SitesBLAST

P0A9J8 Bifunctional chorismate mutase/prephenate dehydratase; Chorismate mutase-prephenate dehydratase; P-protein; EC 5.4.99.5; EC 4.2.1.51 from Escherichia coli (strain K12)
29% identity, 97% coverage: 8:352/356 of query aligns to 11:376/386 of P0A9J8

query
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P0A9J8

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R11 (= R8) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
R28 (= R25) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
K39 (= K36) mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
E52 (= E49) mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.
Q88 (≠ E84) mutation Q->A,E,K: Important decrease in catalytic efficiency and affinity.

3mwbA The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
36% identity, 75% coverage: 91:356/356 of query aligns to 5:279/306 of 3mwbA

query
sites
3mwbA

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active site: T176 (= T256), F178 (= F258)
binding phenylalanine: D205 (≠ K283), H206 (vs. gap), L210 (= L287), N223 (= N300), L224 (≠ M301), S225 (≠ T302), R226 (≠ K303), S229 (= S306), F241 (= F318)

3mwbB The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
36% identity, 75% coverage: 91:356/356 of query aligns to 5:276/303 of 3mwbB

query
sites
3mwbB

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active site: T176 (= T256), F178 (= F258)
binding magnesium ion: A155 (= A235), Q158 (≠ K238), L161 (= L241)
binding phenylalanine: D205 (≠ K283), H206 (vs. gap), L210 (= L287), N223 (= N300), L224 (≠ M301), S225 (≠ T302), R226 (≠ K303), I227 (= I304), Y236 (= Y316), F238 (= F318)

6vh5D Crystal structure of prephenate dehydratase from brucella melitensis biovar abortus 2308 in complex with phenylalanine
30% identity, 75% coverage: 85:351/356 of query aligns to 5:276/282 of 6vh5D

query
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6vh5D

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binding phenylalanine: N207 (≠ H282), V208 (≠ K283), L212 (= L287), N225 (= N300), M226 (= M301), T227 (= T302), K228 (= K303), S231 (= S306), T241 (≠ Y316), F243 (= F318)

7am0B Gqqa- a novel type of quorum quenching acylases (see paper)
31% identity, 74% coverage: 89:352/356 of query aligns to 4:270/278 of 7am0B

