SitesBLAST
Comparing 350276 FitnessBrowser__Btheta:350276 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)
47% identity, 99% coverage: 1:303/305 of query aligns to 8:315/318 of Q63XL8
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
47% identity, 98% coverage: 1:299/305 of query aligns to 3:299/300 of 3dahC
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)
47% identity, 98% coverage: 2:300/305 of query aligns to 12:313/317 of P14193
- RQ 102:103 (= RQ 91:92) binding
- K198 (= K187) 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 (= R189) 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 (≠ K191) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N193) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (≠ A196) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 217:221) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7pn0A Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus at r32 space group
46% identity, 100% coverage: 1:305/305 of query aligns to 4:309/312 of 7pn0A
5t3oA Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus (see paper)
46% identity, 99% coverage: 1:303/305 of query aligns to 3:306/307 of 5t3oA
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
48% identity, 96% coverage: 1:293/305 of query aligns to 4:296/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F31), D36 (= D33), E38 (= E35), R95 (= R91), Q96 (= Q92), H130 (= H125)
- binding adenosine monophosphate: R98 (= R94), V100 (≠ D96), Y146 (= Y141), R175 (= R170), A178 (≠ T173), K181 (= K176)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H125), D213 (= D213), D214 (= D214), I215 (= I215), D217 (= D217), T218 (= T218), A219 (= A219), T221 (= T221)
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
47% identity, 96% coverage: 1:293/305 of query aligns to 4:297/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F31), D36 (= D33), E38 (= E35), R95 (= R91), Q96 (= Q92), H130 (= H125)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H125), D214 (= D213), D215 (= D214), I216 (= I215), D218 (= D217), T219 (= T218), A220 (= A219), T222 (= T221)
6asvC E. Coli prpp synthetase (see paper)
44% identity, 99% coverage: 2:303/305 of query aligns to 4:311/311 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)
44% identity, 99% coverage: 2:303/305 of query aligns to 6:313/315 of P0A717
- D129 (= D123) 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 (= D213) 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 (= D214) 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 (= D217) 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
P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
47% identity, 98% coverage: 2:300/305 of query aligns to 6:310/318 of P60891
- S16 (≠ A12) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (≠ H48) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ D109) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L124) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ D127) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (= V137) 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 (≠ H139) mutation to H: No effect on catalytic activity.
- Y146 (= Y141) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K176) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (≠ V183) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ N186) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ A196) to H: in a breast cancer sample; somatic mutation
- V219 (≠ I212) to G: in a breast cancer sample; somatic mutation
- H231 (≠ K224) 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)
47% identity, 98% coverage: 2:300/305 of query aligns to 5:309/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R91), Q96 (= Q92), N199 (= N193)
- binding adenosine-5'-triphosphate: F34 (= F31), N36 (≠ D33), E38 (= E35)
- binding phosphate ion: S46 (= S43), R48 (= R45)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H125), D170 (= D164), G172 (= G166), K193 (= K187), R195 (= R189), D219 (= D213), D220 (= D214), D223 (= D217), T224 (= T218), C225 (≠ A219), G226 (= G220), T227 (= T221)
8dbeA Human prps1 with adp; hexamer (see paper)
47% identity, 98% coverage: 2:300/305 of query aligns to 5:309/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F31), N36 (≠ D33), E38 (= E35), R95 (= R91), Q96 (= Q92), K98 (≠ R94), K99 (= K95), D100 (= D96), S102 (≠ P98), R103 (= R99), H129 (= H125), D142 (= D138), Y145 (= Y141), S307 (= S298), V308 (≠ I299), S309 (= S300)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H125), D170 (= D164), D219 (= D213), D220 (= D214), D223 (= D217), T224 (= T218), G226 (= G220), T227 (= T221)
Sites not aligning to the query:
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
44% identity, 98% coverage: 2:299/305 of query aligns to 5:308/308 of 4s2uA
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
46% identity, 98% coverage: 2:300/305 of query aligns to 4:294/297 of 1ibsA
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
46% identity, 98% coverage: 2:300/305 of query aligns to 6:296/299 of 1ibsB
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
46% identity, 98% coverage: 2:300/305 of query aligns to 4:292/295 of 1dkuA
Sites not aligning to the query:
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
43% identity, 99% coverage: 2:303/305 of query aligns to 4:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F31), D35 (= D33), E37 (= E35), R94 (= R91), R97 (= R94), H129 (= H125)
- binding adenosine monophosphate: R97 (= R94), V99 (≠ D96), R100 (≠ K97), E131 (≠ D127), F145 (≠ Y141), S147 (= S143), V173 (≠ K169), A177 (≠ T173)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D213), D213 (= D214), M214 (≠ I215), D216 (= D217), T217 (= T218), G219 (= G220), T220 (= T221)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
43% identity, 99% coverage: 2:303/305 of query aligns to 4:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F31), D35 (= D33), E37 (= E35), R94 (= R91), Q95 (= Q92), R97 (= R94), R97 (= R94), R100 (≠ K97), H129 (= H125), E131 (≠ D127), F145 (≠ Y141), S147 (= S143), V173 (≠ K169)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D164), D212 (= D213), M214 (≠ I215), D216 (= D217), T217 (= T218)
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)
42% identity, 98% coverage: 2:300/305 of query aligns to 8:313/321 of O94413
- S172 (≠ T162) modified: Phosphoserine
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
45% identity, 98% coverage: 2:300/305 of query aligns to 4:302/305 of 2hcrA
Query Sequence
>350276 FitnessBrowser__Btheta:350276
MVFSGTNSRYLAEKICASLNCPLGNMNITHFADGEFAVSYEESIRGAHVFLVQSTFPNSD
NLMELLLMIDAAKRASAKSVVAVIPYFGWARQDRKDKPRVSIGAKLVADLLSVAGIDRLI
TMDLHADQIQGFFNIPVDHLYASAVFLPYIQSLKLEDLVIATPDVGGSKRASTFSKYLGV
PLVLCNKSREKANEVASMQIIGDVKDKNVVLIDDIVDTAGTITKAANIMMEAGAKSVRAI
ASHCVMSDPASFRVQESGLTEMVFTDSIPYAKKCAKVKQLSIADMFAETIKRVMNNESIS
SQYII
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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