SitesBLAST

R52 (≠ D46) mutation to H: Shows increased expression and forms larger colonies.
H86 (≠ S79) mutation to R: Can be bound and inactivated by MtfA.
F136 (≠ I130) mutation to A: Decreases association with PtsG EIIB domain.
H247 (= H240) binding Zn(2+)
C257 (= C250) binding Zn(2+); mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
C259 (= C252) binding Zn(2+); mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
C264 (= C257) binding Zn(2+)
R306 (≠ E303) mutation to G: Forms dimers but not tetramers; when associated with G-310.
L310 (≠ V307) mutation to G: Forms dimers but not tetramers; when associated with G-306.

1z6rA Crystal structure of mlc from escherichia coli (see paper)
25% identity, 95% coverage: 7:384/399 of query aligns to 2:363/382 of 1z6rA

query
sites
1z6rA

L

I

K

K

Q

Q

I

T

N

N

K

A

L

G

L

A

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V

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Y

K

R

T

L

I

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D

D

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N

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S

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R

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E

E

A

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E

E

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L

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G

Y

-

G

-

K

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S

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H
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H

T

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C
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C

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C

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G

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C

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G

C

A

binding zinc ion: H223 (= H240), C233 (= C250), C235 (= C252), C240 (= C257)

3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
36% identity, 61% coverage: 143:384/399 of query aligns to 59:305/312 of 3vglA

query
sites
3vglA

I

V

G

G

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I

G

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G
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G

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x
D

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x
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G

A

G

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I

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G

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N

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L

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D

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D

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M

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I

I

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G

G

N

G

K
x
G

A
x
V

S

S

F

D

F
x
E

G

G

E

E

L

L

F

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L

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A

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A

E

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L

-

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G

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A

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L

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G

G

C

A

binding phosphoaminophosphonic acid-adenylate ester: G130 (= G214), T131 (≠ I215), G180 (≠ E264), G214 (≠ P294), S218 (≠ I298), G260 (≠ K340), V261 (≠ A341), E264 (≠ F344)
binding beta-D-glucopyranose: G65 (= G149), P78 (= P162), N103 (= N187), D104 (≠ E188), L133 (= L217), G134 (= G218), E153 (= E237), H156 (= H240), E175 (= E259)
binding zinc ion: H156 (= H240), C166 (= C250), C168 (= C252), C173 (= C257)

Sites not aligning to the query:

binding phosphoaminophosphonic acid-adenylate ester: 9, 11, 12

3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
36% identity, 61% coverage: 143:384/399 of query aligns to 59:305/312 of 3vgkB

query
sites
3vgkB

I

V

G

G

I

I

G

G

V

A

P

A

G

G

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Y

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V

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D

K

D

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G

A

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A

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P

N

N

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D

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W

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H

P

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L

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G

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N

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D

A

A

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N

A

A

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A

A

A

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F

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G

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L

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A

G

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I

I

D

G

N

N

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K

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L

F

R

R

R

G

G

A

R

A

F

G

G

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V

A

A

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A

E

E

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G

H
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H

T

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D

D

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D

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C
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C

S

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C
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C

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C
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C

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E

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A

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D

A

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E

E

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L

A

A

E

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W

M

A

G

G

I

A

G

G

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L

A

A

N

D

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L

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A

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S

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L

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F

N

D

P

P

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M

A

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F

I

I

I

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G

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G

K

G

A

V

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S

F

D

F

E

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G

E

E

L

L

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L

L

E

D

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P

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Q

R

R

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F

L

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I

A

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G

F

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R

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H

I

A

E

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V

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L

-

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S

A

K

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L

L

K

G

D

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K

A

A

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V

L

L

V

G

G

C

A

binding zinc ion: H156 (= H240), C166 (= C250), C168 (= C252), C173 (= C257)

2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
29% identity, 71% coverage: 79:361/399 of query aligns to 4:279/308 of 2yi1A

