SitesBLAST
Comparing WP_017550051.1 NCBI__GCF_000330705.1:WP_017550051.1 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)
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)
74% identity, 98% coverage: 5:322/324 of query aligns to 2:316/317 of P14193
- RQ 102:103 (= RQ 105:106) binding ATP
- K198 (= K204) 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 (= R206) 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 (≠ K208) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N210) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E213) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (≠ DTGGT 234:238) binding D-ribose 5-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
71% identity, 97% coverage: 10:322/324 of query aligns to 1:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
72% 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)
70% identity, 96% coverage: 12:322/324 of query aligns to 1:295/295 of 1dkuA
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)
54% identity, 97% coverage: 10:322/324 of query aligns to 4:315/318 of Q63XL8
6asvC E. Coli prpp synthetase (see paper)
50% identity, 96% coverage: 13:322/324 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)
50% identity, 96% coverage: 13:323/324 of query aligns to 4:314/315 of P0A717
- D129 (= D137) 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 (= D230) 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 (= D231) 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 (= D234) 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)
52% identity, 95% coverage: 12:318/324 of query aligns to 1:299/300 of 3dahC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
50% identity, 94% coverage: 13:318/324 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)
49% identity, 96% coverage: 13:323/324 of query aligns to 2:306/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F44), D35 (= D46), E37 (= E48), R94 (= R105), R97 (= R108), H129 (= H139)
- binding adenosine monophosphate: R97 (= R108), V99 (≠ S110), R100 (= R111), E131 (≠ P141), F145 (≠ M155), S147 (≠ V157), V173 (≠ T186), A177 (≠ K190)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D230), D213 (= D231), M214 (≠ I232), D216 (= D234), T217 (= T235), G219 (= G237), T220 (= T238)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
49% identity, 96% coverage: 13:323/324 of query aligns to 2:306/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F44), D35 (= D46), E37 (= E48), R94 (= R105), Q95 (= Q106), R97 (= R108), R97 (= R108), R100 (= R111), H129 (= H139), E131 (≠ P141), F145 (≠ M155), S147 (≠ V157), V173 (≠ T186)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D181), D212 (= D230), M214 (≠ I232), D216 (= D234), T217 (= T235)
5t3oA Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus (see paper)
48% identity, 96% coverage: 13:322/324 of query aligns to 2:306/307 of 5t3oA
7pn0A Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus at r32 space group
48% identity, 96% coverage: 13:322/324 of query aligns to 3:307/312 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)
45% identity, 97% coverage: 10:322/324 of query aligns to 3:316/321 of O94413
- S172 (= S179) modified: Phosphoserine
P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
46% identity, 96% coverage: 12:322/324 of query aligns to 3:313/318 of P60891
- 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 (= N123) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L138) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ P141) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (≠ I151) 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 (≠ H153) mutation to H: No effect on catalytic activity.
- Y146 (≠ M155) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (= D193) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A200) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D203) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E213) to H: in a breast cancer sample; somatic mutation
- V219 (≠ I229) to G: in a breast cancer sample; somatic mutation
- H231 (≠ L241) 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)
46% identity, 96% coverage: 12:322/324 of query aligns to 2:312/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R105), Q96 (= Q106), N199 (= N210)
- binding adenosine-5'-triphosphate: F34 (= F44), N36 (≠ D46), E38 (= E48)
- binding phosphate ion: S46 (= S56), R48 (= R58)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H139), D170 (= D181), G172 (= G183), K193 (= K204), R195 (= R206), D219 (= D230), D220 (= D231), D223 (= D234), T224 (= T235), C225 (≠ G236), G226 (= G237), T227 (= T238)
8dbeA Human prps1 with adp; hexamer (see paper)
46% identity, 96% coverage: 12:322/324 of query aligns to 2:312/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F44), N36 (≠ D46), E38 (= E48), R95 (= R105), Q96 (= Q106), K98 (≠ R108), K99 (= K109), D100 (≠ S110), S102 (≠ A112), R103 (= R113), H129 (= H139), D142 (= D152), Y145 (≠ M155), S307 (= S317), V308 (= V318), S309 (= S319), F312 (= F322)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H139), D170 (= D181), D219 (= D230), D220 (= D231), D223 (= D234), T224 (= T235), G226 (= G237), T227 (= T238)
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
49% identity, 93% coverage: 11:312/324 of query aligns to 1:297/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F44), D36 (= D46), E38 (= E48), R95 (= R105), Q96 (= Q106), H130 (= H139)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H139), D214 (= D230), D215 (= D231), I216 (= I232), D218 (= D234), T219 (= T235), A220 (≠ G236), T222 (= T238)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
49% identity, 93% coverage: 11:312/324 of query aligns to 1:296/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F44), D36 (= D46), E38 (= E48), R95 (= R105), Q96 (= Q106), H130 (= H139)
- binding adenosine monophosphate: R98 (= R108), V100 (≠ S110), Y146 (≠ M155), R175 (= R187), A178 (≠ K190), K181 (≠ D193)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H139), D213 (= D230), D214 (= D231), I215 (= I232), D217 (= D234), T218 (= T235), A219 (≠ G236), T221 (= T238)
P9WKE3 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 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
46% identity, 96% coverage: 12:323/324 of query aligns to 11:323/326 of P9WKE3
- K29 (≠ E30) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>WP_017550051.1 NCBI__GCF_000330705.1:WP_017550051.1
MLASSNQYKNSSLRLFSLKGNEPLAEEIAEQIGIPLGKITVQHFSDEEVQVNIEESVRGC
DVFVVQPTSQPVNEHLMQLLIMIDALKRASAATINIVMPYYGYARQDRKSRAREPITAKL
VANLIETAGADRVISLDLHAPQIQGFFDIPIDHLMGVPILSDYFLEHKDLNFDEVVVVSP
DHGGVTRARKMADRLKTPIAIIDKRRPKPNVAEVMNIVGEIEGRTAIIIDDIIDTGGTMK
LAAQALLDKGAKEVYACCTHPVLSGPAISRIEESVIKELVVTNSIQLPEEKKIDKIVGLS
VGELMAQAIVRVYEEESVSILFDT
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