query
sites
7am0B

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L

T

V

L

P

P

V

C

R

Q

T

T

I

F

P

A

E

Q

V

T

F

I

D

A

N

A

V

V

E

H

R

D

G

G

R

R

M

A

G

E

F

L

G

A

I

M

V

L

P

A

V

C

E

E

N

N

S

S

L

L

E

A

G

G

V

R

V

V

N

P

H

D

T

I

L

H

D

A

T

L

F

L

V

P

T

E

S

A

H

G

L

L

K

F

I

I

S

V

G

G

E

E

I

H

F

F

L

Q

E

R

V

V

T

E

H

H

N

C

L

L

M

L

N

G

R

I

S

P

G

G

D

S

-

T

I

L

G

A

D

D

I

A

K

R

H

R

I

I

Y

H

S

T

H

H

I

P

Q

V

A

A

I

M

G

A

Q

Q

C

V

R

R

K

G

W

I

L

I

A

T

E

E

N

L

C

G

P

L

N

D

I

-

P

P

V

V

Q

V

E

E

V

F

E

D

S

-

T

T

A

A

K

G

A

A

E

E

M

M

-

V

-

R

-

E

-

W

A

G

S

R

R

K

D

E

D

D

S

-

T

-

A

V

A

A

I

V

A

A

S

S

E

A

M

L

A

A

V

A

L

E

K

L

Y

N

S

G

L

L

R

E

F

I

V

L

E

R

R

R

S

N

I

V

E

E

D

D

N

A

S

T

S

H

N

N

Y

T

T

T

R

R

F

F

L

Y

I

I

I

A

G

S

D

R

F

R

E

P

-

A

-

T

-

L

P

P

L

P

P

P

T

G

G

P

N

G

D

F

K

M

T

T

S

T

I

L

V

L

F

F

A

R

A

V

A
x
N

H
x
N

K
x
Q

A
x
P

G

G

S

A

L
|
L

Y

Y

E

K

V

A

L

L

S

G

I

G

F

L

A

A

R

T

K

A

N

G

I

V

N
|
N

M
|
M

T
|
T

K
x
R

I

L

E

E

S

S

R

Y

P

M

S

L

R

E

Q

G

K

S

A

F

W

S

E

A

Y
x
T

V

Q

F
|
F

F

L

V

M

D

D

L

V

D

E

G

G

H

H

K

P

D

E

D

A

E

P

P

P

I

L

A

A

E

R

A

A

L

L

N

D

E

E

L

L

I

S

E

F

H

F

T

S

A

E

F

Q

V

Q

K

E

V

I

L

L

G

G

S

V

Y

Y

P

P

binding phenylalanine: N199 (≠ A281), N200 (≠ H282), Q201 (≠ K283), P202 (≠ A284), L205 (= L287), N218 (= N300), M219 (= M301), T220 (= T302), R221 (≠ K303), T234 (≠ Y316), F236 (= F318)

3luyA Putative chorismate mutase from bifidobacterium adolescentis
28% identity, 76% coverage: 87:355/356 of query aligns to 4:287/326 of 3luyA

query
sites
3luyA

Q

R

K

K

V

L

G

F

Y

Y

L

L

G

G

P

P

E

Q

G

G

T

T

F

F

T

T

N

H

L

Q

A

A

-

V

-

N

-

A

-

Q

-

E

L

L

K

A

Q

R

F

F

G

E

L

P

S

Q

A

G

-

F

E

D

L

L

V

M

P

P

V

M

R

D

T

D

I

V

P

P

E

Q

V

I

F

L

D

D

N

A

V

A

E

Q

R

H

G

G

R

D

M

-

G

G

F

W

G

G

I

I

V

V

P

A

V

W

E

E

N

N

S

N

L

V

E

E

G

G

V

Y

V

V

N

V

H

P

T

N

L

L

D

D

T

A

F

L

V

I

T

D

S

A

H

K

L

D

K

L

I

V

S

G

G

-

E

-

I

-

F

F

L

A

E

R

V

V

T

G

H

V

N

N

L

V

-

E

-

F

-

D

-

A

-

Y

M

V

N

A

R

Q

S

G

G

A

D

D

I

P

G

A

D

E

I

A

K

R

H

I

I

A

Y

T

S

A

H

H

I

P

Q

H

A

G

I

L

G

A

Q

Q

C

C

R

K

K

R

W

F

L

I

A

A

E

E

N

H

C

-

P

-

N

R

I

L

P

S

V

T

Q

Q

E

P

V

A

E

T

S

S

T

N

A

A

K

A

A

A

A

-

E

-

M

-

A

-

S

C

R

R

D

D

D

L

S

I

T

P

A

G

A

E

I

I

A

A

S

F

E

G

M

P

A

A

V

I

L

C

K

G

-

E

-

L

Y

Y

S

D

L

I

R

T

F

R

V

I

E

G

R

T

S

A

I

I

E

Q

D

D

N

Y

S

Q

S

G

N

A

Y

A

T
|
T

R

D

F

F

L

L

I

V

I

L

G

S

D

P

-

R

-

A

-

E

-

V

-

A

-

R

-

L

F

A

E

K

P

P

L

R

P

A

T

E

G

A

N

N

-

V

-

E

-

Y

D

E

K

S

T

V

S

L

I

T

V

L

F

I

A

P

A

L

A

V

H

T

K
x
G

A

P

G

G

S

V

L
|
L

Y

A

E

N

V

L

L

L

S

D

I

V

F

F

A

R

R

D

K

A

N

G

I

L

N

N

M

M

T

T

K

S

I

F

E

I

S

S

R

R

P

P

S

I

R

K

Q

G

K

R

A

T

W

G

E

T

Y
|
Y

V

S

F
|
F

F

I

V

V

D

T

L

L

D

D

G

A

H

A

K

P

D

W

D

E

E

E

P

R

I

F

A

R

E

D

A

A

L

L

N

V

E

E

L

I

I

A

E

E

H

H

T

G

A

D

F

W

V

A

K

K

V

T

L

L

G

A

S

V

Y

Y

P

P

K

R

G

R

E

E

active site: T177 (= T256)
binding 3-phenylpyruvic acid: G215 (≠ K283), L219 (= L287), Y248 (= Y316), F250 (= F318)