query
sites
2yi1A

S

S

I

A

I

L

G

A

I

V

D

D

L

L

G
|
G

V
x
G

D
x
T

Y
x
N

I

L

H
x
R

V

V

I

A

L

I

S

V

N

S

F

M

V

K

G

G

E

E

V

I

I

V

F

-

E

K

Y

Y

A

T

E

Q

M

F

K

N

M

P

G

K

E

T

D

Y

K

E

D

E

K

R

L

I

F

-

D

N

L

L

L

I

F

L

D

Q

L

M

I

C

E

V

K

E

A

A

I

A

D

A

R

E

A

A

P

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H

K

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L

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N

K

C

G

R

I

I

L

L

G

G

I

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G

G

I

I

G

S

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T

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x
G

G
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G

I
x
R

V

V

E

N

K

P

E

R

S

E

G

G

I

I

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V

L

L

I

H

A
x
S

P
x
T

N

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L
|
L

-

I

-

Q

K

E

W

W

K

N

N

S

V

V

H

D

L

L

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R

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S

Q

D

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T

F

L

N

H

L

L

P

P

V

V

Y

W

I

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D

D

N
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N

E
x
D

A

G

N
|
N

A

C

G

A

A

A

L

L

G

A

E

E

K

R

W

K

F

F

G

G

E

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G

G

K

K

G

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N

L

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L

S

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T

G
|
G

I
x
T

G
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G

L
x
I

G

G

A
x
G

G

G

I

I

I

H

D

Q

N

H

K

E

L

L

F

I

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H

G

G

A

S

G

F

F

C

A

A

G
x
A

E
|
E

V

L

G

G

H
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H

T

L

T

V

I

V

N

S

F

L

Q

D

D

G

D

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V

D

C
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C

S

S

C
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C

G

G

N

S

I

H

G

G

C
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C

L

I

E
|
E

N

A

F

Y

A

A

S

S

E
x
G

R

M

A

A

L

L

L

Q

S

R

V

E

I

A

K

K

L

L

V

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K

-

Q

-

G

-

V

H

E

D

D

E

R

D

Y

L

I

L

S

L

C

V

E

E

N

G

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M

H

S

E

A

I

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T

G

P

A

S
x
L

R

H

I

L

I

I

Q

Q

A

A

K

K

E

L

G

G

S

N

R

A

V

K

C

A

R

Q

M

S

A

I

I

L

L

R

E

T

V

A

A

G

E

T

K

A

M

L

G

G

I

L

G

G

V

V

A

V

N

N

L

I

V

L

N

H

I

T

F

M

N

N

P

P

E

S

M

L

V

V

I

I

I

L

G

-

N

-

K

-

A

S

S

G

F
x
V

F

L

G

A

E

S

L

H

F

Y

L

I

E

H

K

I

L

V

R

K

E

D

V

V

I

I

N

R

Q

Q

R

Q

S

A

F

L

binding adenosine-5'-diphosphate: G11 (= G86), T13 (≠ D88), N14 (≠ Y89), R16 (≠ H91), T140 (≠ I215), G189 (≠ E264), L216 (≠ S295), V261 (≠ F343)
binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (≠ V87), G71 (≠ P148), G72 (= G149), R73 (≠ I150), S84 (≠ A161), T85 (≠ P162), L87 (= L164), N112 (= N187), D113 (≠ E188), G139 (= G214), T140 (≠ I215), G141 (= G216), I142 (≠ L217), E162 (= E237), H165 (= H240), E184 (= E259)
binding calcium ion: N112 (= N187), N115 (= N190), G144 (≠ A219), A161 (≠ G236)
binding zinc ion: H165 (= H240), C175 (= C250), C177 (= C252), C182 (= C257)

2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
29% identity, 71% coverage: 79:361/399 of query aligns to 4:279/308 of 2yhyA

