SitesBLAST

H86 (≠ Y92) mutation to R: Can be bound and inactivated by MtfA.
F136 (≠ M143) mutation to A: Decreases association with PtsG EIIB domain.
H247 (= H251) binding
C257 (= C262) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
C259 (= C264) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
C264 (= C269) binding
R306 (≠ A317) mutation to G: Forms dimers but not tetramers; when associated with G-310.
L310 (≠ R321) mutation to G: Forms dimers but not tetramers; when associated with G-306.

Sites not aligning to the query:

52 R→H: Shows increased expression and forms larger colonies.

1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
30% identity, 67% coverage: 134:411/412 of query aligns to 121:389/396 of 1z05A

query
sites
1z05A

K

E

I

I

G

E

D

E

F

F

M

F

E

Q

T

T

Y

Y

M

A

Q

A

E

Q

S

L

G

-

I

-

P

-

N

-

E

D

K

R

I

V

I

T

A

S

I

I

G

A

M

I

S

T

M

L

P

P

G

G

L

L

V

V

D

N

S

S

V

E

N

Q

G

G

V

I

N

V

H

L

T

Q

Y

M

L

P

K

H

F

Y

G

N

K

V

K

K

S

N

L

L

V

A

-

L

-

G

-

P

E

E

N

I

F

Y

E

K

A

A

R

T

F

-

D

G

R

L

K

P

V

V

F

F

I

V

E

A

N

N

D

D

A

T

R

R

A

A

M

W

T

A

L

L

A

A

E

E

F

K

K

L

F

F

S

G

Q

H

D

S

Q

Q

K

D

Y

V

N

D

N

N

V

S

L

V

G

L

I

I

F

S

V

I

G

H

W

H

G

G

I

L

G

G

L

A

G

G

I

I

I

V

I

L

D

D

G

G

K

R

L

V

Y

L

R

Q

G

G

G

R

A

H

G

G

F

N

A

I

G

G

E

E

F

L

S

G

H
|
H

S

I

P

Q

I

I

F

-

E

D

S

P

R

Q

E

G

I

K

S

R

C
|
C

T

H

C
|
C

G

G

K

N

K

Y

G

G

C
|
C

L

L

E

E

A

T

V

V

A

A

S

S

G

S

T

Q

A

A

M

I

V

R

R

D

M

Q

A

V

E

T

E

A

A

R

I

I

E

Q

K

A

D

G

S

E

D

P

S

S

I

C

L

L

S

A

R

T

M

V

A

-

R

-

E

-

R

-

G

-

E

E

G

E

I

I

D

S

P

I

S

E

L

D

I

I

V

C

D

A

A

A

L

A

A

D

G

G

D

D

Q

P

R

L

A

A

I

V

T

D

I

V

L

I

S

Q

D

Q

V

L

G

G

L

R

D

Y

L

L

G

G

R

A

G

A

I

I

S

A

I

I

L

V

I

I

Q

N

L

L

L

F

N

N

P

P

D

E

L

K

I

I

I

L

V

I

G

G

S

V

V

I

A

N

E

Q

A

A

Q

K

Q

S

Y

I

L

L

I

Y

T

P

P

S

I

I

Q

E

Q

Q

A

C

L

I

N

R

I

E

F

Q

S

S

M

L

A

P

K

V

S

Y

R

H

E

Q

K

D

S

L

E

K

L

L

T

V

L

E

Y

S

K

R

L

F

G

Y

K

K

E

Q

V

-

G

A

L

T

L

M

G

P

G

G

V

A

A

A

V

L

V

I

I

K

E

Q

N

A

I

L

F

Y

E

D

D

G

I

L

binding zinc ion: H236 (= H251), C246 (= C262), C248 (= C264), C253 (= C269)

2qm1B Crystal structure of glucokinase from enterococcus faecalis
30% identity, 62% coverage: 151:404/412 of query aligns to 66:321/325 of 2qm1B

query
sites
2qm1B

E

E

K

D

I

F

I

V

A

G

I

I

G

G

M

M

S

G

M

T

P

P

G

G

L

S

V

V

D

D

S

I

V

E

N

K

G

G

-

T

-

V

-

G

-

A

-

Y

-

N

V

L

N

N

H

W

T

T

Y

T

L

V

K

Q

F

-

G

-

K

-

S

P

L

V

V

K

E

E

N

Q

F

I

E

E

A

S

R

A

F

L

D

G

R

I

K

P

V

F

F

A

I

L

E

D

N
|
N

D

D

A

A

R
x
N

A

V

M

A

T

A

L

L

A

G

E

E

F

R

K

W

F

K

S

G

Q

A

D

G

Q

E

K

N

Y

N

N

P

N

D

V

V

L

I

G

F

I

I

F

T

V

L

G

G

W

T

G

G

I

V

G

G

L
x
G

G

G

I

I

I

V

I

A

D

A

G

G

K

K

L

L

Y

L

R

H

G

G

G

V

A

A

G

G

F

C

A

A

G

G

E

E

F

V

S

G

H
|
H

S

V

P

T

I

V

F

-

E

D

S

P

R

N

E

G

I

F

S

D

C
|
C

T

T

C
|
C

G

G

K

K

K

R

G

G

C
|
C

L

L

E

E

A

T

V

V

A

S

S

S

G

A

T

T

A

G

M

V

V

V

R

R

M

V

A

A

E

R

E

H

A

L

I

S

E

E

K

E

D

F

S

A

D

G

S

D

I

S

L

E

S

L

R

K

M

Q

A

A

R

I

E

D

R

D

G

G

E

Q

G

D

I

V

D

S

P

S

S

K

L

D

I

V

V

F

D

E

A

F

A

A

L

E

A

K

G

G

D

D

Q

H

R

F

A

A

I

L

T

M

I

V

L

V

S

D

D

R

V

V

G

C

L

F

D

Y

L

L

G

G

R

L

G

A

I

T

S

G

I

N

L

L

I

G

Q

N

L

T

L

L

N

N

P

P

D

D

L

S

I

V

V

I

G

G

S

G

V

V

A

S

E

A

A

A

Q

G

Q

E

Y

F

L

L

I

R

T

S

P

R

I

V

Q

E

Q

K

A

Y

L

F

N

Q

I

E

F

F

S

T

M

F

A

P

K

Q

S

V

R

R

E

N

K

S

S

T

E

K

L

I

T

K

L

L

Y

A

K

E

L

L

G

G

K

N

E

E

V

A

G

G

L

V

L

I

G

G

G

A

V

A

A

S

V

L

V

A

I

L

E

Q

binding magnesium ion: N116 (= N198), N119 (≠ R201), G148 (≠ L230)
binding zinc ion: H169 (= H251), C179 (= C262), C181 (= C264), C186 (= C269)

