SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_026939600.1 NCBI__GCF_000420385.1:WP_026939600.1 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)

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)
57% identity, 99% coverage: 3:311/312 of query aligns to 9:316/317 of P14193

query
sites
P14193

Q

N

L

L

K

K

L

I

I

F

S

S

G

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T

N

A

S

N

N

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P

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E

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N

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Y

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P

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V

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D

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A

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L

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K

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S

A

A

S

K

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R

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x
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E

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D

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RQ 102:103 (= RQ 96:97) binding ATP
K198 (= K193) 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 (= R195) 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 (≠ K197) mutation to A: 3-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
N204 (= N199) mutation to A: 4.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
E207 (= E202) mutation to A: 2.5-fold decrease in the affinity binding for ATP. Slight decrease of the Vmax value.
DTAGT 228:232 (= DTAGT 223:227) binding D-ribose 5-phosphate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1dkuA Crystal structures of bacillus subtilis phosphoribosylpyrophosphate synthetase: molecular basis of allosteric inhibition and activation. (see paper)
55% identity, 99% coverage: 3:311/312 of query aligns to 1:295/295 of 1dkuA

query
sites
1dkuA

Q

N

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L

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K

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x
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F

binding methyl phosphonic acid adenosine ester: R94 (= R96), H128 (= H130)
binding phosphomethylphosphonic acid adenosyl ester: K98 (= K100), S101 (≠ P103), R102 (= R104), D141 (= D143), S290 (= S306), V291 (≠ L307), S292 (= S308), F295 (= F311)

1ibsB Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
55% identity, 99% coverage: 3:311/312 of query aligns to 3:299/299 of 1ibsB

query
sites
1ibsB

Q

N

L

L

K

K

L

I

I

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S

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N

A

S

N

N

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N

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H

H

E

K

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E

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S

L

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F

binding methyl phosphonic acid adenosine ester: R96 (= R96), Q97 (= Q97), R99 (= R99)

1ibsA Phosphoribosyldiphosphate synthetase in complex with cadmium ions (see paper)
55% identity, 99% coverage: 3:311/312 of query aligns to 1:297/297 of 1ibsA

query
sites
1ibsA

Q

N

L

L

K

K

L

I

I

F

S

S

G

L

T

N

A

S

N

N

K

P

L

E

L

L

A

A

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K

E

E

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A

N

D

Y

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R

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F

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S

D

D

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G

E

E

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Y

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N

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E

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R

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Y

Y

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D

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R

K

K

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-

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H

A

A

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G

F

F

D

D

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H

H

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A

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K

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R

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M

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D

T
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T

A
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A

G

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T
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T

L

I

T

T

N

L

A

A

K

N

A

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I

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S

V

E

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E

N

G

G

A

A

E

K

E

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Y

Y

A

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C

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H

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L

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G

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A

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K

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E

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T

N

N

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K

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G

A

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E

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A

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I

R

R

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H

H

E

K

Q

E

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S

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L

F

F

binding methyl phosphonic acid adenosine ester: R94 (= R96), Q95 (= Q97), R97 (= R99), H126 (= H130)
binding sulfate ion: D209 (= D223), T210 (= T224), A211 (= A225), T213 (= T227)

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)
53% identity, 99% coverage: 4:311/312 of query aligns to 7:315/318 of Q63XL8