5j6fA Crystal structure of dah7ps-cm complex from geobacillus sp. With prephenate (see paper)
39% identity, 23% coverage: 4:85/356 of query aligns to 4:85/352 of 5j6fA

query
sites
5j6fA

L

L

D

D

T

E

H

L

R

R

I

A

N

R

I

V

D

D

T

E

I

I

D

N

K

L

E

Q

I

L

L

L

E

K

L

L

L

I

N

N

K

E

R
|
R

A

G

K

R

E

L

A

V

M

Q

S

E

I
|
I

G

G

E

K

I

I

K
|
K

K

E

A

A

E

Q

G

G

A

T

P

H

L

R

Y
|
Y

V
x
D

P

P

S

V

R
|
R

E

E

K

R

K

K

I
x
M

F

L

E

D

R

L

L

I

T

S

S

E

I

H

N

N

S

D

G

G

P

P

F

F

P

E

N

T

D

S

A

T

L

L

K

Q

A

H

V

I

F

F

R

K

E

E

I

I

I

F

S

K

A

A

S

A

L

L

S

E

L

L

E

Q

E

E

binding prephenic acid: R25 (= R25), I32 (= I32), K36 (= K36), Y44 (= Y44), D45 (≠ V45), R48 (= R48), M52 (≠ I52)

Sites not aligning to the query:

binding manganese (ii) ion: 124, 294, 320, 331

5gmuB Crystal structure of chorismate mutase like domain of bifunctional dahp synthase of bacillus subtilis in complex with chlorogenic acid (see paper)
35% identity, 23% coverage: 3:85/356 of query aligns to 4:86/87 of 5gmuB

query
sites
5gmuB

E

E

L

L

D

E

T

L

H

L

R

R

I

Q

N

K

I

A

D

D

T

E

I

L

D

N

K

L

E

Q

I

I

L

L

E

K

L

L

L

I

N

N

K

E

R
|
R

A

G

K

N

E

V

A

V

M

K

S

E

I

I

G

G

E

K

I

A

K

K

K

E

A

A

E

Q

G

G

A

V

P

N

L
x
R

Y
x
F

V
x
D

P

P

S

V

R

R

E
|
E

K

R

K

T

I

M

F

L

E

N

R

N

L

I

T

I

S

E

I

N

N

N

S

D

G

G

P

P

F

F

P

E

N

N

D

S

A

T

L

I

K

Q

A

H

V

I

F

F

R

K

E

E

I

I

I
x
F

S
x
K

A

A

S

G

L
|
L

S

E

L

L

E
x
Q

E

E

binding (1R,3R,4S,5R)-3-[3-[3,4-bis(oxidanyl)phenyl]propanoyloxy]-1,4,5-tris(oxidanyl)cyclohexane-1-carboxylic acid: R26 (= R25), R44 (≠ L43), F45 (≠ Y44), D46 (≠ V45), E50 (= E49), F78 (≠ I77), K79 (≠ S78), L82 (= L81), Q85 (≠ E84)

P39912 Protein AroA(G); EC 2.5.1.54; EC 5.4.99.5 from Bacillus subtilis (strain 168) (see paper)
35% identity, 23% coverage: 3:85/356 of query aligns to 5:87/358 of P39912

query
sites
P39912

E

E

L

L

D

E

T

L

H

L

R

R

I

Q

N

K

I

A

D

D

T

E

I

L

D

N

K

L

E

Q

I

I

L

L

E

K

L

L

L

I

N

N

K

E

R

R

A

G

K

N

E

V

A

V

M

K

S

E

I

I

G

G

E

K

I

A

K

K

K

E

A

A

E

Q

G

G

A

V

P

N

L

R

Y

F

V

D

P

P

S

V

R

R

E

E

K

R

K

T

I

M

F

L

E

N

R

N

L

I

T

I

S

E

I

N

N

N

S

D

G

G

P

P

F

F

P

E

N

N

D

S

A

T

L

I

K

Q

A

H

V

I

F

F

R

K

E

E

I

I

I

F

S

K

A

A

S

G

L

L

S

E

L

L

E

Q

E

E

Sites not aligning to the query:

2 modified: Phosphoserine

7alzA Gqqa- a novel type of quorum quenching acylases (see paper)
32% identity, 28% coverage: 254:352/356 of query aligns to 85:186/194 of 7alzA

query
sites
7alzA

N

N

Y

T

T

T

R

R

F

F

L

Y

I

I

I

A

G

S

D

R

F

R

E

P

-

A

-

T

-

L

P

P

L

P

P

P

T

G

G

P

N

G

D

F

K

M

T

T

S

T

I

L

V

L

F

F

A

R

A

V

A

N

H

N

K
x
Q

A

P

G

G

S

A

L
|
L

Y

Y

E

K

V

A

L

L

S

G

I

G

F

L

A

A

R

T

K

A

N

G

I

V

N
|
N

M
|
M

T
|
T

K
x
R

I

L

E

E

S

S

R

Y

P

M

S

L

R

E

Q

G

K

S

A

F

W

S

E

A

Y
x
T

V

Q

F
|
F

F

L

V

M

D

D

L

V

D

E

G

G

H

H

K

P

D

E

D

A

E

P

P

P

I

L

A

A

E

R

A

A

L

L

N

D

E

E

L

L

I

S

E

F

H

F

T

S

A

E

F

Q

V

Q

K

E

V

I

L

L

G

G

S

V

Y

Y

P

P

binding phenylalanine: Q117 (≠ K283), L121 (= L287), N134 (= N300), M135 (= M301), T136 (= T302), R137 (≠ K303), T150 (≠ Y316), F152 (= F318)

3nvtA 1.95 angstrom crystal structure of a bifunctional 3-deoxy-7- phosphoheptulonate synthase/chorismate mutase (aroa) from listeria monocytogenes egd-e (see paper)
33% identity, 22% coverage: 8:85/356 of query aligns to 3:75/345 of 3nvtA

query
sites
3nvtA

R

R

I

T

N

Q

I

V

D

D

T

Q

I

L

D

N

K

I

E

D

I

L

L

L

E

E

L

L

L

I

N

S

K

K

R

R

A

A

K

N

E

L

A

V

M

Q

S

E

I

I

G

G

E

K

I

I

K

K

K

G

A

R

E

-

G

-

A

-

P

-

L

-

Y

F

V

D

P

P

S

L

R

R

E

E

K

R

K

E

I

M

F

L

E

N

R

T

L

I

T

L

S

A

I

A

N

N

S

E

G

G

P

P

F

F

P

E

N

D

D

S

A

T

L

V

K

Q

A

K

V

L

F

F

R

K

E

E

I

I

I

F

S

K

A

A

S

G

L

L

S

E

L

L

E

Q

E

E

Sites not aligning to the query:

binding manganese (ii) ion: 114, 284, 310, 321

3tfcA 1.95 angstrom crystal structure of a bifunctional 3-deoxy-7- phosphoheptulonate synthase/chorismate mutase (aroa) from listeria monocytogenes egd-e in complex with phosphoenolpyruvate (see paper)
33% identity, 22% coverage: 8:85/356 of query aligns to 2:74/343 of 3tfcA

query
sites
3tfcA

R

R

I

T

N

Q

I

V

D

D

T

Q

I

L

D

N

K

I

E

D

I

L

L

L

E

E

L

L

L

I

N

S

K

K

R

R

A

A

K

N

E

L

A

V

M

Q

S

E

I

I

G

G

E

K

I

I

K

K

K

L

A

R

E

-

G

-

A

-

P

-

L

-

Y

F

V

D

P

P

S

L

R

R

E

E

K

R

K

E

I

M

F

L

E

N

R

T

L

I

T

L

S

A

I

A

N

N

S

E

G

G

P

P

F

F

P

E

N

D

D

S

A

T

L

V

K

Q

A

K

V

L

F

F

R

K

E

E

I

I

I

F

S

K

A

A

S

G

L

L

S

E

L

L

E

Q

E

E

Sites not aligning to the query:

binding manganese (ii) ion: 113, 283, 309, 320
binding phosphoenolpyruvate: 137, 193, 196, 218, 248, 283

