SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Ac3H11_1847 FitnessBrowser__acidovorax_3H11:Ac3H11_1847 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)

3tcyA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site (see paper)
55% identity, 89% coverage: 17:274/290 of query aligns to 2:259/277 of 3tcyA

query
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3tcyA

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active site: H132 (= H147), H137 (= H152), E178 (= E193), S197 (= S212)
binding cobalt (ii) ion: H132 (= H147), H137 (= H152), E178 (= E193)
binding phenylalanine: A152 (≠ R167), Y153 (= Y168), K159 (= K174), L169 (= L184), T248 (= T263), P250 (≠ A265), D251 (= D266), F252 (= F267)

1ltvA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized fe(iii) (see paper)
56% identity, 87% coverage: 22:274/290 of query aligns to 5:257/275 of 1ltvA

query
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1ltvA

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active site: H130 (= H147), H135 (= H152), E176 (= E193), S195 (= S212)
binding fe (iii) ion: H130 (= H147), H135 (= H152), E176 (= E193)

4etlA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum f258a mutation (see paper)
55% identity, 89% coverage: 17:274/290 of query aligns to 2:259/277 of 4etlA

query
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4etlA

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active site: H132 (= H147), H137 (= H152), E178 (= E193), S197 (= S212)
binding cobalt (ii) ion: H132 (= H147), H137 (= H152), E178 (= E193)

1ltzA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin (see paper)
55% identity, 89% coverage: 17:274/290 of query aligns to 2:256/274 of 1ltzA

query
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1ltzA

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active site: H132 (= H147), H137 (= H152), E178 (= E193), S197 (= S212)
binding fe (iii) ion: H132 (= H147), H137 (= H152), E178 (= E193)
binding 7,8-dihydrobiopterin: I96 (= I111), D98 (≠ E113), F101 (= F116), Y173 (= Y188)

2v27B Structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34h (see paper)
39% identity, 79% coverage: 43:272/290 of query aligns to 14:243/272 of 2v27B

query
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2v27B

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T

I

Y

M

Q

Q

Q

P

T

I

Y

Y

F

Y

V

M

I

L

D

T

S

K

F

V

E

S

Q

D

L

L

F

D

E

E

M

I

T

R

A

K

A

F

D

E

F

V

A

D

P

D

I

I

Y

M

E

E

active site: H119 (= H147), H124 (= H152), E164 (= E193), S183 (= S212)
binding fe (iii) ion: H119 (= H147), H124 (= H152), E164 (= E193)

5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
37% identity, 73% coverage: 46:258/290 of query aligns to 153:368/400 of 5jk5A

query
sites
5jk5A

Y

Y

T

T

D

E

A

E

D

E

H

I

D

K

T

T

Y

W

R

G

R

V

L

V

Y

Y

E

N

R

R

Q

L

R

K

A

E

L

L

L

F

P

P

G

T

L

N

A

A

S

C

Q

H

A

Q

F

H

I

A

D

Y

A

I

L

F

P

P

S

L

L

L

G

E

A

Q

S

N

-

C

-

G

-

Y

-

S

-

P

D

D

Q

N

I

I

P

P

R

Q

F

L

E

Q

E

D

V

I

N

S

E

N

R

F

L

L

Y

Q

K

E

A

C

T
|
T

G

G

W

W

E

R

L

I

V

R

G

P

V

V

P

Q

G
|
G

L
|
L

I
x
L

P

S

E

A

V

R

P

D

F
|
F

F
x
L

T

N

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

A

T

T

D

Q

W

Y

I

I

R

R

K

H

P

P

E

S

E

V

F

P

E

L

Y

Y

I

T

V

P

E

E

P

P

D

D

I

C

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

F

A

N

D

P
|
P

V

D

F

F

A

A

D
|
D

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

I

K

G

A

A

Q

S

G

D

L

-

G

E

S

D

C

I

E

Q

M

L

L

L

S
|
S

R

T

L

C

Y
|
Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

E

A

G

G

D

E

T

L

I

R

R

A

A

Y

Y

G

G

A

A

G

G

I

I

L

L

S
|
S

S

S

S

T

G

G

E

E

L

M

A

E

Y

H

S

F

V

L

Q

-

S

T

P

D

E

K

P

A

Q

K

R

K

I

L

P

P

L

F

A

N

L

P

E

F

R

D

T

A

M

C

R

N

T

T

R

E

Y

Y

K

P

I

I

D

T

T

T

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

Q

Q

K

active site: H259 (= H147), H264 (= H152), E304 (= E193), S323 (= S212)
binding fe (iii) ion: H259 (= H147), H264 (= H152), E304 (= E193)
binding 7,8-dihydrobiopterin: G221 (= G109), L222 (= L110), L223 (≠ I111), F228 (= F116), L229 (≠ F117), S296 (= S185), Y299 (= Y188)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T212 (= T100), P271 (= P159), D275 (= D163)

