SitesBLAST
Comparing 5210475 FitnessBrowser__PV4:5210475 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)
83% identity, 97% coverage: 10:324/324 of query aligns to 1:315/315 of P0A717
- M1 (≠ V10) modified: Initiator methionine, Removed
- D129 (= D138) 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 (= D229) 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 (= D230) 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 (= D233) 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.
6asvC E. Coli prpp synthetase (see paper)
83% identity, 96% coverage: 12:322/324 of query aligns to 1:311/311 of 6asvC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
83% identity, 95% coverage: 11:318/324 of query aligns to 1:308/308 of 4s2uA
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
82% identity, 97% coverage: 12:324/324 of query aligns to 1:307/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F44), D35 (= D46), E37 (= E48), R94 (= R105), R97 (= R108), H129 (= H140)
- binding adenosine monophosphate: R97 (= R108), V99 (= V110), R100 (= R111), E131 (= E142), F145 (= F156), S147 (= S158), V173 (= V184), A177 (= A188)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D229), D213 (= D230), M214 (= M231), D216 (= D233), T217 (= T234), G219 (= G236), T220 (= T237)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
82% identity, 97% coverage: 12:324/324 of query aligns to 1:307/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F44), D35 (= D46), E37 (= E48), R94 (= R105), Q95 (= Q106), R97 (= R108), R97 (= R108), R100 (= R111), H129 (= H140), E131 (= E142), F145 (= F156), S147 (= S158), V173 (= V184)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D179), D212 (= D229), M214 (= M231), D216 (= D233), T217 (= T234)
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)
63% identity, 96% coverage: 13:322/324 of query aligns to 7:315/318 of Q63XL8
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
64% identity, 92% coverage: 15:313/324 of query aligns to 5:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F44), D36 (= D46), E38 (= E48), R95 (= R105), Q96 (= Q106), H130 (= H140)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H140), D214 (= D229), D215 (= D230), I216 (≠ M231), D218 (= D233), T219 (= T234), A220 (≠ G235), T222 (= T237)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
64% identity, 92% coverage: 15:313/324 of query aligns to 5:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F44), D36 (= D46), E38 (= E48), R95 (= R105), Q96 (= Q106), H130 (= H140)
- binding adenosine monophosphate: R98 (= R108), V100 (= V110), Y146 (≠ F156), R175 (= R185), A178 (= A188), K181 (= K191)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H140), D213 (= D229), D214 (= D230), I215 (≠ M231), D217 (= D233), T218 (= T234), A219 (≠ G235), T221 (= T237)
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
61% identity, 94% coverage: 13:318/324 of query aligns to 2:299/300 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)
51% identity, 96% coverage: 12:322/324 of query aligns to 9:316/317 of P14193
- RQ 102:103 (= RQ 105:106) binding
- K198 (= K203) 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 (= R205) 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 (≠ Q207) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N209) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (≠ Q212) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (≠ DTGGT 233:237) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
49% identity, 96% coverage: 12:322/324 of query aligns to 3:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
49% identity, 96% coverage: 12:322/324 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)
49% identity, 96% coverage: 12:322/324 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)
48% identity, 97% coverage: 10:324/324 of query aligns to 1:315/318 of P60891
- M1 (≠ V10) modified: Initiator methionine, Removed
- S16 (≠ A25) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D61) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ D124) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L139) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ E142) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V152) 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 (= N154) mutation to H: No effect on catalytic activity.
- Y146 (≠ F156) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K191) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A199) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D202) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ Q212) to H: in a breast cancer sample; somatic mutation
- V219 (= V228) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K240) to D: in a colorectal cancer sample; somatic mutation
8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
48% identity, 97% coverage: 11:324/324 of query aligns to 1:314/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R105), Q96 (= Q106), N199 (= N209)
- binding adenosine-5'-triphosphate: F34 (= F44), N36 (≠ D46), E38 (= E48)
- binding phosphate ion: S46 (≠ N56), R48 (= R58)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H140), D170 (= D179), G172 (= G181), K193 (= K203), R195 (= R205), D219 (= D229), D220 (= D230), D223 (= D233), T224 (= T234), C225 (≠ G235), G226 (= G236), T227 (= T237)
8dbeA Human prps1 with adp; hexamer (see paper)
48% identity, 97% coverage: 11:324/324 of query aligns to 1:314/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F44), N36 (≠ D46), E38 (= E48), R95 (= R105), Q96 (= Q106), K98 (≠ R108), K99 (≠ R109), D100 (≠ V110), S102 (= S112), R103 (= R114), H129 (= H140), D142 (= D153), Y145 (≠ F156), S307 (= S317), V308 (≠ I318), S309 (= S319), F312 (= F322)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H140), D170 (= D179), D219 (= D229), D220 (= D230), D223 (= D233), T224 (= T234), G226 (= G236), T227 (= T237)
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, 96% coverage: 13:322/324 of query aligns to 6:316/321 of O94413
- S172 (= S177) modified: Phosphoserine
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
47% identity, 97% coverage: 11:324/324 of query aligns to 1:307/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F44), N36 (≠ D46), E38 (= E48), R95 (= R105), Q96 (= Q106), K98 (≠ R108), H129 (= H140)
- binding phosphate ion: S46 (≠ N56), R48 (= R58), D216 (= D233), T217 (= T234), C218 (≠ G235), T220 (= T237)
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
47% identity, 96% coverage: 12:322/324 of query aligns to 1:305/305 of 2hcrA
7yk1A Structural basis of human prps2 filaments (see paper)
46% identity, 97% coverage: 11:324/324 of query aligns to 1:305/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F44), N36 (≠ D46), E38 (= E48), S46 (≠ N56), R48 (= R58), R95 (= R105), K99 (≠ R109), D100 (≠ V110), K101 (≠ R111), S102 (= S112), R103 (= R114), H129 (= H140), D142 (= D153), S298 (= S317), S300 (= S319), F303 (= F322)
- binding phosphate ion: D214 (= D233), C216 (≠ G235), T218 (= T237)
Query Sequence
>5210475 FitnessBrowser__PV4:5210475
MKHTPEVHTVPDIKLFAGNATPSLAKKIADRLFCKLGDAEVGVFSDGEISVQINENVRGA
DVFIIQSTCAPTNDNLMELIVMVDALRRASAGRITAVIPYFGYARQDRRVRSARVPITAK
VVADFLSSVGVDRVLTCDLHAEQIQGFFDVPVDNVFGSPVLLEDMLAKQLDNPVVVSPDI
GGVVRARAVAKLLDDSDLAIIDKRRPQANVAQVMHIIGDVQGRDCIIVDDMIDTGGTLCK
AAEALKEHGANRVFAYATHPVFSGNAPKNIAESVIDEVIVTDTIPLSEEMAALDKVTQLT
MSSVMAEAIRRVSNEESISAMFKH
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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