P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
45% identity, 15% coverage: 271:323/356 of query aligns to 32:84/452 of P00439

query
sites
P00439

N

N

D

G

K

A

T

I

S

S

I

L

V

I

F
|
F

A

S

A
x
L

A
x
K

H

E

K

E

A

V

G
|
G

S
x
A

L
|
L

Y

A

E

K

V

V

L

L

S

R

I

L

F
|
F

A
x
E

R

E

K

N

N

D

I

V

N

N

M

L

T
|
T

K
x
H

I
|
I

E

E

S
|
S

R
|
R

P

P

S

S

R

R

Q

L

K

K

A

K

W

D

E
|
E

Y

Y

V

E

F

F

V

T

D

H

L

L

D
|
D

F39 (= F278) to L: in HPA and PKU; haplotype 1; dbSNP:rs62642926; natural variant: Missing (in PKU; haplotypes 9,21)
L41 (≠ A280) to P: in PKU; mild; dbSNP:rs62642916
K42 (≠ A281) to I: in PKU; haplotype 21; dbSNP:rs62635346
G46 (= G285) to S: in PKU; haplotype 5; significantly reduces phenylalanine binding; dbSNP:rs74603784
A47 (≠ S286) to V: in non-PKU HPA; haplotype 4; significantly reduces phenylalanine binding; dbSNP:rs118203925
L48 (= L287) to S: in PKU; mild; haplotypes 3,4; dbSNP:rs5030841
F55 (= F294) to L: in HPA and PKU; does not affect oligomerization; results in loss of substrate activation; dbSNP:rs199475598
E56 (≠ A295) to D: in PKU; haplotype 10; dbSNP:rs199475567
TH 63:64 (≠ TK 302:303) natural variant: TH -> PN (in PKU; haplotype 1; abolishes phenylalanine binding)
I65 (= I304) to S: in PKU; results in disturbed oligomerization; results in loss of substrate activation; dbSNP:rs75193786; to T: in PKU; haplotypes 1,5,9,21,B; abolishes phenylalanine binding; dbSNP:rs75193786; to V: in HPA and PKU; dbSNP:rs199475643
S67 (= S306) to P: in PKU; haplotype 4; dbSNP:rs5030842
R68 (= R307) to S: in PKU; haplotype 1; dbSNP:rs76394784
E76 (= E315) to G: in non-PKU HPA; dbSNP:rs62507347
D84 (= D323) to Y: in PKU; haplotype 4; dbSNP:rs62514902

