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 18 papers)
29% identity, 66% coverage: 11:214/307 of query aligns to 411:625/722 of Q9Y223

query
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Q9Y223

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D413 (≠ E13) binding
G416 (= G16) binding
T417 (= T17) binding
N418 (≠ K18) binding
R420 (≠ M20) binding
I472 (≠ V64) 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 (= G68) binding ; binding
R477 (≠ P69) binding ; binding
T489 (≠ P86) binding ; binding
N516 (≠ T111) binding ; binding
D517 (= D112) 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 (= N114) 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 (= A119) 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 (≠ W123) 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 (= G140) binding
E566 (= E159) binding
H569 (= H162) binding ; binding ; binding
V572 (= V165) 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 (≠ P173) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
C579 (≠ G176) binding
C581 (= C178) binding
C586 (= C184) binding
I587 (≠ L185) 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 (= E186) binding ; binding

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
630 A → T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
631 A → 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; A → 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.
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.

2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
30% identity, 60% coverage: 11:194/307 of query aligns to 7:192/308 of 2yi1A

query
sites
2yi1A

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binding adenosine-5'-diphosphate: G11 (= G15), T13 (= T17), N14 (≠ K18), R16 (≠ M20), T140 (= T139), G189 (= G191)
binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G16), G71 (≠ F67), G72 (= G68), R73 (≠ P69), S84 (≠ T85), T85 (≠ P86), L87 (vs. gap), N112 (≠ T111), D113 (= D112), G139 (= G138), T140 (= T139), G141 (= G140), I142 (≠ V141), E162 (= E159), H165 (= H162), E184 (= E186)
binding calcium ion: N112 (≠ T111), N115 (= N114), G144 (≠ V143), A161 (≠ P158)
binding zinc ion: H165 (= H162), C175 (≠ G176), C177 (= C178), C182 (= C184)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 216, 261

2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
30% identity, 60% coverage: 11:194/307 of query aligns to 7:192/308 of 2yhyA

query
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2yhyA

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binding adenosine-5'-diphosphate: G11 (= G15), G12 (= G16), T13 (= T17), N14 (≠ K18), R16 (≠ M20), T140 (= T139), G189 (= G191)
binding calcium ion: N112 (≠ T111), N115 (= N114), G144 (≠ V143), A161 (≠ P158)
binding zinc ion: H165 (= H162), C175 (≠ G176), C177 (= C178), C182 (= C184)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 216, 261

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)
29% identity, 66% coverage: 11:214/307 of query aligns to 411:625/722 of O35826

query
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O35826

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L
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L

D413 (≠ E13) 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 (≠ M20) mutation to M: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.

Sites not aligning to the query:

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

2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
29% identity, 60% coverage: 11:194/307 of query aligns to 7:192/309 of 2yhwA