query
sites
Q63XL8

L

L

K

M

L

V

I

F

S

T

G

G

T

N

A

A

N

N

K

P

L

A

L

L

A

A

E

Q

E

E

I

V

S

V

N

K

Y

I

L

L

G

G

I

I

P

P

L

L

A

G

K

K

A

A

Q

M

I

V

S

S

R

R

F

F

S

S

D

D

G

G

E

E

I

I

Y

Q

V

V

Q

E

I

I

D

Q

E

E

S

N

V

V

R

R

G

G

A

K

D

D

V

V

F

F

L

V

I

L

Q

Q

S

S

L

T

S

C

S

A

P

P

V

T

N

N

D

D

N

N

I

L

M

M

E

E

L

L

L

M

V

I

T

M

L

V

D

D

A

A

L

L

K

K

R

R

S

A

S

S

A

A

S

G

S

R

I

I

T

T

V

A

V

I

P

P

Y

Y

Y

F

A

G

Y

Y

A

A

R
|
R

Q
|
Q

D

D

R

R

K

R

V

P

L

R

-

S

P

A

R

R

V

V

P

A

I

I

S

S

A

A

K

K

L

V

A

A

D

N

L

M

I

L

T

E

T

I

A

A

G

G

A

V

D

E

R

R

I

I

M

I

S

T

M

M

D

D

L

L

H

H

A

A

G

D

Q

Q

I

I

Q

Q

G

G

F

F

D

D

I

I

P

P

V

V

D

D

H

N

L

I

Y

Y

A

A

A

T

P

P

I

I

M

L

L

L

K

G

Y

D

I

L

R

R

E

K

N

Q

I

-

G

N

T

Y

E

P

N

D

I

L

V

L

I

V

V

V

S

S

P

P

D

D

A

V

G

G

V

V

E

V

R

R

A

A

R

R

Y

A

Y

L

A

A

K

K

K

Q

L

L

G

N

C

C

S

D

I

L

A

A

I

I

D

D

K

K

R

R

P

P

K

K

P

A

N

N

V

V

S

A

E

E

I

V

M

M

H

N

I

I

G

G

D

E

V

V

K

E

G

G

K

R

K

T

A

C

I

V

I

I

V

M

D

D

I

M

V

V

D

D

T

T

A

A

G

G

T

T

L

L

T

C

N

K

A

A

K

Q

A

V

I

L

S

K

E

E

E

R

G

G

A

A

E

K

E

Q

V

V

Y

F

A

A

C

Y

I

A

T

T

H

H

P

P

V

V

L

L

S

S

G

G

N

G

A

A

I

A

E

D

K

R

V

I

N

A

S

S

P

A

L

L

K

D

E

E

L

L

V

V

T

T

N

D

T

T

I

I

T

P

F

L

K

S

-

A

K

E

P

S

V

L

P

A

T

C

D

P

K

K

I

I

K

R

V

A

L

L

S

S

V

S

A

A

E

G

I

L

G

A

E

E

A

T

I

F

R

S

R

R

V

I

F

R

H

R

K

G

E

D

S

S

L

V

S

M

V

S

I

L

F

F

RQ 99:100 (= RQ 96:97) binding ATP

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, 100% coverage: 1:312/312 of query aligns to 1:314/315 of P0A717

