SitesBLAST
Comparing WP_029935763.1 NCBI__GCF_000711195.1:WP_029935763.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q63XL8 Ribose-phosphate pyrophosphokinase; RPPK; 5-phospho-D-ribosyl alpha-1-diphosphate synthase; Phosphoribosyl diphosphate synthase; Phosphoribosyl pyrophosphate synthase; P-Rib-PP synthase; PRPP synthase; PRPPase; EC 2.7.6.1 from Burkholderia pseudomallei (strain K96243) (see paper)
64% identity, 99% coverage: 2:318/319 of query aligns to 3:317/318 of Q63XL8
6asvC E. Coli prpp synthetase (see paper)
61% identity, 97% coverage: 8:316/319 of query aligns to 4:311/311 of 6asvC
P0A717 Ribose-phosphate pyrophosphokinase; RPPK; 5-phospho-D-ribosyl alpha-1-diphosphate synthase; Phosphoribosyl diphosphate synthase; Phosphoribosyl pyrophosphate synthase; P-Rib-PP synthase; PRPP synthase; PRPPase; EC 2.7.6.1 from Escherichia coli (strain K12) (see 4 papers)
61% identity, 97% coverage: 8:316/319 of query aligns to 6:313/315 of P0A717
- D129 (= D132) to A: in mutant PRSA1; alters the binding of divalent cations, especially magnesium. Little alteration in the affinity for ribose 5-phosphate and 27-fold decrease of the affinity for ATP. Absence of inhibition by AMP
- D220 (= D223) mutation to E: 4-fold decrease in the affinity binding for Rib-5-P in the presence of magnesium ions. In the presence of cobalt ions, it shows a 15-fold decrease in the affinity binding for Rib-5-P.; mutation to F: With magnesium or manganese ions, the affinity binding values for ATP and Rib-5-P are comparable to those of the wild-type.
- D221 (= D224) mutation to A: The affinity binding for ATP is comparable to those of the wild-type, apart from a slight decrease in the presence of manganese ions. The affinity binding for Rib-5-P is greatly decreased in the presence of both manganese and cobalt ions but only about 2-fold in the presence of magnesium ions.
- D224 (= D227) mutation to A: With magnesium or manganese ions, the affinity binding values for ATP and Rib-5-P are comparable to those of the wild-type.; mutation to S: With magnesium or manganese ions, the affinity binding values for ATP and Rib-5-P are comparable to those of the wild-type.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
61% identity, 97% coverage: 5:312/319 of query aligns to 2:308/308 of 4s2uA
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
66% identity, 95% coverage: 6:307/319 of query aligns to 3:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F37), D36 (= D39), E38 (= E41), R95 (= R99), Q96 (= Q100), H130 (= H134)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H134), D214 (= D223), D215 (= D224), I216 (≠ M225), D218 (= D227), T219 (= T228), A220 (= A229), T222 (= T231)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
65% identity, 95% coverage: 6:307/319 of query aligns to 3:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F37), D36 (= D39), E38 (= E41), R95 (= R99), Q96 (= Q100), H130 (= H134)
- binding adenosine monophosphate: R98 (= R102), V100 (≠ P104), Y146 (= Y150), R175 (= R180), A178 (= A183), K181 (= K186)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H134), D213 (= D223), D214 (= D224), I215 (≠ M225), D217 (= D227), T218 (= T228), A219 (= A229), T221 (= T231)
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
63% identity, 97% coverage: 5:312/319 of query aligns to 1:299/300 of 3dahC
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
60% identity, 97% coverage: 8:316/319 of query aligns to 4:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F37), D35 (= D39), E37 (= E41), R94 (= R99), R97 (= R102), H129 (= H134)
- binding adenosine monophosphate: R97 (= R102), V99 (≠ P104), R100 (≠ H105), E131 (≠ D136), F145 (≠ Y150), S147 (= S152), V173 (= V179), A177 (= A183)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D223), D213 (= D224), M214 (= M225), D216 (= D227), T217 (= T228), G219 (= G230), T220 (= T231)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
60% identity, 97% coverage: 8:316/319 of query aligns to 4:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F37), D35 (= D39), E37 (= E41), R94 (= R99), Q95 (= Q100), R97 (= R102), R97 (= R102), R100 (≠ H105), H129 (= H134), E131 (≠ D136), F145 (≠ Y150), S147 (= S152), V173 (= V179)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D174), D212 (= D223), M214 (= M225), D216 (= D227), T217 (= T228)
P14193 Ribose-phosphate pyrophosphokinase; RPPK; 5-phospho-D-ribosyl alpha-1-diphosphate synthase; Phosphoribosyl diphosphate synthase; Phosphoribosyl pyrophosphate synthase; P-Rib-PP synthase; PPRibP synthase; PRPP synthase; PRPPase; EC 2.7.6.1 from Bacillus subtilis (strain 168) (see 4 papers)
51% identity, 99% coverage: 2:316/319 of query aligns to 6:316/317 of P14193
- RQ 102:103 (= RQ 99:100) binding ATP
- K198 (= K197) mutation to A: Strong decrease of the Vmax value compared to that of the wild-type. The affinity binding for ATP and Rib-5-P are slightly altered compared to the wild-type. The cooperativity of ADP binding is reduced.
- R200 (= R199) mutation to A: Strong decrease of the Vmax value compared to that of the wild-type enzyme. The affinity binding for ATP and Rib-5-P are slightly altered compared to the wild-type.
- R202 (≠ K201) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N203) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (≠ Q206) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 227:231) binding D-ribose 5-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
49% identity, 98% coverage: 3:316/319 of query aligns to 1:299/299 of 1ibsB
P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
47% identity, 99% coverage: 5:319/319 of query aligns to 3:316/318 of P60891
- S16 (≠ A18) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D54) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ D118) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L133) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ D136) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V146) to L: found in a patient with an intermediate phenotype between ARTS and PRPS1 superactivity; likely pathogenic; normal PRPP synthetase activity in fibroblasts; loss of activity in erythrocytes; dbSNP:rs398122855
- N144 (= N148) mutation to H: No effect on catalytic activity.
- Y146 (= Y150) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K186) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A193) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D196) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ Q206) to H: in a breast cancer sample; somatic mutation
- V219 (= V222) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K234) to D: in a colorectal cancer sample; somatic mutation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
47% identity, 99% coverage: 5:319/319 of query aligns to 2:315/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R99), Q96 (= Q100), N199 (= N203)
- binding adenosine-5'-triphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41)
- binding phosphate ion: S46 (= S49), R48 (= R51)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H134), D170 (= D174), G172 (= G176), K193 (= K197), R195 (= R199), D219 (= D223), D220 (= D224), D223 (= D227), T224 (= T228), C225 (≠ A229), G226 (= G230), T227 (= T231)
8dbeA Human prps1 with adp; hexamer (see paper)
47% identity, 99% coverage: 5:319/319 of query aligns to 2:315/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41), R95 (= R99), Q96 (= Q100), K98 (≠ R102), K99 (≠ R103), D100 (≠ P104), S102 (= S106), R103 (= R108), H129 (= H134), D142 (= D147), Y145 (= Y150), S307 (= S311), V308 (= V312), S309 (≠ T313), F312 (≠ M316)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H134), D170 (= D174), D219 (= D223), D220 (= D224), D223 (= D227), T224 (= T228), G226 (= G230), T227 (= T231)
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
49% identity, 98% coverage: 5:316/319 of query aligns to 1:297/297 of 1ibsA