Sites not aligning to the query:

binding piperazine-n,n'-bis(2-ethanesulfonic acid): 374

5jk8A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
37% identity, 73% coverage: 46:258/290 of query aligns to 144:359/390 of 5jk8A

query
sites
5jk8A

Y

Y

T

T

D

E

A

E

D

E

H

I

D

K

T

T

Y

W

R

G

R

V

L

V

Y

Y

E

N

R

R

Q

L

R

K

A

E

L

L

L

F

P

P

G

T

L

N

A

A

S

C

Q

H

A

Q

F

H

I

A

D

Y

A

I

L

F

P

P

S

L

L

L

G

E

A

Q

S

N

-

C

-

G

-

Y

-

S

-

P

D

D

Q

N

I

I

P

P

R

Q

F

L

E

Q

E

D

V

I

N

S

E

N

R

F

L

L

Y

Q

K

E

A

C

T
|
T

G

G

W

W

E

R

L

I

V

R

G

P

V

V

P

Q

G

G

L

L

I
x
L

P

S

E
x
A

V

R

P

D

F
|
F

F

L

T

N

L

G

L

L

A

A

N

F

R
|
R

Q

V

F

F

P

H

V

A

T

T

D

Q

W

Y

I

I

R

R

K

H

P

P

E

S

E

V

F

P

E

L

Y
|
Y

I
x
T

V

P

E

E

P

P

D

D

I

C

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

F

A

N

D

P

P

V

D

F

F

A

A

D
|
D

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

I

K

G

A

A

Q

S

G

D

L

-

G

E

S

D

C

I

E

Q

M

L

L

L

S
|
S

R

T

L

C

Y
|
Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

E

A

G

G

D

E

T

L

I

R

R

A

A

Y

Y

G

G

A

A

G

G

I

I

L

L

S
|
S

S

T

G

G

E

E

L

M

A

E

Y

H

S

F

V

L

Q

-

S

T

P

D

E

K

P

A

Q

K

R

K

I

L

P

P

L

F

A

N

L

P

E

F

R

D

T

A

M

C

R

N

T

T

R

E

Y

Y

K

P

I

I

D

T

T

T

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

Q

Q

K

active site: H250 (= H147), H255 (= H152), E295 (= E193), S314 (= S212)
binding fe (iii) ion: H250 (= H147), H255 (= H152), E295 (= E193)
binding 7,8-dihydrobiopterin: L214 (≠ I111), A216 (≠ E113), F219 (= F116), S287 (= S185), Y290 (= Y188)
binding norleucine: Y242 (= Y139), T243 (≠ I140), H250 (= H147), S314 (= S212), S315 (= S213)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T203 (= T100), R226 (= R123), D266 (= D163)

Sites not aligning to the query:

binding piperazine-n,n'-bis(2-ethanesulfonic acid): 44, 365, 382

P04176 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Rattus norvegicus (Rat) (see 2 papers)
38% identity, 73% coverage: 46:256/290 of query aligns to 179:392/453 of P04176

query
sites
P04176

Y

Y

T

T

D

E

A

E

D

E

H

K

D

Q

T

T

Y

W

R

G

R

T

L

V

Y

F

E

R

R

T

Q

L

R

K

A

A

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

H

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

R

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I

L

P

S

E

S

V

R

P

D

F

F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

E

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

D

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

C

T

Q

R

E

Y

Y

K

S

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

H285 (= H147) binding
H290 (= H152) binding
E330 (= E193) binding

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA

5fgjA Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453 (see paper)
38% identity, 73% coverage: 46:256/290 of query aligns to 157:370/428 of 5fgjA

query
sites
5fgjA

Y

Y

T

T

D

E

A

E

D

E

H

K

D

Q

T

T

Y

W

R

G

R

T

L

V

Y

F

E

R

R

T

Q

L

R

K

A

A

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

H

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

R

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I

L

P

S

E

S

V

R

P

D

F

F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

E

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

D

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

C

T

Q

R

E

Y

Y

K

S

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

active site: H263 (= H147), H268 (= H152), E308 (= E193), S327 (= S212)
binding fe (iii) ion: H263 (= H147), H268 (= H152), E308 (= E193)

P16331 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Mus musculus (Mouse) (see paper)
37% identity, 73% coverage: 46:257/290 of query aligns to 179:393/453 of P16331

query
sites
P16331

Y

Y

T

T

D

E

A

E

D

E

H

R

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

R

R

T

Q

L

R

K

A

A

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

H

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

R

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I

L

P

S

E

S

V

R

P

D

F

F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F
|
F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H

H

D

E

L

L

F

L

G

G

H

H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

I

V

E

E

F

F

G

G

L

L

I

C

R

K

E

E

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

D

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

C

T

Q

R

E

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

F263 (= F125) mutation to S: Mutant mice have features of phenylketonuria.

