SitesBLAST
Comparing WP_010964137.1 NCBI__GCF_000008765.1:WP_010964137.1 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)
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)
25% identity, 93% coverage: 12:357/371 of query aligns to 3:314/315 of P0A717
- D129 (= D156) 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 (= D260) 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 (= D261) 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 (≠ A264) 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)
26% identity, 93% coverage: 12:355/371 of query aligns to 1:310/311 of 6asvC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
26% identity, 92% coverage: 12:352/371 of query aligns to 2:308/308 of 4s2uA
7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
25% identity, 93% coverage: 12:357/371 of query aligns to 1:306/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F51), D35 (≠ N53), E37 (= E55), R94 (= R125), R97 (= R128), H129 (= H158)
- binding adenosine monophosphate: R97 (= R128), V99 (vs. gap), R100 (vs. gap), E131 (≠ P160), F145 (≠ V181), S147 (≠ T183), V173 (≠ D209), A177 (≠ Y213)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D260), D213 (= D261), M214 (= M262), D216 (≠ A264), T217 (≠ S265), G219 (≠ E267), T220 (≠ S268)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
25% identity, 93% coverage: 12:357/371 of query aligns to 1:306/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F51), D35 (≠ N53), E37 (= E55), R94 (= R125), Q95 (= Q126), R97 (= R128), R97 (= R128), R100 (vs. gap), H129 (= H158), E131 (≠ P160), F145 (≠ V181), S147 (≠ T183), V173 (≠ D209)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D204), D212 (= D260), M214 (= M262), D216 (≠ A264), T217 (≠ S265)
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)
26% identity, 91% coverage: 15:353/371 of query aligns to 8:313/321 of O94413
- S172 (= S202) modified: Phosphoserine
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)
28% identity, 67% coverage: 50:296/371 of query aligns to 37:258/318 of Q63XL8
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)
24% identity, 93% coverage: 8:353/371 of query aligns to 5:313/317 of P14193
- RQ 102:103 (= RQ 125:126) binding ATP
- K198 (= K227) 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 (= R229) 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 (≠ H231) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (≠ T233) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (≠ N236) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (≠ ASGES 264:268) binding D-ribose 5-phosphate
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)
27% identity, 67% coverage: 50:296/371 of query aligns to 32:246/300 of 3dahC
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
24% identity, 89% coverage: 22:353/371 of query aligns to 11:302/305 of 2hcrA
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
25% identity, 82% coverage: 50:353/371 of query aligns to 32:294/297 of 1ibsA
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
25% identity, 82% coverage: 50:353/371 of query aligns to 34:296/299 of 1ibsB
8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
24% identity, 89% coverage: 22:353/371 of query aligns to 12:309/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R125), Q96 (= Q126), N199 (= N239)
- binding adenosine-5'-triphosphate: F34 (= F51), N36 (= N53), E38 (= E55)
- binding phosphate ion: S46 (= S63), R48 (= R65)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H158), D170 (= D204), G172 (= G206), K193 (= K227), R195 (= R229), D219 (= D260), D220 (= D261), D223 (≠ A264), T224 (≠ S265), C225 (≠ G266), G226 (≠ E267), T227 (≠ S268)
8dbeA Human prps1 with adp; hexamer (see paper)
24% identity, 89% coverage: 22:353/371 of query aligns to 12:309/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F51), N36 (= N53), E38 (= E55), R95 (= R125), Q96 (= Q126), K98 (≠ R128), K99 (≠ R129), D100 (vs. gap), S102 (≠ G131), R103 (= R132), H129 (= H158), D142 (≠ E172), Y145 (= Y175), S307 (= S351), V308 (≠ I352), S309 (≠ A353)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H158), D170 (= D204), D219 (= D260), D220 (= D261), D223 (≠ A264), T224 (≠ S265), G226 (≠ E267), T227 (≠ S268)
Sites not aligning to the query:
P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
24% identity, 89% coverage: 22:353/371 of query aligns to 13:310/318 of P60891
- S16 (≠ G25) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D68) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (≠ Q142) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (≠ A157) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ P160) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (≠ L168) 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 (= N173) mutation to H: No effect on catalytic activity.
- Y146 (= Y175) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ S216) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (≠ G223) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ Y226) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ V242) to H: in a breast cancer sample; somatic mutation
- V219 (= V259) to G: in a breast cancer sample; somatic mutation
- H231 (≠ D271) to D: in a colorectal cancer sample; somatic mutation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
25% identity, 79% coverage: 3:295/371 of query aligns to 2:265/326 of P9WKE3
- K29 (≠ N30) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
23% identity, 80% coverage: 51:347/371 of query aligns to 34:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F51), D36 (≠ N53), E38 (= E55), R95 (= R125), Q96 (= Q126), H130 (= H158)
- binding adenosine monophosphate: R98 (= R128), V100 (vs. gap), Y146 (= Y175), R175 (= R210), A178 (≠ Y213), K181 (≠ S216)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H158), D213 (= D260), D214 (= D261), I215 (≠ M262), D217 (≠ A264), T218 (≠ S265), A219 (≠ G266), T221 (≠ S268)
1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
24% identity, 82% coverage: 50:353/371 of query aligns to 32:292/295 of 1dkuA
Sites not aligning to the query:
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
23% identity, 80% coverage: 51:347/371 of query aligns to 34:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F51), D36 (≠ N53), E38 (= E55), R95 (= R125), Q96 (= Q126), H130 (= H158)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H158), D214 (= D260), D215 (= D261), I216 (≠ M262), D218 (≠ A264), T219 (≠ S265), A220 (≠ G266), T222 (≠ S268)
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
24% identity, 89% coverage: 22:353/371 of query aligns to 12:302/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F51), N36 (= N53), E38 (= E55), R95 (= R125), Q96 (= Q126), K98 (≠ R128), H129 (= H158)
- binding phosphate ion: S46 (= S63), R48 (= R65), D216 (≠ A264), T217 (≠ S265), C218 (≠ G266), T220 (≠ S268)
Query Sequence
>WP_010964137.1 NCBI__GCF_000008765.1:WP_010964137.1
MNSQDFNYRNGELGIVALESCRELGQKIDNRIKTKRKSEDSFLIPTQEIRFSNGEGKVKL
SESVRGKDIYILCDVGNYSCTYNMFGIENHKGPDEHFQDIKRTVSAIRGKARRITVIMPL
LYESRQHRRKGRESLDCALALQELERLGVQEVLTFDAHDPNVQNAIPLMSFENLYPTYDI
VKTIIMEEKNIEVNKNSMLVISPDTGAMDRAIYYSSVLGVDVGLFYKRRDHSTIVNGKNP
IVKHEYMGRDVENQDVLIVDDMIASGESVLDIAKELKARKARNIYVATTFAFFTEGLEKF
QKYYDDNIISRVYSTNLTYIPPELEKTEWFRKVDMSELISRIIHKLNKDESIAKFMDATY
VLHELLNSRKK
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