query
sites
2yhyA

S

S

I

A

I

L

G

A

I

V

D

D

L

L

G
|
G

V
x
G

D
x
T

Y
x
N

I

L

H
x
R

V

V

I

A

L

I

S

V

N

S

F

M

V

K

G

G

E

E

V

I

I

V

F

-

E

K

Y

Y

A

T

E

Q

M

F

K

N

M

P

G

K

E

T

D

Y

K

E

D

E

K

R

L

I

F

-

D

N

L

L

L

I

F

L

D

Q

L

M

I

C

E

V

K

E

A

A

I

A

D

A

R

E

A

A

P

V

H

K

T

L

P

N

K

C

G

R

I

I

L

L

G

G

I

V

G

G

I

I

G

S

V

T

P

G

G

G

I

R

V

V

E

N

K

P

E

R

S

E

G

G

I

I

V

V

L

L

I

H

A

S

P

T

N

K

L

L

-

I

-

Q

K

E

W

W

K

N

N

S

V

V

H

D

L

L

K

R

S

T

I

P

V

L

Q

S

Q

D

R

T

F

L

N

H

L

L

P

P

V

V

Y

W

I

V

D

D

N
|
N

E

D

A

G

N
|
N

A

C

G

A

A

A

L

L

G

A

E

E

K

R

W

K

F

F

G

G

E

Q

W

G

G

K

K

G

V

L

S

E

D

N

L

F

I

V

Y

T

L

L

S

I

V

T

G

G

I
x
T

G

G

L

I

G

G

A
x
G

G

G

I

I

I

H

D

Q

N

H

K

E

L

L

F

I

R

H

G

G

A

S

G

F

F

C

A

A

G
x
A

E

E

V

L

G

G

H
|
H

T

L

T

V

I

V

N

S

F

L

Q

D

D

G

D

P

V

D

C
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C

S

S

C
|
C

G

G

N

S

I

H

G

G

C
|
C

L

I

E

E

N

A

F

Y

A

A

S

S

E
x
G

R

M

A

A

L

L

L

Q

S

R

V

E

I

A

K

K

L

L

V

-

K

-

Q

-

G

-

V

H

E

D

D

E

R

D

Y

L

I

L

S

L

C

V

E

E

N

G

V

M

H

S

E

A

I

V

T

G

P

A

S
x
L

R

H

I

L

I

I

Q

Q

A

A

K

K

E

L

G

G

S

N

R

A

V

K

C

A

R

Q

M

S

A

I

I

L

L

R

E

T

V

A

A

G

E

T

K

A

M

L

G

G

I

L

G

G

V

V

A

V

N

N

L

I

V

L

N

H

I

T

F

M

N

N

P

P

E

S

M

L

V

V

I

I

I

L

G

-

N

-

K

-

A

S

S

G

F
x
V

F

L

G

A

E

S

L

H

F

Y

L

I

E

H

K

I

L

V

R

K

E

D

V

V

I

I

N

R

Q

Q

R

Q

S

A

F

L

binding adenosine-5'-diphosphate: G11 (= G86), G12 (≠ V87), T13 (≠ D88), N14 (≠ Y89), R16 (≠ H91), T140 (≠ I215), G189 (≠ E264), L216 (≠ S295), V261 (≠ F343)
binding calcium ion: N112 (= N187), N115 (= N190), G144 (≠ A219), A161 (≠ G236)
binding zinc ion: H165 (= H240), C175 (= C250), C177 (= C252), C182 (= C257)

2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
29% identity, 71% coverage: 79:361/399 of query aligns to 4:280/309 of 2yhwA

query
sites
2yhwA

S

S

I

A

I

L

G

A

I

V

D

D

L

L

G

G

V

G

D

T

Y

N

I

L

H

R

V

V

I

A

L

I

S

V

N

S

F

M

V

K

G

G

E

E

V

I

I

V

F

-

E

K

Y

Y

A

T

E

Q

M

F

K

N

M

P

G

K

E

T

D

Y

K

E

D

E

K

R

L

I

F

-

D

N

L

L

L

I

F

L

D

Q

L

M

I

C

E

V

K

E

A

A

I

A

D

A

R

E

A

A

P

V

H

K

T

L

P

N

K

C

G

R

I

I

L

L

G

G

I

V

G

G

I

I

G

S

V

T

P

G

G

G

I

R

V

V

E

N

K

P

E

R

S

E

G

G

I

I

V

V

L

L

I

H

A

S

P

T

N

K

L

L

-

I

-

Q

K

E

W

W

K

N

N

S

V

V

H

D

L

L

K

R

S

T

I

P

V

L

Q

S

Q

D

R

T

F

L

N

H

L

L

P

P

V

V

Y

W

I

V

D

D

N
|
N

E

D

A

G

N
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N

A

C

G

A

A

A

L

L

G

A

E

E

K

R

W

K

F

F

G

G

E

Q

W

G

G

K

K

G

V

L

S

E

D

N

L

F

I

V

Y

T

L

L

S

I

V

T

G

G

I

T

G

G

L

I

G

G

A
x
G

G

G

I

I

I

H

D

Q

N

H

K

E

L

L

F

I

R

H

G

G

A

S

G

F

F

C

A

A

G
x
A

E

E

V

L

G

G

H
|
H

T

L

T

V

I

V

N

S

F

L

Q

N

D

G

D

P

V

D

C
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C

S

S

C
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C

G

G

N

S

I

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G

G

C
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C

L

I

E

E

N

A

F

Y

A

A

S

S

E

G

R

M

A

A

L

L

L

Q

S

R

V

E

I

A

K

K

L

L

V

H

K

D

Q

E

G

D

-

L

V

V

E

E

D

G

R

M

Y

S

I

V

S

A

C

V

E

G

N

A

V

L

H

H

E

-

I

-

T

-

P

-

S

-

R

-

I

L

I

I

Q

Q

A

A

K

K

E

L

G

G

S

N

R

A

V

K

C

A

R

Q

M

S

A

I

I

L

L

R

E

T

V

A

A

G

E

T

K

A

M

L

G

G

I

L

G

G

V

V

A

V

N

N

L

I

V

L

N

H

I

T

F

M

N

N

P

P

E

S

M

L

V

V

I

I

I

L

G

-

N

-

K

-

A

S

S

G

F

V

F

L

G

A

E

S

L

H

F

Y

L

I

E

H

K

I

L

V

R

K

E

D

V

V

I

I

N

R

Q

Q

R

Q

S

A

F

L

binding calcium ion: N112 (= N187), N115 (= N190), G144 (≠ A219), A161 (≠ G236)
binding zinc ion: H165 (= H240), C175 (= C250), C177 (= C252), C182 (= C257)

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 26 papers)
29% identity, 74% coverage: 68:361/399 of query aligns to 391:688/722 of Q9Y223

query
sites
Q9Y223

P

P

V

V

L

K

L

E

Q

N

V

I

N

S

K

Q

D

D

V

I

G

D

S

H

I

I

I

L

-

E

-

T

-

L

-

S

-

A

-

L

G

A

I

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D
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D

