SitesBLAST

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 16 papers)
33% identity, 51% coverage: 140:339/395 of query aligns to 467:669/722 of Q9Y223

query
sites
Q9Y223

L

I

L

L

G

G

I

V

G

G

I
|
I

G

S

M

T

P

G

G

G

F

R

V

V

N

N

A

P

E

R

K

E

G

G

M

I

-

V

-

L

-

H

N

S

Y

T

S

K

F

L

M

I

Q

Q

V

E

E

W

N

N

D

S

I

V

S

D

L

L

Q

R

D

T

Y

P

L

L

A

S

K

D

K

T

L

L

R

H

L

L

P

P

V

V

Y

W

I

V

D

D

N

N

D
|
D

S

G

S
x
N

L

C

I

A

A

A

L

L

A
|
A

E

E

L

R

N

K

F
|
F

G

G

E

Q

A

G

R

K

N

G

L

L

K

E

D

N

V

F

L

V

V

T

V

L

N

I

I

T

G

G

W

T

G

G

T

I

G

G

L

G

G

G

M

I

I

I

I

H

N

Q

G

H

K

E

L

L

Y

I

R

H

G

G

S

S

G

F

Y

C

A

A

G

A

E

E

F

L

S

G

H

H

I

L

P

V

L
x
V

S

S

N

L

S

D

N
x
G

T

P

L

D

C

C

S

S

C

C

G

G

K

S

R

H

G

G

C

C

L
x
I

E

E

V

A

E

Y

T

A

S

S

L

G

L

M

V

A

M

L

V

-

Q

-

K

-

A

Q

E

R

E

E

A

A

V

K

K

K

N

L

G

H

E

D

E

E

T

D

S

L

L

L

-

L

-

V

-

E

-

G

K

M

T

S

L

V

F

P

N

K

D

D

K

E

S

A

K

V

S

G

H

A

V

L

D

-

H

H

F

L

L

I

N

Q

A
|
A

V
x
A

V

K

K

L

Q

G

D

N

P

A

V

K

A

A

I

Q

S

S

I

I

L

L

A

R

D

T

A

A

A

G

F

T

Q

A

I

L

G

G

K

L

G

G

L

V

A

V

T

N

L

I

I

L

H

H

I

T

M

M

N

N

P

P

E

S

R

L

I

V

V

I

L

L

S

S

G

G

I472 (= I145) to T: in NM; results in decreased epimerase activity corresponding to 50% of the wild-type; severely decreased kinase activity corresponding to less than 10% of wild-type activity
D517 (= D187) active site
N519 (≠ S189) to S: in NM; decreased epimerase activity; decreased kinase activity; dbSNP:rs1554658910
A524 (= A194) to V: in NM; results in decreased epimerase activity corresponding to less than 10% of wild-type activity; decreased kinase activity; impaired homohexamers formation; dbSNP:rs764698870
F528 (= F198) to C: in NM; retains 70% of wild-type epimerase; decreased kinase activity; dbSNP:rs986773986
V572 (≠ L242) to L: in NM; retains 70-80% of wild-type epimerase activity; severely decreased kinase activity corresponding to less than 10% of wild-type activity; does not affect homohexamers formation; dbSNP:rs121908632
G576 (≠ N246) to E: in NM; decreased epimerase activity; decreased kinase activity; dbSNP:rs121908625
I587 (≠ L257) to T: in NM; decreased epimerase activity; decreased kinase activity; dbSNP:rs748949603
A630 (= A300) to T: in NM; decreased kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
A631 (≠ V301) to T: in NM; retains 80% of wild-type epimerase activity; retains 75% of wild-type kinase activity; dbSNP:rs121908626; to V: in NM; retains 70% of wild-type epimerase activity; decreased kinase activity; does not affect homohexamers formation; dbSNP:rs62541771

Sites not aligning to the query:

