SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011938377.1 NCBI__GCF_000016745.1:WP_011938377.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

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)
31% identity, 99% coverage: 1:355/358 of query aligns to 1:376/386 of P0A9J8

query
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P0A9J8

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R11 (= R11) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
R28 (= R28) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
K39 (= K39) mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
E52 (= E52) mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.
Q88 (≠ E87) 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
39% identity, 74% coverage: 94:357/358 of query aligns to 5:277/306 of 3mwbA

query
sites
3mwbA

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active site: T176 (= T259), F178 (= F261)
binding phenylalanine: D205 (= D285), H206 (≠ E286), L210 (= L290), N223 (= N303), L224 (= L304), S225 (= S305), R226 (≠ K306), S229 (= S309), F241 (= F321)

3mwbB The crystal structure of prephenate dehydratase in complex with l-phe from arthrobacter aurescens to 2.0a
39% identity, 74% coverage: 94:357/358 of query aligns to 5:274/303 of 3mwbB

query
sites
3mwbB

F

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active site: T176 (= T259), F178 (= F261)
binding magnesium ion: A155 (= A238), Q158 (≠ M241), L161 (= L244)
binding phenylalanine: D205 (= D285), H206 (≠ E286), L210 (= L290), N223 (= N303), L224 (= L304), S225 (= S305), R226 (≠ K306), I227 (= I307), Y236 (= Y319), F238 (= F321)

2qmxA The crystal structure of l-phe inhibited prephenate dehydratase from chlorobium tepidum tls (see paper)
36% identity, 73% coverage: 92:354/358 of query aligns to 4:273/278 of 2qmxA

query
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2qmxA

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active site: T169 (= T259), F171 (= F261)
binding phenylalanine: N204 (≠ D285), E205 (= E286), L209 (= L290), D222 (≠ N303), L223 (= L304), T224 (≠ S305), K225 (= K306), S228 (= S309), Y238 (= Y319), F240 (= F321)

6vh5D Crystal structure of prephenate dehydratase from brucella melitensis biovar abortus 2308 in complex with phenylalanine
31% identity, 74% coverage: 91:354/358 of query aligns to 8:276/282 of 6vh5D