L

L

G

G

V
x
G

D
x
T

Y
x
N

I

L

H
x
R

V
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V

I
x
A

L
x
I

S
x
V

N
x
S

F
x
M

V
x
K

G
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G

E
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E

V
x
I

I
x
V

F

-

E
x
K

Y
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Y

A
x
T

E
x
Q

M
x
F

K
x
N

M
x
P

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x
K

E
x
T

D
x
Y

K
x
E

D
x
E

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x
R

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x
I

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x
N

L
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L

L
x
I

F
x
L

D
x
Q

L
x
M

I
x
C

E
x
V

K
x
E

A
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A

I
x
A

D
x
A

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x
E

A
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A

P
x
V

H
x
K

T
x
L

P
x
N

K
x
C

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x
R

I
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I

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L

G
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G

I
x
V

G
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G

I
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I

G
x
S

V
x
T

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x
G

G
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G

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x
R

V
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V

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x
N

K
x
P

E
x
R

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x
E

G
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G

I
|
I

V
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V

L
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L

I
x
H

A
x
S

P
x
T

N
x
K

L
|
L

-
x
I

-
x
Q

K
x
E

W
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W

K
x
N

N
x
S

V
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V

H
x
D

L
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L

K
x
R

S
x
T

I
x
P

V
x
L

Q
x
S

Q
x
D

R
x
T

F
x
L

N
x
H

L
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L

P
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P

V
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V

Y
x
W

I
x
V

D
|
D

N
|
N

E
x
D

A
x
G

N
|
N

A
x
C

G
x
A

A
|
A

L
|
L

G
x
A

E
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E

K
x
R

W
x
K

F
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F

G
|
G

E
x
Q

W
x
G

G
x
K

K
x
G

V
x
L

S
x
E

D
x
N

L
x
F

I
x
V

Y
x
T

L
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L

S
x
I

V
x
T

G
|
G

I
x
T

G
|
G

L
x
I

G
|
G

A
x
G

G
|
G

I
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I

I
x
H

D
x
Q

N
x
H

K
x
E

L
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L

F
x
I

R
x
H

G
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G

A
x
S

G
x
F

F
x
C

A
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A

G
x
A

E
|
E

V
x
L

G
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G

H
|
H

T
x
L

T
x
V

I
x
V

N
x
S

F
x
L

Q
x
D

D
x
G

D
x
P

V
x
D

C
|
C

S
|
S

C
|
C

G
|
G

N
x
S

I
x
H

G
|
G

C
|
C

L
x
I

E
|
E

N
x
A

F
x
Y

A
|
A

S
|
S

E
x
G

R
x
M

A
|
A

L
|
L

L
x
Q

S
x
R

V
x
E

I
x
A

K
|
K

L
|
L

V
x
H

K
x
D

Q
x
E

G
x
D

-
x
L

V
|
V

E
|
E

D
x
G

R

-

Y

-

I
x
M

S
|
S

C
x
V

E
x
P

N
x
K

V
x
D

H
x
E

E
x
A

I
x
V

T
x
G

P
x
A

S
x
L

R
x
H

I
x
L

I
|
I

Q
|
Q

A
|
A

K
|
K

E
x
L

G
|
G

S
x
N

R
x
A

V
x
K

C
x
A

R
x
Q

M
x
S

A
x
I

I
x
L

L
x
R

E
x
T

V
x
A

A
x
G

E
x
T

K
x
A

M
x
L

G
|
G

I
x
L

G
|
G

V
|
V

A
x
V

N
|
N

L
x
I

V
x
L

N
x
H

I
x
T

F
x
M

N
|
N

P
|
P

E
x
S

M
x
L

V
|
V

I
|
I

I
x
L

G

-

N

-

K

-

A
x
S

S
x
G

F
x
V

F
x
L

G
x
A

E
x
S

L
x
H

F
x
Y

L
x
I

E
x
H

K
x
I

L
x
V

R
x
K

E
x
D

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V

I
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I

N
x
R

Q
|
Q

R
x
Q

S
x
A

F
x
L

D413 (= D84) binding Mg(2+); to Y: in THC12; likely pathogenic; dbSNP:rs1280775456
G416 (≠ V87) binding an N-acyl-D-mannosamine 6-phosphate
T417 (≠ D88) binding ADP; to M: in THC12; likely pathogenic; dbSNP:rs1554659711
N418 (≠ Y89) binding ADP
R420 (≠ H91) binding ADP; to Q: in THC12; likely pathogenic; dbSNP:rs780092539
I472 (= I145) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity corresponding to less than 10% of wild-type activity
G475 (≠ P148) to F: in THC12; likely pathogenic; requires 2 nucleotide substitutions
G476 (= G149) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
R477 (≠ I150) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
V485 (= V158) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells; requires 2 nucleotide substitutions
L486 (= L159) to P: in THC12; uncertain significance; dbSNP:rs774867424
T489 (≠ P162) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
N516 (= N187) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
D517 (≠ E188) active site; binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; mutation D->A,N: Loss of N-acylmannosamine kinase activity. Decreased affinity for N-acyl-D-mannosamine. No effect on structure.
N519 (= N190) to S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910
A524 (≠ G195) 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 (= F199) to C: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986
T544 (≠ I215) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells
G545 (= G216) binding an N-acyl-D-mannosamine 6-phosphate
C563 (≠ F234) to Y: in THC12; likely pathogenic; results in severely decreased cell surface sialylation
E566 (= E237) binding an N-acyl-D-mannosamine
H569 (= H240) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
V572 (≠ I243) to L: in NM and THC12; likely pathogenic; mildly decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity corresponding to less than 10% of wild-type activity; does not affect homohexamers formation; dbSNP:rs121908632
G576 (≠ D247) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
C579 (= C250) binding Zn(2+)
C581 (= C252) binding Zn(2+)
C586 (= C257) binding Zn(2+)
I587 (≠ L258) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603
E588 (= E259) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
A630 (= A300) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
A631 (= A301) to V: in NM; does not affect homohexamers formation; dbSNP:rs62541771

