SitesBLAST

R52 (≠ A49) mutation to H: Shows increased expression and forms larger colonies.
H86 (≠ L83) mutation to R: Can be bound and inactivated by MtfA.
F136 (≠ V132) mutation to A: Decreases association with PtsG EIIB domain.
H247 (= H245) binding
C257 (= C255) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
C259 (= C257) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
C264 (= C262) binding
R306 (≠ D295) mutation to G: Forms dimers but not tetramers; when associated with G-310.
L310 (≠ V299) mutation to G: Forms dimers but not tetramers; when associated with G-306.

5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
26% identity, 84% coverage: 1:331/392 of query aligns to 2:336/396 of 5f7qE

query
sites
5f7qE

M

I

L

L

P

R

R
x
K

V

G

N

N

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x
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A

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x
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G

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-

A

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x
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x
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G

binding zinc ion: H243 (= H245), C253 (= C255), C255 (= C257), C260 (= C262)
binding : K5 (≠ R4), K8 (≠ S7), K12 (≠ R11), N15 (= N14), T32 (≠ R31), S43 (≠ A42), T44 (= T43), T67 (≠ R67), G68 (≠ I68), G68 (≠ I68), G69 (= G69), G69 (= G69), R70 (= R70), R70 (= R70), R71 (≠ P71), A72 (≠ E72), K73 (≠ T73)

1z6rA Crystal structure of mlc from escherichia coli (see paper)
27% identity, 96% coverage: 10:386/392 of query aligns to 2:372/382 of 1z6rA

query
sites
1z6rA

I

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H

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C

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A

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N

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M

M

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A

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M

K

D

D

G

A

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Y

S

N

binding zinc ion: H223 (= H245), C233 (= C255), C235 (= C257), C240 (= C262)

5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
29% identity, 64% coverage: 82:331/392 of query aligns to 1:252/306 of 5f7rA

query
sites
5f7rA

G

G

L

F

L

V

V

V

G

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A

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R
x
K

L

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x
E

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D
x
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A

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A

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G

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A

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A

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E
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I

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H
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C

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C
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C

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G

C
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C

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E
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E

T

M

Y

Y

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A

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I

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A

N

Q

R

A

G

A

E

E

E

R

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G

K

R

E

A

A

L

Y

P

P

-

L

-

N

-

D

-

F

D

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L

F

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D

A

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A

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A

A

A

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A

S

A

A

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A

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G

D

D

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E

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M

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T

E

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E

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E

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A

M

G

G

S

E

H

Y

L

L

G

G

F

Y

A

G

L

I

S

R

H

N

L

I

V

I

N

N

L

T

A

F

N

N

P

P

G

E

L

K

V

V

V

I

L

I

G

V

G

G

binding alpha-D-glucopyranose: K7 (≠ R88), E10 (≠ P91), G70 (≠ A155), N110 (≠ D193), N110 (≠ D193), S134 (≠ T217), V135 (≠ G218), G138 (= G221), L139 (≠ V222), G140 (= G223), E159 (= E242), H162 (= H245), E181 (= E264)
binding zinc ion: H162 (= H245), C172 (= C255), C174 (= C257), C179 (= C262)

Sites not aligning to the query:

binding alpha-D-glucopyranose: 253, 293

2qm1B Crystal structure of glucokinase from enterococcus faecalis
31% identity, 76% coverage: 84:381/392 of query aligns to 8:320/325 of 2qm1B

query
sites
2qm1B

L

I

V

I

G

G

A

I

R

D

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L

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G

G

T

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T

I

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A

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E

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I

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S

-

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D

N

L

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A

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A

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H

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D

R

I

E

E

-

K

G

G

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V

L

G

A

A

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Y

N

N

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N

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A

A

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L

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G

A

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A

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D

D

N
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N

D

D

T

A

K
x
N

A

V

A

A

M

L

A

G

E

E

R

R

L

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G

G

A

A

C

G

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G

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D

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F

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G

G

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A

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G

G

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A

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A

A

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G

E

E

I

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G

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H
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H

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G

G

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C
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C

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C
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C

G

G

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K

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R

G

G

C
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C

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L

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E

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A

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G

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A

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G

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Q

A

A

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D

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D

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A

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E

-

F

A

A

R

E

D

K

G

G

D

D

P

H

V

F

V

A

R

L

T

M

L

V

E

D

E

R

A

V

G

C

S

F

H

Y

L

L

G

G

F

L

A

A

L

T

S

G

H

N

L

L

V

G

N

N

L

T

A

L

N

N

P

P

G

D

L

S

V

V

L

I

G

G

N

G

L

V

A

S

I

A

V

A

A

G

E

E

F

F

I

L

L

R

P

S

A

R

L

V

N

E

A

K

A

Y

L

F

G

Q

E

E

H

F

A

T

L

F

E

P

P

Q

L

V

R

R

R

N

D

S

L

T

R

K

L

I

L

K

V

L

S

A

P

E

L

L

G

G

P

N

D

E

A

A

V

G

P

V

M

I

G

G

G

A

I

A

A

S

L

L

A

A

M

L

binding magnesium ion: N116 (= N192), N119 (≠ K195), G148 (= G224)
binding zinc ion: H169 (= H245), C179 (= C255), C181 (= C257), C186 (= C262)

