SitesBLAST
Comparing GFF2178 FitnessBrowser__psRCH2:GFF2178 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)
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)
32% identity, 96% coverage: 8:312/317 of query aligns to 6:300/315 of P0A717
- D129 (≠ E134) 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 (= D231) 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 (= D232) 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 (≠ S235) 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
32% identity, 96% coverage: 8:312/317 of query aligns to 5:299/308 of 4s2uA
6asvC E. Coli prpp synthetase (see paper)
32% identity, 96% coverage: 8:312/317 of query aligns to 4:298/311 of 6asvC
8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
30% identity, 96% coverage: 8:312/317 of query aligns to 5:299/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R102), Q96 (≠ K103), N199 (= N210)
- binding adenosine-5'-triphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41)
- binding phosphate ion: S46 (≠ P49), R48 (≠ E51)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H136), D170 (= D177), G172 (= G179), K193 (≠ M204), R195 (≠ K206), D219 (= D231), D220 (= D232), D223 (≠ S235), T224 (= T236), C225 (≠ G237), G226 (= G238), T227 (= T239)
8dbeA Human prps1 with adp; hexamer (see paper)
30% identity, 96% coverage: 8:312/317 of query aligns to 5:299/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41), R95 (= R102), Q96 (≠ K103), K98 (≠ R105), K99 (≠ R106), D100 (≠ T107), S102 (≠ F109), R103 (≠ Q110), H129 (= H136), D142 (≠ R150), Y145 (≠ E153)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H136), D170 (= D177), D219 (= D231), D220 (= D232), D223 (≠ S235), T224 (= T236), G226 (= G238), T227 (= T239)
Sites not aligning to the query:
7yk1A Structural basis of human prps2 filaments (see paper)
30% identity, 97% coverage: 7:312/317 of query aligns to 4:290/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41), S46 (≠ P49), R48 (≠ E51), R95 (= R102), K99 (≠ R106), D100 (≠ T107), K101 (≠ Q108), S102 (≠ F109), R103 (≠ Q110), H129 (= H136), D142 (≠ R150)
- binding phosphate ion: D214 (≠ S235), C216 (≠ G237), T218 (= T239)
Sites not aligning to the query:
P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
30% identity, 96% coverage: 8:312/317 of query aligns to 6:300/318 of P60891
- S16 (≠ A18) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (≠ K54) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ A120) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (≠ V135) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ A139) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (≠ T149) 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 (≠ H151) mutation to H: No effect on catalytic activity.
- Y146 (≠ E153) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ R189) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (≠ G200) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ Y203) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ T214) to H: in a breast cancer sample; somatic mutation
- V219 (= V230) to G: in a breast cancer sample; somatic mutation
- H231 (≠ R242) to D: in a colorectal cancer sample; somatic mutation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
30% identity, 96% coverage: 8:312/317 of query aligns to 4:292/305 of 2hcrA
5t3oA Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus (see paper)
34% identity, 94% coverage: 5:301/317 of query aligns to 1:285/307 of 5t3oA
7pn0A Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus at r32 space group
34% identity, 94% coverage: 5:301/317 of query aligns to 2:286/312 of 7pn0A
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
32% identity, 96% coverage: 8:312/317 of query aligns to 4:292/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F37), D35 (= D39), E37 (= E41), R94 (= R102), R97 (= R105), H129 (= H136)
- binding adenosine monophosphate: R97 (= R105), V99 (≠ T107), R100 (≠ Q108), E131 (vs. gap), F145 (≠ E153), S147 (≠ A155), V173 (≠ K182), A177 (≠ S186)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D231), D213 (= D232), M214 (≠ L233), D216 (≠ S235), T217 (= T236), G219 (= G238), T220 (= T239)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
32% identity, 96% coverage: 8:312/317 of query aligns to 4:292/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F37), D35 (= D39), E37 (= E41), R94 (= R102), Q95 (≠ K103), R97 (= R105), R97 (= R105), R100 (≠ Q108), H129 (= H136), E131 (vs. gap), F145 (≠ E153), S147 (≠ A155), V173 (≠ K182)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D177), D212 (= D231), M214 (≠ L233), D216 (≠ S235), T217 (= T236)
O94413 Ribose-phosphate pyrophosphokinase 2; Phosphoribosyl pyrophosphate synthase 2; EC 2.7.6.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 90% coverage: 1:286/317 of query aligns to 1:279/321 of O94413
- S172 (= S175) modified: Phosphoserine
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
30% identity, 96% coverage: 8:312/317 of query aligns to 5:292/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41), R95 (= R102), Q96 (≠ K103), K98 (≠ R105), H129 (= H136)
- binding phosphate ion: S46 (≠ P49), R48 (≠ E51), D216 (≠ S235), T217 (= T236), C218 (≠ G237), T220 (= T239)
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)
30% identity, 97% coverage: 1:309/317 of query aligns to 1:299/318 of Q63XL8
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)
27% identity, 96% coverage: 8:312/317 of query aligns to 12:303/317 of P14193
- RQ 102:103 (≠ RK 102:103) binding
- K198 (= K206) 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 (= R208) 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 (≠ N210) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (≠ I212) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (≠ G215) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (≠ STGGT 235:239) binding
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)
29% identity, 96% coverage: 7:309/317 of query aligns to 3:287/300 of 3dahC
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
28% identity, 88% coverage: 8:285/317 of query aligns to 4:262/295 of 1dkuA
Sites not aligning to the query:
P9WKE3 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 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
29% identity, 98% coverage: 7:316/317 of query aligns to 13:313/326 of P9WKE3
- K29 (≠ R23) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
27% identity, 96% coverage: 8:312/317 of query aligns to 6:286/299 of 1ibsB
Query Sequence
>GFF2178 FitnessBrowser__psRCH2:GFF2178
MSNHPPLLFALQGTQEYAARVARHMGLELAEIEERAFEDGEHKSRALTPVEGRKVAVFHA
LYGDDERSVNDKLCRLLFFCGALKDAGARHVQVVAPYLCYARKERRTQFQDPIITRYVAA
LFEACRVDRLTTLEVHNLAAFDNAFRIPTRHIESAELFAAHFAQLSADAELVAVSPDAGG
AKRAESFRRALQQHTGRSVGSAYMEKYRSNDIVTGTMLVGDVRDRIAIIVDDLISTGGTL
LRAGEACRKAGARQVHAAAAHGLFTGGPELLESPVFDQLVITDTVPPFRLDPDLAGRRLT
VLDSSAMLAAALAAEYR
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory