SitesBLAST
Comparing WP_013554179.1 NCBI__GCF_000186245.1:WP_013554179.1 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)
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)
59% identity, 99% coverage: 5:311/311 of query aligns to 8:318/318 of Q63XL8
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)
56% identity, 99% coverage: 1:308/311 of query aligns to 1:313/315 of P0A717
- M1 (= M1) modified: Initiator methionine, Removed
- D129 (= D128) 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 (= D218) 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 (= D219) 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 (= D222) 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)
57% identity, 97% coverage: 6:308/311 of query aligns to 4:311/311 of 6asvC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
57% identity, 96% coverage: 6:304/311 of query aligns to 5:308/308 of 4s2uA
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
57% identity, 96% coverage: 5:304/311 of query aligns to 3:299/300 of 3dahC
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
56% identity, 97% coverage: 6:308/311 of query aligns to 4:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F35), D35 (= D37), E37 (= E39), R94 (= R96), R97 (= R99), H129 (= H130)
- binding adenosine monophosphate: R97 (= R99), V99 (≠ A101), R100 (vs. gap), E131 (≠ S132), F145 (≠ Y146), S147 (= S148), V173 (≠ A174), A177 (≠ Y178)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D218), D213 (= D219), M214 (= M220), D216 (= D222), T217 (= T223), G219 (= G225), T220 (= T226)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
56% identity, 97% coverage: 6:308/311 of query aligns to 4:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F35), D35 (= D37), E37 (= E39), R94 (= R96), Q95 (= Q97), R97 (= R99), R97 (= R99), R100 (vs. gap), H129 (= H130), E131 (≠ S132), F145 (≠ Y146), S147 (= S148), V173 (≠ A174)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D169), D212 (= D218), M214 (= M220), D216 (= D222), T217 (= T223)
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
57% identity, 96% coverage: 2:299/311 of query aligns to 1:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F35), D36 (= D37), E38 (= E39), R95 (= R96), Q96 (= Q97), H130 (= H130)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H130), D214 (= D218), D215 (= D219), I216 (≠ M220), D218 (= D222), T219 (= T223), A220 (= A224), T222 (= T226)
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, 99% coverage: 3:309/311 of query aligns to 9:317/317 of P14193
- RQ 102:103 (= RQ 96:97) binding ATP
- K198 (= K192) 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 (= R194) 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 (≠ K196) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N198) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E201) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 222:226) binding D-ribose 5-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
57% identity, 96% coverage: 2:299/311 of query aligns to 1:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F35), D36 (= D37), E38 (= E39), R95 (= R96), Q96 (= Q97), H130 (= H130)
- binding adenosine monophosphate: R98 (= R99), V100 (≠ A101), Y146 (= Y146), R175 (= R175), A178 (≠ Y178), K181 (≠ S181)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H130), D213 (= D218), D214 (= D219), I215 (≠ M220), D217 (= D222), T218 (= T223), A219 (= A224), T221 (= T226)
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
53% identity, 98% coverage: 3:308/311 of query aligns to 1:295/295 of 1dkuA
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
52% identity, 98% coverage: 3:308/311 of query aligns to 3:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
52% identity, 98% coverage: 3:308/311 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, 99% coverage: 1:309/311 of query aligns to 1:314/318 of P60891
- M1 (= M1) modified: Initiator methionine, Removed
- S16 (= S16) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D52) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ D114) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L129) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (= S132) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V142) 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 (= N144) mutation to H: No effect on catalytic activity.
- Y146 (= Y146) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ S181) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (≠ V188) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D191) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E201) to H: in a breast cancer sample; somatic mutation
- V219 (≠ I217) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K229) 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, 99% coverage: 3:309/311 of query aligns to 2:313/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R96), Q96 (= Q97), N199 (= N198)
- binding adenosine-5'-triphosphate: F34 (= F35), N36 (≠ D37), E38 (= E39)
- binding phosphate ion: S46 (= S47), R48 (= R49)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H130), D170 (= D169), G172 (= G171), K193 (= K192), R195 (= R194), D219 (= D218), D220 (= D219), D223 (= D222), T224 (= T223), C225 (≠ A224), G226 (= G225), T227 (= T226)
8dbeA Human prps1 with adp; hexamer (see paper)
48% identity, 99% coverage: 3:309/311 of query aligns to 2:313/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F35), N36 (≠ D37), E38 (= E39), R95 (= R96), Q96 (= Q97), K98 (≠ R99), K99 (= K100), D100 (≠ A101), S102 (≠ P103), R103 (= R104), H129 (= H130), D142 (= D143), Y145 (= Y146), S307 (= S303), V308 (= V304), S309 (≠ N305), F312 (= F308)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H130), D170 (= D169), D219 (= D218), D220 (= D219), D223 (= D222), T224 (= T223), G226 (= G225), T227 (= T226)
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
48% identity, 98% coverage: 3:308/311 of query aligns to 1:305/305 of 2hcrA
7yk1A Structural basis of human prps2 filaments (see paper)
47% identity, 99% coverage: 3:309/311 of query aligns to 2:304/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F35), N36 (≠ D37), E38 (= E39), S46 (= S47), R48 (= R49), R95 (= R96), K99 (= K100), D100 (≠ A101), K101 (≠ A102), S102 (≠ P103), R103 (= R104), H129 (= H130), D142 (= D143), S298 (= S303), S300 (≠ N305), F303 (= F308)
- binding phosphate ion: D214 (= D222), C216 (≠ A224), T218 (= T226)
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
47% identity, 99% coverage: 3:309/311 of query aligns to 2:306/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F35), N36 (≠ D37), E38 (= E39), R95 (= R96), Q96 (= Q97), K98 (≠ R99), H129 (= H130)
- binding phosphate ion: S46 (= S47), R48 (= R49), D216 (= D222), T217 (= T223), C218 (≠ A224), T220 (= T226)
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, 98% coverage: 6:309/311 of query aligns to 8:317/321 of O94413
- S172 (= S167) modified: Phosphoserine
Query Sequence
>WP_013554179.1 NCBI__GCF_000186245.1:WP_013554179.1
MSNYMLFSGTANPPLSQAIADYLEMPLSGATINRFSDGEINVQIAESVRGKDVFIIQPTC
APANANLMELLIMTDALKRSSAKSITAVVPYYGYARQDRKAAPRVPITAKLVADMMEKAG
ITRVVTVDLHASQIQGFFDIPVDNLYGSILFIDYIRSKNFANPIIASPDIGGVARARYFA
SRLGMDMVIVDKRREKANVAEVMNIIGDVRGRDVILIDDMVDTAGTMVKGAAALKEAGAT
SVMACCTHPVLSGPAIDRIRDGALDELVVSDTIPLKAECKKIKVLSTAQMLGEVIRRVQN
NESVNSLFATT
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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