3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
33% identity, 66% coverage: 102:361/392 of query aligns to 15:277/312 of 3vglA

query
sites
3vglA

A

A

G

G

T

V

V

V

V

D

E

E

Q

E

S

G

Q

R

I

I

P

L

G

S

S

T

T

F

D

K

L

V

A

A

T

T

A

P

L

-

R

-

H

P

L

T

H

A

E

E

G

G

I

I

-

V

D

D

A

A

V

I

V

C

A

A

S

V

R

-

P

-

E

A

G

G

G

A

A

S

A

E

T

G

P

H

P

D

L

V

C

E

G

A

I

V

G

G

V

I

G

G

I

A

P

A

A
x
G

L

Y

M

V

D

D

-

D

R

K

E

R

G

A

R

T

L

V

V

L

L

F

A

A

P
|
P

N

N

L

I

G

D

W

W

R

R

D

H

T

E

P

P

I

L

R

K

P

D

L

K

L

V

E

E

E

Q

A

R

L

V

G

G

A

L

P

P

V

V

H

V

V

V

D

E

N
|
N

D
|
D

T

A

K

N

A

A

M

W

A

G

E

E

R

Y

L

R

F

F

G

G

A

A

C

G

R

Q

G

G

V

H

E

D

D

D

F

V

V

I

Y

C

L

I

T

T

G

L

H
x
G

S
x
T

G

G

V
x
L

G
|
G

G

G

L

I

F

I

G

G

G

N

R

K

L

L

Y

R

R

R

G

G

A

R

Q

F

G

G

F

V

A

A

G

A

E
|
E

I

F

G

G

H
|
H

L

I

T

R

I

V

V

V

P

P

G

D

G

G

R

L

A

L

C
|
C

G

G

C
|
C

G

G

K

S

R

Q

G

G

C
|
C

L

W

E
|
E

T

Q

Y

Y

V

A

S

S

E
x
G

T

R

S

A

I

L

L

V

A

R

Q

Y

A

A

A

K

E

Q

R

R

G

A

R

N

A

A

L

T

P

P

D

E

L

N

W

A

A

A

A

V

-

L

-

G

-

L

-

G

-

D

-

G

-

S

-

V

-

D

-

G

-

I

-

E

-
x
G

-

K

-

H

-

I

A
x
S

A

E

A

A

R

R

D

Q

G

G

D

D

P

P

V

V

V

A

R

V

T

D

L

S

L

F

E

R

E

E

A

L

G

A

S

R

H

W

L

A

G

G

F

A

A

G

L

L

S

A

H

D

L

L

V

A

N

S

L

L

A

F

N

D

P

P

G

S

L

A

V

F

V

I

L

V

G

G

N
x
G

L
x
V

A

S

I

D

V
x
E

A

G

E

E

F

L

I

V

L

-

P

-

A

-

L

-

N

-

A

-

L

-

G

-

E

-

H

-

A

-

L

L

E

D

P

P

L

I

R

R

R

K

D

S

L

F

R

R

binding phosphoaminophosphonic acid-adenylate ester: G130 (≠ H219), T131 (≠ S220), G180 (≠ E269), G214 (vs. gap), S218 (≠ A290), G260 (≠ N332), V261 (≠ L333), E264 (≠ V336)
binding beta-D-glucopyranose: G65 (≠ A155), P78 (= P167), N103 (= N192), D104 (= D193), L133 (≠ V222), G134 (= G223), E153 (= E242), H156 (= H245), E175 (= E264)
binding zinc ion: H156 (= H245), C166 (= C255), C168 (= C257), C173 (= C262)

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)
33% identity, 66% coverage: 102:361/392 of query aligns to 15:277/312 of 3vgkB