query
sites
2yhwA

A

A

I

V

E

D

L

L

G

G

T

T

K

N

V

L

M

R

V

V

A

A

F

I

G

V

S

S

G

M

P

K

D

G

D

E

L

I

S

V

P

K

P

-

L

-

R

K

I

Y

P

T

T

Q

T

F

T

N

P

P

A

K

E

T

T

Y

L

E

A

E

R

R

I

I

E

N

D

L

A

I

L

L

-

Q

-

M

-

C

-

V

-

E

-

A

A

A

E

E

Q

A

G

V

R

K

F

L

D

N

A

C

-

R

-

I

-

L

-

G

I

V

G

G

V

I

A

S

S

T

F

G

G

G

P

R

I

V

R

N

L

-

D

-

P

-

A

-

P

P

D

R

W

E

G

G

H

I

I

V

L

L

K

H

T

S

P

T

K

K

-

L

-

I

P

Q

G

E

W

W

S

N

H

S

A

V

D

D

V

L

A

R

A

T

R

P

L

L

V

S

R

D

R

T

F

L

D

H

R

L

P

P

L

V

A

W

L

V

D

D

T
x
N

D

D

V

G

N
|
N

G

C

A

A

V

L

A

A

E

E

G

R

L

K

W

F

G

G

A

Q

A

G

K

K

G

G

L

L

G

E

D

N

Y

F

A

V

Y

T

V

L

T

I

V

T

G

G

T

T

G

G

V

I

G

G

V
x
G

G

G

L

I

V

I

V

H

N

Q

G

H

A

E

P

L

T

I

H

H

G

G

-

S

L

F

L

C

H

A

P
x
A

E

E

A

L

G

G

H
|
H

I

L

L

V

V

V

R

-

D

-

A

-

A

S

L

L

D

N

P

G

F

P

T

D

G
x
C

S

S

C
|
C

P

G

F

S

H

H

G

G

D

-

C
|
C

L

I

E

E

G

A

L

Y

I

A

S

S

G

G

P

M

A

A

L

L

binding calcium ion: N112 (≠ T111), N115 (= N114), G144 (≠ V143), A161 (≠ P158)
binding zinc ion: H165 (= H162), C175 (≠ G176), C177 (= C178), C182 (= C184)

1woqA Crystal structure of inorganic polyphosphate/atp-glucomannokinase from arthrobacter sp. Strain km at 1.8 a resolution (see paper)
25% identity, 50% coverage: 90:241/307 of query aligns to 91:214/253 of 1woqA

query
sites
1woqA

W

W

S

L

H

N

A

T

D

D

V

I

A

D

A

A

R

L

L

L

V

T

R

A

R

R

F

L

D

G

R

R

P

P

L

V

A

E

L

V

D

I

T
x
N

D
|
D

V

A

N

D

G

A

A

A

A

G

V

L

A

A

E

E

G

A

L

R

W

Y

G

G

A

A

A

G

K

A

G

G

L

V

-

K

G

G

D

T

Y

V

A

L

Y

V

V

I

T

T

V

L

G

G

T
|
T

G

G

V
x
I

G
|
G

V

S

G

A

L

F

V

I

V

F

N

D

G

G

-

K

-

L

A

V

P

P

T

N

H

A

G
x
E

L

L

L

G

H
|
H

P

L

E

E

A

I

-

D

G

G

H

H

I

-

L

-

V

-

R

-

D

-

A

-

L

-

D

-

P

-

F

-

T

-

G

-

S

-

C

-

P

-

F

-

H

-

G

-

D

-

C

-

L

-

E

-

G

-

L

-

I

-

S

-

G

-

P

-

A

-

L

-

A

D

A

A

R
x
E

T

T

G

K

A

A

P

S

G

A

E

V

S

A

L

R

S

E

K

R

D

D

D

G

P

L

V

S

W

W

A

D

L

E

V

Y

A

S

D

V

Y

L

L

L

A

Q

Q

R

L

Y

V

F

A

S

N

H

L

V

A

E

L

F

I

L

A

F

S

S

P

P

R

E

R

L

V

F

I

I

I

V

G

G

V

I

binding beta-D-glucopyranose: N112 (≠ T111), D113 (= D112), I143 (≠ V141), G144 (= G142), E158 (≠ G154), H161 (= H157), E170 (≠ R197)
binding phosphate ion: T141 (= T139)

Sites not aligning to the query:

Query Sequence

>CCNA_01192 FitnessBrowser__Caulo:CCNA_01192
MAGRPMSRIAAIELGGTKVMVAFGSGPDDLSPPLRIPTTTPAETLARIEDALAAEQGRFD
AIGVASFGPIRLDPAAPDWGHILKTPKPGWSHADVAARLVRRFDRPLALDTDVNGAAVAE
GLWGAAKGLGDYAYVTVGTGVGVGLVVNGAPTHGLLHPEAGHILVRRDAALDPFTGSCPF
HGDCLEGLISGPALAARTGAPGESLSKDDPVWALVADYLAQLVANLALIASPRRVIIGGG
VGGNPQLLEQTRTRLQTHLAGYLAPLEQRSDIDAFVAAPGLGANSGLLGAVALGLRHDAI
LRQDLMP

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