5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
29% identity, 62% coverage: 152:407/412 of query aligns to 60:306/306 of 5f7rA

query
sites
5f7rA

K

H

I

L

A

G

I

V

G

G

M

I

S

A

M

I

P

S

G
|
G

L

L

V

V

D

N

S

R

V

K

N

K

G

G

-

T

-

V

V

I

N

R

H

S

T

T

Y

M

L

L

K

G

F

W

G

E

K

N

K

V

S

A

L

L

V

E

E

A

N

M

F

L

E

H

A

A

R

H

F

F

-

P

D

D

R

I

K

P

V

V

F

Y

I

V

E

D

N

K

D
x
N

A

I

R

N

A

C

M

Y

T

T

L

L

A

A

E

E

F

L

K

W

F

L

S

G

Q

E

D

G

Q

K

K

Q

Y

S

N

N

V

F

L

A

G

T

I

V

F
x
S

V
|
V

G

G

W

A

G
|
G

I
x
L

G
|
G

L

L

G

S

I

V

I

I

D

N

G

R

K

Q

L

I

Y

Y

R

Y

G

G

G

A

A

Q

G

G

F

G

A

A

G

G

E
|
E

F

F

S

G

H
|
H

S

T

P

T

I

I

F

-

E

Q

S

P

R

G

E

G

I

Y

S

K

C
|
C

T

H

C
|
C

G

G

K

Q

K

K

G

G

C
|
C

L

L

E
|
E

A

M

V

Y

A

A

S

S

G

E

T

F

A

Y

M

F

V

R

R

N

M

R

A

G

E

E

A

L

I

K

E

E

K

A

D

Y

-

P

-

L

S

N

D

D

S

F

I

H

L

F

S

D

R

K

M

V

A

A

R

K

E

-

R

-

G

-

E

-

G

-

I

-

D

-

P

-

S

-

L

-

I

-

V

-

D

-

A

S

A

A

L

R

A

A

G

G

D

D

Q

E

R

M

A

A

I

T

T

E

I

L

L

M

S

G

D

K

V

M

G

G

L

E

D

Y

L

L

G

G

R

Y

G

G

I

I

S

R

I

N

L

I

I

I

Q

N

L

T

L

F

N

N

P

P

D

E

L

K

I

V

I

I

V

I

G

V

G

G

S
x
E

V

G

A

L

E

H

A

H

Q

R

Q

D

Y

L

L

F

I

L

T

T

P

K

I

I

Q

D

Q

E

-

I

-

A

A

S

L

Q

N

N

I

F

F

F

S

S

M

G

A

A

K

G

S

F

R

-

E

-

K

E

S

T

E

E

L

I

T

T

L

T

Y

T

K

S

L

L

G

E

K

D

E

P

V

A

G
x
W

L

L

L

Q

G

G

G

A

V

A

A

L

V

L

V

V

I

I

E

H

N

Q

I

L

F

F

binding alpha-D-glucopyranose: G70 (= G162), N110 (≠ D199), N110 (≠ D199), S134 (≠ F223), V135 (= V224), G138 (= G227), L139 (≠ I228), G140 (= G229), E159 (= E248), H162 (= H251), E181 (= E271), E253 (≠ S354), W293 (≠ G394)
binding zinc ion: H162 (= H251), C172 (= C262), C174 (= C264), C179 (= C269)

Sites not aligning to the query:

binding alpha-D-glucopyranose: 7, 10

3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
27% identity, 74% coverage: 94:397/412 of query aligns to 4:304/312 of 3vglA

query
sites
3vglA

L

I

A

G

L

V

D

D

I

I

S
x
G

K

G

F
x
T

V
x
K

V

I

R

A

A

A

A

G

I

V

Y

V

D

D

S

E

N

G

Q

R

A

I

V

L

T

S

E

-

T

-

G

-

T

T

F

F

K

K

I

V

-

A

T

T

L

P

N

P

N

T

E

A

K

E

S

G

T

I

F

V

D

D

K

A

I

I

G

C

D

A

F

A

M

V

E

A

T

G

Y

A

M

S

Q

E

E

-

S

-

G

-

I

-

P

-

N

G

E

H

K

D

I

V

I

E

A

A

I

V

G

G

M

I

S

G

M

A

P

A

G
|
G

L

Y

V

V

D

D

S

D

V

K

N

R

G

A

-

T

-

V

V

L

N

F

H

A

T
x
P

Y

N

L

I

K

D

F

W

G

R

K

H

K

E

S

P

L

L

V

K

E

D

N

K

F

V

E

E

A

Q

R

R

F

V

D

G

R

L

K

P

V

V

F

V

I

V

E

E

N
|
N

D
|
D

A

A

R

N

A

A

M

A

T

A

L

W

A

G

E

E

F

Y

K

R

F

F

S

G

Q

A

D

G

Q

Q

K

G

Y

H

N

D

V

V

L

I

G

C

I

I

F

T

V

L

G
|
G

W
x
T

G

G

I
x
L

G
|
G

L

G

G

G

I

I

D

G

G

N

K

K

L

L

Y

R

R

R

G

G

G

R

A

F

G

G

F

V

A

A

G

A

E
|
E

F

F

S

G

H
|
H

S

I

P

R

I

V

F

V

E

P

S

D

R

-

E

G

I

L

S

L

C
|
C

T

G

C
|
C

G

G

K

S

K

Q

G

G

C
|
C

L

W

E
|
E

A

Q

V

Y

A

A

S

S

G
|
G

T

R

A

A

M

L

V

V

R

R

M

Y

A

A

E

K

E

Q

A

R

I

A

E

N

-

A

-

T

K

P

D

E

S

N

D

A

S

A

I

V

L

L

S

L

R

G

M

L

A

G

R

D

E

G

R

S

G

V

E

D

G

G

I

I

D

E

P
x
G

S

K

L

H

I

I

V
x
S

D

E

A

A

L

R

A

Q

G

G

D

D

Q

P

R

V

A

A

I

V

T

D

I

S

L

F

S

R

D

E

V

L

G

A

L

R

D

W

L

A

G

G

R

A

G

G

I

L

S

A

I

D

L

L

I

A

Q

S

L

L

L

F

N

D

P

P

D

S

L

A

I

F

I

I

V

V

G

G

S
x
G

V
|
V

A

S

E

D

A
x
E

Q

G

Q

E

Y

L

L

V

I

L

T

D

P

P

I

I

Q

R

Q

K

A

S

L

F

N

R

I

R

F

W

S

L

M

I

-

G

A

G

K

E

S

W

R

R

E

P

K

H

S

A

E

Q

L

V

T

L

L

A

Y

A

K

Q

L

L

G

G

K

G

E

K

V

A

G

G

L

L

L

V

G

G

binding phosphoaminophosphonic acid-adenylate ester: G9 (≠ S99), T11 (≠ F101), K12 (≠ V102), G130 (= G225), T131 (≠ W226), G180 (= G276), G214 (≠ P308), S218 (≠ V312), G260 (≠ S354), V261 (= V355), E264 (≠ A358)
binding beta-D-glucopyranose: G65 (= G162), P78 (≠ T173), N103 (= N198), D104 (= D199), L133 (≠ I228), G134 (= G229), E153 (= E248), H156 (= H251), E175 (= E271)
binding zinc ion: H156 (= H251), C166 (= C262), C168 (= C264), C173 (= C269)