query
sites
P0A717

M
|
M

S

P

Q

D

L

M

K

K

L

L

I

F

S

A

G

G

T

N

A

A

N

T

K

P

L

E

L

L

A

A

E

Q

E

R

I

I

S

A

N

N

Y

R

L

L

G

Y

I

T

P

S

L

L

A

G

K

D

A

A

Q

A

I

V

S

G

R

R

F

F

S

S

D

D

G

G

E

E

I

V

Y

S

V

V

Q

Q

I

I

D

N

E

E

S

N

V

V

R

R

G

G

A

G

D

D

V

I

F

F

L

I

I

I

Q

Q

S

S

L

T

S

C

S

A

P

P

V

T

N

N

D

D

N

N

I

L

M

M

E

E

L

L

L

V

V

V

T

M

L

V

D

D

A

A

L

L

K

R

R

R

S

A

S

S

A

A

S

G

S

R

I

I

T

T

V

A

V

V

V

I

P

P

Y

Y

Y

F

A

G

Y

Y

A

A

R

R

Q

Q

D

D

R

R

K

R

V

V

L

R

P

S

-

A

R

R

V

V

P

P

I

I

S

T

A

A

K

K

L

V

A

A

D

D

L

F

I

L

T

S

A

V

G

G

A

V

D

D

R

R

I

V

M

L

S

T

M

V

D
|
D

L

L

H

H

A

A

G

E

Q

Q

I

I

Q

Q

G

G

F

F

D

D

I

V

P

P

V

V

D

D

H

N

L

V

Y

F

A

G

A

S

P

P

I

I

M

L

L

L

K

E

Y

D

I

M

R

L

E

Q

N

-

I

L

G

N

T

L

E

D

N

N

I

P

V

I

I

V

V

V

S

S

P

P

D

D

A

I

G

G

V

V

E

V

R

R

A

A

R

R

Y

A

Y

I

A

A

K

K

K

L

L

L

G

N

-

D

C

T

S

D

I

M

A

A

I

I

D

D

K

K

R

R

P

P

K

R

P

A

N

N

V

V

S

S

E

Q

I

V

M

M

H

H

I

I

G

G

D

D

V

V

K

A

G

G

K

R

K

D

A

C

I

V

I

L

V

V

D
|
D

I

M

V

I

D
|
D

T

T

A

G

G

G

T

T

L

L

T

C

N

K

A

A

K

E

A

A

I

L

S

K

E

E

E

R

G

G

A

A

E

K

E

R

V

V

Y

F

A

A

C

Y

I

A

T

T

H

H

P

P

V

I

L

F

S

S

G

G

N

N

A

A

I

A

E

N

K

N

V

L

N

R

N

N

S

S

P

V

L

I

K

D

E

E

L

V

V

V

T

C

N

D

T

T

I

I

T

P

F

L

K

S

K

D

P

E

V

I

P

K

T

S

-

L

D

P

K

N

I

V

K

R

V

T

L

L

S

T

V

L

A

S

E

G

I

M

I

L

G

A

E

E

A

A

I

I

R

R

V

I

F

S

H

N

K

E

E

E

S

S

L

I

S

S

V

A

I

M

F

F

E

E

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 (= D219) 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 (= D220) 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 (= D223) 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, 99% coverage: 4:311/312 of query aligns to 2:311/311 of 6asvC