query
sites
3vgkB

A

A

G

G

T

V

V

V

V

D

E

E

Q

E

S

G

Q

R

I

I

P

L

G

S

S

T

T

F

D

K

L

V

A

A

T

T

A

P

L

-

R

-

H

P

L

T

H

A

E

E

G

G

I

I

-

V

D

D

A

A

V

I

V

C

A

A

S

V

R

-

P

-

E

A

G

G

G

A

A

S

A

E

T

G

P

H

P

D

L

V

C

E

G

A

I

V

G

G

V

I

G

G

I

A

P

A

A

G

L

Y

M

V

D

D

-

D

R

K

E

R

G

A

R

T

L

V

V

L

L

F

A

A

P

P

N

N

L

I

G

D

W

W

R

R

D

H

T

E

P

P

I

L

R

K

P

D

L

K

L

V

E

E

E

Q

A

R

L

V

G

G

A

L

P

P

V

V

H

V

V

V

D

E

N

N

D

D

T

A

K

N

A

A

M

W

A

G

E

E

R

Y

L

R

F

F

G

G

A

A

C

G

R

Q

G

G

V

H

E

D

D

D

F

V

V

I

Y

C

L

I

T

T

G

L

H

G

S

T

G

G

V

L

G

G

L

I

F

I

G

G

G

N

R

K

L

L

Y

R

R

R

G

G

A

R

Q

F

G

G

F

V

A

A

G

A

E

E

I

F

G

G

H
|
H

L

I

T

R

I

V

V

V

P

P

G

D

G

G

R

L

A

L

C
|
C

G

G

C
|
C

G

G

K

S

R

Q

G

G

C
|
C

L

W

E

E

T

Q

Y

Y

V

A

S

S

E

G

T

R

S

A

I

L

L

V

A

R

Q

Y

A

A

A

K

E

Q

R

R

G

A

R

N

A

A

L

T

P

P

D

E

L

N

W

A

A

A

A

V

-

L

-

G

-

L

-

G

-

D

-

G

-

S

-

V

-

D

-

G

-

I

-

E

-

G

-

K

-

H

-

I

A

S

A

E

A

A

R

R

D

Q

G

G

D

D

P

P

V

V

V

A

R

V

T

D

L

S

L

F

E

R

E

E

A

L

G

A

S

R

H

W

L

A

G

G

F

A

A

G

L

L

S

A

H

D

L

L

V

A

N

S

L

L

A

F

N

D

P

P

G

S

L

A

V

F

V

I

L

V

G

G

N

G

L

V

A

S

I

D

V

E

A

G

E

E

F

L

I

V

L

-

P

-

A

-

L

-

N

-

A

-

L

-

G

-

E

-

H

-

A

-

L

L

E

D

P

P

L

I

R

R

R

K

D

S

L

F

R

R

binding zinc ion: H156 (= H245), C166 (= C255), C168 (= C257), C173 (= C262)

3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
42% identity, 54% coverage: 149:358/392 of query aligns to 61:275/298 of 3vovB

query
sites
3vovB

I

I

G

G

V

L

G

G

I

T

P

P

A

G

L

P

M

L

D

D

R

F

E

R

G

-

R

R

L

G

V

V

L

I

A

R

P

P

N

N

L

I

-

P

G

G

W

V

R

Q

D

D

T

F

P

P

I

I

R

R

P

R

L

I

L

L

E

E

A

A

L

T

G

G

A

R

P

P

V

V

H

F

V

L

D

E

N

N

D

D

T

A

K

N

A

A

M

L

A

A

E

E

R

H

L

H

F

L

G

G

A

A

C

A

R

Q

G

G

V

E

E

E

D

S

F

S

V

L

Y

Y

L

L

T

T

G

V

H

S

S

T

G

G

V

I

G

G

L

V

F

V

F

L

G

G

R

R

L

V

Y

L

R

R

G

G

A

E

Q

R

G

G

F

Q

A

G

G

G

E

E

I

L

G

G

H
|
H

L

L

T

T

I

L

V

L

P

P

G

G

R

P

A

A

C
|
C

G

G

C
|
C

G

G

K

L

R

E

G

G

C
|
C

L

L

E

E

T

A

Y

L

V

A

S

A

E

G

T

R

S

A

I

L

L

E

A

R

Q

D

A

A

A

T

E

Y

R

A

G

F

R

Q

A

R

L

P

P

V

D

D

L

T

W

R

A

E

A

L

A

F

A

R

A

L

A

F

R

Q

D

A

G

G

D

D

P

P

V

K

V

A

R

E

T

R

L

L

L

V

E

L

E

Q

A

A

G

A

S

R

H

Y

L

V

G

G

F

I

A

G

L

L

S

A

H

S

L

L

V

V

N

K

L

A

A

F

N

D

P

P

G

G

L

V

V

V

L

L

G

G

N

G

L

V

A

A

I

L

V

N

A

A

-

P

-

E

-

G

-

Y

-

W

E

E

F

A

I

L

L

L

P

E

A

A

L

Y

N

R

A

R

A

Y

L

L

G

Q

E

G

H

W

A

E

L

A

E

P

P

P

L

L

R

R

binding zinc ion: H157 (= H245), C167 (= C255), C169 (= C257), C174 (= C262)

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)
31% identity, 62% coverage: 93:334/392 of query aligns to 418:672/722 of Q9Y223