3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
27% identity, 74% coverage: 94:397/412 of query aligns to 4:304/312 of 3vgkB

query
sites
3vgkB

L

I

A

G

L

V

D

D

I

I

S

G

K

G

F

T

V

K

V

I

R

A

A

A

A

G

I

V

Y

V

D

D

S

E

N

G

Q

R

A

I

V

L

T

S

E

-

T

-

G

-

T

T

F

F

K

K

I

V

-

A

T

T

L

P

N

P

N

T

E

A

K

E

S

G

T

I

F

V

D

D

K

A

I

I

G

C

D

A

F

A

M

V

E

A

T

G

Y

A

M

S

Q

E

E

-

S

-

G

-

I

-

P

-

N

G

E

H

K

D

I

V

I

E

A

A

I

V

G

G

M

I

S

G

M

A

P

A

G

G

L

Y

V

V

D

D

S

D

V

K

N

R

G

A

-

T

-

V

V

L

N

F

H

A

T

P

Y

N

L

I

K

D

F

W

G

R

K

H

K

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L

L

V

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D

N

K

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E

A

Q

R

R

F

V

D

G

R

L

K

P

V

V

F

V

I

V

E

E

N

N

D

D

A

A

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N

A

A

M

A

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A

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W

A

G

E

E

F

Y

K

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A

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Q

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N

D

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I

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V

L

G

G

W

T

G

G

I

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G

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L

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G

G

I

I

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G

G

N

K

K

L

L

Y

R

R

R

G

G

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R

A

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G

G

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A

A

G

A

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H
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H

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R

-

E

G

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C
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C

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C
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C

G

G

K

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Q

G

G

C
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C

L

W

E

E

A

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Y

A

A

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S

G

G

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R

A

A

M

L

V

V

R

R

M

Y

A

A

E

K

E

Q

A

R

I

A

E

N

-

A

-

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K

P

D

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N

D

A

S

A

I

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L

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I

I

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A

A

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A

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G

D

D

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R

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A

A

I

V

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D

I

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A

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A

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A

G

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A

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S

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N

D

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P

D

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A

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I

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V

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G

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G

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V

A

S

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D

A

E

Q

G

Q

E

Y

L

L

V

I

L

T

D

P

P

I

I

Q

R

Q

K

A

S

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F

N

R

I

R

F

W

S

L

M

I

-

G

A

G

K

E

S

W

R

R

E

P

K

H

S

A

E

Q

L

V

T

L

L

A

Y

A

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Q

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L

G

G

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G

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K

V

A

G

G

L

L

L

V

G

G

binding zinc ion: H156 (= H251), C166 (= C262), C168 (= C264), C173 (= C269)

Q9Y223 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase; UDP-GlcNAc-2-epimerase/ManAc kinase; EC 3.2.1.183; EC 2.7.1.60 from Homo sapiens (Human) (see 18 papers)
28% identity, 68% coverage: 89:370/412 of query aligns to 405:688/722 of Q9Y223

query
sites
Q9Y223

D

E

S

T

F

L

Y

S

V

A

L

L

A

A

L

V

D
|
D

I

L

S

G

K
x
G

F
x
T

V
x
N

V

L

R
|
R

A

V

A

A

I

I

Y

V

D

S

S

M

S

K

N

G

Q

E

A

I

V

V

T

K

E

K

T

Y

G

T

T

Q

F

F

K

-

I

-

T

-

L

-

N

-

N

N

E

P

K

K

S

T

T

Y

F

E

D

E

K

R

I

I

G

N

D

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T

M

Y

C

M

V

Q

E

-

A

E

E

S

A

G

V

I

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P

L

N

N

E

C

K

R

I

I

I

L

A

G

I

V

G

G

M
x
I

S

S

M

T

P

G

G
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G

L
x
R

V

V

D

N

S

P

V

R

N

E

G

G

V

I

-

V

-

L

N

H

H

S

T
|
T

Y

K

L

L

-

I

-

Q

K

E

F

W

G

N

K

S

K

V

S

D

L

L

V

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E

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N

P

F

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E

S

A

D

R

T

F

L

D

H

R

L

K

P

V

V

F

W

I

V

E

D

N
|
N

D
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D

A

G

R
x
N

A

C

M

A

T

A

L

L

A
|
A

E

E

F

R

K

K

F
|
F

S

G

Q

Q

D

G

Q

K

K

G

Y

L

N

E

N

N

V

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G

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I

L

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G

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G

I

I

G

G

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G

G

G

I

I

I

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D

Q

G

H

K

E

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L

Y

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G

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A

A

G

A

E
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E

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G

H
|
H

S

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-

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x
V

E

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S

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R

D

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x
G

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C

T

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C
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C

G

G

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S

K

H

G

G

C
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C

L
x
I

E
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E

A

A

V

Y

A

A

S

S

G

G

T

M

A

A

M

L

V

Q

R

R

M

E

A

A

E

K

A

L

I

-

E

-

K

H

D

D

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E

D

D

S

L

I

L

L

L

S

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-

G

M

M

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A

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I

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A

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A

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Q

A

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K

A

A

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A

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G

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A

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N

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L

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I

I

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Y

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-

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Q

A

A

L

L

D413 (= D97) binding
G416 (≠ K100) binding
T417 (≠ F101) binding
N418 (≠ V102) binding
R420 (= R104) binding
I472 (≠ M158) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 50% of the wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to less than 10% of wild-type activity
G476 (= G162) binding ; binding
R477 (≠ L163) binding ; binding
T489 (= T173) binding ; binding
N516 (= N198) binding ; binding
D517 (= D199) active site; binding ; binding ; mutation D->A,N: Loss of N-acylmannosamine kinase activity. Decreased affinity for N-acyl-D-mannosamine. No effect on structure.
N519 (≠ R201) to S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910; mutation to S: Decreased N-acylmannosamine kinase activity.
A524 (= A206) to V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 10% of wild-type activity; decreased N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs764698870
F528 (= F210) to C: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70% of wild-type activity; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986; mutation to C: Decreased N-acylmannosamine kinase activity.
G545 (= G227) binding
E566 (= E248) binding
H569 (= H251) binding ; binding ; binding
V572 (≠ F255) to L: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70-80% of wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to less than 10% of wild-type activity; does not affect homohexamers formation; dbSNP:rs121908632
G576 (≠ E259) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
C579 (= C262) binding
C581 (= C264) binding
C586 (= C269) binding
I587 (≠ L270) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603; mutation to T: Decreased N-acylmannosamine kinase activity.
E588 (= E271) binding ; binding
A630 (= A314) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
A631 (= A315) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 80% of wild-type activity; decreased N-acylmannosamine kinase activity; retains 75% of wild-type activity; dbSNP:rs121908626; to V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70% of wild-type activity; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs62541771; mutation A->V,T: Decreased N-acylmannosamine kinase activity.