query
sites
6vh5D

K

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F

Q

G

G

P

E

K

A

A

G

T

A

F

N

T

S

H

D

M

T

A

A

A

C

M

R

Q

N

Q

M

F

F

G

P

L

-

S

D

A

M

E

E

L

P

V

L

P

P

Q

C

K

P

S

T

I

F

P

E

A

D

V

A

F

F

E

N

E

A

V

V

E

E

K

T

G

G

R

A

A

A

L

D

Y

L

G

A

V

M

V

I

P

P

V

I

E

E

N

N

S

T

T

L

E

A

G

G

M

R

V

V

S

A

H

D

T

I

L

H

D

Y

M

L

F

L

M

P

E

L

S

A

E

D

L

M

K

H

V

I

N

V

A

G

E

E

V

Y

L

F

L

L

E

P

I

I

H

H

H

F

Y

Q

L

L

L

M

S

V

R

L

T

P

G

G

-

V

R

R

M

R

E

E

D

E

I

I

K

K

K

T

V

V

C

H

S

S

H

H

Q

I

Q

H

P

A

I

L

A

G

Q

Q

C

C

R

R

N

N

W

V

L

I

A

R

E

Q

N

N

L

-

P

-

N

G

V

W

P

K

V

G

V

V

D

I

V

A

A

G

S

D

T

T

A

A

V

G

A

A

Q

R

I

L

V

V

S

A

E

D

-

V

-

K

D

D

Y

R

T

S

A

M

A

A

I

L

A

A

S

P

E

R

L

L

A

A

S

D

M

L

Y

Y

D

G

L

L

K

D

V

I

V

L

R

E

E

E

R

N

I

V

E

E

D

D

Q

S

V

E

N

N

F

V

T

T

R

R

F

F

L

V

I

V

I

L

-

S

-

K

G

N

K

K

K

Q

M

W

A

A

E

A

K

R

S

P

G

E

D

N

D

D

K

E

-

R

-

I

-

V

T

T

S

T

L

F

M

V

F

F

S

R

V

V

K

R

D
x
N

E
x
V

V

P

G

A

I

A

L
|
L

Y

Y

H

K

M

A

L

L

E

G

P

G

F

F

A

A

K

T

R

N

G

G

I

V

N
|
N

L
x
M

S
x
T

K
|
K

I

L

E

E

S
|
S

R

Y

P

Q

L

L

K

G

K

R

A

F

W

I

E

A

Y
x
T

I

Q

F
|
F

F

Y

L

A

D

D

L

I

V

E

G

G

H

H

I

P

S

E

D

E

P

R

V

S

I

V

A

Q

E

L

A

A

V

L

Q

E

E

E

L

L

K

R

G

F

C

F

C

T

Q

K

F

E

V

V

K

R

V

I

L

L

G

G

S

V

Y

Y

binding phenylalanine: N207 (≠ D285), V208 (≠ E286), L212 (= L290), N225 (= N303), M226 (≠ L304), T227 (≠ S305), K228 (= K306), S231 (= S309), T241 (≠ Y319), F243 (= F321)

7am0B Gqqa- a novel type of quorum quenching acylases (see paper)
30% identity, 74% coverage: 92:355/358 of query aligns to 4:270/278 of 7am0B

query
sites
7am0B

V

I

A

A

F

F

F

Q

G

G

P

R

K

P

A

G

T

A

F

Y

T

S

H

D

M

L

A

A

A

C

M

R

Q

Q

-

A

Q

R

F

P

G

G

L

W

S

T

A

T

E

-

L

-

V

L

P

P

Q

C

K

Q

S

T

I

F

P

A

A

Q

V

T

F

I

E

A

V

V

E

H

K

D

G

G

R

R

A

A

L

E

Y

L

G

A

V

M

V

L

P

A

V

C

E

E

N

N

S

S

T

L

E

A

G

G

M

R

V

V

S

P

H

D

T

I

L

H

D

A

M

L

F

L

M

P

E

E

S

A

E

G

L

L

K

F

V

I

N

V

A

G

E

E

V

H

L

F

L

Q

E

R

I

V

H

E

H

H

Y

C

L

L

S

G

R

I

T

P

G

G

R

S

-

T

M

L

E

A

D

D

I

A

K

R

V

I

C

H

S

T

H

H

Q

P

Q

V

P

A

I

M

A

A

Q

Q

C

V

R

R

N

G

W

I

L

I

A

T

E

E

N

-

L

L

P

G

N

L

V

D

P

P

V

V

D

E

V

F

A

-

S

D

T

T

A

A

V

G

A

A

Q

E

I

M

V

V

S

R

E

E

-

W

-

G

D

R

Y

K

T

E

A

D

A

V

A

A

I

V

A

A

S

S

E

A

L

L

A

A

S

E

M

L

Y

N

D

G

L

L

K

E

V

I

V

L

R

R

E

R

R

N

I

V

E

E

D

D

Q

A

V

T

N

H

N

N

F

T

T

T

R

R

F

F

L

Y

I

I

I

A

G

S

K

R

M

P

A

A

E

T

K

L

S

P

G

P

D

P

D

G

K

P

-

G

-

F

-

M

T

T

S

T

L

L

M

L

F

F

S

R

V

V

K
x
N

D
x
N

E
x
Q

V
x
P

G

G

I

A

L
|
L

Y

Y

H

K

M

A

L

L

E

G

P

G

F

L

A

A

K

T

R

A

G

G

I

V

N
|
N

L
x
M

S
x
T

K
x
R

I

L

E

E

S

S

R

Y

P

M

L

L

K

E

K

G

K

S

A

F

W

S

E

A

Y
x
T

I

Q

F
|
F

F

L

L

M

D

D

L

V

V

E

G

G

H

H

I

P

S

E

D

A

P

P

V

P

I

L

A

A

E

R

A

A

V

L

Q

D

E

E

L

L

K

S

G

F

C

F

C

S

Q

E

F

Q

V

Q

K

E

V

I

L

L

G

G

S

V

Y

Y

P

P

binding phenylalanine: N199 (≠ K284), N200 (≠ D285), Q201 (≠ E286), P202 (≠ V287), L205 (= L290), N218 (= N303), M219 (≠ L304), T220 (≠ S305), R221 (≠ K306), T234 (≠ Y319), F236 (= F321)

