SitesBLAST
Comparing WP_092482873.1 NCBI__GCF_900115975.1:WP_092482873.1 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)
66% identity, 98% coverage: 5:313/314 of query aligns to 8:316/317 of P14193
- RQ 102:103 (= RQ 99:100) binding ATP
- 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 (≠ E199) 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 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)
63% identity, 98% coverage: 5:313/314 of query aligns to 2:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
64% identity, 98% coverage: 6:313/314 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)
63% identity, 98% coverage: 6:313/314 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)
56% identity, 100% coverage: 1:313/314 of query aligns to 1:315/318 of Q63XL8
6asvC E. Coli prpp synthetase (see paper)
54% identity, 98% coverage: 7:313/314 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)
54% identity, 98% coverage: 7:314/314 of query aligns to 4:314/315 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
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
54% identity, 96% coverage: 7:309/314 of query aligns to 3:308/308 of 4s2uA
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
55% identity, 96% coverage: 7:309/314 of query aligns to 2:299/300 of 3dahC
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
53% identity, 98% coverage: 7:314/314 of query aligns to 2:306/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F38), D35 (= D40), E37 (= E42), R94 (= R99), R97 (= R102), H129 (= H133)
- binding adenosine monophosphate: R97 (= R102), V99 (≠ T104), R100 (= R105), E131 (≠ G135), F145 (≠ P149), S147 (≠ V151), V173 (≠ Q177), A177 (≠ D181)
- 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)
53% identity, 98% coverage: 7:314/314 of query aligns to 2:306/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F38), D35 (= D40), E37 (= E42), R94 (= R99), Q95 (= Q100), R97 (= R102), R97 (= R102), R100 (= R105), H129 (= H133), E131 (≠ G135), F145 (≠ P149), S147 (≠ V151), V173 (≠ Q177)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D172), D212 (= D221), M214 (≠ I223), D216 (= D225), T217 (= T226)
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
52% identity, 95% coverage: 7:304/314 of query aligns to 3:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F38), D36 (= D40), E38 (= E42), 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
52% identity, 95% coverage: 7:304/314 of query aligns to 3:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F38), D36 (= D40), E38 (= E42), R95 (= R99), Q96 (= Q100), H130 (= H133)
- binding adenosine monophosphate: R98 (= R102), V100 (≠ T104), Y146 (≠ P149), R175 (= R178), A178 (≠ D181), K181 (≠ E184)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H133), D213 (= D221), D214 (= D222), I215 (= I223), D217 (= D225), T218 (= T226), A219 (= A227), T221 (= T229)
7pn0A Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus at r32 space group
47% identity, 98% coverage: 7:313/314 of query aligns to 3:307/312 of 7pn0A
5t3oA Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus (see paper)
47% identity, 98% coverage: 7:313/314 of query aligns to 2:306/307 of 5t3oA
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)
47% identity, 99% coverage: 3:314/314 of query aligns to 8:323/326 of P9WKE3
- K29 (≠ H24) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
46% identity, 98% coverage: 7:313/314 of query aligns to 6:316/321 of O94413
- S172 (= S170) 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)
45% identity, 98% coverage: 6:313/314 of query aligns to 3:313/318 of P60891
- S16 (≠ A19) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D55) 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 (≠ G135) 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 (≠ P149) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ E184) 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 (≠ I220) to G: in a breast cancer sample; somatic mutation
- H231 (≠ Q232) 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)
45% identity, 98% coverage: 6:313/314 of query aligns to 2:312/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R99), Q96 (= Q100), N199 (= N201)
- binding adenosine-5'-triphosphate: F34 (= F38), N36 (≠ D40), E38 (= E42)
- binding phosphate ion: S46 (= S50), R48 (= R52)
- 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)
45% identity, 98% coverage: 6:313/314 of query aligns to 2:312/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F38), N36 (≠ D40), E38 (= E42), R95 (= R99), Q96 (= Q100), K98 (≠ R102), K99 (= K103), D100 (≠ T104), S102 (≠ A106), R103 (= R107), H129 (= H133), D142 (= D146), Y145 (≠ P149), S307 (= S308), V308 (= V309), S309 (= S310), F312 (= F313)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H133), D170 (= D172), D219 (= D221), D220 (= D222), D223 (= D225), T224 (= T226), G226 (= G228), T227 (= T229)
Query Sequence
>WP_092482873.1 NCBI__GCF_900115975.1:WP_092482873.1
MSSRQRLKIFTGNANAALAEEIAHYLGVSVGAAKVSRFSDGEIQVKINESVRGADVFIIQ
PTCEPVNEHLMELLVMVDAVRRASARRITAVMPYYGYARQDRKTRARDPITAKLVANLLF
ASGARRVITMDLHAGQIQGFFDIPVDHLPGVPLLAQYFMQQKLKDVVVVSPDLGGVQRAR
DLAERIGAPIAIIDKRRPEPNVAEIMNIIGDIRGKKVIMIDDIIDTAGTITQGAAALKEW
GATDIYVCCTHPVLSGPAVDRLVGAPIKEVLVTNTIPLPEDKTLEKIKILSVAPLLGEAI
IRIHEDLSVSKLFD
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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