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA; S → P: in PKU; uncertain significance; dbSNP:rs62642946
87 S → R: in non-PKU HPA; haplotype 1; dbSNP:rs62516151
94 natural variant: Missing (in PKU; mild; haplotype 2)
98 L → S: in non-PKU HPA; dbSNP:rs62517167
104 A → D: in PKU; mild; haplotype 1; dbSNP:rs62642929
124 T → I: in PKU; haplotype 28; dbSNP:rs199475571
143 D → G: in PKU; haplotype 11; dbSNP:rs199475572
148 G → S: in PKU; haplotypes 1,2,7; dbSNP:rs80297647
151 D → H: in PKU; haplotypes 1,8; dbSNP:rs199475597
157 R → N: in PKU; severe; 5% activity; requires 2 nucleotide substitutions; dbSNP:rs1565853495
158 R → Q: in PKU; haplotypes 1,2,4,7,16, 28; dbSNP:rs5030843
161 F → S: in PKU; haplotype 4; dbSNP:rs79635844
164 I → T: in PKU; haplotype 1; dbSNP:rs199475595
170 H → Q: in PKU; does not affect oligomerization; dbSNP:rs199475652
171 G → A: in PKU; haplotype 1; dbSNP:rs199475596
173 P → T: in PKU; haplotype 4; dbSNP:rs199475574
174 I → T: in PKU; haplotype 1; dbSNP:rs138809906
176 R → L: in non-PKU HPA and PKU; dbSNP:rs74486803
177 V → L: in PKU; haplotype 6; dbSNP:rs199475602
178 E → G: in non-PKU HPA; dbSNP:rs77958223
190 V → A: in PKU; haplotype 3; dbSNP:rs62514919
201 H → Y: in non-PKU HPA; haplotype 1; dbSNP:rs62517205
204 Y → C: in PKU; mild; haplotypes 3,4; dbSNP:rs62514927
207 N → S: in PKU; severe; haplotype 4; dbSNP:rs62508721
211 P → T: in PKU; haplotype 4; dbSNP:rs62514931
213 L → P: in PKU; severe; dbSNP:rs62516109
218 G → V: in PKU; haplotypes 1,2; dbSNP:rs62514933
221 E → G: in PKU; haplotype 4; dbSNP:rs62514934
222 D → V: in PKU; haplotypes 3,4; dbSNP:rs62507319
224 I → M: in PKU; haplotype 4; dbSNP:rs199475576
225 P → T: in PKU; haplotype 1; dbSNP:rs199475589
230 V → I: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62516152
233 F → L: in PKU; haplotypes 2,3; dbSNP:rs62517208
238 T → P: in PKU; haplotype 4; dbSNP:rs199475577
241 R → C: in non-PKU HPA and PKU; haplotype 34; dbSNP:rs76687508; R → H: in PKU; haplotypes 1,5; dbSNP:rs62508730
243 R → Q: in non-PKU HPA and PKU; haplotypes 4,7,9; dbSNP:rs62508588
244 P → L: in PKU; haplotype 12; dbSNP:rs118203923
245 V → A: in PKU, HPA and non-PKU HPA; haplotypes 3,7; dbSNP:rs76212747; V → E: in PKU; haplotype 11; dbSNP:rs76212747
247 G → V: in PKU; haplotype 4; dbSNP:rs199475579
249 L → F: in PKU; haplotype 1; dbSNP:rs74503222
252 R → G: in PKU; haplotype 7; dbSNP:rs5030847; R → Q: in PKU; haplotype 1; dbSNP:rs62644503; R → W: in PKU; haplotypes 1,6,7,8,42, 69; complete loss of activity; dbSNP:rs5030847
255 L → S: in PKU; haplotype 36; dbSNP:rs62642930; L → V: in PKU; haplotypes 18,21; dbSNP:rs62642931
259 A → T: in PKU; haplotype 3; dbSNP:rs62642932; A → V: in PKU; haplotypes 7,42; dbSNP:rs118203921
261 R → Q: in HPA and PKU; mild; haplotypes 1,2,4,22, 24,28; dbSNP:rs5030849
269 I → L: in non-PKU HPA; dbSNP:rs62508692
270 R → S: in PKU; haplotype 1; dbSNP:rs62514951
273 S → F: in PKU; haplotype 7; dbSNP:rs62514953
275 P → L: in PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity; dbSNP:rs62508715
276 M → V: in PKU; haplotype 4; dbSNP:rs62516149
277 Y → D: in PKU; haplotype 2; dbSNP:rs78655458
280 E → K: in PKU; haplotypes 1,2,4,16,38; partial residual activity; dbSNP:rs62508698
281 P → L: in PKU; haplotypes 1,4; dbSNP:rs5030851
282 D → N: in PKU; haplotype 1; dbSNP:rs199475582
283 I → F: in PKU; haplotype 21; dbSNP:rs62517168; I → N: in PKU; severe; dbSNP:rs62508693; I→C: Loss of positive cooperativity and reduction of fold-activation by L-Phe preincubation.
297 R → C: in PKU; haplotype 4; dbSNP:rs62642945
299 F → C: in PKU; haplotype 8; dbSNP:rs62642933
300 A → S: in PKU and HPA; haplotype 1; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030853
303 S → P: in PKU; haplotype 5; dbSNP:rs199475608
306 I → V: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642934
309 A → D: in PKU; haplotype 7; dbSNP:rs62642935
310 S → F: in PKU; haplotype 7; dbSNP:rs62642913; S → Y: in HPA; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62642913
311 L → P: in PKU; haplotypes 1,7,10; dbSNP:rs62642936
314 P → S: in HPA; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs199475650
318 I → T: in PKU; partial loss of activity; dbSNP:rs62642918
322 A → G: in PKU; haplotype 12; dbSNP:rs62514958; A → T: in PKU; haplotype 1; dbSNP:rs62514957
331 F → L: in PKU; haplotype 1; dbSNP:rs62517179
338 D → Y: in PKU; haplotype 4; dbSNP:rs62516150
342 A → T: in PKU; haplotype 5; dbSNP:rs62507282
345 A → T: in PKU; haplotype 7; dbSNP:rs62516062
348 L → V: in PKU; mild haplotype 9; dbSNP:rs62516092
349 S → L: in PKU; severe; dbSNP:rs62507279; S → P: in PKU; haplotypes 1,4; dbSNP:rs62508646
350 S → T: in PKU; haplotype 2; dbSNP:rs62517183
364 natural variant: Missing (in PKU; haplotype 5; dbSNP:rs62516096)
377 Y → C: in PKU; haplotype 4; dbSNP:rs62642942
380 T → M: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642937
387 Y → H: in PKU; haplotype 1; dbSNP:rs62517194
388 V → M: in PKU; haplotypes 1,4; dbSNP:rs62516101
390 E → G: in PKU and non-PKU HPA; haplotype 4; dbSNP:rs5030856
395 A → P: in PKU; haplotype 1; dbSNP:rs62516103
403 A → V: in non-PKU HPA and PKU; haplotype 43; dbSNP:rs5030857
408 R → Q: in PKU; haplotypes 4,12; dbSNP:rs5030859; R → W: in HPA and PKU; haplotypes 1,2,4,5,13,34,41,44; most common mutation; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030858
410 F → S: in PKU; mild; dbSNP:rs62644475
413 R → P: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs79931499; R → S: in PKU; haplotype 1; dbSNP:rs62644467
414 Y → C: in HPA and PKU; haplotype 4; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030860
415 D → N: in PKU, HPA and non-PKU HPA; haplotype 1; dbSNP:rs62644499
417 Y → H: in PKU; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62644471
418 T → P: in PKU; haplotype 4; dbSNP:rs62644501