query
sites
Q9Y223

T
x
N

I

L

R
|
R

I

V

V

A

S

I

T

V

T

S

L

M

A

K

G

G

T

E

V

I

V

V

E

K

Q

K

-

Y

S

T

Q

Q

I

F

P

N

G

P

S

K

T

T

D

-

L

-

A

-

T

-

A

-

L

-

R

-

H

-

L

Y

H

E

E

E

G

R

I

I

D

N

A

L

V

I

V

L

A

Q

A

M

S

C

R

V

P

E

E

A

G

A

A

E

A

A

T

V

P

K

P

L

L

N

C

C

G

R

I

I

-

L

G

G

V

V

G

G

I
|
I

P

S

A

T

-

G

-
x
G

-
x
R

L

V

M

N

D

P

R

R

E

E

G

G

R

I

L

V

V

L

L

H

A

S

P
x
T

N

K

L

L

-

I

-

Q

G

E

W

W

R

N

D

S

T

V

P

D

I

L

R

R

P

T

L

P

L

L

E

S

E

D

A

T

L

L

G

H

A

L

P

P

V

V

H

W

V

V

D

D

N
|
N

D
|
D

T

G

K
x
N

A

C

A

A

M

L

A
|
A

E

E

R

R

L

K

F
|
F

G

G

A

Q

C

G

R

K

G

G

V

L

E

E

D

N

F

F

V

V

Y

T

L

L

T

I

G

T

H

G

S

T

G
|
G

V

I

G

G

L

I

F

I

F

H

G

Q

G

H

R

E

L

L

Y

I

R

H

G

G

A

S

Q

S

G

F

F

C

A

A

G

A

E
|
E

I

L

G

G

H
|
H

L

L

T

V

I
x
V

V

S

P

L

G

D

G
|
G

R

P

A

D

C
|
C

G

S

C
|
C

G

G

K

S

R

H

G

G

C
|
C

L
x
I

E
|
E

T

A

Y

Y

V

A

S

S

E

G

T

M

S

A

I

L

L

Q

A

R

Q

E

A

A

A

K

E

K

-

L

-

H

-

D

-

E

-

D

-

L

-

V

R

E

G

G

R

M

A

S

L

V

P

P

D

K

L

D

W

E

A

A

A

V

A

G

A

A

-

L

-

H

-

L

-

I

-

Q

A
|
A

R

K

D

L

G

G

D

N

P

A

V

K

V

A

R

Q

T

S

L

I

L

L

E

R

E

T

A

A

G

G

S

T

H

A

L

L

G

G

F

L

A

G

L

V

S

V

H

N

L

I

V

L

N

H

L

T

A

M

N

N

P

P

G

S

L

L

V

V

V

I

L

L

G

S

G

G

N

V

L

L

A

A

N418 (≠ T93) binding
R420 (= R95) binding
I472 (= I153) 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 (vs. gap) binding ; binding
R477 (vs. gap) binding ; binding
T489 (≠ P167) binding ; binding
N516 (= N192) binding ; binding
D517 (= D193) 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 (≠ K195) 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 (= A200) 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 (= F204) 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 (= G221) binding
E566 (= E242) binding
H569 (= H245) binding ; binding ; binding
V572 (≠ I248) 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 (= G252) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
C579 (= C255) binding
C581 (= C257) binding
C586 (= C262) binding
I587 (≠ L263) 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 (= E264) binding ; binding
A630 (= A292) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
A631 (= A293) 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
413 binding
416 binding
417 binding
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)
35% identity, 47% coverage: 149:334/392 of query aligns to 468:672/722 of O35826

query
sites
O35826

I
x
L

G
|
G

V
|
V

G
|
G

I
|
I

P
x
S

A
x
T

-
x
G

-
x
R

L
x
V

M
x
N

D
x
P

R
x
Q

E
|
E

G
|
G

R
x
V

L
x
V

V
x
L

L
x
H

A
x
S

P
x
T

N
x
K

L
|
L

-
x
I

-
x
Q

G
x
E

W
|
W

R
x
N

D
x
S

T
x
V

P
x
D

I
x
L

R
|
R

P
x
T

L
x
P

L
|
L

E
x
S

E
x
D

A
x
T

L
|
L

G
x
H

A
x
L

P
|
P

V
|
V

H
x
W

V
|
V

D
|
D

N
|
N

D
|
D

T
x
G

K
x
N

A
x
C

A
|
A

M
|
M

A
|
A

E
|
E

R
|
R

L
x
K

F
|
F

G
|
G

A
x
Q

C
x
G

R
x
K

G
|
G

V
x
Q

E
|
E

D
x
N

F
|
F

V
|
V

Y
x
T

L
|
L

T
x
I

G
x
T

H
x
G

S
x
T

G
|
G

V
x
I

G
|
G

L
x
I

F
x
I

F
x
H

G
x
Q

G
x
H

R
x
E

L
|
L

Y
x
I

R
x
H

G
|
G

A
x
S

Q
x
S

G
x
F

F
x
C

A
|
A

G
x
A

E
|
E

I
x
L

G
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G

H
|
H

L
|
L

T
x
V

I
x
V

V
x
S

P
x
L

G
x
D

G
|
G

R
x
P

A
x
D

C
|
C

G
x
S

C
|
C

G
|
G

K
x
S

R
x
H

G
|
G

C
|
C

L
x
I

E
|
E

T
x
A

Y
|
Y

V
x
A

S
|
S

E
x
G

T
x
M

S
x
A

I
x
L

L
x
Q

A
x
R

Q
x
E

A
|
A

A
x
K

E
x
K

-
x
L

-
x
H

-
x
D

-
x
E

-
x
D

-
x
L

-
x
V

R
x
E

G
|
G

R
x
M

A
x
S

L
x
V

P
|
P

D
x
K

L
x
D

W
x
E

A
|
A

A
x
V

A
x
G

A
|
A

-
x
L

-
x
H

-
x
L

-
x
I

-
x
Q

A
|
A

R
x
K

D
x
L

G
|
G

D
x
N

P
x
V

V
x
K

V
x
A

R
x
Q

T
x
S

L
x
I

L
|
L

E
x
R

E
x
T

A
|
A

G
|
G

S
x
T

H
x
A

L
|
L

G
|
G

F
x
L

A
x
G

L
x
V

S
x
V

H
x
N

L
x
I

V
x
L

N
x
H

L
x
T

A
x
M

N
|
N

P
|
P

G
x
S

L
|
L

V
|
V

V
x
I

L
|
L

G
x
S

G
|
G

N
x
V

L
|
L

A
|
A

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
413 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.
420 R→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.