Sites not aligning to the query:

13 C → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; dbSNP:rs1209266607
19 binding
23 binding
113 binding
132 H → Q: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 10% of wild-type activity; impaired homohexamers formation
176 D → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs139425890
177 R → C: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs539332585
200 I → F: in NM; uncertain significance; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 90% of wild-type activity; decreased N-acylmannosamine kinase activity; retains 75% of wild-type activity; dbSNP:rs369328625
206 G → S: in NM; moderate phenotype with unusual involvement of quadriceps; dbSNP:rs766266918
220 binding
253 binding
259 binding
263 R → L: in SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac; dbSNP:rs121908623
266 R → Q: in SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac; dbSNP:rs121908622; R → W: in sialuria; dbSNP:rs121908621
271 binding
280 binding
281 binding
282 binding
301 binding
302 binding
303 C → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 80% of wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to 60% of wild-type activity; requires 2 nucleotide substitutions; dbSNP:rs121908633
307 binding
321 binding
331 V → A: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation
378 D → Y: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 10-30% of wild-type activity; decreased N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs199877522
708 G → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; severely decreased; dbSNP:rs1554657922
712 M→T: Decreased N-acylmannosamine kinase activity.

O35826 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase; UDP-GlcNAc-2-epimerase/ManAc kinase; EC 3.2.1.183; EC 2.7.1.60 from Rattus norvegicus (Rat) (see paper)
28% identity, 68% coverage: 89:370/412 of query aligns to 405:688/722 of O35826

query
sites
O35826

D

E

S
x
T

F
x
L

Y
x
S

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x
A

L
|
L

A
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A

L
x
V

D
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D

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x
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G

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x
G

F
x
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x
N

V
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L

R
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R

A
x
V

A
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A

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I

Y
x
V

D
x
S

S
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M

S
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K

N
x
G

Q
x
E

A
x
I

V
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V

T
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K

E
x
K

T
x
Y

G
x
T

T
x
Q

F
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F

K

-

I

-

T

-

L

-

N

-

N
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N

E
x
P

K
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K

S
x
T

T
x
Y

F
x
E

D
x
E

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I

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M

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M
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Q
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E

-
x
A

E
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E

S
x
A

G
x
V

I
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K

P
x
L

N
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N

E
x
C

K
x
R

I
|
I

I
x
L

A
x
G

I
x
V

G
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G

M
x
I

S
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S

M
x
T

P
x
G

G
|
G

L
x
R

V
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V

D
x
N

S
x
P

V
x
Q

N
x
E

G
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G

V
|
V

-
x
V

-
x
L

N
x
H

H
x
S

T
|
T

Y
x
K

L
|
L

-
x
I

-
x
Q

K
x
E

F
x
W

G
x
N

K
x
S

K
x
V

S
x
D

L
|
L

V
x
R

E
x
T

N
x
P

F
x
L

E
x
S

A
x
D

R
x
T

F
x
L

D
x
H

R
x
L

K
x
P

V
|
V

F
x
W

I
x
V

E
x
D

N
|
N

D
|
D

A
x
G

R
x
N

A
x
C

M
x
A

T
x
A

L
x
M

A
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A

E
|
E

F
x
R

K
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K

F
|
F

S
x
G

Q
|
Q

D
x
G

Q
x
K

K
x
G

Y
x
Q

N
x
E

N
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N

V
x
F

L
x
V

G
x
T

I
x
L

F
x
I

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x
T

G
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G

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T

G
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G

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I

G
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G

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x
G

G
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G

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I

I
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H

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Q

G
x
H

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x
E

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L

Y
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I

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H

G
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G

G
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S

A
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S

G
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F

F
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C

A
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A

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A

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E

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H

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C

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C

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G

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S

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H

G
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G

C
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C

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x
I

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E

A
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A

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Y

A
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A

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S

G
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G

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M

A
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A

M
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R

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A

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D

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L

L
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L

S
x
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x
E

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x
G

M
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M

A
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S

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V

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K

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x
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E
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E

G
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A

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G

P
x
A

S
x
L

L
x
H

I
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L

V
x
I

D
x
Q

A
|
A

L
x
K

A
x
L

G
|
G

D
x
N

Q
x
V

R
x
K

A
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A

I
x
Q

T
x
S

I
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I

L
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L

S
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R

D
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T

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x
A

G
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G

L
x
T

D
x
A

L
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L

G
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G

R
x
L

G
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G

I
x
V

S
x
V

I
x
N

L
x
I

I
x
L

Q
x
H

L
x
T

L
x
M

N
|
N

P
|
P

D
x
S

L
|
L

I
x
V

I
|
I

V
x
L

G
x
S

G
|
G

S
x
V

V
x
L

A
|
A

E
x
S

A
x
H

Q
x
Y

Q
x
I

Y
x
H

L
x
I

I
x
V

T
x
R

P
x
D

I
x
V

-
x
I

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x
R

Q
|
Q

A
|
A

L
|
L

D413 (= D97) mutation D->K,N: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.
R420 (= R104) mutation to M: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.

Sites not aligning to the query:

1 UDP-N-acetylglucosamine 2-epimerase
49 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Does not interfere with enzyme oligomerization.
110 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process.
132 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process.
155 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process.
157 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process.
406:722 N-acetylmannosamine kinase

2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
28% identity, 68% coverage: 90:370/412 of query aligns to 2:280/309 of 2yhwA

