SitesBLAST
Comparing Synpcc7942_2113 FitnessBrowser__SynE:Synpcc7942_2113 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)
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)
55% identity, 94% coverage: 19:330/331 of query aligns to 7:316/317 of P14193
- RQ 102:103 (≠ RA 114:115) binding
- K198 (= K211) 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 (= R213) 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 (≠ A215) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (= N217) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E220) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (= DTAGT 241:245) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
55% identity, 93% coverage: 22:330/331 of query aligns to 7:315/318 of Q63XL8
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
54% identity, 94% coverage: 19:330/331 of query aligns to 1:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
54% identity, 93% coverage: 22:330/331 of query aligns to 2:297/297 of 1ibsA
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
54% identity, 93% coverage: 22:330/331 of query aligns to 2:295/295 of 1dkuA
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
53% identity, 92% coverage: 22:326/331 of query aligns to 2:299/300 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)
50% identity, 95% coverage: 16:330/331 of query aligns to 1:313/315 of P0A717
- M1 (≠ L16) modified: Initiator methionine, Removed
- D129 (= D146) 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 (= D237) 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 (= D238) 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 (= D241) 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)
50% identity, 93% coverage: 22:330/331 of query aligns to 2:311/311 of 6asvC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
50% identity, 92% coverage: 22:326/331 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)
50% identity, 93% coverage: 22:330/331 of query aligns to 2:305/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F53), D35 (= D55), E37 (= E57), R94 (= R114), R97 (= R117), H129 (= H148)
- binding adenosine monophosphate: R97 (= R117), V99 (≠ T119), R100 (vs. gap), E131 (≠ A150), F145 (≠ Y164), S147 (= S166), V173 (≠ A192), A177 (= A196)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D237), D213 (= D238), M214 (= M239), D216 (= D241), T217 (= T242), G219 (= G244), T220 (= T245)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
50% identity, 93% coverage: 22:330/331 of query aligns to 2:305/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F53), D35 (= D55), E37 (= E57), R94 (= R114), Q95 (≠ A115), R97 (= R117), R97 (= R117), R100 (vs. gap), H129 (= H148), E131 (≠ A150), F145 (≠ Y164), S147 (= S166), V173 (≠ A192)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D187), D212 (= D237), M214 (= M239), D216 (= D241), T217 (= T242)
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, 95% coverage: 18:330/331 of query aligns to 7:322/326 of P9WKE3
- K29 (≠ R39) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
47% identity, 91% coverage: 22:321/331 of query aligns to 3:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F53), D36 (= D55), E38 (= E57), R95 (= R114), Q96 (≠ A115), H130 (= H148)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H148), D214 (= D237), D215 (= D238), I216 (≠ M239), D218 (= D241), T219 (= T242), A220 (= A243), T222 (= T245)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
47% identity, 91% coverage: 22:321/331 of query aligns to 3:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F53), D36 (= D55), E38 (= E57), R95 (= R114), Q96 (≠ A115), H130 (= H148)
- binding adenosine monophosphate: R98 (= R117), V100 (≠ T119), Y146 (= Y164), R175 (= R193), A178 (= A196), K181 (= K199)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H148), D213 (= D237), D214 (= D238), I215 (≠ M239), D217 (= D241), T218 (= T242), A219 (= A243), T221 (= T245)
5t3oA Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus (see paper)
48% identity, 93% coverage: 22:330/331 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, 93% coverage: 22:330/331 of query aligns to 3:307/312 of 7pn0A
8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
45% identity, 93% coverage: 22:330/331 of query aligns to 3:312/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R114), Q96 (≠ A115), N199 (= N217)
- binding adenosine-5'-triphosphate: F34 (= F53), N36 (≠ D55), E38 (= E57)
- binding phosphate ion: S46 (= S65), R48 (= R67)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H148), D170 (= D187), G172 (= G189), K193 (= K211), R195 (= R213), D219 (= D237), D220 (= D238), D223 (= D241), T224 (= T242), C225 (≠ A243), G226 (= G244), T227 (= T245)
8dbeA Human prps1 with adp; hexamer (see paper)
45% identity, 93% coverage: 22:330/331 of query aligns to 3:312/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F53), N36 (≠ D55), E38 (= E57), R95 (= R114), Q96 (≠ A115), K98 (≠ R117), K99 (= K118), D100 (≠ T119), S102 (≠ G121), R103 (= R122), H129 (= H148), D142 (= D161), Y145 (= Y164), S307 (= S325), V308 (= V326), S309 (= S327), F312 (= F330)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H148), D170 (= D187), D219 (= D237), D220 (= D238), D223 (= D241), T224 (= T242), G226 (= G244), T227 (= T245)
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, 93% coverage: 22:330/331 of query aligns to 4:313/318 of P60891
- S16 (= S34) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D70) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (= N132) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L147) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ A150) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (≠ F160) 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 (≠ H162) mutation to H: No effect on catalytic activity.
- Y146 (= Y164) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ K199) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A207) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D210) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E220) to H: in a breast cancer sample; somatic mutation
- V219 (= V236) to G: in a breast cancer sample; somatic mutation
- H231 (≠ E248) to D: in a colorectal cancer sample; somatic mutation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
44% identity, 93% coverage: 22:330/331 of query aligns to 2:305/305 of 2hcrA
Query Sequence
>Synpcc7942_2113 FitnessBrowser__SynE:Synpcc7942_2113
VIRSATLPFASALPSLPDNHRLRLFSGSSNSALSQEVSRYLGIDLGPMIRKRFADGELYV
QIQESIRGCDVYLMQPTCWPVNDHLMELLIMIDACRRASARQITAVLPYYGYARADRKTA
GRESITAKLVANLITQAGANRVLAMDLHSAQIQGYFDIPFDHVYGSPVLIDYLRSKNLAD
LVVVSPDVGGVARARAFAKKLDDAPLAIIDKRRQAHNVAEVLNVIGDVQGKTAVLVDDMI
DTAGTICEGARLLRKQGASQVYACATHAVFSPPAIERLSASGLFEEVIVTNTIPIPEENR
FPQLTILSVANLLGETIWRIHEESSVSSMFR
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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