2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
34% identity, 47% coverage: 149:334/392 of query aligns to 64:263/308 of 2yi1A

query
sites
2yi1A

I

L

G

G

V

V

G

G

I

I

P

S

A

T

-
x
G

-
x
R

L

V

M

N

D

P

R

R

E

E

G

G

R

I

L

V

V

L

L

H

A
x
S

P
x
T

N

K

L
|
L

-

I

-

Q

G

E

W

W

R

N

D

S

T

V

P

D

I

L

R

R

P

T

L

P

L

L

E

S

E

D

A

T

L

L

G

H

A

L

P

P

V

V

H

W

V

V

D

D

N
|
N

D
|
D

T

G

K
x
N

A

C

A

A

M

L

A

A

E

E

R

R

L

K

F

F

G

G

A

Q

C

G

R

K

G

G

V

L

E

E

D

N

F

F

V

V

Y

T

L

L

T

I

G

T

H
x
G

S
x
T

G
|
G

V
x
I

G

G

G
|
G

G

G

L

I

F

I

F

H

G

Q

G

H

R

E

L

L

Y

I

R

H

G

G

A

S

Q

S

G

F

F

C

A

A

G
x
A

E
|
E

I

L

G

G

H
|
H

L

L

T

V

I

V

V

S

P

L

G

D

G

G

R

P

A

D

C
|
C

G

S

C
|
C

G

G

K

S

R

H

G

G

C
|
C

L

I

E
|
E

T

A

Y

Y

V

A

S

S

E
x
G

T

M

S

A

I

L

L

Q

A

R

Q

E

A

A

A

K

E

K

-

L

-

H

-

D

-

E

-

D

-

L

-

V

R

E

G

G

R

M

A

S

L

A

P

V

D

G

L

A

W
x
L

A

H

A

L

A

I

A

Q

A

A

R

K

D

L

G

G

D

N

P

A

V

K

V

A

R

Q

T

S

L

I

L

L

E

R

E

T

A

A

G

G

S

T

H

A

L

L

G

G

F

L

A

G

L

V

S

V

H

N

L

I

V

L

N

H

L

T

A

M

N

N

P

P

G

S

L

L

V

V

V

I

L

L

G

S

G

G

N
x
V

L

L

A

A

binding adenosine-5'-diphosphate: T140 (≠ S220), G189 (≠ E269), L216 (≠ W287), V261 (≠ N332)
binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G71 (vs. gap), G72 (vs. gap), R73 (vs. gap), S84 (≠ A166), T85 (≠ P167), L87 (= L169), N112 (= N192), D113 (= D193), G139 (≠ H219), T140 (≠ S220), G141 (= G221), I142 (≠ V222), E162 (= E242), H165 (= H245), E184 (= E264)
binding calcium ion: N112 (= N192), N115 (≠ K195), G144 (= G224), A161 (≠ G241)
binding zinc ion: H165 (= H245), C175 (= C255), C177 (= C257), C182 (= C262)

Sites not aligning to the query:

2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
34% identity, 47% coverage: 149:334/392 of query aligns to 64:263/308 of 2yhyA

query
sites
2yhyA

I

L

G

G

V

V

G

G

I

I

P

S

A

T

-

G

-

R

L

V

M

N

D

P

R

R

E

E

G

G

R

I

L

V

V

L

L

H

A

S

P

T

N

K

L

L

-

I

-

Q

G

E

W

W

R

N

D

S

T

V

P

D

I

L

R

R

P

T

L

P

L

L

E

S

E

D

A

T

L

L

G

H

A

L

P

P

V

V

H

W

V

V

D

D

N
|
N

D

D

T

G

K
x
N

A

C

A

A

M

L

A

A

E

E

R

R

L

K

F

F

G

G

A

Q

C

G

R

K

G

G

V

L

E

E

D

N

F

F

V

V

Y

T

L

L

T

I

G

T

H

G

S
x
T

G

G

V

I

G

G

G
|
G

G

G

L

I

F

I

F

H

G

Q

G

H

R

E

L

L

Y

I

R

H

G

G

A

S

Q

S

G

F

F

C

A

A

G
x
A

E

E

I

L

G

G

H
|
H

L

L

T

V

I

V

V

S

P

L

G

D

G

G

R

P

A

D

C
|
C

G

S

C
|
C

G

G

K

S

R

H

G

G

C
|
C

L

I

E

E

T

A

Y

Y

V

A

S

S

E
x
G

T

M

S

A

I

L

L

Q

A

R

Q

E

A

A

A

K

E

K

-

L

-

H

-

D

-

E

-

D

-

L

-

V

R

E

G

G

R

M

A

S

L

A

P

V

D

G

L

A

W
x
L

A

H

A

L

A

I

A

Q

A

A

R

K

D

L

G

G

D

N

P

A

V

K

V

A

R

Q

T

S

L

I

L

L

E

R

E

T

A

A

G

G

S

T

H

A

L

L

G

G

F

L

A

G

L

V

S

V

H

N

L

I

V

L

N

H

L

T

A

M

N

N

P

P

G

S

L

L

V

V

V

I

L

L

G

S

G

G

N
x
V

L

L

A

A

binding adenosine-5'-diphosphate: T140 (≠ S220), G189 (≠ E269), L216 (≠ W287), V261 (≠ N332)
binding calcium ion: N112 (= N192), N115 (≠ K195), G144 (= G224), A161 (≠ G241)
binding zinc ion: H165 (= H245), C175 (= C255), C177 (= C257), C182 (= C262)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 11, 12, 13, 14, 16