3luyA Putative chorismate mutase from bifidobacterium adolescentis
25% identity, 74% coverage: 91:356/358 of query aligns to 5:285/326 of 3luyA

query
sites
3luyA

K

K

V

L

A

F

F

Y

F

L

G

G

P

P

K

Q

A

G

T

T

F

F

T

T

H

H

M

Q

A

A

M

V

-

N

-

A

-

Q

-

E

-

L

-

A

-

R

-

F

-

E

-

P

Q

Q

Q

G

F

F

G

-

L

-

S

-

A

-

E

D

L

L

V

M

P

P

Q

M

K

D

S

D

I

V

P

P

A

Q

V

I

F

L

E

D

E

A

V

A

E

Q

K

H

G

G

R

D

A

G

L

-

Y

W

G

G

V

I

V

V

P

A

V

W

E

E

N

N

S

N

T

V

E

E

G

G

M

Y

V

V

S

V

H

P

T

N

L

L

D

D

M

A

F

L

M

I

E

D

S

A

E

K

L

D

K

L

V

V

N

G

-

F

-

A

-

R

A

V

E

G

V

V

L

N

L

V

E

E

I

F

H

D

H

A

Y

Y

L

V

L

A

S

Q

R

G

T

A

G

D

R

P

M

A

E

E

D

-

I

A

K

R

K

I

V

A

C

T

S

A

H

H

Q

P

Q

H

P

G

I

L

A

A

Q

Q

C

C

R

K

N

R

W

F

L

I

A

A

E

E

N

H

L

R

P

L

N

S

V

T

P

Q

V

P

V

A

D

T

V

S

A

N

S

A

T

A

A

A

V

C

A

R

A

D

Q

L

I

I

V

P

S

G

E

E

D

I

Y

A

T

F

A

G

A

P

A

A

I

I

A

C

S

G

E

E

L

L

A

-

S

-

M

-

Y

Y

D

D

L

I

K

T

V

R

V

I

R

G

E

T

R

A

I

I

E

Q

D

D

Q

Y

V

Q

N

G

N

A

F

A

T
|
T

R

D

F

F

L

L

I

V

I

L

-

S

-

P

-

R

-

A

-

E

-

V

-

A

-

R

-

L

G

A

K

K

K

P

M

R

A

A

E

E

K

A

S

N

G

V

D

E

D

Y

K

E

T

S

S

V

L

L

-

T

M

L

F

I

S

P

V

L

K

V

D

T

E
x
G

V

P

G

G

I

V

L
|
L

Y

A

H

N

M

L

L

L

E

D

P

V

F

F

A

R

K

D

R

A

G

G

I

L

N

N

L

M

S

T

K

S

I

F

E

I

S

S

R

R

P

P

L

I

K

K

K

G

K

R

A

T

W

G

E

T

Y
|
Y

I

S

F
|
F

F

I

L

V

D

T

L

L

V

D

G

A

H

A

I

P

S

W

D

E

P

E

V

R

I

F

A

R

E

D

A

A

V

L

Q

V

E

E

L

I

K

A

G

E

C

H

C

G

Q

D

F

W

V

A

K

K

V

T

L

L

G

A

S

V

Y

Y

P

P

R

R

active site: T177 (= T259)
binding 3-phenylpyruvic acid: G215 (≠ E286), L219 (= L290), Y248 (= Y319), F250 (= F321)

5j6fA Crystal structure of dah7ps-cm complex from geobacillus sp. With prephenate (see paper)
35% identity, 23% coverage: 7:87/358 of query aligns to 4:84/352 of 5j6fA

query
sites
5j6fA

L

L

S

D

D

E

L

L

R

R

K

A

E

R

I

V

D

D

S

E

L

I

D

N

D

L

R

Q

M

L

L

L

E

K

L

L

L

I

N

N

E

E

R
|
R

A

G

S

R

R

L

V

V

I

Q

E

E

V
x
I

G

G

R

K

L

I

K
|
K

A

E

G

A

S

Q

K

G

S

T

D

H

F

R

H
x
Y

V
x
D

P

P

S

V

R
|
R

E

E

R

R

E

K

I
x
M

Y

L

E

D

R

L

L

I

I

S

A

E

Q

H

N

N

R

D

G

G

P

P

F

F

P

E

S

T

Q

S

A

T

L

L

K

Q

S

H

V

I

F

F

R

K

E

E

I

I

I

F

S

K

A

A

S

A

L

L

A

E

L

L

E

Q

binding prephenic acid: R25 (= R28), I32 (≠ V35), K36 (= K39), Y44 (≠ H47), D45 (≠ V48), R48 (= R51), M52 (≠ I55)