query
sites
6asvC

L

M

K

K

L

L

I

F

S

A

G

G

T

N

A

A

N

T

K

P

L

E

L

L

A

A

E

Q

E

R

I

I

S

A

N

N

Y

R

L

L

G

Y

I

T

P

S

L

L

A

G

K

D

A

A

Q

A

I

V

S

G

R

R

F

F

S

S

D

D

G

G

E

E

I

V

Y

S

V

V

Q

Q

I

I

D

N

E

E

S

N

V

V

R

R

G

G

A

G

D

D

V

I

F

F

L

I

I

I

Q

Q

S

S

L

T

S

C

S

A

P

P

V

T

N

N

D

D

N

N

I

L

M

M

E

E

L

L

L

V

V

V

T

M

L

V

D

D

A

A

L

L

K

R

R

R

S

A

S

S

A

A

S

G

S

R

I

I

T

T

V

A

V

V

V

I

P

P

Y

Y

Y

F

A

G

Y

Y

A

A

R

R

Q

Q

D

D

R

R

K

R

V

V

L

R

P

S

-

A

R

R

V

V

P

P

I

I

S

T

A

A

K

K

L

V

A

A

D

D

L

F

I

L

T

S

A

V

G

G

A

V

D

D

R

R

I

V

M

L

S

T

M

V

D

D

L

L

H

H

A

A

G

E

Q

Q

I

I

Q

Q

G

G

F

F

D

D

I

V

P

P

V

V

D

D

H

N

L

V

Y

F

A

G

A

S

P

P

I

I

M

L

L

L

K

E

Y

D

I

M

R

L

E

Q

N

-

I

L

G

N

T

L

E

D

N

N

I

P

V

I

I

V

V

V

S

S

P

P

D
|
D

A

I

G

G

V

V

E

V

R

R

A

A

R

R

Y

A

Y

I

A

A

K

K

K

L

L

L

G

N

-

D

C

T

S

D

I

M

A

A

I

I

D

D

K

K

R

R

P

P

K

R

P

A

N

N

V

V

S

S

E

Q

I

V

M

M

H

H

I

I

G

G

D

D

V

V

K

A

G

G

K

R

K

D

A

C

I

V

I

L

V

V

D
|
D

I

M

V

I

D
|
D

T
|
T

A
x
G

G

G

T
|
T

L
|
L

T

C

N

K

A

A

K

E

A

A

I

L

S

K

E

E

E

R

G

G

A

A

E

K

E

R

V

V

Y

F

A

A

C

Y

I

A

T

T

H

H

P

P

V

I

L

F

S

S

G

G

N

N

A

A

I

A

E

N

K

N

V

L

N

R

N

N

S

S

P

V

L

I

K

D

E

E

L

V

V

V

T

C

N

D

T

T

I

I

T

P

F

L

K

S

K

D

P

E

V

I

P

K

T

S

-

L

D

P

K

N

I

V

K

R

V

T

L

L

S

T

V

L

A

S

E

G

I

M

I

L

G

A

E

E

A

A

I

I

R

R

V

I

F

S

H

N

K

E

E

E

S

S

L

I

S

S

V

A

I

M

F

F

binding phosphate ion: D168 (= D170), D218 (= D219), D219 (= D220), D222 (= D223), T223 (= T224), G224 (≠ A225), T226 (= T227), L227 (= L228)

4s2uA Crystal structure of the phosphorybosylpyrophosphate synthetase from e. Coli
50% identity, 97% coverage: 4:307/312 of query aligns to 3:308/308 of 4s2uA

query
sites
4s2uA

L

M

K

K

L

L

I

F

S

A

G

G

T

N

A

A

N

T

K

P

L

E

L

L

A

A

E

Q

E

R

I

I

S

A

N

N

Y

R

L

L

G

Y

I

T

P

S

L

L

A

G

K

D

A

A

Q

A

I

V

S

G

R

R

F

F

S

S

D

D

G

G

E

E

I

V

Y

S

V

V

Q

Q

I

I

D

N

E

E

S

N

V

V

R

R

G

G

A

G

D

D

V

I

F

F

L

I

I

I

Q

Q

S

S

L

T

S

C

S

A

P

P

V

T

N

N

D

D

N

N

I

L

M

M

E

E

L

L

L

V

V

V

T

M

L

V

D

D

A

A

L

L

K

R

R

R

S

A

S

S

A

A

S

G

S

R

I

I

T

T

V

A

V

V

V

I

P

P

Y

Y

Y

F

A

G

Y

Y

A

A

R

R

Q

Q

D

D

R

R

K

R

V

V

L

R

P

S

-

A

R

R

V

V

P

P

I

I

S

T

A

A

K

K

L

V

A

A

D

D

L

F

I

L

T

S

A

V

G

G

A

V

D

D

R

R

I

V

M

L

S

T

M

V

D

D

L

L

H

H

A

A

G

E

Q

Q

I

I

Q

Q

G

G

F

F

D

D

I

V

P

P

V

V

D

D

H

N

L

V

Y

F

A

G

A

S

P

P

I

I

M

L

L

L

K

E

Y

D

I

M

R

L

E

Q

N

-

I

L

G

N

T

L

E

D

N

N

I

P

V

I

I

V

V

V

S

S

P

P

D

D

A

I

G

G

V

V

E

V

R

R

A

A

R

R

Y

A

Y

I

A

A

K

K

K

L

L

L

G

N

-

D

C

T

S

D

I

M

A

A

I

I

D

D

K

K

R

R

P

P

K

R

P

A

N

N

V

V

S

S

E

Q

I

V

M

M

H

H

I

I

G

G

D

D

V

V

K

A

G

G

K

R

K

D

A

C

I

V

I

L

V

V

D

D

I

M

V

I

D
|
D

T

T

A

G

G

G

T
|
T

L

L

T

C

N

K

A

A

K

E

A

A

I

L

S

K

E

E

E

R

G

G

A

A

E

K

E

R

V

V

Y

F

A

A

C

Y

I

A

T

T

H

H

P

P

V

I

L

F

S

S

G

G

N

N

A

A

I

A

E

N

K

N

V

L

N

R

N

N

S

S

P

V

L

I

K

D

E

E

L

V

V

V

T

C

N

D

T

T

I

I

T

P

F

L

K

S

K

D

P

E

V

I

P

K

T

S

-

L

D

P

K

N

I

V

K

R

V

T

L

L

S

T

V

L

A

S

E

G

I

M

I

L

G

A

E

E

A

A

I

I

R

R

V

I

F

S

H

N

K

E

E

E

S

S

L

I

binding magnesium ion: D223 (= D223), T227 (= T227)