2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
34% identity, 47% coverage: 149:334/392 of query aligns to 64:264/309 of 2yhwA

query
sites
2yhwA

I

L

G

G

V

V

G

G

I

I

P

S

A

T

-

G

-

R

L

V

M

N

D

P

R

R

E

E

G

G

R

I

L

V

V

L

L

H

A

S

P

T

N

K

L

L

-

I

-

Q

G

E

W

W

R

N

D

S

T

V

P

D

I

L

R

R

P

T

L

P

L

L

E

S

E

D

A

T

L

L

G

H

A

L

P

P

V

V

H

W

V

V

D

D

N
|
N

D

D

T

G

K
x
N

A

C

A

A

M

L

A

A

E

E

R

R

L

K

F

F

G

G

A

Q

C

G

R

K

G

G

V

L

E

E

D

N

F

F

V

V

Y

T

L

L

T

I

G

T

H

G

S

T

G

G

V

I

G

G

G
|
G

G

G

L

I

F

I

F

H

G

Q

G

H

R

E

L

L

Y

I

R

H

G

G

A

S

Q

S

G

F

F

C

A

A

G
x
A

E

E

I

L

G

G

H
|
H

L

L

T

V

I

V

V

S

P

L

G

N

G

G

R

P

A

D

C
|
C

G

S

C
|
C

G

G

K

S

R

H

G

G

C
|
C

L

I

E

E

T

A

Y

Y

V

A

S

S

E

G

T

M

S

A

I

L

L

Q

A

R

Q

E

A

A

A

K

-

K

-

L

-

H

E

D

R

E

G

D

R

L

A

L

L

L

P

V

D

E

L

G

W

M

A

S

A

V

A

A

A

V

-

G

-

A

-

L

-

H

-

L

-

I

-

Q

A

A

R

K

D

L

G

G

D

N

P

A

V

K

V

A

R

Q

T

S

L

I

L

L

E

R

E

T

A

A

G

G

S

T

H

A

L

L

G

G

F

L

A

G

L

V

S

V

H

N

L

I

V

L

N

H

L

T

A

M

N

N

P

P

G

S

L

L

V

V

V

I

L

L

G

S

G

G

N

V

L

L

A

A

binding calcium ion: N112 (= N192), N115 (≠ K195), G144 (= G224), A161 (≠ G241)
binding zinc ion: H165 (= H245), C175 (= C255), C177 (= C257), C182 (= C262)

3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
36% identity, 41% coverage: 174:334/392 of query aligns to 69:243/288 of 3eo3A

query
sites
3eo3A

T

T

P

D

I

L

R

R

P

T

L

P

L

L

E

S

E

D

A

T

L

L

G

H

A

L

P

P

V

V

H

W

V

V

D

D

N

N

D

D

T

G

K

N

A

C

A

A

M

L

A

A

E

E

R

R

L

K

F

F

G

G

A

Q

C

G

R

K

G

G

V

L

E

E

D

N

F

F

V

V

Y

T

L

L

T

I

G

T

H

G

S

T

G

G

V

I

G

G

L

I

F

I

F

H

G

Q

G

H

R

E

L

L

Y

I

R

H

G

G

A

S

Q

S

G

F

F

C

A

A

G

A

E

E

I

L

G

G

H
|
H

L

L

T

V

I

V

V

S

P

L

G

D

G

G

R

P

A

D

C
|
C

G

S

C
|
C

G

G

K

S

R

H

G

G

C
|
C

L

I

E

E

T

A

Y

Y

V

A

S

S

E

G

T

M

S

A

I

L

L

Q

A

R

Q

E

A

A

A

K

E

K

-

L

-

H

-

D

-

E

-

D

-

L

-

V

R

E

G

G

R

M

A

S

L

V

P

P

D

K

L

D

W

E

A

A

A

V

A

G

A

A

-

L

-

H

-

L

-

I

-

Q

A

A

R

K

D

L

G

G

D

N

P

A

V

K

V

A

R

Q

T

S

L

I

L

L

E

R

E

T

A

A

G

G

S

T

H

A

L

L

G

G

F

L

A

G

L

V

S

V

H

N

L

I

V

L

N

H

L

T

A

M

N

N

P

P

G

S

L

L

V

V

V

I

L

L

G

S

G

G

N

V

L

L

A

A

binding zinc ion: H140 (= H245), C150 (= C255), C152 (= C257), C157 (= C262)

6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
33% identity, 38% coverage: 170:318/392 of query aligns to 81:229/269 of 6jdcA

query
sites
6jdcA

G

G

W

L

R

A

D

E

T

F

P

P

I

L

R

K

P

A

L

S

L

I

E

A

E

K

A

H

L

T

G

D

A

K

P

P

V

I

H

G

V

L

D

L

N

N

D

D

T

A

K

Q

A

A

A

T

M

Y

A

A

E

E

R

Y

L

Q

F

L

G

Q

A

N

C

F

R

E

G

Q

V

V

E

S

D

N

F

F

V

V

Y

F

L

I

T

T

G

V

H

S

S

T

G

G

V

V

G

G

L

I

F

V

F

L

G

N

G

Q

R

I

L

L

Y

Q

R

T

G

G

A

S

Q

R

G

G

F

I

A

A

G

G

E

H

I

I

G

G

H
|
H

L

T

T

L

I

A

V

D

P

P

G

N

G

G

R

A

A

I

C
|
C

G

G

C
|
C

G

G

K

R

R

R

G

G

C
|
C

L

V

E

E

T

A

Y

I

V

A

S

S

E

G

T

R

S

A

I

I

L

-

A

-

Q

E

A

A

A

V

E

S

R

S

G

A

R

T

A

A

L

L

P

V

D

E

L

R

W

S

A

A

A

K

A

A

A

I

A

A

A

N

R

L

D

I

G

A

D

D

P

L

V

V

V

I

R

S

T

L

L

D

L

I

E

Q

E

K

-

I

-

A

A

I

G

G

S

G

H

S

L

V

G

G

F

L

A

A

L

E

S

G

H

Y

L

L

binding zinc ion: H156 (= H245), C166 (= C255), C168 (= C257), C173 (= C262)

