SitesBLAST
Comparing WP_013419358.1 NCBI__GCF_000166055.1:WP_013419358.1 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)
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, 100% coverage: 1:310/310 of query aligns to 4:314/315 of P0A717
- D129 (= D125) 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 (= D216) 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 (= D217) 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 (= D220) 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)
56% identity, 100% coverage: 1:309/310 of query aligns to 2:311/311 of 6asvC
4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
56% identity, 98% coverage: 1:305/310 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)
55% identity, 100% coverage: 1:310/310 of query aligns to 2:306/307 of 7xmvA
- binding adenosine-5'-diphosphate: F33 (= F32), D35 (= D34), E37 (= E36), R94 (= R93), R97 (= R96), H129 (= H127)
- binding adenosine monophosphate: R97 (= R96), V99 (≠ T98), R100 (≠ L99), E131 (≠ G129), F145 (≠ Y143), S147 (≠ A145), V173 (= V172), A177 (≠ S176)
- binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D216), D213 (= D217), M214 (≠ I218), D216 (= D220), T217 (≠ S221), G219 (= G223), T220 (= T224)
7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
55% identity, 100% coverage: 1:310/310 of query aligns to 2:306/307 of 7xmuA
- binding adenosine-5'-diphosphate: F33 (= F32), D35 (= D34), E37 (= E36), R94 (= R93), Q95 (= Q94), R97 (= R96), R97 (= R96), R100 (≠ L99), H129 (= H127), E131 (≠ G129), F145 (≠ Y143), S147 (≠ A145), V173 (= V172)
- binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D167), D212 (= D216), M214 (≠ I218), D216 (= D220), T217 (≠ S221)
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, 100% coverage: 1:309/310 of query aligns to 7:315/318 of Q63XL8
3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
55% identity, 98% coverage: 1:305/310 of query aligns to 2:299/300 of 3dahC
6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
55% identity, 97% coverage: 1:300/310 of query aligns to 3:298/299 of 6nfeB
- binding adenosine-5'-diphosphate: F34 (= F32), D36 (= D34), E38 (= E36), R95 (= R93), Q96 (= Q94), H130 (= H127)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H127), D214 (= D216), D215 (= D217), I216 (= I218), D218 (= D220), T219 (≠ S221), A220 (≠ G222), T222 (= T224)
6nfeA Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
54% identity, 97% coverage: 1:300/310 of query aligns to 3:297/298 of 6nfeA
- binding adenosine-5'-diphosphate: F34 (= F32), D36 (= D34), E38 (= E36), R95 (= R93), Q96 (= Q94), H130 (= H127)
- binding adenosine monophosphate: R98 (= R96), V100 (≠ T98), Y146 (= Y143), R175 (= R173), A178 (≠ S176), K181 (≠ S179)
- binding 5-O-phosphono-alpha-D-ribofuranose: H130 (= H127), D213 (= D216), D214 (= D217), I215 (= I218), D217 (= D220), T218 (≠ S221), A219 (≠ G222), T221 (= T224)
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)
52% identity, 100% coverage: 1:309/310 of query aligns to 10:316/317 of P14193
- RQ 102:103 (= RQ 93:94) binding ATP
- K198 (= K190) 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 (= R192) 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 (= R194) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- N204 (≠ G196) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- E207 (= E199) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
- DTAGT 228:232 (≠ DSGGT 220:224) binding D-ribose 5-phosphate
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, 100% coverage: 1:309/310 of query aligns to 3:312/316 of 8dbkB
- binding adenosine monophosphate: R95 (= R93), Q96 (= Q94), N199 (≠ G196)
- binding adenosine-5'-triphosphate: F34 (= F32), N36 (≠ D34), E38 (= E36)
- binding phosphate ion: S46 (≠ N44), R48 (= R46)
- binding 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose: H129 (= H127), D170 (= D167), G172 (= G169), K193 (= K190), R195 (= R192), D219 (= D216), D220 (= D217), D223 (= D220), T224 (≠ S221), C225 (≠ G222), G226 (= G223), T227 (= T224)
8dbeA Human prps1 with adp; hexamer (see paper)
47% identity, 100% coverage: 1:309/310 of query aligns to 3:312/316 of 8dbeA
- binding adenosine-5'-diphosphate: F34 (= F32), N36 (≠ D34), E38 (= E36), R95 (= R93), Q96 (= Q94), K98 (≠ R96), K99 (= K97), D100 (≠ T98), S102 (≠ P100), R103 (= R101), H129 (= H127), D142 (= D140), Y145 (= Y143), S307 (= S304), V308 (= V305), S309 (= S306), F312 (= F309)
- binding 5-O-phosphono-alpha-D-ribofuranose: H129 (= H127), D170 (= D167), D219 (= D216), D220 (= D217), D223 (= D220), T224 (≠ S221), G226 (= G223), T227 (= T224)
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, 100% coverage: 1:309/310 of query aligns to 4:313/318 of P60891
- S16 (≠ A13) to P: found in patients with phosphoribosyl pyrophosphate synthetase I deficiency; likely pathogenic; dbSNP:rs869025594
- D52 (= D49) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852542
- N114 (= N111) to S: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852540
- L129 (= L126) to I: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852543
- S132 (≠ G129) mutation to A: Reduces catalytic activity.; mutation to F: No effect on catalytic activity.