13 C → S: in NM; results in decreased epimerase activity corresponding to 20% of wild-type activity; no effect on kinase activity; dbSNP:rs1209266607
132 H → Q: in NM; results in decreased epimerase activity corresponding to less than 10% of wild-type activity; impaired homohexamers formation
176 D → V: in NM; results in decreased epimerase activity corresponding to 20% of wild-type activity; no effect on kinase activity; impaired homohexamers formation; dbSNP:rs139425890
177 R → C: in NM; results in decreased epimerase activity corresponding to less than 20% of wild-type activity; no effect on kinase activity; impaired homohexamers formation; dbSNP:rs539332585
200 I → F: in NM; unknown pathological significance; retains 90% of wild-type epimerase activity; retains 75% of wild-type kinase activity; dbSNP:rs369328625
206 G → S: in NM; moderate phenotype with unusual involvement of quadriceps; dbSNP:rs766266918
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
303 C → V: in NM; retains 80% of wild-type epimerase activity; decreased kinase activity corresponding to 60% of wild-type; requires 2 nucleotide substitutions; dbSNP:rs121908633
331 V → A: in NM; results in decreased epimerase activity corresponding to 20% of wild-type activity; no effect on kinase activity; impaired homohexamers formation
378 D → Y: in NM; results in decreased epimerase activity corresponding to 10-30% of wild-type activity; decreased kinase activity; impaired homohexamers formation; dbSNP:rs199877522
708 G → S: in NM; decreased epimerase activity; severely decreased kinase activity; dbSNP:rs1554657922

2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
33% identity, 51% coverage: 140:339/395 of query aligns to 63:261/309 of 2yhwA

query
sites
2yhwA

L

I

L

L

G

G

I

V

G

G

I

I

G

S

M

T

P

G

G

G

F

R

V

V

N

N

A

P

E

R

K

E

G

G

M

I

-

V

-

L

-

H

N

S

Y

T

S

K

F

L

M

I

Q

Q

V

E

E

W

N

N

D

S

I

V

S

D

L

L

Q

R

D

T

Y

P

L

L

A

S

K

D

K

T

L

L

R

H

L

L

P

P

V

V

Y

W

I

V

D

D

N
|
N

D

D

S

G

S
x
N

L

C

I

A

A

A

L

L

A

A

E

E

L

R

N

K

F

F

G

G

E

Q

A

G

R

K

N

G

L

L

K

E

D

N

V

F

L

V

V

T

V

L

N

I

I

T

G

G

W

T

G

G

T

I

G

G

L
x
G

G

G

M

I

I

I

I

H

N

Q

G

H

K

E

L

L

Y

I

R

H

G

G

S

S

G

F

Y

C

A

A

G
x
A

E

E

F

L

S

G

H
|
H

I

L

P

V

L

V

S

S

N

L

S

N

N

G

T

P

L

D

C
|
C

S

S

C
|
C

G

G

K

S

R

H

G

G

C
|
C

L

I

E

E

V

A

E

Y

T

A

S

S

L

G

L

M

V

A

M

L

V

Q

Q

R

K

E

A

A

E

-

A

-

V

-

K

K

N

K

G

L

E

H

E

D

T

E

S

D

L

L

K

L

T

L

L

V

F

E

N

G

D

M

K

S

S

V

K

A

S

V

H

G

V

A

D

L

H

H

F

L

L

I

N

Q

A

A

V

A

V

K

K

L

Q

G

D

N

P

A

V

K

A

A

I

Q

S

S

I

I

L

L

A

R

D

T

A

A

A

G

F

T

Q

A

I

L

G

G

K

L

G

G

L

V

A

V

T

N

L

I

I

L

H

H

I

T

M

M

N

N

P

P

E

S

R

L

I

V

V

I

L

L

S

S

G

G

binding calcium ion: N112 (= N186), N115 (≠ S189), G144 (≠ L218), A161 (≠ G235)
binding zinc ion: H165 (= H239), C175 (= C249), C177 (= C251), C182 (= C256)

