SitesBLAST
Comparing WP_012408935.1 NCBI__GCF_000020025.1:WP_012408935.1 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)
56% identity, 92% coverage: 27:337/338 of query aligns to 7:316/317 of P14193
- RQ 102:103 (≠ RA 122:123) binding ATP
- K198 (= K219) 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 (= R221) 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 (≠ A223) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N225) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E228) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (≠ DTGGT 249:253) 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)
54% identity, 92% coverage: 27:337/338 of query aligns to 1:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
54% identity, 91% coverage: 30:337/338 of query aligns to 2:297/297 of 1ibsA
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)
53% identity, 93% coverage: 24:337/338 of query aligns to 1:315/318 of Q63XL8
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
55% identity, 91% coverage: 30:337/338 of query aligns to 2:295/295 of 1dkuA
6asvC E. Coli prpp synthetase (see paper)
51% identity, 91% coverage: 30:337/338 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)
51% identity, 91% coverage: 30:337/338 of query aligns to 4:313/315 of P0A717
- D129 (= D154) 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 (= D245) 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 (= D246) 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 (= D249) 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, 90% coverage: 30:333/338 of query aligns to 2:299/300 of 3dahC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
51% identity, 90% coverage: 30:333/338 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)
51% identity, 91% coverage: 30:337/338 of query aligns to 2:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F61), D35 (= D63), E37 (= E65), R94 (= R122), R97 (= R125), H129 (= H156)
- binding adenosine monophosphate: R97 (= R125), V99 (≠ T127), R100 (vs. gap), E131 (≠ A158), F145 (≠ Y172), S147 (= S174), V173 (≠ A200), A177 (= A204)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D245), D213 (= D246), M214 (= M247), D216 (= D249), T217 (= T250), G219 (= G252), T220 (= T253)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
51% identity, 91% coverage: 30:337/338 of query aligns to 2:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F61), D35 (= D63), E37 (= E65), R94 (= R122), Q95 (≠ A123), R97 (= R125), R97 (= R125), R100 (vs. gap), H129 (= H156), E131 (≠ A158), F145 (≠ Y172), S147 (= S174), V173 (≠ A200)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D195), D212 (= D245), M214 (= M247), D216 (= D249), T217 (= T250)
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)
48% identity, 94% coverage: 21:337/338 of query aligns to 2:322/326 of P9WKE3
- K29 (≠ R47) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5t3oA Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus (see paper)
48% identity, 91% coverage: 30:337/338 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, 91% coverage: 30:337/338 of query aligns to 3:307/312 of 7pn0A
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, 91% coverage: 30:337/338 of query aligns to 4:313/318 of P60891
- S16 (= S42) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D78) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (= N140) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L155) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ A158) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (≠ F168) 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 (≠ H170) mutation to H: No effect on catalytic activity.
- Y146 (= Y172) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K207) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A215) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D218) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E228) to H: in a breast cancer sample; somatic mutation
- V219 (= V244) to G: in a breast cancer sample; somatic mutation
- H231 (≠ E256) 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, 91% coverage: 30:337/338 of query aligns to 3:312/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R122), Q96 (≠ A123), N199 (= N225)
- binding adenosine-5'-triphosphate: F34 (= F61), N36 (≠ D63), E38 (= E65)
- binding phosphate ion: S46 (= S73), R48 (= R75)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H156), D170 (= D195), G172 (= G197), K193 (= K219), R195 (= R221), D219 (= D245), D220 (= D246), D223 (= D249), T224 (= T250), C225 (≠ G251), G226 (= G252), T227 (= T253)
8dbeA Human prps1 with adp; hexamer (see paper)
45% identity, 91% coverage: 30:337/338 of query aligns to 3:312/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F61), N36 (≠ D63), E38 (= E65), R95 (= R122), Q96 (≠ A123), K98 (≠ R125), K99 (= K126), D100 (≠ T127), S102 (≠ G129), R103 (= R130), H129 (= H156), D142 (= D169), Y145 (= Y172), S307 (= S332), V308 (= V333), S309 (= S334), F312 (= F337)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H156), D170 (= D195), D219 (= D245), D220 (= D246), D223 (= D249), T224 (= T250), G226 (= G252), T227 (= T253)
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
45% identity, 91% coverage: 30:337/338 of query aligns to 2:305/305 of 2hcrA
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
46% identity, 88% coverage: 30:328/338 of query aligns to 3:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F61), D36 (= D63), E38 (= E65), R95 (= R122), Q96 (≠ A123), H130 (= H156)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H156), D214 (= D245), D215 (= D246), I216 (≠ M247), D218 (= D249), T219 (= T250), A220 (≠ G251), T222 (= T253)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
46% identity, 88% coverage: 30:328/338 of query aligns to 3:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F61), D36 (= D63), E38 (= E65), R95 (= R122), Q96 (≠ A123), H130 (= H156)
- binding adenosine monophosphate: R98 (= R125), V100 (≠ T127), Y146 (= Y172), R175 (= R201), A178 (= A204), K181 (= K207)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H156), D213 (= D245), D214 (= D246), I215 (≠ M247), D217 (= D249), T218 (= T250), A219 (≠ G251), T221 (= T253)
Query Sequence
>WP_012408935.1 NCBI__GCF_000020025.1:WP_012408935.1
MNSNRGSAVLSSATFKVQASSTGMTDNHRLRLFSGSANLQLSQEVARYVGMDLGPMIRKR
FADGELYVQIQESIRGCDVYLIQPCCQPVNDHLMELLIMVDACRRASARQVTAVIPYYGY
ARADRKTAGRESITAKLVANLITEAGANRVLAMDLHSAQIQGYFDIPFDHVYGSPVLLDY
LASKELPDLVVVSPDVGGVARARAFAKKLNDAPLAIIDKRRQAHNVAEVLNIIGDVKGKT
AVLVDDMIDTGGTIAEGARLLREEGARQVYACATHAVFSPPAMERLSSGLFEEVIVTNTI
PIPENNRFPQLVVLSVANLLGETIWRIHEDTSVSSMFR
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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