3dahC 2.3 a crystal structure of ribose-phosphate pyrophosphokinase from burkholderia pseudomallei (see paper)
52% identity, 97% coverage: 4:307/312 of query aligns to 2:299/300 of 3dahC

query
sites
3dahC

L

L

K

M

L

V

I

F

S

T

G

G

T

N

A

A

N

N

K

P

L

A

L

L

A

A

E

Q

E

E

I

V

S

V

N

K

Y

I

L

L

G

G

I

I

P

P

L

L

A

G

K

K

A

A

Q

M

I

V

S

S

R

R

F
|
F

S

S

D
|
D

G

G

E
|
E

I

I

Y

Q

V

V

Q

E

I

I

D

Q

E

E

S

N

V

V

R

R

G

G

A

K

D

D

V

V

F

F

L

V

I

L

Q

Q

S

S

L

T

S

C

S

A

P

P

V

T

N

N

D

D

N

N

I

L

M

M

E

E

L

L

L

M

V

I

T

M

L

V

D

D

A

A

L

L

K

K

R

R

S

A

S

S

A

A

S

G

S

R

I

I

T

T

V

A

V

I

P

P

Y

Y

Y

F

A

G

Y

Y

A

A

R
|
R

Q
|
Q

D

D

R

R

K

R

V

P

L

R

-

S

P

A

R

R

V

V

P

A

I

I

S

S

A

A

K

K

L

V

A

A

D

N

L

M

I

L

T

E

T

I

A

A

G

G

A

V

D

E

R

R

I

I

M

I

S

T

M

M

D

D

L

L

H

H

A

A

G

D

Q

Q

I

I

Q

Q

G

G

F

F

D

D

I

I

P

P

V

V

D

D

H

N

L

I

Y

Y

A

A

A

T

P

P

I

I

M

L

L

L

K

G

Y

D

I

L

R

R

E

K

N

Q

I

-

G

N

T

Y

E

P

N

D

I

L

V

L

I

V

V

V

S

S

P

P

D

D

A

V

G

G

V

V

E

V

R

R

A

A

R

R

Y

A

Y

L

A

A

K

K

K

Q

L

L

G

N

C

C

S

D

I

L

A

A

I

I

D

D

K

K

R

R

P

-

K

-

P

-

N

-

V

-

S

-

E

-

I

V

M

M

H

N

I

I

G

G

D

E

V

V

K

E

G

G

K

R

K

T

A

C

I

V

I

I

V

M

D

D

I

M

V

V

D

D

T

T

A

A

G

G

T

T

L

L

T

C

N

K

A

A

K

Q

A

V

I

L

S

K

E

E

E

R

G

G

A

A

E

K

E

Q

V

V

Y

F

A

A

C

Y

I

A

T

T

H

H

P

P

V

V

L

L

S

S

G

G

N

G

A

A

I

A

E

D

K

R

V

I

N

A

S

S

P

A

L

L

K

D

E

E

L

L

V

V

T

T

N

D

T

T

I

I

T

P

F

L

K

S

-

A

K

E

P

S

V

L

P

A

T

C

D

P

K

K

I

I

K

R

V

A

L

L

S

S

V

S

A

A

E

G

I

L

G

A

E

E

A

T

I

F

R

S

R

R

V

I

F

R

H

R

K

G

E

D

S

S

L

V

binding adenosine monophosphate: F33 (= F35), D35 (= D37), E37 (= E39), R94 (= R96), Q95 (= Q97)

7xmvA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a(amp/adp) filament bound with adp, amp and r5p (see paper)
49% identity, 99% coverage: 4:312/312 of query aligns to 2:306/307 of 7xmvA

