SitesBLAST
Comparing HSERO_RS19570 FitnessBrowser__HerbieS:HSERO_RS19570 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)
84% identity, 99% coverage: 4:316/316 of query aligns to 5:317/318 of Q63XL8
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
82% identity, 97% coverage: 5:311/316 of query aligns to 1:300/300 of 3dahC
6asvC E. Coli prpp synthetase (see paper)
64% identity, 98% coverage: 5:314/316 of query aligns to 1:311/311 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)
64% identity, 99% coverage: 3:314/316 of query aligns to 1:313/315 of P0A717
- M1 (≠ L3) modified: Initiator methionine, Removed
- 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.
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
64% identity, 97% coverage: 5:310/316 of query aligns to 2:308/308 of 4s2uA
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
65% identity, 95% coverage: 6:304/316 of query aligns to 3:297/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F37), D36 (= D39), E38 (= E41), R95 (= R98), Q96 (= Q99), H130 (= H133)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H133), D214 (= D221), D215 (= D222), I216 (≠ M223), 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
65% identity, 95% coverage: 6:304/316 of query aligns to 3:296/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F37), D36 (= D39), E38 (= E41), R95 (= R98), Q96 (= Q99), H130 (= H133)
- binding adenosine monophosphate: R98 (= R101), V100 (≠ P103), Y146 (= Y149), R175 (= R178), A178 (= A181), K181 (= K184)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H133), D213 (= D221), D214 (= D222), I215 (≠ M223), D217 (= D225), T218 (= T226), A219 (= A227), T221 (= T229)
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
62% identity, 98% coverage: 5:314/316 of query aligns to 1:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F37), D35 (= D39), E37 (= E41), R94 (= R98), R97 (= R101), H129 (= H133)
- binding adenosine monophosphate: R97 (= R101), V99 (≠ P103), R100 (= R104), E131 (≠ D135), F145 (≠ Y149), S147 (= S151), V173 (= V177), A177 (= A181)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D221), D213 (= D222), M214 (= M223), 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)
62% identity, 98% coverage: 5:314/316 of query aligns to 1:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F37), D35 (= D39), E37 (= E41), R94 (= R98), Q95 (= Q99), R97 (= R101), R97 (= R101), R100 (= R104), H129 (= H133), E131 (≠ D135), F145 (≠ Y149), S147 (= S151), V173 (= V177)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D172), D212 (= D221), M214 (= M223), D216 (= D225), T217 (= T226)
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)
55% identity, 99% coverage: 4:315/316 of query aligns to 8:317/317 of P14193
- RQ 102:103 (= RQ 98:99) 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 (≠ K199) 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
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
53% identity, 98% coverage: 4:314/316 of query aligns to 2:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
53% identity, 98% coverage: 5:314/316 of query aligns to 1:297/297 of 1ibsA
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
54% identity, 98% coverage: 5:314/316 of query aligns to 1:295/295 of 1dkuA
P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
47% identity, 99% coverage: 3:316/316 of query aligns to 1:315/318 of P60891
- M1 (≠ L3) modified: Initiator methionine, Removed
- S16 (≠ A18) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D54) 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 (≠ D135) 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 (= N147) mutation to H: No effect on catalytic activity.
- Y146 (= Y149) 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 (= A191) 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 (≠ M220) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K232) to D: in a colorectal cancer sample; somatic mutation
8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
47% identity, 99% coverage: 5:316/316 of query aligns to 2:314/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R98), Q96 (= Q99), N199 (= N201)
- binding adenosine-5'-triphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41)
- binding phosphate ion: S46 (≠ N49), R48 (= R51)
- 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)
47% identity, 99% coverage: 5:316/316 of query aligns to 2:314/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41), R95 (= R98), Q96 (= Q99), K98 (≠ R101), K99 (≠ R102), D100 (≠ P103), S102 (= S105), R103 (= R107), H129 (= H133), D142 (= D146), Y145 (= Y149), S307 (= S309), V308 (= V310), S309 (≠ M311), F312 (= F314)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H133), D170 (= D172), D219 (= D221), D220 (= D222), D223 (= D225), T224 (= T226), G226 (= G228), T227 (= T229)
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)
47% identity, 100% coverage: 1:315/316 of query aligns to 1:317/321 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)
46% identity, 98% coverage: 5:314/316 of query aligns to 1:305/305 of 2hcrA
7yk1A Structural basis of human prps2 filaments (see paper)
46% identity, 99% coverage: 5:316/316 of query aligns to 2:305/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F37), N36 (≠ D39), E38 (= E41), S46 (≠ N49), R48 (= R51), R95 (= R98), K99 (≠ R102), D100 (≠ P103), K101 (≠ R104), S102 (= S105), R103 (= R107), H129 (= H133), D142 (= D146), S298 (= S309), S300 (≠ M311), F303 (= F314)
- binding phosphate ion: D214 (= D225), C216 (≠ A227), T218 (= T229)
7pn0A Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus at r32 space group
46% identity, 98% coverage: 6:314/316 of query aligns to 3:307/312 of 7pn0A
Query Sequence
>HSERO_RS19570 FitnessBrowser__HerbieS:HSERO_RS19570
MALENLMVFTGNANPELARGVAEKLGIPLGKANVSKFSDGEVMVEINENVRGKDVFVLQS
TCAPTNDNLMEIMIMVDALKRASAGRITAAIPYYGYARQDRRPRSARVAISAKVVANMLQ
EAGVERVLIMDLHADQIQGFFDIPVDNIYASPILLGDLVNKNYEDLLVVSPDVGGVVRAR
ALAKRLNCDLAIIDKRRPKANVSEVMNIIGEVEGRNCVIMDDMVDTAGTLTKAAEVLKER
GAKKVVAYCTHPVLSGPAIERIANSPLDELVVTDTIPLSPAARGCPKVRQLTCADLLAET
FKRITKGDSVMSLFAE
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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