- V142 (≠ T139) 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 (= N141) mutation to H: No effect on catalytic activity.
- Y146 (= Y143) mutation to F: No effect on catalytic activity.; mutation to M: Reduces catalytic activity.
- D183 (≠ S179) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
- A190 (= A186) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
- H193 (≠ D189) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
- D203 (≠ E199) to H: in a breast cancer sample; somatic mutation
- V219 (≠ I215) to G: in a breast cancer sample; somatic mutation
- H231 (≠ N227) to D: in a colorectal cancer sample; somatic mutation
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
50% identity, 100% coverage: 1:309/310 of query aligns to 4:299/299 of 1ibsB
1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
50% identity, 100% coverage: 1:309/310 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)
50% identity, 100% coverage: 1:309/310 of query aligns to 2:295/295 of 1dkuA
2hcrA Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with amp(atp), cadmium and sulfate ion (see paper)
47% identity, 100% coverage: 1:309/310 of query aligns to 2:305/305 of 2hcrA
8dbgA Human prps1 with phosphate and atp; hexamer (see paper)
47% identity, 100% coverage: 1:309/310 of query aligns to 3:305/309 of 8dbgA
- binding adenosine-5'-triphosphate: F34 (= F32), N36 (≠ D34), E38 (= E36), R95 (= R93), Q96 (= Q94), K98 (≠ R96), H129 (= H127)
- binding phosphate ion: S46 (≠ N44), R48 (= R46), D216 (= D220), T217 (≠ S221), C218 (≠ G222), T220 (= T224)
7yk1A Structural basis of human prps2 filaments (see paper)
46% identity, 99% coverage: 3:309/310 of query aligns to 5:303/306 of 7yk1A
- binding adenosine-5'-diphosphate: F34 (= F32), N36 (≠ D34), E38 (= E36), S46 (≠ N44), R48 (= R46), R95 (= R93), K99 (= K97), D100 (≠ T98), K101 (≠ L99), S102 (≠ P100), R103 (= R101), H129 (= H127), D142 (= D140), S298 (= S304), S300 (= S306), F303 (= F309)
- binding phosphate ion: D214 (= D220), C216 (≠ G222), T218 (= T224)
7pn0A Crystal structure of the phosphorybosylpyrophosphate synthetase ii from thermus thermophilus at r32 space group
46% identity, 99% coverage: 3:309/310 of query aligns to 5:307/312 of 7pn0A
Query Sequence
>WP_013419358.1 NCBI__GCF_000166055.1:WP_013419358.1
MKLVAGNSNRPLANAIAAYLKTPLTECLVRRFSDMEIFVEVRENVRGEDIFVIQSTSYPA
NDNLMELLILTDALRRASARRITAVIPYFGYARQDRKTLPRTPISAKLVANLITHAGADR
VLTVDLHAGQIQGFFDIPTDNLYAAPVMVRDITKRYTDGNITVVSPDVGGVVRARSLASR
IDAPLAIIDKRRDRPGESEVMNVIGNVTGRHCILIDDIIDSGGTLCNAAHALIEKGACSV
AAYATHGVFSGGAVARIQASKIDTLVITDTIVPTEAVRVASNIEVLSLSALIGEAILRTS
GEESVSSLFD
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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