Sites not aligning to the query:

13 C → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; no effect on N-acylmannosamine kinase activity; dbSNP:rs1209266607
19 binding UDP
23 binding UDP
113 binding UDP
132 H → Q: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; impaired homohexamers formation
157 H → Y: in THC12; likely pathogenic
176 D → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase 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; impaired homohexamers formation; dbSNP:rs539332585
200 I → F: in NM; uncertain significance; dbSNP:rs369328625
206 G → S: in NM; moderate phenotype with unusual involvement of quadriceps; dbSNP:rs766266918
220 binding UDP
253 binding UDP
259 binding CMP-N-acetyl-beta-neuraminate
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 CMP-N-acetyl-beta-neuraminate
280 binding CMP-N-acetyl-beta-neuraminate
281 binding CMP-N-acetyl-beta-neuraminate
282 binding UDP
301 binding UDP
302 binding UDP
303 C → V: in NM; requires 2 nucleotide substitutions; dbSNP:rs121908633
307 binding UDP
321 binding UDP
331 V → A: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation
378 D → Y: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; impaired homohexamers formation; dbSNP:rs199877522
420:722 natural variant: Missing (in THC12; likely pathogenic)
704 P → R: in THC12; likely pathogenic; the orthologous mutation in mouse embryos results in cerebrospinal hemorrhages and defective angiogenesis; results in loss of cell surface sialylation
708 G → S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; severely decreased N-acylmannosamine kinase activity; dbSNP:rs1554657922
712 M → T: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs28937594

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, 74% coverage: 68:361/399 of query aligns to 391:688/722 of O35826

query
sites
O35826

P

P

V

V

L

K

L

E

Q

N

V

I

N

S

K

Q

D

D

V

I

G

D

S

H

I

I

I

L

-

E

-
x
T

-
x
L

-
x
S

-
x
A

-
x
L

G
x
A

I
x
V

D
|
D

L
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L

G
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G

V
x
G

D
x
T

Y
x
N

I
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L

H
x
R

V
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V

I
x
A

L
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S
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V

N
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S

F
x
M

V
x
K

G
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G

E
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E

V
x
I

I
x
V

F

-

E
x
K

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Y

A
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E
x
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F

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M
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G
x
K

E
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D
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L

L
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A

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A

P
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-
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S

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x
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L

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E

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S

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G

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-

A
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S
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E
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L

D413 (= D84) 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 (≠ H91) 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

Q91WG8 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 Mus musculus (Mouse) (see paper)
28% identity, 74% coverage: 68:361/399 of query aligns to 391:688/722 of Q91WG8

query
sites
Q91WG8

P

P

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D

N

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M

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F

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x
C

A

A

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A

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M

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R

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A

A

G

E

T

K

A

M

L

G

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L

G

G

V

V

A

V

N

N

L

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H

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M

N

N

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M

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N

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-

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L

C563 (≠ F234) mutation to Y: Loss-of-function mutant resulting in impaired sialic acid biosynthesis.

Sites not aligning to the query:

704 P→R: Homozygous embryos exhibit cerebrospinal hemorrhages and defective angiogenesis in the diencephalon at 11 dpc, and become non-viable between 11.5 and 12.5 dpc. Loss-of-function mutant resulting in impaired sialic acid biosynthesis.

7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
29% identity, 53% coverage: 143:352/399 of query aligns to 61:267/303 of 7p9lAAA

query
sites
7p9lAAA

I

V

G

G

I

I

G

G

V

I

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P

G
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G

I

I

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A

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G

G

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L

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A
x
S

P

-

N

N

L

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W

A

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N

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H

-

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R

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I

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N
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N

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x
D

A

A

N

N

A

C

G

F

A

A

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L

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E

E

K

A

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W

F

D

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E

D

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D

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G

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x
T

G
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G

L
x
V

G
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G

A

G

G

G

I

L

I

I

I

F

D

N

N

G

K

K

L

V

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H

R

S

G

G

A

R

A

A

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N

F

I

A

A

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E
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E

V

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G

G

H
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H

T

T

T

R

I

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N

P

F

Y

Q

D

D

A

-

L

-

K

-

L

-

G

-

M

-

E

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N

-

A

-

P

-

I

D

F

V

P

C
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C

S

G

C
|
C

G

K

N

N

I

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G

G

C
|
C

L

I

E
x
D

N

N

F

Y

A

L

S

S

E

G

R

R

A

G

L

F

L

-

S

-

V

-

I

-

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L

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K

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E

G

Q

V

L

E

Y

D

D

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Y

Y

I

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S

C

-

E

-

N

-

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-

H

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I

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A

S

P

R
x
E

I

I

Q

A

A
x
H

A

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K

E

E

Q

G

G

S

E

R

R

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R

C

A

R

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A

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E

E

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V

F

A

M

E

E

K

L

M

L

G

A

I

I

G

C

V

L

A

A

N

N

L

I

V

F

N

T

I

C

F

L

N

D

P

P

E

H

M

V

V

V

I

V

I

L

G

G

N

G

K

G

A

L

S

S

F

N

F

F

G

-

E

E

L

L

F

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Y

E

Q

K

E

L

L

binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P148), G67 (= G149), S79 (≠ A161), N105 (= N187), D106 (≠ E188), G132 (= G214), T133 (≠ I215), G134 (= G216), V135 (≠ L217), G136 (= G218), E155 (= E237), H158 (= H240), D188 (≠ E259)
binding zinc ion: H158 (= H240), C179 (= C250), C181 (= C252), C186 (= C257), E212 (≠ R296), H216 (≠ A300)