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)
32% identity, 51% coverage: 140:339/395 of query aligns to 467:669/722 of O35826

query
sites
O35826

L

I

L

L

G

G

I

V

G

G

I

I

G

S

M

T

P

G

G

G

F

R

V

V

N

N

A

P

E

Q

K

E

G

G

M

V

-

V

-

L

-

H

N

S

Y

T

S

K

F

L

M

I

Q

Q

V

E

E

W

N

N

D

S

I

V

S

D

L

L

Q

R

D

T

Y

P

L

L

A

S

K

D

K

T

L

L

R

H

L

L

P

P

V

V

Y

W

I

V

D

D

N

N

D

D

S

G

S

N

L

C

I

A

A

A

L

M

A

A

E

E

L

R

N

K

F

F

G

G

E

Q

A

G

R

K

N

G

L

Q

K

E

D

N

V

F

L

V

V

T

V

L

N

I

I

T

G

G

W

T

G

G

T

I

G

G

L

G

G

G

M

I

I

I

I

H

N

Q

G

H

K

E

L

L

Y

I

R

H

G

G

S

S

G

F

Y

C

A

A

G

A

E

E

F

L

S

G

H

H

I

L

P

V

L

V

S

S

N

L

S

D

N

G

T

P

L

D

C

C

S

S

C

C

G

G

K

S

R

H

G

G

C

C

L

I

E

E

V

A

E

Y

T

A

S

S

L

G

L

M

V

A

M

L

V

-

Q

-

K

-

A

Q

E

R

E

E

A

A

V

K

K

K

N

L

G

H

E

D

E

E

T

D

S

L

L

L

-

L

-

V

-

E

-

G

K

M

T

S

L

V

F

P

N

K

D

D

K

E

S

A

K

V

S

G

H

A

V

L

D

-

H

H

F

L

L

I

N

Q

A

A

V

A

V

K

K

L

Q

G

D

N

P

V

V

K

A

A

I

Q

S

S

I

I

L

L

A

R

D

T

A

A

A

G

F

T

Q

A

I

L

G

G

K

L

G

G

L

V

A

V

T

N

L

I

I

L

H

H

I

T

M

M

N

N

P

P

E

S

R

L

I

V

V

I

L

L

S

S

G

G

Sites not aligning to the query:

49 H→A: Does not affect kinase activity; almost complete loss of epimerase activity; does not interfere with enzyme oligomerization.
110 H→A: Does not affect kinase activity; almost complete loss of epimerase activity; partial reduction of the dimerization process.
132 H→A: Does not affect kinase activity; almost complete loss of epimerase activity; partial reduction of the dimerization process.
155 H→A: Does not affect kinase activity; almost complete loss of epimerase activity; strong reduction of the dimerization process.
157 H→A: Does not affect kinase activity; almost complete loss of epimerase activity; strong reduction of the dimerization process.
413 mutation D->K,N: Does not affect epimerase activity; does not affect feedback inhibition by CMP-Neu5Ac; almost complete loss of kinase activity; does not interfere with oligomerization.
420 R→M: Does not affect epimerase activity; does not affect feedback inhibition by CMP-Neu5Ac; almost complete loss of kinase activity; does not interfere with oligomerization.

3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
32% identity, 46% coverage: 157:339/395 of query aligns to 58:240/288 of 3eo3A