4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
29% identity, 47% coverage: 149:334/392 of query aligns to 68:264/311 of 4db3A

query
sites
4db3A

I

I

G

G

V

L

G

G

I

L

P

P

A

G

L

M

M

E

D

D

R

A

E

D

G

D

R

A

L

T

V

V

L

L

A

T

P

V

N

N

L

V

-

P

G

A

W

A

R

K

D

G

T

K

P

P

I

L

R

R

P

A

L

D

L

L

E

E

E

A

A

K

L

I

G

G

A

R

P

S

V

V

H

K

V

I

D

E

N

N

D

D

T

A

K

N

A

C

A

F

A

A

M

L

A

S

E

E

R

A

L

W

F

D

G

E

A

E

C

L

R

Q

G

D

V

A

E

P

D

S

F

V

V

M

Y

G

L

L

T

I

G

L

H

G

S

T

G

G

V

F

G

G

L

L

F

I

F

Y

G

E

G

G

R

K

L

V

Y

F

R

S

G

G

A

R

Q

N

G

N

F

V

A

A

G

G

E

E

I

L

G

G

H
|
H

L

M

T

R

I

L

-

P

-

L

-

D

-

A

-

W

-

F

V

H

P

L

G

G

G

D

R

N

A

A

-

P

-

L

-

G

C
|
C

G

G

C
|
C

G

G

K

K

R

K

G

G

C
|
C

L

L

E

D

T

S

Y

Y

V

L

S

S

-

G

-

R

-

G

-

F

E

E

T

L

S

L

I

Y

L

A

A

H

Q

Y

A

Y

A

G

E

E

R

E

G

K

R

K

A

A

L

I

P

D

D

I

L

I

W

K

A

A

A

N

A

A

A

-

R

-

D

-

G

G

D

D

P

E

V

K

V

A

R

A

T

E

L

H

L

V

E

E

E

R

A

F

G

M

S

E

H

L

L

L

G

A

F

I

A

C

L

F

S

G

H

N

L

I

V

F

N

T

L

A

A

N

N

D

P

P

G

H

L

V

V

V

V

A

L

L

G

G

N

G

L

L

A

S

binding zinc ion: H165 (= H245), C185 (= C255), C187 (= C257), C192 (= C262)

6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
36% identity, 28% coverage: 170:278/392 of query aligns to 80:188/290 of 6jdbA

query
sites
6jdbA

G

G

W

L

R

A

D

E

T

F

P

P

I

L

R

K

P

A

L

S

L

I

E

A

E

K

A

H

L

T

G

D

A

K

P

P

V

I

H

G

V

L

D

L

N
|
N

D
|
D

T

A

K

Q

A

A

A

T

M

Y

A

A

E

E

R

Y

L

Q

F

L

G

Q

A

N

C

F

R

E

G

Q

V

V

E

S

D

N

F

F

V

V

Y

F

L

I

T

T

G

V

H
x
S

S
x
T

G

G

V

V

G

G

L

I

F

V

F

L

G

N

G

Q

R

I

L

L

Y

Q

R

T

G

G

A

S

Q

R

G

G

F

I

A

A

G

G

E
x
H

I

I

G

G

H
|
H

L

T

T

L

I

A

V

D

P

P

G

N

G

G

R

A

A

I

C
|
C

G

G

C
|
C

G

G

K

R

R

R

G

G

C
|
C

L

V

E
|
E

T

A

Y

I

V

A

S

S

E

G

T

R

S

A

I

I

L

E

A

A

Q

V

A

S

E

Q

binding adenosine-5'-diphosphate: S129 (≠ H219), T130 (≠ S220)
binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: N102 (= N192), D103 (= D193), S129 (≠ H219), T130 (≠ S220), H152 (≠ E242), H155 (= H245), E174 (= E264)
binding zinc ion: H155 (= H245), C165 (= C255), C167 (= C257), C172 (= C262)

Sites not aligning to the query:

P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
30% identity, 53% coverage: 148:356/392 of query aligns to 66:271/309 of P32718

