SitesBLAST
Comparing WP_086509887.1 NCBI__GCF_002151265.1:WP_086509887.1 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)
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)
72% identity, 100% coverage: 2:309/309 of query aligns to 6:314/315 of P0A717
- D129 (= D125) 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 (= D215) 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 (= D216) 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 (= D219) 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
6asvC E. Coli prpp synthetase (see paper)
72% identity, 99% coverage: 2:308/309 of query aligns to 4:311/311 of 6asvC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
72% identity, 98% coverage: 2:304/309 of query aligns to 5:308/308 of 4s2uA
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)
70% identity, 100% coverage: 1:308/309 of query aligns to 8:315/318 of Q63XL8
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
71% identity, 100% coverage: 2:309/309 of query aligns to 4:306/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F31), D35 (= D33), E37 (= E35), R94 (= R92), R97 (= R95), H129 (= H127)
- binding adenosine monophosphate: R97 (= R95), V99 (= V97), R100 (= R98), E131 (≠ D129), F145 (≠ Y143), S147 (= S145), V173 (= V171), A177 (= A175)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D215), D213 (= D216), M214 (= M217), D216 (= D219), T217 (= T220), G219 (= G222), T220 (= T223)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
71% identity, 100% coverage: 2:309/309 of query aligns to 4:306/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F31), D35 (= D33), E37 (= E35), R94 (= R92), Q95 (= Q93), R97 (= R95), R97 (= R95), R100 (= R98), H129 (= H127), E131 (≠ D129), F145 (≠ Y143), S147 (= S145), V173 (= V171)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D166), D212 (= D215), M214 (= M217), D216 (= D219), T217 (= T220)
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
70% identity, 98% coverage: 1:304/309 of query aligns to 3:299/300 of 3dahC
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
68% identity, 97% coverage: 1:299/309 of query aligns to 4:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F31), D36 (= D33), E38 (= E35), R95 (= R92), Q96 (= Q93), H130 (= H127)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H127), D214 (= D215), D215 (= D216), I216 (≠ M217), D218 (= D219), T219 (= T220), A220 (= A221), T222 (= T223)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
68% identity, 97% coverage: 1:299/309 of query aligns to 4:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F31), D36 (= D33), E38 (= E35), R95 (= R92), Q96 (= Q93), H130 (= H127)
- binding adenosine monophosphate: R98 (= R95), V100 (= V97), Y146 (= Y143), R175 (= R172), A178 (= A175), K181 (= K178)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H127), D213 (= D215), D214 (= D216), I215 (≠ M217), D217 (= D219), T218 (= T220), A219 (= A221), T221 (= T223)
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)
53% identity, 99% coverage: 2:308/309 of query aligns to 12:316/317 of P14193
- RQ 102:103 (= RQ 92:93) binding
- K198 (= K189) 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 (= R191) 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 (≠ Q193) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N195) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (≠ Q198) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 219:223) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
51% identity, 99% coverage: 2:308/309 of query aligns to 4:295/295 of 1dkuA
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
50% identity, 99% coverage: 2:308/309 of query aligns to 6:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
50% identity, 99% coverage: 2:308/309 of query aligns to 4:297/297 of 1ibsA
P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
49% identity, 99% coverage: 2:308/309 of query aligns to 6:313/318 of P60891
- S16 (≠ A12) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D48) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ D111) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L126) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ D129) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V139) 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 (= N141) mutation to H: No effect on catalytic activity.
- Y146 (= Y143) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K178) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A185) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D188) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ Q198) to H: in a breast cancer sample; somatic mutation
- V219 (= V214) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K226) 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)
49% identity, 99% coverage: 2:308/309 of query aligns to 5:312/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R92), Q96 (= Q93), N199 (= N195)
- binding adenosine-5'-triphosphate: F34 (= F31), N36 (≠ D33), E38 (= E35)
- binding phosphate ion: S46 (≠ N43), R48 (= R45)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H127), D170 (= D166), G172 (= G168), K193 (= K189), R195 (= R191), D219 (= D215), D220 (= D216), D223 (= D219), T224 (= T220), C225 (≠ A221), G226 (= G222), T227 (= T223)
8dbeA Human prps1 with adp; hexamer (see paper)
49% identity, 99% coverage: 2:308/309 of query aligns to 5:312/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F31), N36 (≠ D33), E38 (= E35), R95 (= R92), Q96 (= Q93), K98 (≠ R95), K99 (≠ R96), D100 (≠ V97), S102 (= S99), R103 (= R101), H129 (= H127), D142 (= D140), Y145 (= Y143), S307 (= S303), V308 (= V304), S309 (= S305), F312 (= F308)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H127), D170 (= D166), D219 (= D215), D220 (= D216), D223 (= D219), T224 (= T220), G226 (= G222), T227 (= T223)
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
48% identity, 99% coverage: 2:308/309 of query aligns to 4:305/305 of 2hcrA
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)
49% identity, 99% coverage: 2:308/309 of query aligns to 8:316/321 of O94413
- S172 (= S164) modified: Phosphoserine
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
48% identity, 99% coverage: 2:308/309 of query aligns to 5:305/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F31), N36 (≠ D33), E38 (= E35), R95 (= R92), Q96 (= Q93), K98 (≠ R95), H129 (= H127)
- binding phosphate ion: S46 (≠ N43), R48 (= R45), D216 (= D219), T217 (= T220), C218 (≠ A221), T220 (= T223)
7yk1A Structural basis of human prps2 filaments (see paper)
46% identity, 100% coverage: 1:308/309 of query aligns to 4:303/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F31), N36 (≠ D33), E38 (= E35), S46 (≠ N43), R48 (= R45), R95 (= R92), K99 (≠ R96), D100 (≠ V97), K101 (≠ R98), S102 (= S99), R103 (= R101), H129 (= H127), D142 (= D140), S298 (= S303), S300 (= S305), F303 (= F308)
- binding phosphate ion: D214 (= D219), C216 (≠ A221), T218 (= T223)
Query Sequence
>WP_086509887.1 NCBI__GCF_002151265.1:WP_086509887.1
MVFAGNANPELAQKIAESLDTRMGNATVGQFSDGEIAVEINENVRGKDVFILQSTCAPTN
DNLMELILMVDALRRASATRITAVVPYFGYARQDRRVRSARVPISAKVVADMMVKAGVDR
VMTMDLHADQIQGFFDVPVDNVYGSPILLDDIERQNYDDLVVVSPDVGGVVRARAIAKQL
NADLAIIDKRRPQANQAQVMHIIGEIENRTCVVVDDMIDTAGTLCKAGDALKEHGARRVV
AYATHPILSGPAVENITGSVLDEVVVTDTIPLSDVARRSGKIRQLSVAGLIAEAIRRVSN
EESVSAMFH
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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