SitesBLAST
Comparing CA265_RS24735 FitnessBrowser__Pedo557:CA265_RS24735 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)
51% identity, 96% coverage: 10:311/313 of query aligns to 9:315/318 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)
50% identity, 97% coverage: 8:311/313 of query aligns to 10:316/317 of P14193
- RQ 102:103 (= RQ 99:100) binding
- K198 (= K195) 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 (= R197) 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 (= R199) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N201) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E204) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 225:229) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6asvC E. Coli prpp synthetase (see paper)
49% identity, 97% coverage: 8:311/313 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)
49% identity, 97% coverage: 8:311/313 of query aligns to 4:313/315 of P0A717
- D129 (= D131) 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 (= D221) 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 (= D222) 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 (= D225) 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)
50% identity, 95% coverage: 10:307/313 of query aligns to 4:299/300 of 3dahC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
49% identity, 96% coverage: 8:307/313 of query aligns to 3:308/308 of 4s2uA
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
50% identity, 97% coverage: 8:311/313 of query aligns to 2:295/295 of 1dkuA
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
48% identity, 97% coverage: 8:311/313 of query aligns to 2:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F39), D35 (= D41), E37 (= E43), R94 (= R99), R97 (= R102), H129 (= H133)
- binding adenosine monophosphate: R97 (= R102), V99 (≠ D104), R100 (≠ K105), E131 (≠ A135), F145 (≠ D149), S147 (= S151), V173 (≠ Y177), A177 (≠ T181)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D221), D213 (= D222), M214 (≠ I223), D216 (= D225), T217 (= T226), G219 (= G228), T220 (= T229)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
48% identity, 97% coverage: 8:311/313 of query aligns to 2:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F39), D35 (= D41), E37 (= E43), R94 (= R99), Q95 (= Q100), R97 (= R102), R97 (= R102), R100 (≠ K105), H129 (= H133), E131 (≠ A135), F145 (≠ D149), S147 (= S151), V173 (≠ Y177)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D172), D212 (= D221), M214 (≠ I223), D216 (= D225), T217 (= T226)
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
49% identity, 97% coverage: 8:311/313 of query aligns to 4:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
49% identity, 97% coverage: 8:311/313 of query aligns to 2:297/297 of 1ibsA
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
50% identity, 94% coverage: 10:302/313 of query aligns to 5:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F39), D36 (= D41), E38 (= E43), R95 (= R99), Q96 (= Q100), H130 (= H133)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H133), D214 (= D221), D215 (= D222), I216 (= I223), D218 (= D225), T219 (= T226), A220 (= A227), T222 (= T229)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
50% identity, 94% coverage: 10:302/313 of query aligns to 5:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F39), D36 (= D41), E38 (= E43), R95 (= R99), Q96 (= Q100), H130 (= H133)
- binding adenosine monophosphate: R98 (= R102), V100 (≠ D104), Y146 (≠ D149), R175 (= R178), A178 (≠ T181), K181 (= K184)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H133), D213 (= D221), D214 (= D222), I215 (= I223), D217 (= D225), T218 (= T226), A219 (= A227), T221 (= T229)
8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
44% identity, 97% coverage: 8:311/313 of query aligns to 3:312/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R99), Q96 (= Q100), N199 (= N201)
- binding adenosine-5'-triphosphate: F34 (= F39), N36 (≠ D41), E38 (= E43)
- binding phosphate ion: S46 (= S51), R48 (= R53)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H133), D170 (= D172), G172 (= G174), K193 (= K195), R195 (= R197), D219 (= D221), D220 (= D222), D223 (= D225), T224 (= T226), C225 (≠ A227), G226 (= G228), T227 (= T229)
8dbeA Human prps1 with adp; hexamer (see paper)
44% identity, 97% coverage: 8:311/313 of query aligns to 3:312/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F39), N36 (≠ D41), E38 (= E43), R95 (= R99), Q96 (= Q100), K98 (≠ R102), K99 (= K103), D100 (= D104), S102 (≠ P106), R103 (= R107), H129 (= H133), D142 (= D146), Y145 (≠ D149), S307 (= S306), V308 (≠ I307), S309 (= S308), F312 (= F311)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H133), D170 (= D172), D219 (= D221), D220 (= D222), D223 (= D225), T224 (= T226), G226 (= G228), T227 (= T229)
P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
44% identity, 97% coverage: 8:311/313 of query aligns to 4:313/318 of P60891
- S16 (= S20) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D56) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (= N117) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L132) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ A135) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V145) 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 (≠ H147) mutation to H: No effect on catalytic activity.
- Y146 (≠ D149) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K184) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (≠ I191) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D194) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E204) to H: in a breast cancer sample; somatic mutation
- V219 (≠ I220) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K232) to D: in a colorectal cancer sample; somatic mutation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5t3oA Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus (see paper)
42% identity, 97% coverage: 7:311/313 of query aligns to 1:306/307 of 5t3oA
7pn0A Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus at r32 space group
42% identity, 98% coverage: 6:311/313 of query aligns to 1:307/312 of 7pn0A
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)
41% identity, 98% coverage: 6:313/313 of query aligns to 4:318/321 of O94413
- S172 (= S170) modified: Phosphoserine
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
43% identity, 97% coverage: 8:311/313 of query aligns to 2:305/305 of 2hcrA
Query Sequence
>CA265_RS24735 FitnessBrowser__Pedo557:CA265_RS24735
MPLQFNPVKLFSGTGSRGLSLKIAEHYGKPLGSVTIHKFSDGEFQPSFDESIRGSDVFLI
QSTYQPSDNLMELLLMVDAAKRASAHYITAVVPYYGLARQDRKDKPRVAIGAKLVANLLK
SAGIHRIMTMDLHAAQIQGFFDIPVDHLDGSVIFVPYIKSLGLKNLTIASPDMGGSYRAR
TFAKFFNAEVIICDKRRKRANEIESMSIIGDVTGQDVVLIDDICDTAGTLSKAAALIMEN
GAASVRAVCTHAVLSGKAIETVENSVLTELIVTDTIPLKQESPKIRVLSTAGLFARAIAN
VNEHGSISDLFRV
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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