7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
29% identity, 53% coverage: 143:352/399 of query aligns to 62:268/304 of 7p9pAAA

query
sites
7p9pAAA

I

V

G

G

I

I

G

G

V

I

P

P

G

G

I

I

V

A

E

D

K

V

E

E

S

T

G

G

I

K

V

L

L

L

I

T

A

S

P

-

N

N

L

I

K

P

W

A

K

A

N

M

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G

H

H

-

T

L

L

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Q

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R

I

D

V

L

Q

E

R

R

F

L

N

Q

L

R

P

P

V

V

Y

K

I

I

D

E

N

N

E

D

A

A

N

N

A

C

G

F

A

A

L

L

G

S

E

E

K

A

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W

F

D

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E

E

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D

S

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|
G

I
x
T

G

G

L

V

G

G

A

G

G

G

I

L

I

I

I

F

D

N

N

G

K

K

L

V

F

H

R

S

G

G

A

R

A

A

G

N

F

I

A

A

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G

E

E

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I

G

G

H
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H

T

T

T

R

I

L

N

P

F

Y

Q

D

D

A

-

L

-

K

-

L

-

G

-

M

-

E

-

N

-

A

-

P

-

I

D

F

V

P

C
|
C

S

G

C
|
C

G

K

N

N

I

S

G

G

C
|
C

L

I

E

D

N

N

F

Y

A

L

S

S

E
x
G

R

R

A

G

L

F

L

-

S

-

V

-

I

-

K

-

L

-

V

-

K

-

Q
x
E

G

Q

V

L

E

Y

D

D

R

H

Y

Y

I

F

S

S

C

-

E

-

N

-

V

-

H

E

E

K

I

L

T

S

P
x
A

S

P

R
x
E

I

I

Q

A

A
x
H

A

Y

K

E

E

Q

G

G

S

E

R

R

V

R

C

A

R

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M

Q

A

H

I

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L

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E

R

V

F

A

M

E

E

K

L

M

L

G

A

I

I

G

C

V

L

A

A

N

N

L

I

V

F

N

T

I

C

F

L

N

D

P

P

E

H

M

V

V

V

I

V

I

L

G

G

N
x
G

K
x
G

A

L

S

S

F
x
N

F

F

G

-

E

E

L

L

F

I

L

Y

E

Q

K

E

L

L

binding phosphoaminophosphonic acid-adenylate ester: G133 (= G214), T134 (≠ I215), G194 (≠ E264), E198 (≠ Q277), A211 (≠ P294), G256 (≠ N339), G257 (≠ K340), N260 (≠ F343)
binding zinc ion: H159 (= H240), C180 (= C250), C182 (= C252), C187 (= C257), E213 (≠ R296), H217 (≠ A300)

Sites not aligning to the query:

binding phosphoaminophosphonic acid-adenylate ester: 11, 12, 13

7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
29% identity, 53% coverage: 143:352/399 of query aligns to 64:270/306 of 7p7wBBB

