFVFLFA
160 170 180 190 200
QYYHPAMKNV ANVRKTLGIR TIFNILGPLT NPANAKYQLM GVFSKDHLDL
210 220 230 240 250
LSKSAYELDF NKIILVYGEP GIDEVSPIGN TFMKIVSKRG IEEVKLNVTD
260 270 280 290 300
FGISPIPIEK LIVNSAEDSA IKIVRAFLGK DEHVAEFIKI NTAVALFALD
310 320 330 340
RVGDFREGYE YADHLIEKSL DKLNEIISMN GDVTKLKTIV VKSSG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z50014 Genomic DNA Translation: CAA90309.1 AE006641 Genomic DNA Translation: AAK41173.1 |
PIRi | F90239 |
RefSeqi | WP_009992305.1, NC_002754.1 |
Genome annotation databases
EnsemblBacteriai | AAK41173; AAK41173; SSO0890 |
GeneIDi | 44129821 |
KEGGi | sso:SSO0890 |
PATRICi | fig|273057.12.peg.894 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z50014 Genomic DNA Translation: CAA90309.1 AE006641 Genomic DNA Translation: AAK41173.1 |
PIRi | F90239 |
RefSeqi | WP_009992305.1, NC_002754.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1GXB | X-ray | 2.70 | A/B/C/D | 1-345 | [»] | |
1O17 | X-ray | 2.05 | A/B/C/D | 1-345 | [»] | |
1ZXY | X-ray | 2.56 | A/B/C/D | 1-345 | [»] | |
1ZYK | X-ray | 2.40 | A/B/C/D | 1-345 | [»] | |
2GVQ | X-ray | 2.43 | A/B/C/D | 1-345 | [»] | |
3GBR | X-ray | 2.25 | A/B | 1-345 | [»] | |
SMRi | P50384 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 273057.SSO0890 |
Genome annotation databases
EnsemblBacteriai | AAK41173; AAK41173; SSO0890 |
GeneIDi | 44129821 |
KEGGi | sso:SSO0890 |
PATRICi | fig|273057.12.peg.894 |
Phylogenomic databases
eggNOGi | arCOG02012, Archaea |
HOGENOMi | CLU_034315_2_1_2 |
InParanoidi | P50384 |
OMAi | LYHQSFK |
Enzyme and pathway databases
UniPathwayi | UPA00035;UER00041 |
BioCyci | SSOL273057:G1FZF-929-MONOMER |
BRENDAi | 2.4.2.18, 6163 |
SABIO-RKi | P50384 |
Miscellaneous databases
EvolutionaryTracei | P50384 |
Family and domain databases
Gene3Di | 1.20.970.10, 1 hit 3.40.1030.10, 1 hit |
HAMAPi | MF_00211, TrpD, 1 hit |
InterProi | View protein in InterPro IPR005940, Anthranilate_Pribosyl_Tfrase IPR000312, Glycosyl_Trfase_fam3 IPR017459, Glycosyl_Trfase_fam3_N_dom IPR036320, Glycosyl_Trfase_fam3_N_dom)sf IPR035902, Nuc_phospho_transferase |
Pfami | View protein in Pfam PF02885, Glycos_trans_3N, 1 hit PF00591, Glycos_transf_3, 1 hit |
SUPFAMi | SSF47648, SSF47648, 1 hit SSF52418, SSF52418, 1 hit |
TIGRFAMsi | TIGR01245, trpD, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TRPD_SACS2 | |
Accessioni | P50384Primary (citable) accession number: P50384 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | December 2, 2020 | |
This is version 143 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families