SitesBLAST
Comparing WP_210399235.1 NCBI__GCF_001579945.1:WP_210399235.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
66% identity, 99% coverage: 1:310/312 of query aligns to 7:315/318 of Q63XL8
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
66% identity, 96% coverage: 1:300/312 of query aligns to 3:297/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F32), D36 (= D34), E38 (= E36), R95 (= R93), Q96 (= Q94), H130 (= H128)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H128), D214 (= D217), D215 (= D218), I216 (≠ L219), D218 (= D221), T219 (= T222), A220 (= A223), T222 (= T225)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
66% identity, 96% coverage: 1:300/312 of query aligns to 3:296/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F32), D36 (= D34), E38 (= E36), R95 (= R93), Q96 (= Q94), H130 (= H128)
- binding adenosine monophosphate: R98 (= R96), V100 (≠ P98), Y146 (= Y144), R175 (= R173), A178 (= A176), K181 (= K179)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H128), D213 (= D217), D214 (= D218), I215 (≠ L219), D217 (= D221), T218 (= T222), A219 (= A223), T221 (= T225)
6asvC E. Coli prpp synthetase (see paper)
62% identity, 99% coverage: 1:310/312 of query aligns to 2:311/311 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)
62% identity, 99% coverage: 1:310/312 of query aligns to 4:313/315 of P0A717
- D129 (= D126) 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 (= D217) 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 (= D218) 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 (= D221) 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
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
65% identity, 98% coverage: 1:306/312 of query aligns to 2:299/300 of 3dahC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
63% identity, 98% coverage: 1:306/312 of query aligns to 3:308/308 of 4s2uA
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
61% identity, 99% coverage: 1:310/312 of query aligns to 2:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F32), D35 (= D34), E37 (= E36), R94 (= R93), R97 (= R96), H129 (= H128)
- binding adenosine monophosphate: R97 (= R96), V99 (≠ P98), R100 (= R99), E131 (≠ D130), F145 (≠ Y144), S147 (= S146), V173 (= V172), A177 (= A176)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D217), D213 (= D218), M214 (≠ L219), D216 (= D221), T217 (= T222), G219 (= G224), T220 (= T225)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
61% identity, 99% coverage: 1:310/312 of query aligns to 2:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F32), D35 (= D34), E37 (= E36), R94 (= R93), Q95 (= Q94), R97 (= R96), R97 (= R96), R100 (= R99), H129 (= H128), E131 (≠ D130), F145 (≠ Y144), S147 (= S146), V173 (= V172)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D167), D212 (= D217), M214 (≠ L219), D216 (= D221), T217 (= T222)
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)
54% identity, 99% coverage: 1:310/312 of query aligns to 10:316/317 of P14193
- RQ 102:103 (= RQ 93:94) binding ATP
- K198 (= K191) 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 (= R193) 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 (= R195) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N197) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E200) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 221:225) 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)
51% identity, 99% coverage: 1:310/312 of query aligns to 4:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
51% identity, 99% coverage: 1:310/312 of query aligns to 2:297/297 of 1ibsA
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
51% identity, 99% coverage: 1:310/312 of query aligns to 2:295/295 of 1dkuA
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: 1:310/312 of query aligns to 4:313/318 of P60891
- S16 (≠ A13) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D49) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (= N112) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L127) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ D130) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V140) 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 (= N142) mutation to H: No effect on catalytic activity.
- Y146 (= Y144) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K179) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A187) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D190) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E200) to H: in a breast cancer sample; somatic mutation
- V219 (= V216) to G: in a breast cancer sample; somatic mutation
- H231 (= H228) 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: 1:310/312 of query aligns to 3:312/316 of 8dbkB