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.

P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
36% identity, 73% coverage: 46:257/290 of query aligns to 179:393/452 of P00439

query
sites
P00439

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L
x
V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L
x
H

A

A

S

C

Q
x
Y

A

E

F

Y

I
x
N

D

H

A

I

L

F

P
|
P

S

L

L
|
L

G

E

A

K

-

Y

-

C

-
x
G

-

F

-

H

S
x
E

D
|
D

Q

N

I
|
I

P
|
P

R

Q

F

L

E

E

E

D

V
|
V

N

S

E

Q

R
x
F

L

L

Y

Q

K

T

A

C

T
|
T

G

G

W

F

E
x
R

L

L

V
x
R

G
x
P

V
|
V

P

A

G
|
G

L

L

I
x
L

P

S

E

S

V
x
R

P

D

F

F

F
x
L

T

G

L

G

L

L

A
|
A

N

F

R
|
R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I
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I

R
|
R

K

H

P

G

E
x
S

E

K

F
x
P

E
x
M

Y
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Y

I

T

V

P

E
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E

P
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P

D
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D

I
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I

F

C

H

H

D

E

L

L

F

L

G

G

H

H

V

V

P

P

L

L

L

F

F

S

N

D

P
x
R

V

S

F
|
F

A
|
A

D

Q

Y

F

V
x
S

Q

Q

R

E

Y
x
I

G

G

Q

L

G
x
A

G
x
S

L
|
L

K

G

A

A

Q
x
P

G

D

L

-

G

E

S

Y

C
x
I

E

E

M

K

L

L

S
x
A

R

T

L

I

Y

Y

W

W

Y

F

T

T

I

V

E

E

F
|
F

G

G

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L

I

C

R

K

E

Q

A

G

G
x
D

E

S

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R

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A
|
A

Y

Y

G

G

A
|
A

G

G

I

L

L
|
L

S
|
S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R
x
L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y
|
Y

