SitesBLAST

R95 (= R95) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K119 (= K119) mutation to A: Does not affect the nucleotide pyrophosphohydrolysis activity.
K168 (= K167) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KVYEE 168:172 (≠ KVEEE 167:171) binding ATP
E171 (= E170) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E172 (= E171) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
E175 (= E174) binding ATP; mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
K189 (≠ E183) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
KLEE 189:192 (≠ ELKH 183:186) binding ATP
E192 (≠ H186) mutation to A: Does not affect nucleotide pyrophosphohydrolysis activity.
E193 (= E187) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
D196 (= D190) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K222 (≠ R216) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
KFERR 222:226 (≠ RFEER 216:220) binding ATP
R226 (= R220) mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
W253 (= W247) binding ATP; mutation to A: Loss of pyrophosphohydrolysis activity against both ATP and dTTP.
K257 (= K251) 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)
46% identity, 98% coverage: 5:253/253 of query aligns to 8:252/255 of Q9X015

query
sites
Q9X015

F

F

D

E

R

E

L

L

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A

A

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R

H

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P

H

H

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F

F

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G

N

D

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-

K

-

I

-

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-

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A

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K

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x
E

E
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E

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N

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G

E41 (= E38) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-42.
E42 (= E39) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity; when associated with Q-41.
E45 (= E42) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
E61 (= E58) mutation to Q: Reduces the NTPase activity to 10% of the wild-type activity.
R97 (= R94) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-98.
R98 (= R95) mutation to A: Reduces the NTPase activity to 10% of the wild-type activity; when associated with A-97.
K118 (= K119) mutation to E: Reduces the NTPase activity to 10% of the wild-type activity.
E173 (= E174) mutation to A: Has little effects on the NTPase activity.
E176 (= E177) mutation to A: Has little effects on the NTPase activity.
EE 185:186 (≠ HE 186:187) 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)
37% identity, 99% coverage: 4:253/253 of query aligns to 2:224/225 of 3crcA

query
sites
3crcA

S

Q

F

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R

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L

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-

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-

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M

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G

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R

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Q

binding adenosine-5'-triphosphate: F190 (= F217), R193 (= R220), W218 (= W247)

3crcB Crystal structure of escherichia coli mazg, the regulator of nutritional stress response (see paper)
34% identity, 98% coverage: 5:252/253 of query aligns to 3:217/220 of 3crcB

query
sites
3crcB

F

I

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E

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E

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G

G

D
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D

L

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L

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F

A

A

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N

N

F

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A

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binding adenosine-5'-triphosphate: F116 (= F156), W118 (= W158), K127 (= K167), E131 (= E171), E134 (= E174)
binding magnesium ion: E131 (= E171), E134 (= E174), E152 (= E187), D155 (= D190)

A0R3C4 Nucleoside triphosphate pyrophosphohydrolase; NTP-PPase; EC 3.6.1.8 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
34% identity, 74% coverage: 6:192/253 of query aligns to 85:270/324 of A0R3C4

query
sites
A0R3C4

D

E

R

R

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x
A

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L

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M

A222 (≠ P140) 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)
36% identity, 61% coverage: 2:156/253 of query aligns to 81:235/325 of P96379

query
sites
P96379

S

S

E

Q

S

R

F

G

D

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D

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A

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A

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x
A

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K

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G

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L

A219 (≠ P140) mutation to E: Pyrophosphohydrolase activity is reduced 20-fold. It affects the magnesium binding and the protein structure.

7yh5B Mazg(mycobacterium tuberculosis) (see paper)
39% identity, 37% coverage: 2:95/253 of query aligns to 81:173/177 of 7yh5B

query
sites
7yh5B

S

S

E

Q

S

R

F

G

D

E

R

R

L

L

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V

N

D

I

A

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K

A

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M

-

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K

L

L

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R

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T

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-

N

-

G

A

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W

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K

E

Q

Q

T

T

L

H

Y

D

S

S

L

L

K

R

Q

R

N

Y

V

L

I

L

E

E

E
|
E

V

T

F

Y

E
|
E

L

L

I

L

D

D

A

A

L

V

D

R

R

S

K

G

D

S

I

V

E

D

N

Q

I

L

K

R

E

E

E
|
E

L

L

G

G

D
|
D

M

L

L

L

H

Q

V

V

V

L

F

F

H

H

S

A

Q

R

I

I

A

A

E

E

E

D

-

A

-

S

E

Q

N

S

L

P

F

F

S

T

I

I

D

D

M

-

I

-

N

-

G

-

I

V

S

A

D

D

K

T

L

L

I

M

R

R

R

K

binding magnesium ion: E119 (= E39), E122 (= E42), E138 (= E58), D141 (= D61)

2yxhA Crystal structure of mazg-related protein from thermotoga maritima
29% identity, 43% coverage: 5:113/253 of query aligns to 2:110/114 of 2yxhA

query
sites
2yxhA

F

V

D

E

R

R

L

L

V

L

N

E

I

I

V

I

K

E

R

R

L

-

R

-

S

S

P

L

N

R

G

K

C

C

P

P

W

W

D

L

R

E

K

K

Q

Q

T

S

L

I

Y

E

S

T

L

L

K

L

Q

E

N

A

V

L

I

A

E

S

E
|
E

V

I

F

E

E
|
E

L

V

I

A

D

E

A

A

L

V

D

K

R

K

K

N

D

D

I

L

E

A

N

N

I

L

K

E

E

E

E
|
E

L

I

G

G

D
|
D

M

M

L

I

L

Y

H
x
D

V

A

V

L

F

L

H

V

S

A

Q

A

I

V

A

A

E

Q

E

R

E

D

N

Y

L

G

F

I

S

D

I

L

D

E

D

S

M

A

I

I

N

Q

G

K

I

V

S

V

D

E

K

K

L

I

I

S

R

H

R

R

H

K

P

P

H

W

V

L

F

F

G

W

N

E

V

E

K

K

I

I

-

S

-

L

E

E

N

E

A

A

D

E

E

K

V

I

L

W

K

K

binding magnesium ion: E34 (= E39), E34 (= E39), E37 (= E42), E53 (= E58), D56 (= D61), D60 (≠ H65)

Query Sequence

>WP_022670473.1 NCBI__GCF_000420385.1:WP_022670473.1
MSESFDRLVNIVKRLRSPNGCPWDRKQTLYSLKQNVIEEVFELIDALDRKDIENIKEELG
DMLLHVVFHSQIAEEENLFSIDDMINGISDKLIRRHPHVFGNVKIENADEVLKNWEKIKE
NEKKEKPKHYLDSVPPSLPPIERAYKLQKKAAKVGFDWSSPEECFKKVEEEFNELKEARN
EKELKHEIGDLMFALINFARLNKIDPSEALREANIRFEERFNCIEDKLKEKNKNLNESNL
EEMDKLWDKCKKS

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