query
sites
7xmvA

L

M

K

K

L

L

I

F

S

A

G

G

T

N

A

A

N

T

K

P

L

E

L

L

A

A

E

Q

E

R

I

I

S

A

N

N

Y

R

L

L

G

Y

I

T

P

S

L

L

A

G

K

D

A

A

Q

A

I

V

S

G

R

R

F
|
F

S

S

D
|
D

G

G

E
|
E

I

V

Y

S

V

V

Q

Q

I

I

D

N

E

E

S

N

V

V

R

R

G

G

A

G

D

D

V

I

F

F

L

I

I

I

Q

Q

S

S

L

T

S

C

S

A

P

P

V

T

N

N

D

D

N

N

I

L

M

M

E

E

L

L

L

V

V

V

T

M

L

V

D

D

A

A

L

L

K

R

R

R

S

A

S

S

A

A

S

G

S

R

I

I

T

T

V

A

V

V

V

I

P

P

Y

Y

Y

F

A

G

Y

Y

A

A

R
|
R

Q

Q

D

D

R
|
R

K

R

V
|
V

L
x
R

P

S

-

A

R

R

V

V

P

P

I

I

S

T

A

A

K

K

L

V

A

A

D

D

L

F

I

L

T

S

A

V

G

G

A

V

D

D

R

R

I

V

M

L

S

T

M

V

D

D

L

L

H
|
H

A

A

G
x
E

Q

Q

I

I

Q

Q

G

G

F

F

D

D

I

V

P

P

V

V

D

D

H

N

L

V

Y
x
F

A

G

A
x
S

P

P

I

I

M

L

L

L

K

E

Y

D

I

M

R

L

E

Q

N

-

I

L

G

N

T

L

E

D

N

N

I

P

V

I

I

V

V

V

S

S

P

P

D

D

A

I

G

G

V

V

E
x
V

R

R

A

A

R

R

Y
x
A

Y

I

A

A

K

K

K

L

L

L

G

N

-

D

C

T

S

D

I

M

A

A

I

I

D

D

K

K

R

R

P

-

K

-

P

-

N

-

V

-

S

-

E

Q

I

V

M

M

H

H

I

I

G

G

D

D

V

V

K

A

G

G

K

R

K

D

A

C

I

V

I

L

V

V

D
|
D

I
x
M

V

I

D
|
D

T
|
T

A

G

G
|
G

T
|
T

L

L

T

C

N

K

A

A

K

E

A

A

I

L

S

K

E

E

E

R

G

G

A

A

E

K

E

R

V

V

Y

F

A

A

C

Y

I

A

T

T

H

H

P

P

V

I

L

F

S

S

G

G

N

N

A

A

I

A

E

N

K

N

V

L

N

R

N

N

S

S

P

V

L

I

K

D

E

E

L

V

V

V

T

C

N

D

T

T

I

I

T

P

F

L

K

S

K

D

P

E

V

I

P

K

T

S

-

L

D

P

K

N

I

V

K

R

V

T

L

L

S

T

V

L

A

S

E

G

I

M

I

L

G

A

E

E

A

A

I

I

R

R

V

I

F

S

H

N

K

E

E

E

S

S

L

I

S

S

V

A

I

M

F

F

E

E

binding adenosine-5'-diphosphate: F33 (= F35), D35 (= D37), E37 (= E39), R94 (= R96), R97 (= R99), H129 (= H130)
binding adenosine monophosphate: R97 (= R99), V99 (= V101), R100 (≠ L102), E131 (≠ G132), F145 (≠ Y146), S147 (≠ A148), V173 (≠ E175), A177 (≠ Y179)
binding 5-O-phosphono-alpha-D-ribofuranose: D212 (= D219), D213 (= D220), M214 (≠ I221), D216 (= D223), T217 (= T224), G219 (= G226), T220 (= T227)

7xmuA E.Coli phosphoribosylpyrophosphate (prpp) synthetase type a filament bound with adp, pi and r5p (see paper)
49% identity, 99% coverage: 4:312/312 of query aligns to 2:306/307 of 7xmuA