query
sites
2yhwA

S

T

F

L

Y

S

V

A

L

L

A

A

L

V

D

D

I

L

S

G

K

G

F

T

V

N

V

L

R

R

A

V

A

A

I

I

Y

V

D

S

S

M

S

K

N

G

Q

E

A

I

V

V

T

K

E

K

T

Y

G

T

T

Q

F

F

K

-

I

-

T

-

L

-

N

-

N

N

E

P

K

K

S

T

T

Y

F

E

D

E

K

R

I

I

G

N

D

L

F

I

M

L

E

Q

T

M

Y

C

M

V

Q

E

-

A

E

E

S

A

G

V

I

K

P

L

N

N

E

C

K

R

I

I

I

L

A

G

I

V

G

G

M

I

S

S

M

T

P

G

G

G

L

R

V

V

D

N

S

P

V

R

N

E

G

G

V

I

-

V

-

L

N

H

H

S

T

T

Y

K

L

L

-

I

-

Q

K

E

F

W

G

N

K

S

K

V

S

D

L

L

V

R

E

T

N

P

F

L

E

S

A

D

R

T

F

L

D

H

R

L

K

P

V

V

F

W

I

V

E

D

N
|
N

D

D

A

G

R
x
N

A

C

M

A

T

A

L

L

A

A

E

E

F

R

K

K

F

F

S

G

Q

Q

D

G

Q

K

K

G

Y

L

N

E

N

N

V

F

L

V

G

T

I

L

F

I

V

T

G

G

W

T

G

G

I

I

G

G

L
x
G

G

G

I

I

I

H

D

Q

G

H

K

E

L

L

Y

I

R

H

G

G

G

S

A

S

G

F

F

C

A

A

G
x
A

E

E

F

L

S

G

H
|
H

S

L

P

-

I

V

F

V

E

S

S

L

R

N

E

G

I

P

S

D

C
|
C

T

S

C
|
C

G

G

K

S

K

H

G

G

C
|
C

L

I

E

E

A

A

V

Y

A

A

S

S

G

G

T

M

A

A

M

L

V

Q

R

R

M

E

A

A

E

K

A

L

I

-

E

-

K

H

D

D

S

E

D

D

S

L

I

L

L

L

S

V

R

-

M

-

A

-

R

-

E

-

R

-

G

-

E

E

G

G

I

M

D

S

P

V

S

A

L

V

-

G

-

A

-

L

-

H

I

L

V

I

D

Q

A

A

L

K

A

L

G

G

D

N

Q

A

R

K

A

A

I

Q

T

S

I

I

L

L

S

R

D

T

V

A

G

G

L

T

D

A

L

L

G

G

R

L

G

G

I

V

S

V

I

N

L

I

I

L

Q

H

L

T

L

M

N

N

P

P

D

S

L

L

I

V

I

I

V

L

G

S

G

G

S

V

V

L

A

A

E

S

A

H

Q

Y

Q

I

Y

H

L

I

I

V

T

K

P

D

I

V

-

I

-

R

Q

Q

A

A

L

L

binding calcium ion: N112 (= N198), N115 (≠ R201), G144 (≠ L230), A161 (≠ G247)
binding zinc ion: H165 (= H251), C175 (= C262), C177 (= C264), C182 (= C269)

2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
28% identity, 68% coverage: 90:370/412 of query aligns to 2:279/308 of 2yi1A

query
sites
2yi1A

S

T

F

L

Y

S

V

A

L

L

A

A

L

V

D

D

I

L

S
x
G

K
x
G

F
x
T

V
x
N

V

L

R
|
R

A

V

A

A

I

I

Y

V

D

S

S

M

S

K

N

G

Q

E

A

I

V

V

T

K

E

K

T

Y

G

T

T

Q

F

F

K

-

I

-

T

-

L

-

N

-

N

N

E

P

K

K

S

T

T

Y

F

E

D

E

K

R

I

I

G

N

D

L

F

I

M

L

E

Q

T

M

Y

C

M

V

Q

E

-

A

E

E

S

A

G

V

I

K

P

L

N

N

E

C

K

R

I

I

I

L

A

G

I

V

G

G

M

I

S

S

M

T

P
x
G

G
|
G

L
x
R

V

V

D

N

S

P

V

R

N

E

G

G

V

I

-

V

-

L

N

H

H
x
S

T
|
T

Y

K

L
|
L

-

I

-

Q

K

E

F

W

G

N

K

S

K

V

S

D

L

L

V

R

E

T

N

P

F

L

E

S

A

D

R

T

F

L

D

H

R

L

K

P

V

V

F

W

I

V

E

D

N
|
N

D
|
D

A

G

R
x
N

A

C

M

A

T

A

L

L

A

A

E

E

F

R

K

K

F

F

S

G

Q

Q

D

G

Q

K

K

G

Y

L

N

E

N

N

V

F

L

V

G

T

I

L

F

I

V

T

G
|
G

W
x
T

G
|
G

I
|
I

G

G

L
x
G

G

G

I

I

I

H

D

Q

G

H

K

E

L

L

Y

I

R

H

G

G

G

S

A

S

G

F

F

C

A

A

G
x
A

E
|
E

F

L

S

G

H
|
H

S

L

P

-

I

V

F

V

E

S

S

L

R

D

E

G

I

P

S

D

C
|
C

T

S

C
|
C

G

G

K

S

K

H

G

G

C
|
C

L

I

E
|
E

A

A

V

Y

A

A

S

S

G
|
G

T

M

A

A

M

L

V

Q

R

R

M

E

A

A

E

K

A

L

I

-

E

-

K

H

D

D

S

E

D

D

S

L

I

L

L

L

S

V

R

-

M

-

A

-

R

-

E

E

R

G

G

M

E

S

G

A

I

V

D

G

P

A

S
x
L

L

H

I

L

V

I

D

Q

A

A

L

K

A

L

G

G

D

N

Q

A

R

K

A

A

I

Q

T

S

I

I

L

L

S

R

D

T

V

A

G

G

L

T

D

A

L

L

G

G

R

L

G

G

I

V

S

V

I

N

L

I

I

L

Q

H

L

T

L

M

N

N

P

P

D

S

L

L

I

V

I

I

V

L

G

S

G

G

S
x
V

V

L

A

A

E

S

A

H

Q

Y

Q

I

Y

H

L

I

I

V

T

K

P

D

I

V

-

I

-

R

Q

Q

A

A

L

L

binding adenosine-5'-diphosphate: G11 (≠ S99), T13 (≠ F101), N14 (≠ V102), R16 (= R104), T140 (≠ W226), G189 (= G276), L216 (≠ S309), V261 (≠ S354)
binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (≠ K100), G71 (≠ P161), G72 (= G162), R73 (≠ L163), S84 (≠ H172), T85 (= T173), L87 (= L175), N112 (= N198), D113 (= D199), G139 (= G225), T140 (≠ W226), G141 (= G227), I142 (= I228), E162 (= E248), H165 (= H251), E184 (= E271)
binding calcium ion: N112 (= N198), N115 (≠ R201), G144 (≠ L230), A161 (≠ G247)
binding zinc ion: H165 (= H251), C175 (= C262), C177 (= C264), C182 (= C269)

