SitesBLAST

R95 (= R110) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K134) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (≠ G184) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ GVWEK 184:188) binding ATP
E171 (= E187) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (≠ K188) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E191) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (= K205) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ KVHQ 205:208) binding ATP
E192 (≠ Q208) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E211) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D214) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (≠ R240) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (≠ RFIQR 240:244) binding ATP
R226 (= R244) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W268) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K272) mutation to 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)
38% identity, 92% coverage: 19:272/277 of query aligns to 8:250/255 of Q9X015

query
sites
Q9X015

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E41 (= E53) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E54) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E57) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E73) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R109) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R110) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K134) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (= E198) mutation to A: Has little effects on the NTPase activity.
E176 (= E201) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ SE 210:211) 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)
35% identity, 92% coverage: 19:274/277 of query aligns to 3:224/225 of 3crcA

query
sites
3crcA

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binding adenosine-5'-triphosphate: F190 (= F241), R193 (= R244), W218 (= W268)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
34% identity, 86% coverage: 38:274/277 of query aligns to 14:218/220 of 3crcB

query
sites
3crcB

W

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binding adenosine-5'-triphosphate: F116 (= F177), W118 (= W179), K127 (≠ G184), E131 (≠ K188), E134 (= E191)
binding magnesium ion: E131 (≠ K188), E134 (= E191), E152 (= E211), D155 (= D214)

A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
29% identity, 73% coverage: 21:222/277 of query aligns to 86:276/324 of A0R3C4

query
sites
A0R3C4

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A222 (≠ P161) mutation to E: Pyrophosphohydrolase activity is reduced 30-fold.

P96379 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 57% coverage: 21:177/277 of query aligns to 86:235/325 of P96379

query
sites
P96379

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A219 (≠ P161) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
41% identity, 32% coverage: 22:110/277 of query aligns to 87:177/177 of 7yh5B

query
sites
7yh5B

L

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M

L

M

R

D

S

K

P

L

D

R

G

T

G

A

C

G

P

P

W

W

D

E

L

S

A

E

Q

Q

T

T

P

H

Q

D

T

S

L

L

I

R

P

R

Y

Y

V

L

I

L

E

E

E
|
E

A

T

Y

Y

E
|
E

V

L

H

D

A

A

I

V

R

R

S

S

D

G

D

S

Q

V

K

D

A

Q

I

L

V

R

E

E

E
|
E

L

L

G

G

D
|
D

L

L

Q

Q

V

V

V

L

L

F

Q

H

A

A

Q

R

I

I

A

A

Q

E

D

D

Y

A

G

S

Y

Q

-

S

-

P

F

F

S

T

L

I

Q

D

E

D

V

V

A

A

E

D

G

T

I

L

T

M

E

R

K

K

L

L

I

G

R

N

R

R

binding magnesium ion: E119 (= E54), E122 (= E57), E138 (= E73), D141 (= D76)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
32% identity, 33% coverage: 36:126/277 of query aligns to 16:108/114 of 2yxhA

query
sites
2yxhA

C

C

P

P

W

W

D

L

L

E

A

K

Q

Q

T

S

P

I

Q

E

T

T

L

L

I

L

P

E

Y

A

V

L

I

A

E

S

E
|
E

A

I

Y

E

E
|
E

V

V

V

A

H

E

A

A

I

V

R

K

S

K

D

N

D

D

Q

L

K

A

A

N

I

L

V

E

E

E

E
|
E

L

I

G

G

D
|
D

L

M

L

I

L

Y

Q
x
D

V

A

V

L

L

L

Q

V

A

A

Q

A

I

V

A

A

Q

Q

-

R

D

D

Y

Y

G

G

Y

-

F

I

S

D

L

L

Q

E

E

S

V

A

A

I

E

Q

G

K

I

V

T

V

E

E

K

K

L

I

I

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

G

W

D

E

-

E

-

K

V

I

A

S

V

L

E

E

N

E

S

A

E

E

E

K

V

I

binding magnesium ion: E34 (= E54), E34 (= E54), E37 (= E57), E53 (= E73), D56 (= D76), D60 (≠ Q80)

Query Sequence

>WP_009547280.1 NCBI__GCF_000017845.1:WP_009547280.1
MSNPQTSQTQTYHAILDALNHLIDVVAKLRSPDGGCPWDLAQTPQTLIPYVIEEAYEVVH
AIRSDDQKAIVEELGDLLLQVVLQAQIAQDYGYFSLQEVAEGITEKLIRRHPHVFGDVAV
ENSEEVRQNWDKIKAEEKGETLEMAQLLSRKLERYNRSLPPLMASSKISVKAAKAGFEWE
NVDGVWEKFSEELTEFKESLETDNKVHQQSELGDLLFTIINIARWYGLDASEALSGTNKR
FIQRLSKMEKFADRPLTDYSLEDLEKLWQQAKKQLNQ

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