query
sites
P32718

G

G

I

L

G

V

V

M

G

G

I

F

P

P

A
|
A

L

L

M

V

D

S

R

K

E

D

G

K

R

R

L

T

V

I

L

I

A

S

-

T

P

P

N

N

L

L

G

P

W

L

R

T

D

A

T

A

P

D

I

L

R

Y

P

D

L

L

-

A

-

D

-

K

L

L

E

E

E

N

A

T

L

L

G

N

A

C

P

P

V

V

H

E

V

F

D

S

N

R

D

D

T

V

K

N

A

L

A

Q

A

L

M

S

A

W

E

D

R

V

L

V

F

E

G

N

A

-

C

-

R

R

G

L

V

T

E

Q

D

Q

F

L

V

V

-

L

-

A

Y

Y

L

L

T

G

G

-

H

-

S

T

G

G

V

M

G

G

G
x
F

G

A

L

V

F

W

F

M

G

N

G

G

R

A

L

P

Y

W

R

T

G

G

A

A

Q

H

G

G

F

V

A

A

G

G

E

E

I

L

G

G

H

H

L

I

T

P

I

L

V

G

P

D

G

M

G

T

R

Q

A

H

C

C

G

A

C

C

G

G

K

N

R

P

G

G

C

C

L

L

E

E

T

T

Y

N

V

C

S

S

E

G

T

M

S

A

I

L

L

R

A

R

Q

W

A

Y

A

E

E

Q

R

Q

G

P

R

R

A

N

L

Y

P

P

-

L

-

R

D

D

L

L

W

F

A

V

A

H

A

A

A

E

A

N

A

A

R

-

D

-

G

-

D

-

P

P

V

F

V

V

R

Q

T

S

L

L

E

E

E

N

A

A

G

A

S

R

H

-

L

-

G

-

F

-

A

A

L

I

S

A

H

T

L

S

V

I

N

N

L

L

A

F

N

D

P

P

G

D

L

A

V

V

V

I

L

L

G

G

N

G

L

V

A

M

I

D

V

M

A

P

E

A

F

F

I

P

L

R

P

E

A

T

L

L

N

V

A

A

A

M

L

T

G

Q

E

K

H

Y

A

L

L

R

E

R

P

P

L

L

A73 (= A155) mutation to 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.
F145 (≠ G224) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.

6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
28% identity, 66% coverage: 89:348/392 of query aligns to 6:257/293 of 6jdoA

query
sites
6jdoA

L

L

E

D

P

I

G

G

T

G

I

T

R

K

I

I

V

A

S

S

T

A

T

I

L

V

A

T

G

D

T

G

V

K

V

I

E

E

Q

Q

S

R

Q

Q

I

Q

P

I

G

A

S

T

-

P

-

Q

T

A

D

D

L

A

A

A

T

N

A

A

L

M

R

H

H

D

L

T

H

L

E

A

G

N

I

I

D

L

A

A

V

L

V

Y

A

A

A

G

S

Q

R

F

P

D

E

Y

G

V

G

A

A

V

A

A

T

S

P

T

P

G

L

I

C

I

G

N

I

H

G

G

V

V

G

-

I

L

P

T

A

A

L

L

M

N

D

P

R

K

E

-

G

-

R

-

L

-

V

-

L

-

A

-

P

-

N

N

L

L

G

G

-

G

W

L

R

A

D

E

T

F

P

P

I

L

R

K

P

E

L

S

L

I

E

A

E

R

A

H

L

T

G

D

A

K

P

P

V

I

H

G

V

L

D

L

N

N

D

D

T

V

K

Q

A

A

M

C

A

A

E

E

R

Y

L

K

F

D

G

E

A

D

C

K

R

N

G

A

V

V

E

Q

D

N

F

F

V

V

Y

F

L

I

T

T

G

V

H
x
S

S
x
T

G

G

V

V

G

G

L

I

F

I

F

L

G

E

G

R

R

R

L

L

Y

L

R

T

G

E

A

P

Q

N

G

G

F

V

A

A

G

G

E

H

I

I

G

G

H
|
H

L

T

T

L

I

A

V

D

P

P

G

N

G

G

R

P

A

V

C
|
C

G

G

C
|
C

G

G

K
x
R

R

V

G

G

C

C

L

V

E

E

T

A

Y

V

V

A

S

A

E
x
G

T

R

S

A

I

I

L

E

A

A

Q

V

A

S

E

Q

R

W

G

N

-

P

R

P

A

C

L

T

P
|
P

D

K

L

-

W

-

A

Q

A

A

A
x
F

A

E

A

L

A

F

R

R

D

K

G

N

D

D

P

E

V

K

V

A

R

T

T

A

L

L

L

I

E

Q

E

R

A

S

G

A

S

S

H

A

L

I

G

A

F

N

A

L

L

I

S

A

H

D

L

L

V

V

N

I

L

G

A

L

N

D

P

V

G

Q

L

K

V

V

L

V

G

G

N
x
S

L

V

A

G

I

L

V

-

A

A

E

E

F

G

I

Y

L

L

P

P

A

L

L

V

N

K

A

Q

A

Y

L

L

binding phosphoaminophosphonic acid-adenylate ester: S130 (≠ H219), T131 (≠ S220), G180 (≠ E269), P196 (= P284), F200 (≠ A290), S242 (≠ N332)
binding calcium ion: H156 (= H245), C166 (= C255), C168 (= C257), R170 (≠ K259)

Query Sequence

>AZOBR_RS27950 FitnessBrowser__azobra:AZOBR_RS27950
MLPRVNSAAIRRLNMVRVFHALRENPRCAQRDLSRLTGLDKATTSAIVAQMIEEGLVERT
EAPRARRIGRPETALGIAPSAGLLVGARLEPGTIRIVSTTLAGTVVEQSQIPGSTDLATA
LRHLHEGIDAVVAASRPEGGAATPPLCGIGVGIPALMDREGRLVLAPNLGWRDTPIRPLL
EEALGAPVHVDNDTKAAAMAERLFGACRGVEDFVYLTGHSGVGGGLFFGGRLYRGAQGFA
GEIGHLTIVPGGRACGCGKRGCLETYVSETSILAQAAERGRALPDLWAAAAAARDGDPVV
RTLLEEAGSHLGFALSHLVNLANPGLVVLGGNLAIVAEFILPALNAALGEHALEPLRRDL
RLLVSPLGPDAVPMGGIALAMDGFLSVPSPIL

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