2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
28% identity, 68% coverage: 90:370/412 of query aligns to 2:279/308 of 2yhyA

query
sites
2yhyA

S

T

F

L

Y

S

V

A

L

L

A

A

L

V

D

D

I

L

S
x
G

K
x
G

F
x
T

V
x
N

V

L

R
|
R

A

V

A

A

I

I

Y

V

D

S

S

M

S

K

N

G

Q

E

A

I

V

V

T

K

E

K

T

Y

G

T

T

Q

F

F

K

-

I

-

T

-

L

-

N

-

N

N

E

P

K

K

S

T

T

Y

F

E

D

E

K

R

I

I

G

N

D

L

F

I

M

L

E

Q

T

M

Y

C

M

V

Q

E

-

A

E

E

S

A

G

V

I

K

P

L

N

N

E

C

K

R

I

I

I

L

A

G

I

V

G

G

M

I

S

S

M

T

P

G

G

G

L

R

V

V

D

N

S

P

V

R

N

E

G

G

V

I

-

V

-

L

N

H

H

S

T

T

Y

K

L

L

-

I

-

Q

K

E

F

W

G

N

K

S

K

V

S

D

L

L

V

R

E

T

N

P

F

L

E

S

A

D

R

T

F

L

D

H

R

L

K

P

V

V

F

W

I

V

E

D

N
|
N

D

D

A

G

R
x
N

A

C

M

A

T

A

L

L

A

A

E

E

F

R

K

K

F

F

S

G

Q

Q

D

G

Q

K

K

G

Y

L

N

E

N

N

V

F

L

V

G

T

I

L

F

I

V

T

G

G

W
x
T

G

G

I

I

G

G

L
x
G

G

G

I

I

I

H

D

Q

G

H

K

E

L

L

Y

I

R

H

G

G

G

S

A

S

G

F

F

C

A

A

G
x
A

E

E

F

L

S

G

H
|
H

S

L

P

-

I

V

F

V

E

S

S

L

R

D

E

G

I

P

S

D

C
|
C

T

S

C
|
C

G

G

K

S

K

H

G

G

C
|
C

L

I

E

E

A

A

V

Y

A

A

S

S

G
|
G

T

M

A

A

M

L

V

Q

R

R

M

E

A

A

E

K

A

L

I

-

E

-

K

H

D

D

S

E

D

D

S

L

I

L

L

L

S

V

R

-

M

-

A

-

R

-

E

E

R

G

G

M

E

S

G

A

I

V

D

G

P

A

S
x
L

L

H

I

L

V

I

D

Q

A

A

L

K

A

L

G

G

D

N

Q

A

R

K

A

A

I

Q

T

S

I

I

L

L

S

R

D

T

V

A

G

G

L

T

D

A

L

L

G

G

R

L

G

G

I

V

S

V

I

N

L

I

I

L

Q

H

L

T

L

M

N

N

P

P

D

S

L

L

I

V

I

I

V

L

G

S

G

G

S
x
V

V

L

A

A

E

S

A

H

Q

Y

Q

I

Y

H

L

I

I

V

T

K

P

D

I

V

-

I

-

R

Q

Q

A

A

L

L

binding adenosine-5'-diphosphate: G11 (≠ S99), G12 (≠ K100), T13 (≠ F101), N14 (≠ V102), R16 (= R104), T140 (≠ W226), G189 (= G276), L216 (≠ S309), V261 (≠ S354)
binding calcium ion: N112 (= N198), N115 (≠ R201), G144 (≠ L230), A161 (≠ G247)
binding zinc ion: H165 (= H251), C175 (= C262), C177 (= C264), C182 (= C269)

6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
28% identity, 50% coverage: 191:397/412 of query aligns to 95:280/290 of 6jdbA

query
sites
6jdbA

D

D

R

K

K

P

V

I

F

G

I

L

E

L

N
|
N

D
|
D

A

A

R

Q

A

A

M

A

T

T

L

Y

A

A

E

E

F

Y

K

Q

F

L

S

Q

Q

N

D

F

Q

E

K

Q

Y

V

N

S

N

N

V

F

L

V

G

F

I

I

F

T

V

V

G
x
S

W
x
T

G

G

I

V

G

G

L

G

G

G

I

I

I

V

I

L

D

N

G

Q

K

I

L

L

Y

Q

R

T

G

G

G

S

A

R

G

G

F

I

A

A

G

G

E
x
H

F

I

S

G

H
|
H

S

T

P

-

I

L

F

A

E

D

S

P

R

N

E

G

I

A

S

I

C
|
C

T

G

C
|
C

G

G

K

R

G

G

C
|
C

L

V

E
|
E

A

A

V

I

A

A

S

S

G

G

T

R

A

A

M

I

V

-

R

-

M

-

A

-

E

-

E

E

A

A

I

V

E

S

K

S

D

Q

S

W

D

E

S

-

I

-

L

-

S

-

R

-

M

-

A

-

R

-

E

-

R

-

G

-

E

D

G

P

I

C

D

D

P
|
P

S
x
K

L

E

I

V

V

F

D

E

A

R

A

F

L

R

A

K

G

N

D

D

Q

E

R

K

A

A

I

T

T

A

I

L

L

V

S

E

D

R

V

S

G

A

L

K

D

A

L

I

G

A

R

N

G

L

I

I

S

A

I

D

L

L

I

V

Q

I

L

S

L

L

N

D

P

I

D

Q

L

K

I

I

I

A

V

I

G

G

S
|
S

V

V

A

G

E

L

A

A

Q

E

Q

G

Y

Y

L

L

I

-

T

S

P

L

I

V

Q

E

Q

K

A

Y

L

L

N

Q

I

D

F

F

S

P

M

-

A

-

K

-

S

S

R

I

E

Y

K

C

S

C

E

E

L

I

T

E

L

T

Y

A

K

K

L

F

G

G

K

Q

E

D

V

A

G

G

L

L

L

I

G

G

binding adenosine-5'-diphosphate: S129 (≠ G225), T130 (≠ W226), P195 (= P308), K196 (≠ S309), S241 (= S354)
binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: N102 (= N198), D103 (= D199), S129 (≠ G225), T130 (≠ W226), H152 (≠ E248), H155 (= H251), E174 (= E271)
binding zinc ion: H155 (= H251), C165 (= C262), C167 (= C264), C172 (= C269)

Sites not aligning to the query:

3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
33% identity, 43% coverage: 194:370/412 of query aligns to 83:259/288 of 3eo3A

query
sites
3eo3A

V

V

F

W

I

V

E

D

N

N

D

D

A

G

R

N

A

C

M

A

T

A

L

L

A

A

E

E

F

R

K

K

F

F

S

G

Q

Q

D

G

Q

K

K

G

Y

L

N

E

N

N

V

F

L

V

G

T

I

L

F

I

V

T

G

G

W

T

G

G

I

I

G

G

L

G

G

G

I

I

I

H

D

Q

G

H

K

E

L

L

Y

I

R

H

G

G

G

S

A

S

G

F

F

C

A

A

G

A

E

E

F

L

S

G

H
|
H

S

L

P

-

I

V

F

V

E

S

S

L

R

D

E

G

I

P

S

D

C
|
C

T

S

C
|
C

G

G

K

S

K

H

G

G

C
|
C

L

I

E

E

A

A

V

Y

A

A

S

S

G

G

T

M

A

A

M

L

V

Q

R

R

M

E

A

A

E

K

A

L

I

-

E

-

K

H

D

D

S

E

D

D

S

L

I

L

L

L

S

V

R

E

-

G

M

M

A

S

R

V

E

P

R

K

G

D

E

E

G

A

I

V

D

G

P

A

S

L

L

H

I

L

V

I

D

Q

A

A

L

K

A

L

G

G

D

N

Q

A

R

K

A

A

I

Q

T

S

I

I

L

L

S

R

D

T

V

A

G

G

L

T

D

A

L

L

G

G

R

L

G

G

I

V

S

V

I

N

L

I

I

L

Q

H

L

T

L

M

N

N

P

P

D

S

L

L

I

V

I

I

V

L

G

S

G

G

S

V

V

L

A

A

E

S

A

H

Q

Y

Q

I

Y

H

L

I

I

V

T

K

P

D

I

V

-

I

-

R

Q

Q

A

A

L

L

binding zinc ion: H140 (= H251), C150 (= C262), C152 (= C264), C157 (= C269)