Sites not aligning to the query:

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

7alzA Gqqa- a novel type of quorum quenching acylases (see paper)
27% identity, 50% coverage: 177:355/358 of query aligns to 9:186/194 of 7alzA

query
sites
7alzA

S

G

R

R

T

P

G

G

R

A

M

Y

E

S

D

D

I

L

K

-

V

A

C

C

S

R

H

Q

Q

A

Q

R

P

P

I

-

A

-

Q

-

C

-

R

-

N

G

W

W

L

T

A

-

E

-

N

-

L

-

P

-

N

T

V

L

P

P

V

C

V

Q

D

T

V

F

A

A

S

Q

T

T

A

I

V

A

A

A

A

V

Q

H

I

D

V

G

S

R

E

A

D

E

Y

L

T

A

A

M

A

L

A

A

I

C

A

E

S

N

E

S

L

L

A

A

A

G

S

R

M

V

Y

P

D

D

-

I

-

H

-

A

-

L

-

P

-

E

-

A

-

G

L

L

K

F

V

I

V

V

R

G

E

E

R

H

I

F

E

Q

D

-

Q

R

V

V

N

H

N

N

F

T

T

T

R

R

F

F

L

Y

I

I

I

A

G

S

K

R

M

P

A

A

E

T

K

L

S

P

G

P

D

P

D

G

K

P

-

G

-

F

-

M

T

T

S

T

L

L

M

L

F

F

S

R

V

V

K

N

D

N

E
x
Q

V

P

G

G

I

A

L
|
L

Y

Y

H

K

M

A

L

L

E

G

P

G

F

L

A

A

K

T

R

A

G

G

I

V

N
|
N

L
x
M

S
x
T

K
x
R

I

L

E

E

S

S

R

Y

P

M

L

L

K

E

K

G

K

S

A

F

W

S

E

A

Y
x
T

I

Q

F
|
F

F

L

L

M

D

D

L

V

V

E

G

G

H

H

I

P

S

E

D

A

P

P

V

P

I

L

A

A

E

R

A

A

V

L

Q

D

E

E

L

L

K

S

G

F

C

F

C

S

Q

E

F

Q

V

Q

K

E

V

I

L

L

G

G

S

V

Y

Y

P

P

binding phenylalanine: Q117 (≠ E286), L121 (= L290), N134 (= N303), M135 (≠ L304), T136 (≠ S305), R137 (≠ K306), T150 (≠ Y319), F152 (= F321)

P39912 Protein AroA(G); EC 2.5.1.54; EC 5.4.99.5 from Bacillus subtilis (strain 168) (see paper)
36% identity, 22% coverage: 10:87/358 of query aligns to 9:86/358 of P39912

query
sites
P39912

L

L

R

R

K

Q

E

K

I

A

D

D

S

E

L

L

D

N

D

L

R

Q

M

I

L

L

E

K

L

L

L

I

N

N

E

E

R

R

A

G

S

N

R

V

V

V

I

K

E

E

V

I

G

G

R

K

L

A

K

K

A

E

G

A

S

Q

K

G

S

V

D

N

F

R

H

F

V

D

P

P

S

V

R

R

E

E

R

R

E

T

I

M

Y

L

E

N

R

N

L

I

I

I

A

E

Q

N

N

N

R

D

G

G

P

P

F

F

P

E

S

N

Q

S

A

T

L

I

K

Q

S

H

V

I

F

F

R

K

E

E

I

I

I

F

S

K

A

A

S

G

L

L

A

E

L

L

E

Q

Sites not aligning to the query:

2 modified: Phosphoserine

3nvtA 1.95 angstrom crystal structure of a bifunctional 3-deoxy-7- phosphoheptulonate synthase/chorismate mutase (aroa) from listeria monocytogenes egd-e (see paper)
38% identity, 22% coverage: 9:87/358 of query aligns to 1:74/345 of 3nvtA

query
sites
3nvtA

D

E

L

L

R

R

K

T

E

Q

I

V

D

D

S

Q

L

L

D

N

D

I

R

D

M

L

L

L

E

E

L

L

L

I

N

S

E

K

R

R

A

A

S

N

R

L

V

V

I

Q

E

E

V

I

G

G

R

K

L

I

K

K

A

G

G

-

S

-

K

R

S

F

D

D

F

-

H

-

V

-

P

P

S

L

R

R

E

E

R

R

E

E

I

M

Y

L

E

N

R

T

L

I

I

L

A

A

Q

A

N

N

R

E

G

G

P

P

F

F

P

E

S

D

Q

S

A

T

L

V

K

Q

S

K

V

L

F

F

R

K

E

E

I

I

I

F

S

K

A

A

S

G

L

L

A

E

L

L

E

Q

Sites not aligning to the query:

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

5gmuB Crystal structure of chorismate mutase like domain of bifunctional dahp synthase of bacillus subtilis in complex with chlorogenic acid (see paper)
36% identity, 23% coverage: 7:87/358 of query aligns to 5:85/87 of 5gmuB

query
sites
5gmuB

L

L

S

E

D

L

L

L

R

R

K

Q

E

K

I

A

D

D

S

E

L

L

D

N

D

L

R

Q

M

I

L

L

E

K

L

L

L

I

N

N

E

E

R
|
R

A

G

S

N

R

V

V

V

I

K

E

E

V

I

G

G

R

K

L

A

K

K

A

E

G

A

S

Q

K

G

S

V

D

N

F
x
R

H
x
F

V
x
D

P

P

S

V

R

R

E
|
E

R

R

E

T

I

M

Y

L

E

N

R

N

L

I

I

I

A

E

Q

N

N

N

R

D

G

G

P

P

F

F

P

E

S

N

Q

S

A

T

L

I

K

Q

S

H

V

I

F

F

R

K

E

E

I

I

I
x
F

S
x
K

A

A

S

G

L
|
L

A

E

L

L

E
x
Q

binding (1R,3R,4S,5R)-3-[3-[3,4-bis(oxidanyl)phenyl]propanoyloxy]-1,4,5-tris(oxidanyl)cyclohexane-1-carboxylic acid: R26 (= R28), R44 (≠ F46), F45 (≠ H47), D46 (≠ V48), E50 (= E52), F78 (≠ I80), K79 (≠ S81), L82 (= L84), Q85 (≠ E87)

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)
38% identity, 22% coverage: 10:87/358 of query aligns to 1:73/343 of 3tfcA

query
sites
3tfcA

L

L

R

R

K

T

E

Q

I

V

D

D

S

Q

L

L

D

N

D

I

R

D

M

L

L

L

E

E

L

L

L

I

N

S

E

K

R

R

A

A

S

N

R

L

V

V

I

Q

E

E

V

I

G

G

R

K

L

I

K

K

A

L

G

-

S

-

K

R

S

F

D

D

F

-

H

-

V

-

P

P

S

L

R

R

E

E

R

R

E

E

I

M

Y

L

E

N

R

T

L

I

I

L

A

A

Q

A

N

N

R

E

G

G

P

P

F

F

P

E

S

D

Q

S

A

T

L

V

K

Q

S

K

V

L

F

F

R

K

E

E

I

I

I

F

S

K

A

A

S

G

L

L

A

E

L

L

E

Q

Sites not aligning to the query:

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

P16331 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Mus musculus (Mouse) (see paper)
41% identity, 18% coverage: 278:343/358 of query aligns to 36:100/453 of P16331

query
sites
P16331

S

S

L

L

M

I

F

F

S

S

V

L

K

K

D

E

E

E

V

V

G

G

I

A

L

L

Y

A

H

K

M

V

L

L

E

R

P

L

F

F

A

E

K

E

R

N

G

E

I

I

N

N

L

L

S

T

K

H

I

I

E

E

S

S

R

R

P

P

-

S

-

R

L

L

K

N

K

K

K

D

A

E

W

Y

E

E

Y

F

I

F

F

T

F

Y

L

L

D

D

L

-

V

-

G

-

H

K

I

R

S

S

D

K

P

P

V

V

I

L

A

G

E

S

A

I

V

I

Q

K

E

S

L

L

K

R

G

N

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.