query
sites
3eo3A

M

L

N

N

Y

C

S

R

F

I

M

L

Q

G

V

V

E

G

N

I

D

S

I

T

S

D

L

L

Q

R

D

T

Y

P

L

L

A

S

K

D

K

T

L

L

R

H

L

L

P

P

V

V

Y

W

I

V

D

D

N

N

D

D

S

G

S

N

L

C

I

A

A

A

L

L

A

A

E

E

L

R

N

K

F

F

G

G

E

Q

A

G

R

K

N

G

L

L

K

E

D

N

V

F

L

V

V

T

V

L

N

I

I

T

G

G

W

T

G

G

T

I

G

G

L

G

G

G

M

I

I

I

I

H

N

Q

G

H

K

E

L

L

Y

I

R

H

G

G

S

S

G

F

Y

C

A

A

G

A

E

E

F

L

S

G

H
|
H

I

L

P

V

L

V

S

S

N

L

S

D

N

G

T

P

L

D

C
|
C

S

S

C
|
C

G

G

K

S

R

H

G

G

C
|
C

L

I

E

E

V

A

E

Y

T

A

S

S

L

G

L

M

V

A

M

L

V

Q

Q

R

K

E

A

A

E

K

A

L

V

-

K

-

N

H

G

D

E

E

E

D

T

L

S

L

L

L

K

V

T

E

L

G

F

M

N

S

D

V

K

P

S

K

K

D

S

E

H

A

V

V

D

G

-

A

-

L

H

H

F

L

L

I

N

Q

A

A

V

A

V

K

K

L

Q

G

D

N

P

A

V

K

A

A

I

Q

S

S

I

I

L

L

A

R

D

T

A

A

A

G

F

T

Q

A

I

L

G

G

K

L

G

G

L

V

A

V

T

N

L

I

I

L

H

H

I

T

M

M

N

N

P

P

E

S

R

L

I

V

V

I

L

L

S

S

G

G

binding zinc ion: H140 (= H239), C150 (= C249), C152 (= C251), C157 (= C256)

P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
29% identity, 50% coverage: 142:339/395 of query aligns to 66:246/309 of P32718

query
sites
P32718

G

G

I

L

G

V

I

M

G

G

M

F

P

P

G
x
A

F

L

V

V

N

S

A

K

E

D

K

K

G

R

M

T

N

I

Y

I

S

S

F

T

-

P

-

N

-

L

-

P

M

L

Q

T

V

A

E

A

N

D

D

L

I

Y

S

D

L

L

Q

A

D

D

Y

K

L

L

A

E

K

N

K

T

L

L

R

N

L

C

P

P

V

V

Y

E

I

F

D

S

N

R

D

D

S

V

S

N

L

L

I

-

A

-

L

-

A

-

E

Q

L

L

N

S

F

W

G

D

E

V

A

V

R

E

N

N

L

R

-

L

-

T

-

Q

K

Q

D

L

V

V

L

L

V

A

N

Y

I

L

G

G

W

T

G

G

T

M

G

G

L
x
F

G

A

M

V

I

W

I

M

N

N

G

G

K

A

L

P

Y

W

R

T

G

G

S

A

S

H

G

G

Y

V

A

A

G

G

E

E

F

L

S

G

H

H

I

I

P

P

L

L

S

G

N

D

S

M

N

T

T

Q

L

H

C

C

S

A

C

C

G

G

K

N

R

P

G

G

C

C

L

L

E

E

V

T

E

N

T

C

S

S

L

G

L

M

V

A

M

L

V

R

Q

R

K

W

A

Y

E

E

E

Q

A

Q

V

P

K

R

N

N

G

-

E

-

T

Y

S

P

L

L

K

R

T

D

L

L

F

F

N

V

D

-

K

-

S

-

K

-

S

-

H

-

V

-

D

-

H

H

F

A

L

E

N

N

A

A

V

-

K

-

Q

-

D

-

P

P

V

F

A

V

I

Q

S

S

I

L

L

L

A

E

D

N

A

A

F

-

Q

-

I

-

G

-

K

R

G

A

L

I

A

A

T

T

L

S

I

I

H

N

I

L

M

F

N

D

P

P

E

D

R

A

I

V

V

I

L

L

S

G

G

G

A73 (≠ G149) 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 (≠ L218) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.

Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
24% identity, 50% coverage: 142:339/395 of query aligns to 56:242/297 of Q93LQ8

query
sites
Q93LQ8

G

G

I

I

G

A

I

I

G

S

M

A

P

P

G

G

F

Y

V

I

N

D

A

P

E

H

K

S

G

G

-

L

-

I

-

T

M

M

N

G

Y

G

S

A

F

I

M

R

Q

R

V

F

E

D

N

N

D

-

I

F

S

A

L

M

Q

K

D

S

Y

W

L

L

A

E

K

T

K

R

L

T

R

G

L

L

P

P

V

V

Y

S

I

V

D

E

N

N

D
|
D

S

A

S

N

L

C

I

V

A

L

L

L

A

A

E

E

L

R

N

W

F

Q

G

G

E

K

A

A

R

A

N

E

L

M

K

A

D

N

V

F

L

L

V

V

V

L

N

T

I

I

G

G

W

T

G
|
G

T

I

G
|
G

L

G

G

A

M

I

I

F

I

C

N

Q

G

H

K

Q

L

L

Y

I

R

N

G

G

S

A

S

R

G

F

Y

R

A

A

G

G

E

E

F

F

S

G

H

Y

I

M

P

L

L

T

S

D

N

R

S

P

N

G

T

G

L

R

C

D

S

P

C

-

G

-

K

R

R

R

G

Y

C

S

L

M

E

N

V

E

E

N

T

C

S

T

L

L

L

R

V

V

M

L

V

R

Q

H

K

R

A

Y

E

A

E

Q

A

H

V

I

K

G

N

A

G

P

E

L

E

D

T

S

S

V

L

T

K

G

T

E

L

L

F

I

N

F

D

D

K

R

S

Y

K

D

S

A

H

-

V

-

D

-

H

-

F

-

L

-

N

-

A

-

V

-

K

-

Q

G

D

D

P

P

V

V

A

C

I

Q

S

R

I

L

L

V

A

A

D

E

A

F

F

N

Q

G

I

L

G

G

K

H

G

G

L

L

A

Y

T

N

L

L

I

V

H

H

I

I

M

F

N

D

P

P

E

Q

R

T

I

I

V

F

L

I

S

G

G

G

D103 (= D187) mutation to G: Loss of catalytic activity.
G131 (= G215) mutation to A: Loss of catalytic activity.
G133 (= G217) 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)
28% identity, 48% coverage: 143:332/395 of query aligns to 61:236/298 of 3vovB

query
sites
3vovB

I

I

G

G

I

L

G

G

M

T

P

P

G

G

F

P

V

L

N

D

A

F

E

R

K

R

G

G

M

V

N

I

Y

R

S

P

F

N

M

I

Q

P

V

G

E

V

N

Q

D

D

I

F

S

P

L

I

Q

R

D

R

Y

I

L

L

A

E

K

E

K

A

L

T

R

G

L

R

P

P

V

V

Y

F

I

L

D

E

N

N

D

D

S

A

S

N

L

A

I

A

A

A

L

L

A

A

E

E

L

H

N

H

F

L

G

G

E

A

A

A

R

Q

N

G

L

E

K

E

D

S

V

S

L

L

V

Y

V

L

N

T

I

V

G

S

W

T

G

G

T

I

G

G

L

G

G

G

M

V

I

V

I

L

N

G

G

G

K

R

L

V

Y

L

R

R

G

G

S

E

S

R

G

G

Y

Q

A

G

G

G

E

E

F

L

S

G

H
|
H

I

L

P

T

L

L

S

L

N

P

S

G

N

G

T

P

L

A

C
|
C

S

G

C
|
C

G

G

K

L

R

E

G

G

C
|
C

L

L

E

E

V

A

E

L

T

A

S

A

L

G

L

R

V

A

M

L

V

E

Q

R

K

D

A

A

E

T

E

Y

A

A

V

F

K

Q

N

R

G

P

E

V

E

D

T

T

-

R

S

E

L

L

K

F

T

R

L

L

F

F

N

Q

D

-

K

-

S

-

K

-

S

-

H

-

V

-

D

-

H

-

F

-

L

-

N

-

A

-

V

-

K

A

Q

G

D

D

P

P

V

K

A

A

I

E

S

R

I

L

L

V

A

L

D

Q

A

A

F

R

Q

Y

I

V

G

G

K

I