4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
28% identity, 54% coverage: 156:378/412 of query aligns to 68:287/311 of 4db3A

query
sites
4db3A

I

I

G

G

M

L

S

G

M

L

P

P

G

G

L

M

V

E

D

D

-

A

-

D

-

A

S

T

V

V

N

L

G

T

V

V

N

N

H

V

T

P

Y

A

L

A

K

K

F

-

G

-

K

G

K

K

S

P

L

L

V

R

E

A

N

D

F

L

E

E

A

A

R

K

F

I

D

G

R

R

K

S

V

V

F

K

I

I

E

E

N

N

D

D

A

A

R

N

A

C

M

F

T

A

L

L

A

S

E

E

F

A

K

W

F

D

S

E

Q

E

D

L

Q

Q

K

D

Y

A

N

P

N

S

V

V

L

M

G

G

I

L

F

I

V

L

G

G

W

T

G

G

I

F

G

G

L

G

G

G

I

L

I

I

I

Y

D

E

G

G

K

K

L

V

Y

F

R

S

G

G

G

R

A

N

G

N

F

V

A

A

G

G

E

E

F

L

S

G

H
|
H

-

M

-

R

-

L

-

P

-

L

S

D

P

A

I

W

F

F

E

H

-

L

-

G

-

D

-

N

S

A

R

P

E

L

I

L

S

G

C
|
C

T

G

C
|
C

G

G

K

K

G

G

C
|
C

L

L

E

D

A

S

V

Y

A

L

S

S

G

G

T

R

A

G

M

F

V

-

R

-

M

-

A

-

E

-

A

-

I

-

E

-

K

-

D

-

S

-

D

E

S

L

I

L

L

Y

S

A

R

H

M

Y

A

Y

R

G

E

E

R

E

G

K

E

K

G

A

I

I

D

D

P

-

S

-

L

-

I

I

V

I

D

K

A

A

A

N

L

A

A

A

G

G

D

D

Q

E

R

K

A

A

I

A

T

E

I

H

L

V

S

E

D

R

V

F

G

M

L

E

D

L

L

L

G

A

R

I

G

C

I

F

S

G

I

N

L

I

I

F

Q

T

L

A

L

N

N

D

P

P

D

H

L

V

I

V

I

A

V

L

G

G

S

G

V

L

A

S

E

N

A

F

Q

E

Q

L

-

I

Y

Y

L

E

I

E

T

M

P

P

I

K

Q

R

Q

V

A

P

L

K

N

Y

I

L

F

L

S

S

M

V

A

A

K

K

S

C

binding zinc ion: H165 (= H251), C185 (= C262), C187 (= C264), C192 (= C269)

6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
32% identity, 35% coverage: 191:334/412 of query aligns to 96:227/269 of 6jdcA

query
sites
6jdcA

D

D

R

K

K

P

V

I

F

G

I

L

E

L

N

N

D

D

A

A

R

Q

A

A

M

A

T

T

L

Y

A

A

E

E

F

Y

K

Q

F

L

S

Q

Q

N

D

F

Q

E

K

Q

Y

V

N

S

N

N

V

F

L

V

G

F

I

I

F

T

V

V

G

S

W

T

G

G

I

V

G

G

L

G

G

G

I

I

I

V

I

L

D

N

G

Q

K

I

L

L

Y

Q

R

T

G

G

G

S

A

R

G

G

F

I

A

A

G

G

E

H

F

I

S

G

H
|
H

S

T

P

-

I

L

F

A

E

D

S

P

R

N

E

G

I

A

S

I

C
|
C

T

G

C
|
C

G

G

K

R

G

G

C
|
C

L

V

E

E

A

A

V

I

A

A

S

S

G

G

T

R

A

A

M

I

-

E

-

A

V

V

R

S

M

S

A

A

E

T

E

A

A

L

I

V

E

E

K

R

D

S

S

A

D

K

S

A

I

I

L

-

S

-

R

-

M

-

A

-

R

-

E

-

R

-

G

-

E

-

G

-

I

-

D

-

P

A

S

N

L

L

I

I

V

A

D

D

A

L

A

V

L

I

A

S

G

L

D

D

Q

I

R

Q

A

K

I

I

T

A

I

I

L

G

S

G

D

S

V

V

G

G

L

L

D

A

L

E

G

G

binding zinc ion: H156 (= H251), C166 (= C262), C168 (= C264), C173 (= C269)

6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
26% identity, 54% coverage: 182:404/412 of query aligns to 87:288/293 of 6jdoA