P04176 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Rattus norvegicus (Rat) (see 2 papers)
40% identity, 18% coverage: 278:343/358 of query aligns to 36:100/453 of P04176

query
sites
P04176

S

S

L

L

M

I

F

F

S

S

V

L

K

K

D

E

E

E

V

V

G

G

I

A

L

L

Y

A

H

K

M

V

L

L

E

R

P

L

F

F

A

E

K

E

R

N

G

D

I

I

N

N

L

L

S

T

K

H

I

I

E

E

S

S

R

R

P

P

-

S

-

R

L

L

K

N

K

K

K

D

A

E

W

Y

E

E

Y

F

I

F

F

T

F

Y

L

L

D

D

L

-

V

-

G

-

H

K

I

R

S

T

D

K

P

P

V

V

I

L

A

G

E

S

A

I

V

I

Q

K

E

S

L

L

K

R

G

N

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)
40% identity, 18% coverage: 278:343/358 of query aligns to 17:81/428 of 5fgjA

query
sites
5fgjA

S

S

L

L

M

I

F

F

S

S

V

L

K

K

D

E

E

E

V

V

G

G

I

A

L

L

Y

A

H

K

M

V

L

L

E

R

P

L

F

F

A

E

K

E

R

N

G

D

I

I

N

N

L

L

S

T

K

H

I

I

E

E

S

S

R

R

P

P

-

S

-

R

L

L

K

N

K

K

K

D

A

E

W

Y

E

E

Y

F

I

F

F

T

F

Y

L

L

D

D

L

-

V

-

G

-

H

K

I

R

S

T

D

K

P

P

V

V

I

L

A

G

E

S

A

I

V

I

Q

K

E

S

L

L

K

R

G

N

Sites not aligning to the query:

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

5fiiB Structure of a human aspartate kinase, chorismate mutase and tyra domain. (see paper)
50% identity, 13% coverage: 278:325/358 of query aligns to 3:50/78 of 5fiiB

query
sites
5fiiB

S

S

L

L

M

I

F

F

S

S

V

L

K

K

D
x
E

E
|
E

V

V

G

G

I

A

L
|
L

Y

A

H

K

M

V

L

L

E

R

P

L

F

F

A

E

K

E

R

N

G

D

I

V

N
|
N

L
|
L

S

T

K
x
H

I
|
I

E

E

S
|
S

R

R

P

P

L

S

K

R

K

L

K

K

A

K

W

D

E

E

Y
|
Y

I

E

F
|
F

F

F

L

T

D

H

L

L

binding phenylalanine: E10 (≠ D285), E11 (= E286), L15 (= L290), N28 (= N303), L29 (= L304), H31 (≠ K306), I32 (= I307), S34 (= S309), Y44 (= Y319), F46 (= F321)

P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
50% identity, 13% coverage: 278:325/358 of query aligns to 36:83/452 of P00439