query
sites
7xmuA

L

M

K

K

L

L

I

F

S

A

G

G

T

N

A

A

N

T

K

P

L

E

L

L

A

A

E

Q

E

R

I

I

S

A

N

N

Y

R

L

L

G

Y

I

T

P

S

L

L

A

G

K

D

A

A

Q

A

I

V

S

G

R

R

F
|
F

S

S

D
|
D

G

G

E
|
E

I

V

Y

S

V

V

Q

Q

I

I

D

N

E

E

S

N

V

V

R

R

G

G

A

G

D

D

V

I

F

F

L

I

I

I

Q

Q

S

S

L

T

S

C

S

A

P

P

V

T

N

N

D

D

N

N

I

L

M

M

E

E

L

L

L

V

V

V

T

M

L

V

D

D

A

A

L

L

K

R

R

R

S

A

S

S

A

A

S

G

S

R

I

I

T

T

V

A

V

V

V

I

P

P

Y

Y

Y

F

A

G

Y

Y

A

A

R
|
R

Q
|
Q

D

D

R
|
R

K

R

V

V

L
x
R

P

S

-

A

R

R

V

V

P

P

I

I

S

T

A

A

K

K

L

V

A

A

D

D

L

F

I

L

T

S

A

V

G

G

A

V

D

D

R

R

I

V

M

L

S

T

M

V

D

D

L

L

H
|
H

A

A

G
x
E

Q

Q

I

I

Q

Q

G

G

F

F

D

D

I

V

P

P

V

V

D

D

H

N

L

V

Y
x
F

A

G

A
x
S

P

P

I

I

M

L

L

L

K

E

Y

D

I

M

R

L

E

Q

N

-

I

L

G

N

T

L

E

D

N

N

I

P

V

I

I

V

V

V

S

S

P

P

D
|
D

A

I

G

G

V

V

E
x
V

R

R

A

A

R

R

Y

A

Y

I

A

A

K

K

K

L

L

L

G

N

-

D

C

T

S

D

I

M

A

A

I

I

D

D

K

K

R

R

P

-

K

-

P

-

N

-

V

-

S

-

E

Q

I

V

M

M

H

H

I

I

G

G

D

D

V

V

K

A

G

G

K

R

K

D

A

C

I

V

I

L

V

V

D
|
D

D

D

I
x
M

V

I

D
|
D

T
|
T

A

G

G

G

T

T

L

L

T

C

N

K

A

A

K

E

A

A

I

L

S

K

E

E

E

R

G

G

A

A

E

K

E

R

V

V

Y

F

A

A

C

Y

I

A

T

T

H

H

P

P

V

I

L

F

S

S

G

G

N

N

A

A

I

A

E

N

K

N

V

L

N

R

N

N

S

S

P

V

L

I

K

D

E

E

L

V

V

V

T

C

N

D

T

T

I

I

T

P

F

L

K

S

K

D

P

E

V

I

P

K

T

S

-

L

D

P

K

N

I

V

K

R

V

T

L

L

S

T

V

L

A

S

E

G

I

M

I

L

G

A

E

E

A

A

I

I

R

R

V

I

F

S

H

N

K

E

E

E

S

S

L

I

S

S

V

A

I

M

F

F

E

E

binding adenosine-5'-diphosphate: F33 (= F35), D35 (= D37), E37 (= E39), R94 (= R96), Q95 (= Q97), R97 (= R99), R97 (= R99), R100 (≠ L102), H129 (= H130), E131 (≠ G132), F145 (≠ Y146), S147 (≠ A148), V173 (≠ E175)
binding 5-O-phosphono-alpha-D-ribofuranose: D168 (= D170), D212 (= D219), M214 (≠ I221), D216 (= D223), T217 (= T224)

6nfeB Crystal structure of ribose-phosphate pyrophosphokinase from legionella pneumophila with bound amp, adp, and ribose-5-phosphate
52% identity, 96% coverage: 2:301/312 of query aligns to 1:297/299 of 6nfeB

