SitesBLAST

R95 (= R106) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K130) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (≠ G176) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ GIRAC 176:180) binding ATP
E171 (≠ A179) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (≠ C180) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (≠ G183) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ Q194) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ QSRA 194:197) binding ATP
E192 (≠ A197) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (≠ L198) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (≠ T201) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.

Sites not aligning to the query:

222 K→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
222:226 binding ATP
226 R→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
253 binding ATP; W→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
257 K→A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.

Q9X015 Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG; NTP-PPase; EC 3.6.1.1; EC 3.6.1.9 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
39% identity, 84% coverage: 22:221/238 of query aligns to 14:209/255 of Q9X015

query
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Q9X015

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E41 (= E49) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E50) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E53) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E69) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R105) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R106) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K130) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (≠ G185) mutation to A: Has little effects on the NTPase activity.
E176 (≠ D188) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ AL 197:198) mutation to AA: Has little effects on the NTPase activity.

3crcA Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
33% identity, 88% coverage: 14:222/238 of query aligns to 1:184/225 of 3crcA

query
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Sites not aligning to the query:

binding adenosine-5'-triphosphate: 190, 193, 218

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
31% identity, 84% coverage: 23:222/238 of query aligns to 3:176/220 of 3crcB

query
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3crcB

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binding adenosine-5'-triphosphate: F116 (≠ A165), W118 (≠ S167), K127 (≠ G176), E131 (≠ C180), E134 (≠ G183)
binding magnesium ion: E131 (≠ C180), E134 (≠ G183), E152 (≠ L198), D155 (≠ T201)

P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
30% identity, 71% coverage: 22:190/238 of query aligns to 93:260/325 of P96379

query
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P96379

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A219 (= A149) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
31% identity, 83% coverage: 22:219/238 of query aligns to 93:288/324 of A0R3C4

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A0R3C4

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A222 (= A149) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
37% identity, 36% coverage: 22:106/238 of query aligns to 93:177/177 of 7yh5B

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7yh5B

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binding magnesium ion: E119 (= E50), E122 (= E53), E138 (= E69), D141 (= D72)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
32% identity, 50% coverage: 16:134/238 of query aligns to 2:114/114 of 2yxhA

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2yxhA

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E

S

E
|
E

A

I

H

E

E
|
E

A

V

A

A

A

E

A

A

I

V

R

K

S

K

G

N

T

D

K

L

E

A

D

N

V

L

A

E

E

E

E
|
E

L

I

G

G

D
|
D

L

M

L

I

F

Y

M
x
D

V

A

L

L

F

L

L

V

V

A

H

A

L

V

Y

A

E

Q

E

R

E

D

E

Y

S

G

F

I

S

D

L

L

E

E

D

S

V

A

C

I

R

Q

A

K

I

V

C

V

E

E

K

K

M

I

I

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

G

W

D

E

V

E

R

K

V

I

K

-

S

S

A

L

K

E

D

E

V

A

R

E

S

K

N

I

W

W

E

-

K

-

I

-

K

K

E

E

R

R

E

K

K

K

binding magnesium ion: E34 (= E50), E34 (= E50), E37 (= E53), E53 (= E69), D56 (= D72), D60 (≠ M76)

Query Sequence

>WP_073035933.1 NCBI__GCF_900129305.1:WP_073035933.1
MSEDKSSQSANRWDGVGRIWEIIDRLRGENGCPWDRKQTPETVQTYLVEEAHEAAAAIRS
GTKEDVAEELGDLLFMVLFLVHLYEEEESFSLEDVCRAICEKMIRRHPHVFGDVRVKSAK
DVRSNWEKIKEREKGGKRQGLGIPKTLPALARAYRIRARQEDGGAVSASLEDAVQGIRAC
VNGLGRTDLRDPDQSRALLGTLLYRTVCLARALGQRPEDSLHAYLDALESSMAGGPDS

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