query
sites
P00439

S

S

L

L

M

I

F
|
F

S

S

V
x
L

K
|
K

D

E

E

E

V

V

G
|
G

I
x
A

L
|
L

Y

A

H

K

M

V

L

L

E

R

P

L

F
|
F

A
x
E

K

E

R

N

G

D

I

V

N

N

L

L

S
x
T

K
x
H

I
|
I

E

E

S
|
S

R
|
R

P

P

L

S

K

R

K

L

K

K

A

K

W

D

E
|
E

Y

Y

I

E

F

F

L

T

D

H

L

L

F39 (= F281) to L: in HPA and PKU; haplotype 1; dbSNP:rs62642926; natural variant: Missing (in PKU; haplotypes 9,21)
L41 (≠ V283) to P: in PKU; mild; dbSNP:rs62642916
K42 (= K284) to I: in PKU; haplotype 21; dbSNP:rs62635346
G46 (= G288) to S: in PKU; haplotype 5; significantly reduces phenylalanine binding; dbSNP:rs74603784
A47 (≠ I289) to V: in non-PKU HPA; haplotype 4; significantly reduces phenylalanine binding; dbSNP:rs118203925
L48 (= L290) to S: in PKU; mild; haplotypes 3,4; dbSNP:rs5030841
F55 (= F297) to L: in HPA and PKU; does not affect oligomerization; results in loss of substrate activation; dbSNP:rs199475598
E56 (≠ A298) to D: in PKU; haplotype 10; dbSNP:rs199475567
TH 63:64 (≠ SK 305:306) natural variant: TH -> PN (in PKU; haplotype 1; abolishes phenylalanine binding)
I65 (= I307) 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 (= S309) to P: in PKU; haplotype 4; dbSNP:rs5030842
R68 (= R310) to S: in PKU; haplotype 1; dbSNP:rs76394784
E76 (= E318) to G: in non-PKU HPA; dbSNP:rs62507347

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA; S → P: in PKU; uncertain significance; dbSNP:rs62642946
84 D → Y: in PKU; haplotype 4; dbSNP:rs62514902
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

5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
44% identity, 14% coverage: 277:325/358 of query aligns to 5:56/400 of 5jk5A

query
sites
5jk5A

T

S

S

S

L

I

M

F

F

F

S

S

V

I

K

S

-

K

-

G

-

S

D

D

E

K

V

I

G

G

I

G

L

L

Y

L

H

E

M

Y

L

L

E

E

P

I

F

I

A

K

K

K

R

H

G

N

I

I

N

N

L

I

S

T

K

R

I

I

E

E

S

S

R

R

P

P

L

S

K

K

K

T

K

E

A

K

W

K

E

D

Y

Y

I

D

F

F

L

L

D

D

L

L

Sites not aligning to the query:

active site: 259, 264, 304, 323
binding fe (iii) ion: 259, 264, 304
binding 7,8-dihydrobiopterin: 221, 222, 223, 228, 229, 296, 299
binding piperazine-n,n'-bis(2-ethanesulfonic acid): 212, 271, 275, 374

5jk8A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
44% identity, 14% coverage: 277:325/358 of query aligns to 5:56/390 of 5jk8A

query
sites
5jk8A

T

S

S

S

L

I

M

F

F

F

S

S

V

I

K

S

-

K

-

G

-

S

D

D

E

K

V

I

G

G

I

G

L

L

Y

L

H

E

M

Y

L

L

E

E

P

I

F

I

A

K

K

K

R

H

G

N

I

I

N

N

L

I

S

T

K

R

I

I

E

E

S

S

R

R

P

P

L

S

K
|
K

K

T

K

E

A

K

W

K

E

D

Y

Y

I

D

F

F

L

L

D

D

L

L

binding piperazine-n,n'-bis(2-ethanesulfonic acid): K44 (= K313)

Sites not aligning to the query:

active site: 250, 255, 295, 314
binding fe (iii) ion: 250, 255, 295
binding 7,8-dihydrobiopterin: 214, 216, 219, 287, 290
binding norleucine: 242, 243, 250, 314, 315
binding piperazine-n,n'-bis(2-ethanesulfonic acid): 203, 226, 266, 365, 382

Query Sequence

>WP_011938377.1 NCBI__GCF_000016745.1:WP_011938377.1
MQKKKTLSDLRKEIDSLDDRMLELLNERASRVIEVGRLKAGSKSDFHVPSREREIYERLI
AQNRGPFPSQALKSVFREIISASLALEAPMKVAFFGPKATFTHMAAMQQFGLSAELVPQK
SIPAVFEEVEKGRALYGVVPVENSTEGMVSHTLDMFMESELKVNAEVLLEIHHYLLSRTG
RMEDIKKVCSHQQPIAQCRNWLAENLPNVPVVDVASTAVAAQIVSEDYTAAAIASELAAS
MYDLKVVRERIEDQVNNFTRFLIIGKKMAEKSGDDKTSLMFSVKDEVGILYHMLEPFAKR
GINLSKIESRPLKKKAWEYIFFLDLVGHISDPVIAEAVQELKGCCQFVKVLGSYPRAK

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