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)
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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I472 (≠ V64) 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 (= D112) active site
N519 (= N114) to S: in NM; decreased epimerase activity; decreased kinase activity; dbSNP:rs1554658910
A524 (= A119) 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 (≠ W123) to C: in NM; retains 70% of wild-type epimerase; decreased kinase activity; dbSNP:rs986773986
V572 (= V165) 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 (≠ P173) to E: in NM; decreased epimerase activity; decreased kinase activity; dbSNP:rs121908625
I587 (≠ L185) to T: in NM; decreased epimerase activity; decreased kinase activity; dbSNP:rs748949603

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
630 A → T: in NM; decreased kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
631 A → T: in NM; retains 80% of wild-type epimerase activity; retains 75% of wild-type kinase activity; dbSNP:rs121908626; A → V: in NM; retains 70% of wild-type epimerase activity; decreased kinase activity; does not affect homohexamers formation; dbSNP:rs62541771
708 G → S: in NM; decreased epimerase activity; severely decreased kinase activity; dbSNP:rs1554657922

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
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2yi1A

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binding adenosine-5'-diphosphate: G11 (= G15), G12 (= G16), T13 (= T17), N14 (≠ K18), R16 (≠ M20), G139 (= G138), T140 (= T139), G189 (= G191)
binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G11 (= G15), G12 (= G16), G71 (≠ F67), G72 (= G68), R73 (≠ P69), S84 (≠ T85), T85 (≠ P86), L87 (vs. gap), I88 (vs. gap), N112 (≠ T111), D113 (= D112), G139 (= G138), T140 (= T139), G141 (= G140), I142 (≠ V141), G143 (= G142), 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), G139 (= G138), 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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D413 (≠ E13) 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.
R420 (≠ M20) mutation to 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.

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.

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
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2yhwA

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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
x
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), A114 (≠ V113), G142 (= G140), I143 (≠ V141), G144 (= G142), E158 (≠ G154), H161 (= H157), E170 (≠ R197)
binding phosphate ion: G140 (= G138), T141 (= T139)

Sites not aligning to the query:

binding beta-D-glucopyranose: 73, 74, 85, 86
binding phosphate ion: 10, 11, 13, 15, 32

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