query
sites
7p7wBBB

I

V

G

G

I

I

G

G

V

I

P

P

G

G

I

I

V

A

E

D

K

V

E

E

S

T

G

G

I

K

V

L

L

L

I

T

A

S

P

-

N

N

L

I

K

P

W

A

K

A

N

M

V

G

H

H

-

T

L

L

K

Q

S

R

I

D

V

L

Q

E

R

R

F

L

N

Q

L

R

P

P

V

V

Y

K

I

I

D

E

N

N

E

D

A

A

N

N

A

C

G

F

A

A

L

L

G

S

E

E

K

A

W

W

F

D

G

E

E

D

W

L

G

R

K

G

V

E

S

P

D

S

L

V

I

L

Y

G

L

L

S

I

V

L

G
|
G

I
x
T

G

G

L

V

G

G

A

G

G

G

I

L

I

I

I

F

D

N

N

G

K

K

L

V

F

H

R

S

G

G

A

R

A

A

G

N

F

I

A

A

G

G

E

E

V

I

G

G

H
|
H

T

T

T

R

I

L

N

P

F

Y

Q

D

D

A

-

L

-

K

-

L

-

G

-

M

-

E

-

N

-

A

-

P

-

I

D

F

V

P

C
|
C

S

G

C
|
C

G

K

N

N

I

S

G

G

C
|
C

L

I

E

D

N

N

F

Y

A

L

S

S

E
x
G

R

R

A

G

L

F

L

-

S

-

V

-

I

-

K

-

L

-

V

-

K

-

Q
x
E

G

Q

V

L

E

Y

D

D

R

H

Y

Y

I

F

S

S

C

-

E

-

N

-

V

-

H

E

E

K

I

L

T

S

P

A

S

P

R

E

I

I

Q

A

A

H

A

Y

K

E

E

Q

G

G

S

E

R

R

V

R

C

A

R

V

M

Q

A

H

I

V

L

E

E

R

V

F

A

M

E

E

K

L

M

L

G

A

I

I

G

C

V

L

A

A

N

N

L

I

V

F

N

T

I

C

F

L

N

D

P

P

E

H

M

V

V

V

I

V

I

L

G

G

N
x
G

K
x
G

A

L

S

S

F
x
N

F

F

G

-

E

E

L

L

F

I

L

Y

E

Q

K

E

L

L

binding adenosine-5'-diphosphate: G135 (= G214), T136 (≠ I215), G196 (≠ E264), E200 (≠ Q277), G258 (≠ N339), G259 (≠ K340), N262 (≠ F343)
binding zinc ion: H161 (= H240), C182 (= C250), C184 (= C252), C189 (= C257)

3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
26% identity, 71% coverage: 79:361/399 of query aligns to 3:259/288 of 3eo3A

query
sites
3eo3A

S

S

I

A

I

L

G

A

I

V

D

D

L

L

G

G

V

G

D

T

Y

N

I

L

H

R

V

V

I

A

L

I

S

V

N

S

F

M

V

K

G

G

E

E

V

I

I

V

F

-

E

K

Y

Y

A

T

E

Q

M

F

K

N

M

P

G

K

E

T

D

Y

K

E

D

E

K

R

L

I

F

-

D

N

L

L

L

I

F

L

D

Q

L

M

I

C

E

V

K

E

A

A

I

A

D

A

R

E

A

A

P

V

H

K

T

L

P

N

K

C

G

R

I

I

L

L

G

G

I

V

G

G

I

I

G

-

V

-

P

-

G

-

I

-

V

-

E

-

K

-

E

-

S

-

G

-

I

-

V

-

L

-

I

-

A

-

P

-

N

-

L

-

K

-

W

-

K

-

N

S

V

T

H

D

L

L

K

R

S

T

I

P

V

L

Q

S

Q

D

R

T

F

L

N

H

L

L

P

P

V

V

Y

W

I

V

D

D

N

N

E

D

A

G

N

N

A

C

G

A

A

A

L

L

G

A

E

E

K

R

W

K

F

F

G

G

E

Q

W

G

G

K

K

G

V

L

S

E

D

N

L

F

I

V

Y

T

L

L

S

I

V

T

G

G

I

T

G

G

L

I

G

G

A

G

G

G

I

I

I

H

D

Q

N

H

K

E

L

L

F

I

R

H

G

G

A

S

G

F

F

C

A

A

G

A

E

E

V

L

G

G

H
|
H

T

L

T

V

I

V

N

S

F

L

Q

D

D

G

D

P

V

D

C
|
C

S

S

C
|
C

G

G

N

S

I

H

G

G

C
|
C

L

I

E

E

N

A

F

Y

A

A

S

S

E

G

R

M

A

A

L

L

L

Q

S

R

V

E

I

A

K

K

L

L

V

H

K

D

Q

E

G

D

-

L

V

V

E

E

D

G

R

-

Y

-

I

M

S

S

C

V

E

P

N

K

V

D

H

E

E

A

I

V

T

G

P

A

S

L

R

H

I

L

I

I

Q

Q

A

A

K

K

E

L

G

G

S

N

R

A

V

K

C

A

R

Q

M

S

A

I

I

L

L

R

E

T

V

A

A

G

E

T

K

A

M

L

G

G

I

L

G

G

V

V

A

V

N

N

L

I

V

L

N

H

I

T

F

M

N

N

P

P

E

S

M

L

V

V

I

I

I

L

G

-

N

-

K

-

A

S

S

G

F

V

F

L

G

A

E

S

L

H

F

Y

L

I

E

H

K

I

L

V

R

K

E

D

V

V

I

I

N

R

Q

Q

R

Q

S

A

F

L

binding zinc ion: H140 (= H240), C150 (= C250), C152 (= C252), C157 (= C257)

Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
27% identity, 49% coverage: 142:338/399 of query aligns to 56:241/297 of Q93LQ8

