SitesBLAST
Comparing GFF727 FitnessBrowser__Marino:GFF727 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)
71% identity, 100% coverage: 1:289/290 of query aligns to 27:315/315 of P0A717
- D129 (= D103) 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 (= D194) 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 (= D195) 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 (= D198) 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)
71% identity, 99% coverage: 1:287/290 of query aligns to 25:311/311 of 6asvC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
70% identity, 98% coverage: 1:283/290 of query aligns to 26:308/308 of 4s2uA
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
69% identity, 100% coverage: 1:289/290 of query aligns to 25:307/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F9), D35 (= D11), E37 (= E13), R94 (= R70), R97 (= R73), H129 (= H105)
- binding adenosine monophosphate: R97 (= R73), V99 (= V75), R100 (= R76), E131 (≠ D107), F145 (≠ Y121), S147 (≠ T123), V173 (= V149), A177 (= A153)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D194), D213 (= D195), M214 (≠ I196), D216 (= D198), T217 (= T199), G219 (= G201), T220 (= T202)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
69% identity, 100% coverage: 1:289/290 of query aligns to 25:307/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F9), D35 (= D11), E37 (= E13), R94 (= R70), Q95 (= Q71), R97 (= R73), R97 (= R73), R100 (= R76), H129 (= H105), E131 (≠ D107), F145 (≠ Y121), S147 (≠ T123), V173 (= V149)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D144), D212 (= D194), M214 (≠ I196), D216 (= D198), T217 (= T199)
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
69% identity, 96% coverage: 1:278/290 of query aligns to 26:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F9), D36 (= D11), E38 (= E13), R95 (= R70), Q96 (= Q71), H130 (= H105)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H105), D214 (= D194), D215 (= D195), I216 (= I196), D218 (= D198), T219 (= T199), A220 (= A200), T222 (= T202)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
69% identity, 96% coverage: 1:278/290 of query aligns to 26:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F9), D36 (= D11), E38 (= E13), R95 (= R70), Q96 (= Q71), H130 (= H105)
- binding adenosine monophosphate: R98 (= R73), V100 (= V75), Y146 (= Y121), R175 (= R150), A178 (= A153), K181 (= K156)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H105), D213 (= D194), D214 (= D195), I215 (= I196), D217 (= D198), T218 (= T199), A219 (= A200), T221 (= T202)
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, 99% coverage: 1:287/290 of query aligns to 30:315/318 of Q63XL8
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
66% identity, 98% coverage: 1:283/290 of query aligns to 25:299/300 of 3dahC
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: 1:287/290 of query aligns to 33:316/317 of P14193
- RQ 102:103 (= RQ 70:71) binding
- K198 (= K168) 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 (= R170) 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 (≠ K172) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N174) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (≠ Q177) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 198:202) 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)
51% identity, 100% coverage: 1:289/290 of query aligns to 27:315/318 of P60891
- D52 (= D26) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ D89) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L104) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ D107) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V117) 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 (= N119) mutation to H: No effect on catalytic activity.
- Y146 (= Y121) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K156) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A164) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D167) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ Q177) to H: in a breast cancer sample; somatic mutation
- V219 (= V193) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K205) to D: in a colorectal cancer sample; somatic mutation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 16 S → P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
51% identity, 100% coverage: 1:289/290 of query aligns to 26:314/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R70), Q96 (= Q71), N199 (= N174)
- binding adenosine-5'-triphosphate: F34 (= F9), N36 (≠ D11), E38 (= E13)
- binding phosphate ion: S46 (≠ N21), R48 (= R23)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H105), D170 (= D144), G172 (= G146), K193 (= K168), R195 (= R170), D219 (= D194), D220 (= D195), D223 (= D198), T224 (= T199), C225 (≠ A200), G226 (= G201), T227 (= T202)
8dbeA Human prps1 with adp; hexamer (see paper)
51% identity, 100% coverage: 1:289/290 of query aligns to 26:314/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F9), N36 (≠ D11), E38 (= E13), R95 (= R70), Q96 (= Q71), K98 (≠ R73), K99 (≠ R74), D100 (≠ V75), S102 (= S77), R103 (= R79), H129 (= H105), D142 (= D118), Y145 (= Y121), S307 (= S282), V308 (≠ I283), S309 (= S284), F312 (= F287)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H105), D170 (= D144), D219 (= D194), D220 (= D195), D223 (= D198), T224 (= T199), G226 (= G201), T227 (= T202)
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
51% identity, 99% coverage: 1:287/290 of query aligns to 25:295/295 of 1dkuA
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
50% identity, 99% coverage: 1:287/290 of query aligns to 25:305/305 of 2hcrA
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
50% identity, 99% coverage: 1:287/290 of query aligns to 25:297/297 of 1ibsA
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
50% identity, 99% coverage: 1:287/290 of query aligns to 27:299/299 of 1ibsB
7yk1A Structural basis of human prps2 filaments (see paper)
49% identity, 100% coverage: 1:289/290 of query aligns to 26:305/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F9), N36 (≠ D11), E38 (= E13), S46 (≠ N21), R48 (= R23), R95 (= R70), K99 (≠ R74), D100 (≠ V75), K101 (≠ R76), S102 (= S77), R103 (= R79), H129 (= H105), D142 (= D118), S298 (= S282), S300 (= S284), F303 (= F287)
- binding phosphate ion: D214 (= D198), C216 (≠ A200), T218 (= T202)
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
49% identity, 100% coverage: 1:289/290 of query aligns to 26:307/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F9), N36 (≠ D11), E38 (= E13), R95 (= R70), Q96 (= Q71), K98 (≠ R73), H129 (= H105)
- binding phosphate ion: S46 (≠ N21), R48 (= R23), D216 (= D198), T217 (= T199), C218 (≠ A200), T220 (= T202)
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, 100% coverage: 1:290/290 of query aligns to 29:319/321 of O94413
- S172 (= S142) modified: Phosphoserine
Query Sequence
>GFF727 FitnessBrowser__Marino:GFF727
MGQATVGRFSDGETTVEINENVRGHDVFIIQPTCYPTNDNLMELIVMADALRRASATRVT
AVIPYYGYARQDRRVRSTRVAISAKVVADMISSIGVDRVLTVDLHADQIQGFFDIPVDNI
YATPVMLEDIFKQRFENFVVVSPDVGGVVRARAVAKRLDDADLAIIDKRRPKANVSQVMH
IIGDVKDKTCILVDDIIDTAGTLCKAANALKEHGAARVVAYITHPVLSGPAIDNINASQL
DELVVCDTIPLGDKAHNCDRIRVLGMAGLLAESIRRVSNEESISAMFENA
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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