query
sites
6nfeB

S

S

Q

T

L

M

K

M

L

I

I

F

S

T

G

G

T

N

A

A

N

N

K

P

L

E

L

L

A

A

E

L

E

K

I

I

S

S

N

S

Y

H

L

L

G

Q

I

I

P

P

L

I

A

G

K

K

A

A

Q

T

I

V

S

G

R

T

F
|
F

S

S

D
|
D

G

G

E
|
E

I

T

Y

M

V

V

Q

E

I

I

D

L

E

E

S

N

V

V

R

R

G

G

A

K

D

D

V

V

F

F

L

V

I

L

Q

Q

S

S

L

T

S

C

S

A

P

P

V

A

N

N

D

N

N

N

I

L

M

M

E

E

L

L

V

I

T

M

L

A

D

D

A

A

L

L

K

R

R

R

S

S

A

A

S

G

S

R

I

I

T

T

V

A

V

V

P

P

Y

Y

Y

F

A

G

Y

Y

A

A

R
|
R

Q
|
Q

D

D

R

R

K

R

V

V

L

R

P

S

-

A

R

R

V

V

P

P

I

I

S

T

A

A

K

K

L

V

A

A

D

D

L

M

I

M

T

A

T

S

A

V

G

G

A

I

D

C

R

R

I

V

M

L

S

T

M

V

D

D

L

L

H
|
H

A

A

G

D

Q

Q

I

I

Q

Q

G

G

F

F

D

Y

I

M

P

P

V

V

D

D

H

N

L

V

Y

Y

A

S

A

T

P

P

I

V

M

L

L

L

K

E

Y

D

I

I

R

T

E

K

N

Q

I

-

G

K

T

L

E

N

N

N

I

I

V

M

I

I

V

V

S

S

P

P

D

D

A

V

G

G

V

V

E

V

R

R

A

A

R

R

Y

A

Y

V

A

A

K

K

K

R

L

L

G

N

-

D

C

A

S

E

I

L

A

S

I

I

D

D

K

K

R

R

P

-

K

-

P

-

N

-

V

-

S

S

E

E

I

V

M

M

H

H

I

I

G

G

D

E

V

P

K

A

G

N

K

K

K

N

A

C

I

I

V

V

D
|
D

I
|
I

V

V

D
|
D

T
|
T

A
|
A

G

G

T
|
T

L

L

T

C

N

T

A

A

K

H

A

E

I

L

S

K

E

K

E

N

G

G

A

A

E

K

E

S

V

V

Y

R

A

A

C

Y

I

I

T

T

H

H

P

P

V

V

L

L

S

S

G

G

N

P

A

A

I

V

E

N

K

N

V

I

N

K

N

H

S

S

P

G

L

L

K

D

E

E

L

V

V

V

T

T

N

D

T

T

I

I

T

P

F

L

K

S

K

A

P

E

V

A

P

Q

-

N

T

C

D

E

K

K

I

I

K

R

V

V

L

V

S

S

V

L

A

A

E

D

I

M

I

L

G

A

E

Q

A

A

I

I

R

K

R

R

V

V

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 (= D219), D215 (= D220), I216 (= I221), D218 (= D223), T219 (= T224), A220 (= A225), T222 (= T227)

P60891 Ribose-phosphate pyrophosphokinase 1; PPRibP; Phosphoribosyl pyrophosphate synthase I; PRS-I; EC 2.7.6.1 from Homo sapiens (Human) (see 5 papers)
49% identity, 100% coverage: 1:311/312 of query aligns to 1:313/318 of P60891

query
sites
P60891

M
|
M

S

P

Q

N

L

I

K

K

L

I

I

F

S

S

G

G

T

S

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x
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F

M1 (= M1) modified: Initiator methionine, Removed
S16 (≠ A16) 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 (≠ G132) 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 (≠ H144) 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 (≠ K182) to H: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852541
A190 (= A189) to V: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852544
H193 (≠ D192) to Q: in PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP; dbSNP:rs137852545
D203 (≠ E202) to H: in a breast cancer sample; somatic mutation
V219 (= V218) to G: in a breast cancer sample; somatic mutation
H231 (≠ N230) to D: in a colorectal cancer sample; somatic mutation

8dbkB Human prps1 with phosphate, atp, and r5p; hexamer with resolved catalytic loops (see paper)
49% identity, 99% coverage: 3:311/312 of query aligns to 2:312/316 of 8dbkB

query
sites
8dbkB

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F

binding adenosine monophosphate: R95 (= R96), Q96 (= Q97), N199 (= N199)
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 (= D170), G172 (= G172), K193 (= K193), R195 (= R195), D219 (= D219), D220 (= D220), D223 (= D223), T224 (= T224), C225 (≠ A225), G226 (= G226), T227 (= T227)

8dbeA Human prps1 with adp; hexamer (see paper)
49% identity, 99% coverage: 3:311/312 of query aligns to 2:312/316 of 8dbeA

query
sites
8dbeA

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x
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x
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x
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A

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A

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A

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