5fiiB Structure of a human aspartate kinase, chorismate mutase and tyra domain. (see paper)
47% identity, 14% coverage: 275:323/356 of query aligns to 3:51/78 of 5fiiB

query
sites
5fiiB

S

S

I

L

V

I

F

F

A

S

A

L

A

K

H
x
E

K
x
E

A

V

G

G

S

A

L
|
L

Y

A

E

K

V

V

L

L

S

R

I

L

F

F

A

E

R

E

K

N

N

D

I

V

N
|
N

M
x
L

T

T

K
x
H

I
|
I

E

E

S
|
S

R

R

P

P

S

S

R

R

Q

L

K

K

A

K

W

D

E

E

Y
|
Y

V

E

F
|
F

F

F

V

T

D

H

L

L

D

D

binding phenylalanine: E10 (≠ H282), E11 (≠ K283), L15 (= L287), N28 (= N300), L29 (≠ M301), H31 (≠ K303), I32 (= I304), S34 (= S306), Y44 (= Y316), F46 (= F318)

P04176 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Rattus norvegicus (Rat) (see 2 papers)
45% identity, 15% coverage: 271:323/356 of query aligns to 32:84/453 of P04176

query
sites
P04176

N

N

D

G

K

A

T

I

S

S

I

L

V

I

F

F

A

S

A

L

A

K

H

E

K

E

A

V

G

G

S

A

L

L

Y

A

E

K

V

V

L

L

S

R

I

L

F

F

A

E

R

E

K

N

N

D

I

I

N

N

M

L

T

T

K

H

I

I

E

E

S

S

R

R

P

P

S

S

R

R

Q

L

K

N

A

K

W

D

E

E

Y

Y

V

E

F

F

V

T

D

Y

L

L

D

D

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA
285 binding Fe cation
290 binding Fe cation
330 binding Fe cation

5fgjA Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453 (see paper)
45% identity, 15% coverage: 271:323/356 of query aligns to 13:65/428 of 5fgjA

query
sites
5fgjA

N

N

D

G

K

A

T

I

S

S

I

L

V

I

F

F

A

S

A

L

A

K

H

E

K

E

A

V

G

G

S

A

L

L

Y

A

E

K

V

V

L

L

S

R

I

L

F

F

A

E

R

E

K

N

N

D

I

I

N

N

M

L

T

T

K

H

I

I

E

E

S

S

R

R

P

P

S

S

R

R

Q

L

K

N

A

K

W

D

E

E

Y

Y

V

E

F

F

V

T

D

Y

L

L

D

D

Sites not aligning to the query:

active site: 263, 268, 308, 327
binding fe (iii) ion: 263, 268, 308

P16331 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Mus musculus (Mouse) (see paper)
43% identity, 17% coverage: 271:331/356 of query aligns to 32:90/453 of P16331

