SitesBLAST
Comparing GFF1073 FitnessBrowser__psRCH2:GFF1073 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)
67% identity, 94% coverage: 20:328/329 of query aligns to 7:315/318 of Q63XL8
6asvC E. Coli prpp synthetase (see paper)
68% identity, 94% coverage: 20:328/329 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)
68% identity, 94% coverage: 20:328/329 of query aligns to 4:313/315 of P0A717
- D129 (= D145) 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 (= D235) 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 (= D236) 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 (= D239) 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
67% identity, 93% coverage: 20:324/329 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)
66% identity, 94% coverage: 20:328/329 of query aligns to 2:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F51), D35 (= D53), E37 (= E55), R94 (= R112), R97 (= R115), H129 (= H147)
- binding adenosine monophosphate: R97 (= R115), V99 (≠ P117), R100 (= R118), E131 (≠ D149), F145 (≠ Y163), S147 (= S165), V173 (= V191), A177 (= A195)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D235), D213 (= D236), M214 (= M237), D216 (= D239), T217 (= T240), G219 (= G242), T220 (= T243)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
66% identity, 94% coverage: 20:328/329 of query aligns to 2:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F51), D35 (= D53), E37 (= E55), R94 (= R112), Q95 (= Q113), R97 (= R115), R97 (= R115), R100 (= R118), H129 (= H147), E131 (≠ D149), F145 (≠ Y163), S147 (= S165), V173 (= V191)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D186), D212 (= D235), M214 (= M237), D216 (= D239), T217 (= T240)
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
66% identity, 93% coverage: 20:324/329 of query aligns to 2:299/300 of 3dahC
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
67% identity, 92% coverage: 18:319/329 of query aligns to 1:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F51), D36 (= D53), E38 (= E55), R95 (= R112), Q96 (= Q113), H130 (= H147)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H147), D214 (= D235), D215 (= D236), I216 (≠ M237), D218 (= D239), T219 (= T240), A220 (= A241), T222 (= T243)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
66% identity, 92% coverage: 18:319/329 of query aligns to 1:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F51), D36 (= D53), E38 (= E55), R95 (= R112), Q96 (= Q113), H130 (= H147)
- binding adenosine monophosphate: R98 (= R115), V100 (≠ P117), Y146 (= Y163), R175 (= R192), A178 (= A195), K181 (= K198)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H147), D213 (= D235), D214 (= D236), I215 (≠ M237), D217 (= D239), T218 (= T240), A219 (= A241), T221 (= T243)
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)
49% identity, 94% coverage: 20:328/329 of query aligns to 10:316/317 of P14193
- RQ 102:103 (= RQ 112:113) binding
- K198 (= K209) 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 (= R211) 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 (≠ K213) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N215) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E218) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 239:243) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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, 93% coverage: 22:328/329 of query aligns to 6:313/318 of P60891
- S16 (≠ A32) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D68) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ D131) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L146) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ D149) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V159) 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 (= N161) mutation to H: No effect on catalytic activity.
- Y146 (= Y163) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K198) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A205) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D208) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E218) to H: in a breast cancer sample; somatic mutation
- V219 (= V234) to G: in a breast cancer sample; somatic mutation
- H231 (= H246) 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, 93% coverage: 22:328/329 of query aligns to 5:312/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R112), Q96 (= Q113), N199 (= N215)
- binding adenosine-5'-triphosphate: F34 (= F51), N36 (≠ D53), E38 (= E55)
- binding phosphate ion: S46 (≠ N63), R48 (= R65)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H147), D170 (= D186), G172 (= G188), K193 (= K209), R195 (= R211), D219 (= D235), D220 (= D236), D223 (= D239), T224 (= T240), C225 (≠ A241), G226 (= G242), T227 (= T243)
8dbeA Human prps1 with adp; hexamer (see paper)
49% identity, 93% coverage: 22:328/329 of query aligns to 5:312/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F51), N36 (≠ D53), E38 (= E55), R95 (= R112), Q96 (= Q113), K98 (≠ R115), K99 (≠ R116), D100 (≠ P117), S102 (= S119), R103 (= R121), H129 (= H147), D142 (= D160), Y145 (= Y163), S307 (= S323), V308 (≠ I324), S309 (= S325), F312 (= F328)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H147), D170 (= D186), D219 (= D235), D220 (= D236), D223 (= D239), T224 (= T240), G226 (= G242), T227 (= T243)
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
48% identity, 94% coverage: 20:328/329 of query aligns to 2:295/295 of 1dkuA
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
47% identity, 94% coverage: 20:328/329 of query aligns to 2:297/297 of 1ibsA
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
47% identity, 94% coverage: 20:328/329 of query aligns to 4:299/299 of 1ibsB
7yk1A Structural basis of human prps2 filaments (see paper)
48% identity, 94% coverage: 20:328/329 of query aligns to 3:303/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F51), N36 (≠ D53), E38 (= E55), S46 (≠ N63), R48 (= R65), R95 (= R112), K99 (≠ R116), D100 (≠ P117), K101 (≠ R118), S102 (= S119), R103 (= R121), H129 (= H147), D142 (= D160), S298 (= S323), S300 (= S325), F303 (= F328)
- binding phosphate ion: D214 (= D239), C216 (≠ A241), T218 (= T243)
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)
48% identity, 95% coverage: 18:328/329 of query aligns to 4:316/321 of O94413
- S172 (= S184) modified: Phosphoserine
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
48% identity, 93% coverage: 22:328/329 of query aligns to 4:305/305 of 2hcrA
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
47% identity, 93% coverage: 22:328/329 of query aligns to 5:305/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F51), N36 (≠ D53), E38 (= E55), R95 (= R112), Q96 (= Q113), K98 (≠ R115), H129 (= H147)
- binding phosphate ion: S46 (≠ N63), R48 (= R65), D216 (= D239), T217 (= T240), C218 (≠ A241), T220 (= T243)
Query Sequence
>GFF1073 FitnessBrowser__psRCH2:GFF1073
MNSFLFIGPTLRQVLRVSKMMVFTGNANPDLARRVVRQLHIPLGDAYVGKFSDGEISVEI
NENVRGKDVFLIQPTCAPTNDNLMELVVLADAFRRSSASRITAVIPYFGYARQDRRPRSA
RVPISAKVVADMLDVVGVNRVLTVDLHADQIQGFFDMPVDNIYGSPVLVDDIQAQRFENL
MIVSPDIGGVVRARAVAKSLGVDLAIIDKRRPKANQSEVMHIIGDIEGRTCILVDDMVDT
AGTLCHAAKALKDHGAAKVYAYCTHPILSGRAIENIEGSVLDELVVTNTIPLSAAAQSCT
RIRQLDIAPVVAEAVRRISNAESISAMFR
Or try a new SitesBLAST search
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