query
sites
6jdoA

L

L

V

K

E

E

N

S

F

I

E

A

A

R

R

H

F

T

D

D

R

K

K

P

V

I

F

G

I

L

E

L

N

N

D

D

A

V

R

Q

A

A

M

A

T

A

L

C

A

A

E

E

F

Y

K

K

F

D

S

E

Q

D

D

K

Q

N

K

A

Y

V

N

Q

N

N

V

F

L

V

G

F

I

I

F

T

V

V

G
x
S

W
x
T

G

G

I

V

G

G

L

G

G

G

I

I

I

L

D

E

G

R

K

R

L

L

Y

L

R

T

G

E

G

P

A

N

G

G

F

V

A

A

G

G

E

H

F

I

S

G

H
|
H

S

T

P

-

I

L

F

A

E

D

S

P

R

N

E

G

I

P

S

V

C
|
C

T

G

C
|
C

G

G

K
x
R

K

V

G

G

C

C

L

V

E

E

A

A

V

V

A

A

S

A

G
|
G

T

R

A

A

M

I

V

-

R

-

M

-

A

-

E

-

E

E

A

A

I

V

E

S

K

S

D

Q

S

W

D

N

S

P

I

P

L

C

S

T

R

-

M

-

A

-

R

-

E

-

R

-

G

-

E

-

G

-

I

-

D

-

P
|
P

S

K

L

Q

I

A

V
x
F

D

E

A

L

A

F

L

R

A

K

G

N

D

D

Q

E

R

K

A

A

I

T

T

A

I

L

L

I

S

Q

D

R

V

S

G

A

L

S

D

A

L

I

G

A

R

N

G

L

I

I

S

A

I

D

L

L

I

V

Q

I

L

G

L

L

N

D

P

V

D

Q

L

K

I

V

V

V

G

G

S
|
S

V

V

A

G

E

L

A

A

Q

E

Q

G

Y

Y

L

L

I

P

T

L

P

-

I

V

Q

K

Q

Q

A

Y

L

L

N

N

I

T

F

M

S

P

M

-

A

-

K

-

S

H

R

F

E

Y

K

H

S

C

E

T

L

V

T

E

L

Q

Y

A

K

R

L

H

G

G

K

Q

E

D

V

A

G

G

L

L

G

G

G

A

V

A

A

W

V

W

V

V

I

A

E

D

binding phosphoaminophosphonic acid-adenylate ester: S130 (≠ G225), T131 (≠ W226), G180 (= G276), P196 (= P308), F200 (≠ V312), S242 (= S354)
binding calcium ion: H156 (= H251), C166 (= C262), C168 (= C264), R170 (≠ K266)

6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
26% identity, 54% coverage: 182:404/412 of query aligns to 87:288/293 of 6jdhA

query
sites
6jdhA

L

L

V

K

E

E

N

S

F

I

E

A

A

R

R

H

F

T

D

D

R

K

K

P

V

I

F

G

I

L

E

L

N

N

D

D

A

V

R

Q

A

A

M

A

T

A

L

C

A

A

E

E

F

Y

K

K

F

D

S

E

Q

D

D

K

Q

N

K

A

Y

V

N

Q

N

N

V

F

L

V

G

F

I

I

F

T

V

V

G

S

W

T

G

G

I

V

G

G

L

G

G

G

I

I

I

L

D

E

G

R

K

R

L

L

Y

L

R

T

G

E

G

P

A

N

G

G

F

V

A

A

G

G

E

H

F

I

S

G

H
|
H

S

T

P

-

I

L

F

A

E

D

S

P

R

N

E

G

I

P

S

V

C
|
C

T

G

C
|
C

G

G

K

R

K

V

G

G

C
|
C

L

V

E

E

A

A

V

V

A

A

S

A

G

G

T

R

A

A

M

I

V

-

R

-

M

-

A

-

E

-

E

E

A

A

I

V

E

S

K

S

D

Q

S

W

D

N

S

P

I

P

L

C

S

T

R

-

M

-

A

-

R

-

E

-

R

-

G

-

E

-

G

-

I

-

D

-

P

P

S

K

L

Q

I

A

V

F

D

E

A

L

A

F

L

R

A

K

G

N

D

D

Q

E

R

K

A

A

I

T

T

A

I

L

L

I

S

Q

D

R

V

S

G

A

L

S

D

A

L

I

G

A

R

N

G

L

I

I

S

A

I

D

L

L

I

V

Q

I

L

G

L

L

N

D

P

V

D

Q

L

K

I

V

V

V

G

G

S

S

V

V

A

G

E

L

A

A

Q

E

Q

G

Y

Y

L

L

I

P

T

L

P

-

I

V

Q

K

Q

Q

A

Y

L

L

N

N

I

T

F

M

S

P

M

-

A

-

K

-

S

H

R

F

E

Y

K

H

S

C

E

T

L

V

T

E

L

Q

Y

A

K

R

L

H

G

G

K

Q

E

D

V

A

G

G

L

L

G

G

G

A

V

A

A

W

V

W

V

V

I

A

E

D

binding zinc ion: H156 (= H251), C166 (= C262), C168 (= C264), C173 (= C269)

P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
27% identity, 39% coverage: 219:380/412 of query aligns to 134:285/309 of P32718

query
sites
P32718

V

V

L

L

G

A

I

A

F

Y

V

L

G

G

W

T

G

G

I

M

G

G

L
x
F

G

A

I

V

I

W

I

M

D

N

G

G

K

A

L

P

Y

W

R

T

G

G

G

A

A

H

G

G

F

V

A

A

G

G

E

E

F

L

S

G

H

H

S

I

P

P

I

L

F

G

E

D

S

M

R

T

E

Q

I

-

S

H

C

C

T

A

C

C

G

G

K

N

K

P

G

G

C

C

L

L

E

E

A

T

V

N

A

C

S

S

G

G

T

M

A

A

M

L

V

R

R

R

M

W

A

Y

E

E

E

Q

A

-

I

-

E

Q

K

P

D

R

S

N

D

Y

S

P

I

L

L

R

S

D

R

L

M

F

A

V

R

H

E

A

R

E

G

N

E

A

G

P

I

F

D

V

P

Q

S

S

L

L

I

L

V

E

D

N

A

A

L

-

A

-

G

-

D

-

Q

-

R

-

A

-

I

-

T

-

I

-

L

-

S

-

D

-

V

-

G

-

L

-

D

-

L

-

G

-

R

R

G

A

I

I

S

A

I

T

L

S

I

I

Q

N

L

L

L

F

N

D

P

P

D

D

L

A

I

V

I

I

V

L

G

G

S

G

-

V

-

M

-

D

-

M

-

P

-

A

-

F

-

P

-

R

-

E

-

T

-

L

V

V

A

A

E

M

A

T

Q

Q

Q

K

Y

Y

L

L

I

R

T

R

P

P

I

L

Q

P

Q

H

A

Q

L

V

N

V

I

R

F

F

S

I

M

A

A

A

K

S

S

S

R

S

E

D

F145 (≠ L230) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.

Sites not aligning to the query:

73 A→G: 60-fold increase in catalytic efficiency for glucose phosphorylation. 45-fold increase in D-glucose affinity. No change in catalytic efficiency for D-allose phosphorylation.

Query Sequence

>Echvi_3892 FitnessBrowser__Cola:Echvi_3892
MNLIDPKKSLDEKEGVVEIKNYLNKIKIIKNLYMNGSNTASEICNEVGISLPTVNSLLTD
LIKAGKLVKQGRAESQGGRKPDLYRLAQDSFYVLALDISKFVVRAAIYDSSNQAVTETGT
FKITLNNEKSTFDKIGDFMETYMQESGIPNEKIIAIGMSMPGLVDSVNGVNHTYLKFGKK
SLVENFEARFDRKVFIENDARAMTLAEFKFSQDQKYNNVLGIFVGWGIGLGIIIDGKLYR
GGAGFAGEFSHSPIFESREISCTCGKKGCLEAVASGTAMVRMAEEAIEKDSDSILSRMAR
ERGEGIDPSLIVDAALAGDQRAITILSDVGLDLGRGISILIQLLNPDLIIVGGSVAEAQQ
YLITPIQQALNIFSMAKSREKSELTLYKLGKEVGLLGGVAVVIENIFEDIIN

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