query
sites
P16331

N

N

D

G

K

A

T

V

S

S

I

L

V

I

F

F

A

S

A

L

A

K

H

E

K

E

A

V

G

G

S

A

L

L

Y

A

E

K

V

V

L

L

S

R

I

L

F

F

A

E

R

E

K

N

N

E

I

I

N

N

M

L

T

T

K

H

I

I

E

E

S

S

R

R

P

P

S

S

R

R

Q

L

K

N

A

K

W

D

E

E

Y

Y

V

E

F

F

V

T

D

Y

L

L

D

D

G

-

H

-

K

K

D

R

D

S

E

K

P

P

I

V

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
106 V→A: Mutant mice have mild features of phenylketonuria.
263 F→S: Mutant mice have features of phenylketonuria.

P70080 Tryptophan 5-hydroxylase 1; Tryptophan 5-monooxygenase 1; EC 1.14.16.4 from Gallus gallus (Chicken) (see paper)
32% identity, 26% coverage: 248:340/356 of query aligns to 2:78/445 of P70080

query
sites
P70080

I

I

E

E

D

D

N

N

S

K

S

E

N

N

Y

-

T

-

R

-

F

-

L

-

I

-

G

K

D

D

F

H

E

A

P

P

L

-

P

-

T

-

G

E

N

R

D

G

K

R

T

T

S

A

I

I

V

I

F

F

A

S

A

L

A

K

H

N

K

E

A

V

G

G

S

G

L

L

Y

V

E

K

V

A

L

L

S

K

I

L

F

F

A

Q

R

E

K

K

N

H

I

V

N

N

M

L

T

V

K

H

I

I

E

E

S

S

R

R

P

K

S

S

R

K

Q

R

K

R

A

N

W

S

E

E

Y

F

V

E

F

I

F

F

V

V

D

D

L

C

D

D

G

S

H

N

K

R

D

-

E

-

P

-

I

-

A

-

E

E

A

Q

L

L

N

N

E

E

L

I

I

F

E

Q

Sites not aligning to the query:

236 binding L-tryptophan
258 binding L-tryptophan
266 binding L-tryptophan
273 binding Fe cation
278 binding Fe cation
318 binding Fe cation
337 binding L-tryptophan
367 binding L-tryptophan

5ckxD Non-covalent complex of dahp synthase and chorismate mutase from mycobacterium tuberculosis with bound transition state analog and feedback effectors tyrosine and phenylalanine (see paper)
42% identity, 18% coverage: 3:67/356 of query aligns to 2:64/79 of 5ckxD

query
sites
5ckxD

E

E

L

I

D

D

T

T

H

L

R

R

I

E

N

E

I

I

D

D

T

R

I

L

D

D

K

A

E

E

I

I

L

L

E

A

L

L

L

V

N

K

K

R

R
|
R

A

A

K

E

E

V

A
x
S

M

K

S

A

I
|
I

G

G

E

K

I

A

K
x
R

K

M

A

A

E

S

G

G

A

G

P

T

L

R

Y

L

V

V

P

H

S

S

R
|
R

E
|
E

K

M

K

K

I

V

F

I

E

E

R

R

L

Y

T

S

S

E

I

L

N

-

S

-

G

G

P

P

F

D

P

G

N

K

D

D

binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: R24 (= R25), S28 (≠ A29), I31 (= I32), R35 (≠ K36), R47 (= R48), E48 (= E49)

Sites not aligning to the query:

binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: 70

Query Sequence

>WP_013012193.1 NCBI__GCF_000025725.1:WP_013012193.1
MKELDTHRINIDTIDKEILELLNKRAKEAMSIGEIKKAEGAPLYVPSREKKIFERLTSIN
SGPFPNDALKAVFREIISASLSLEEVQKVGYLGPEGTFTNLAALKQFGLSAELVPVRTIP
EVFDNVERGRMGFGIVPVENSLEGVVNHTLDTFVTSHLKISGEIFLEVTHNLMNRSGDIG
DIKHIYSHIQAIGQCRKWLAENCPNIPVQEVESTAKAAEMASRDDSTAAIASEMAVLKYS
LRFVERSIEDNSSNYTRFLIIGDFEPLPTGNDKTSIVFAAAHKAGSLYEVLSIFARKNIN
MTKIESRPSRQKAWEYVFFVDLDGHKDDEPIAEALNELIEHTAFVKVLGSYPKGEK

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