query
sites
Q93LQ8

G

G

I

I

G

A

I

I

G

S

V

A

P

P

G

G

I

Y

V

I

E

D

K

P

E

H

S

S

G

G

I

L

V

I

L

T

I

M

A

G

P

G

N

A

L

I

K

R

-

R

W

F

K

D

N

N

V

F

H

A

L

M

K

K

S

S

I

W

V

L

Q

E

Q

T

R

R

F

T

N

G

L

L

P

P

V

V

Y

S

I

V

D

E

N

N

E
x
D

A

A

N

N

A

C

G

V

A

L

L

L

G

A

E

E

K

R

W

W

F

Q

G

G

E

K

W

A

G

A

K

E

V

M

S

A

D

N

L

F

I

L

Y

V

L

L

S

T

V

I

G

G

I

T

G
|
G

L

I

G
|
G

A

G

G

A

I

I

I

F

I

C

D

Q

N

H

K

Q

L

L

F

I

R

N

G

G

A

A

A

R

G

F

F

R

A

A

G

G

E

E

V

F

G

G

H

Y

T

M

T

L

I

T

N

D

F

-

Q

-

D

-

V

-

C

-

S

R

C

P

G

G

N

G

I

R

G

D

C

P

L

R

E

R

N

Y

F

S

A

M

S

N

E

E

R

N

A

C

L

T

L

L

S

R

V

V

I

L

K

R

K

H

L

R

V

Y

K

A

Q

Q

G

H

V

I

E

G

D

-

R

-

Y

-

I

-

S

-

C

-

E

A

N

P

V

L

H

D

E

S

I

V

T

T

P

G

S

E

R

L

I

I

I

F

Q

D

A

R

A

Y

K

D

E

A

G

G

S

D

R

P

V

V

C

C

R

Q

M

R

A

L

I

V

L

A

E

E

V

F

A

F

E

N

K

G

M

L

G

G

I

H

G

G

V

L

A

Y

N

N

L

L

V

V

N

H

I

I

F

F

N

D

P

P

E

Q

M

T

V

I

I

F

I

I

G

G

D103 (≠ E188) mutation to G: Loss of catalytic activity.
G131 (= G216) mutation to A: Loss of catalytic activity.
G133 (= G218) mutation to A: Loss of catalytic activity.

Sites not aligning to the query:

7 D→G: Loss of catalytic activity.
9 G→A: Loss of catalytic activity.

3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
31% identity, 54% coverage: 143:357/399 of query aligns to 61:266/298 of 3vovB

query
sites
3vovB

I

I

G

G

I

L

G

G

V

T

P

P

G

G

I

P

V

L

E

D

K

F

E

R

S

R

G

G

I

V

V

-

L

-

I

I

A

R

P

P

N

N

L

I

K

P

W

G

-

V

K

Q

N

D

V

F

H

P

L

I

K

R

S

R

I

I

V

L

Q

E

R

A

F

T

N

G

L

R

P

P

V

V

Y

F

I

L

D

E

N

N

E

D

A

A

N

N

A

A

G

A

A

A

L

L

G

A

E

E

K

H

W

H

F

L

G

G

E

A

W

A

G

Q

K

G

V

E

S

E

D

S

L

S

I

L

Y

Y

L

L

S

T

V

V

G

S

I

T

G

G

L

I

G

G

A

G

G

G

I

V

I

L

D

G

N

G

K

R

L

V

F

L

R

R

G

G

A

E

A

R

G

G

F

Q

A

G

G

G

E

E

V

L

G

G

H
|
H

T

L

T

T

I

L

N

L

F

P

Q

G

D

G

D

P

V

A

C
|
C

S

G

C
|
C

G

G

N

L

I

E

G

G

C
|
C

L

L

E

E

N

A

F

L

A

A

S

A

E

G

R

R

A

A

L

L

L

E

S

R

V

D

I

A

K

T

K

Y

L

A

V

F

K

Q

Q

R

G

P

V

V

E

D

D

T

R

R

Y

E

I

L

S

-

C

-

E

-

N

-

V

-

H

-

E

-

I

-

T

-

P

-

S

F

R

R

I

L

I

F

Q

Q

A

A

A

-

K

-

E

-

G

G

S

D

R

P

V

K

C

A

R

E

M

R

A

L

I

V

L

L

E

Q

V

A

A

A

E

R

K

Y

M

V

G

G

I

I

G

G

V

L

A

A

N

S

L

L

V

V

N

K

I

A

F

F

N

D

P

P

E

G

M

V

V

V

I

V

I

L

G

G

-

G

-

V

-

A

-

L

N

N

K

A

A

P

S

E

F

G

F

Y

G

W

E

E

L

A

F

L

L

L

E

E

K

A

L

Y

R

R

E

R

V

Y

I

L

N

Q

binding zinc ion: H157 (= H240), C167 (= C250), C169 (= C252), C174 (= C257)

Query Sequence

>WP_013430927.1 NCBI__GCF_000166775.1:WP_013430927.1
MGNHTLLKQINKLLVLKTILDNKIISRAKISRLVDLNKATVSNLTDELIKEGYIVEKGYG
KSKGGRRPVLLQVNKDVGSIIGIDLGVDYIHVILSNFVGEVIFEEYAEMKMGEDKDKLFD
LLFDLIEKAIDRAPHTPKGILGIGIGVPGIVEKESGIVLIAPNLKWKNVHLKSIVQQRFN
LPVYIDNEANAGALGEKWFGEWGKVSDLIYLSVGIGLGAGIIIDNKLFRGAAGFAGEVGH
TTINFQDDVCSCGNIGCLENFASERALLSVIKKLVKQGVEDRYISCENVHEITPSRIIQA
AKEGSRVCRMAILEVAEKMGIGVANLVNIFNPEMVIIGNKASFFGELFLEKLREVINQRS
FIAQFYNLKIEVSKLKDRAVVLGCIAMVISDMLSFPEYA

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