SitesBLAST
Comparing WP_068173800.1 NCBI__GCF_001592305.1:WP_068173800.1 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)
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)
74% identity, 96% coverage: 8:319/324 of query aligns to 7:317/318 of Q63XL8
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
72% identity, 95% coverage: 8:314/324 of query aligns to 2:300/300 of 3dahC
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, 96% coverage: 6:317/324 of query aligns to 2:313/315 of P0A717
- D129 (= D133) 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 (= D223) 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 (= D224) 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 (= D227) 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)
64% identity, 96% coverage: 7:317/324 of query aligns to 1:311/311 of 6asvC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
65% identity, 95% coverage: 6:313/324 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)
63% identity, 96% coverage: 7:317/324 of query aligns to 1:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F39), D35 (= D41), E37 (= E43), R94 (= R100), R97 (= R103), H129 (= H135)
- binding adenosine monophosphate: R97 (= R103), V99 (≠ P105), R100 (= R106), E131 (≠ D137), F145 (≠ Y151), S147 (= S153), V173 (= V179), A177 (= A183)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D223), D213 (= D224), M214 (= M225), D216 (= D227), T217 (= T228), G219 (= G230), T220 (= T231)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
63% identity, 96% coverage: 7:317/324 of query aligns to 1:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F39), D35 (= D41), E37 (= E43), R94 (= R100), Q95 (= Q101), R97 (= R103), R97 (= R103), R100 (= R106), H129 (= H135), E131 (≠ D137), F145 (≠ Y151), S147 (= S153), V173 (= V179)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D174), D212 (= D223), M214 (= M225), D216 (= D227), T217 (= T228)
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
62% identity, 93% coverage: 8:307/324 of query aligns to 3:297/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F39), D36 (= D41), E38 (= E43), R95 (= R100), Q96 (= Q101), H130 (= H135)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H135), D214 (= D223), D215 (= D224), I216 (≠ M225), D218 (= D227), T219 (= T228), A220 (= A229), T222 (= T231)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
61% identity, 93% coverage: 8:307/324 of query aligns to 3:296/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F39), D36 (= D41), E38 (= E43), R95 (= R100), Q96 (= Q101), H130 (= H135)
- binding adenosine monophosphate: R98 (= R103), V100 (≠ P105), Y146 (= Y151), R175 (= R180), A178 (= A183), K181 (= K186)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H135), D213 (= D223), D214 (= D224), I215 (≠ M225), D217 (= D227), T218 (= T228), A219 (= A229), T221 (= T231)
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)
54% identity, 96% coverage: 7:318/324 of query aligns to 9:317/317 of P14193
- RQ 102:103 (= RQ 100:101) binding ATP
- K198 (= K197) 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 (= R199) 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 (≠ K201) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N203) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E206) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 227:231) 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)
52% identity, 96% coverage: 7:317/324 of query aligns to 3:299/299 of 1ibsB
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
52% identity, 96% coverage: 7:317/324 of query aligns to 1:295/295 of 1dkuA
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
52% identity, 96% coverage: 7:317/324 of query aligns to 1:297/297 of 1ibsA
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: 6:318/324 of query aligns to 2:314/318 of P60891
- S16 (≠ A20) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (≠ H56) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (= N119) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L134) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ D137) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V147) 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 (= N149) mutation to H: No effect on catalytic activity.
- Y146 (= Y151) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K186) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A193) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D196) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E206) to H: in a breast cancer sample; somatic mutation
- V219 (≠ M222) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K234) 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)
48% identity, 97% coverage: 6:318/324 of query aligns to 1:313/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R100), Q96 (= Q101), N199 (= N203)
- binding adenosine-5'-triphosphate: F34 (= F39), N36 (≠ D41), E38 (= E43)
- binding phosphate ion: S46 (≠ N51), R48 (= R53)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H135), D170 (= D174), G172 (= G176), K193 (= K197), R195 (= R199), D219 (= D223), D220 (= D224), D223 (= D227), T224 (= T228), C225 (≠ A229), G226 (= G230), T227 (= T231)
8dbeA Human prps1 with adp; hexamer (see paper)
48% identity, 97% coverage: 6:318/324 of query aligns to 1:313/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F39), N36 (≠ D41), E38 (= E43), R95 (= R100), Q96 (= Q101), K98 (≠ R103), K99 (≠ R104), D100 (≠ P105), S102 (= S108), R103 (= R109), H129 (= H135), D142 (= D148), Y145 (= Y151), S307 (= S312), V308 (= V313), S309 (≠ M314), F312 (= F317)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H135), D170 (= D174), D219 (= D223), D220 (= D224), D223 (= D227), T224 (= T228), G226 (= G230), T227 (= T231)
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)
48% identity, 95% coverage: 10:318/324 of query aligns to 8:317/321 of O94413
- S172 (= S172) modified: Phosphoserine
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
47% identity, 95% coverage: 10:317/324 of query aligns to 4:305/305 of 2hcrA
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
47% identity, 97% coverage: 6:318/324 of query aligns to 1:306/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F39), N36 (≠ D41), E38 (= E43), R95 (= R100), Q96 (= Q101), K98 (≠ R103), H129 (= H135)
- binding phosphate ion: S46 (≠ N51), R48 (= R53), D216 (= D227), T217 (= T228), C218 (≠ A229), T220 (= T231)
7yk1A Structural basis of human prps2 filaments (see paper)
46% identity, 97% coverage: 6:318/324 of query aligns to 1:304/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F39), N36 (≠ D41), E38 (= E43), S46 (≠ N51), R48 (= R53), R95 (= R100), K99 (≠ R104), D100 (≠ P105), K101 (≠ R106), S102 (= S108), R103 (= R109), H129 (= H135), D142 (= D148), S298 (= S312), S300 (≠ M314), F303 (= F317)
- binding phosphate ion: D214 (= D227), C216 (≠ A229), T218 (= T231)
Query Sequence
>WP_068173800.1 NCBI__GCF_001592305.1:WP_068173800.1
MQVQPPDFMIFTGNANPVLASEIAQNLGTQLGAANVGRFSDGEVTVEITQNVRARHVFVI
QSTCAPTNENLMELIIMVDALKRASAVSISAVIPYFGYARQDRRPRSSRVPISAKVVANM
LQAVGVNRVLTMDLHADQIQGFFDIPVDNIYASPVLLGDLRQKNYSDLLVVSPDVGGVVR
ARALAKQLNCDMAIIDKRRPKANVSEVMHVIGDIDGRNCVIMDDMIDTAGTLVKAAEVLK
ERGAKHVYSYCTHPIFSGPAIERIAKGTALDEVVVTNTIPLSQAAQACSKIRQLSVAPLM
AETIARIASGESVMSLFADQDNLF
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