K

T

I

V

D
x
T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F
x
Y

V
|
V

I

A

D
x
E

S

S

F

F

E

N

V190 (≠ L57) to A: in PKU; haplotype 3; dbSNP:rs62514919
H201 (≠ L68) to Y: in non-PKU HPA; haplotype 1; dbSNP:rs62517205
Y204 (≠ Q71) to C: in PKU; mild; haplotypes 3,4; dbSNP:rs62514927
N207 (≠ I74) to S: in PKU; severe; haplotype 4; dbSNP:rs62508721
P211 (= P78) to T: in PKU; haplotype 4; dbSNP:rs62514931
L213 (= L80) to P: in PKU; severe; dbSNP:rs62516109
G218 (vs. gap) to V: in PKU; haplotypes 1,2; dbSNP:rs62514933
E221 (≠ S83) to G: in PKU; haplotype 4; dbSNP:rs62514934
D222 (= D84) to V: in PKU; haplotypes 3,4; dbSNP:rs62507319
I224 (= I86) to M: in PKU; haplotype 4; dbSNP:rs199475576
P225 (= P87) to T: in PKU; haplotype 1; dbSNP:rs199475589
V230 (= V92) to I: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62516152
F233 (≠ R95) to L: in PKU; haplotypes 2,3; dbSNP:rs62517208
T238 (= T100) to P: in PKU; haplotype 4; dbSNP:rs199475577
R241 (≠ E103) to C: in non-PKU HPA and PKU; haplotype 34; dbSNP:rs76687508; to H: in PKU; haplotypes 1,5; dbSNP:rs62508730
R243 (≠ V105) to Q: in non-PKU HPA and PKU; haplotypes 4,7,9; dbSNP:rs62508588
P244 (≠ G106) to L: in PKU; haplotype 12; dbSNP:rs118203923
V245 (= V107) to A: in PKU, HPA and non-PKU HPA; haplotypes 3,7; dbSNP:rs796052017; to E: in PKU; haplotype 11; dbSNP:rs76212747
G247 (= G109) to V: in PKU; haplotype 4; dbSNP:rs199475579
L249 (≠ I111) to F: in PKU; haplotype 1; dbSNP:rs74503222
R252 (≠ V114) to G: in PKU; haplotype 7; dbSNP:rs5030847; to Q: in PKU; haplotype 1; dbSNP:rs62644503; to W: in PKU; haplotypes 1,6,7,8,42, 69; complete loss of activity; dbSNP:rs5030847
L255 (≠ F117) to S: in PKU; haplotype 36; dbSNP:rs62642930; to V: in PKU; haplotypes 18,21; dbSNP:rs62642931
A259 (= A121) to T: in PKU; haplotype 3; dbSNP:rs62642932; to V: in PKU; haplotypes 7,42; dbSNP:rs118203921
R261 (= R123) to Q: in HPA and PKU; mild; haplotypes 1,2,4,22, 24,28; dbSNP:rs5030849
I269 (= I131) to L: in non-PKU HPA; dbSNP:rs62508692
R270 (= R132) to S: in PKU; haplotype 1; dbSNP:rs62514951
S273 (≠ E135) to F: in PKU; haplotype 7; dbSNP:rs62514953
P275 (≠ F137) to L: in PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity; dbSNP:rs62508715
M276 (≠ E138) to V: in PKU; haplotype 4; dbSNP:rs62516149
Y277 (= Y139) to D: in PKU; haplotype 2; dbSNP:rs78655458
E280 (= E142) to K: in PKU; haplotypes 1,2,4,16,38; partial residual activity; dbSNP:rs62508698
P281 (= P143) to L: in PKU; haplotypes 1,4; dbSNP:rs5030851
D282 (= D144) to N: in PKU; haplotype 1; dbSNP:rs199475582
I283 (= I145) to F: in PKU; haplotype 21; dbSNP:rs62517168; to N: in PKU; severe; dbSNP:rs62508693; mutation to C: Loss of positive cooperativity and reduction of fold-activation by L-Phe preincubation.
R297 (≠ P159) to C: in PKU; haplotype 4; dbSNP:rs62642945
F299 (= F161) to C: in PKU; haplotype 8; dbSNP:rs62642933
A300 (= A162) to 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
S303 (≠ V165) to P: in PKU; haplotype 5; dbSNP:rs199475608
I306 (≠ Y168) to V: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642934
A309 (≠ G171) to D: in PKU; haplotype 7; dbSNP:rs62642935
S310 (≠ G172) to F: in PKU; haplotype 7; dbSNP:rs62642913; to Y: in HPA; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62642913
L311 (= L173) to P: in PKU; haplotypes 1,7,10; dbSNP:rs62642936
P314 (≠ Q176) to 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
I318 (≠ C181) to T: in PKU; partial loss of activity; dbSNP:rs62642918
A322 (≠ S185) to G: in PKU; haplotype 12; dbSNP:rs62514958; to T: in PKU; haplotype 1; dbSNP:rs62514957
F331 (= F194) to L: in PKU; haplotype 1; dbSNP:rs62517179
D338 (≠ G201) to Y: in PKU; haplotype 4; dbSNP:rs62516150
A342 (= A205) to T: in PKU; haplotype 5; dbSNP:rs62507282
A345 (= A208) to T: in PKU; haplotype 7; dbSNP:rs62516062
L348 (= L211) to V: in PKU; mild haplotype 9; dbSNP:rs62516092
S349 (= S212) to L: in PKU; severe; dbSNP:rs62507279; to P: in PKU; haplotypes 1,4; dbSNP:rs62508646
S350 (= S213) to T: in PKU; haplotype 2; dbSNP:rs62517183
L364 (≠ R228) natural variant: Missing (in PKU; haplotype 5; dbSNP:rs62516096)
Y377 (= Y241) to C: in PKU; haplotype 4; dbSNP:rs62642942
T380 (≠ D244) to M: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642937
Y387 (≠ F251) to H: in PKU; haplotype 1; dbSNP:rs62517194
V388 (= V252) to M: in PKU; haplotypes 1,4; dbSNP:rs62516101
E390 (≠ D254) to G: in PKU and non-PKU HPA; haplotype 4; dbSNP:rs5030856

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA; S → P: in PKU; uncertain significance; dbSNP:rs62642946
39 F → L: in HPA and PKU; haplotype 1; dbSNP:rs62642926; natural variant: Missing (in PKU; haplotypes 9,21)
41 L → P: in PKU; mild; dbSNP:rs62642916
42 K → I: in PKU; haplotype 21; dbSNP:rs62635346
46 G → S: in PKU; haplotype 5; significantly reduces phenylalanine binding; dbSNP:rs74603784
47 A → V: in non-PKU HPA; haplotype 4; significantly reduces phenylalanine binding; dbSNP:rs118203925
48 L → S: in PKU; mild; haplotypes 3,4; dbSNP:rs5030841
55 F → L: in HPA and PKU; does not affect oligomerization; results in loss of substrate activation; dbSNP:rs199475598
56 E → D: in PKU; haplotype 10; dbSNP:rs199475567
63:64 natural variant: TH -> PN (in PKU; haplotype 1; abolishes phenylalanine binding)
65 I → S: in PKU; results in disturbed oligomerization; results in loss of substrate activation; dbSNP:rs75193786; I → T: in PKU; haplotypes 1,5,9,21,B; abolishes phenylalanine binding; dbSNP:rs75193786; I → V: in HPA and PKU; dbSNP:rs199475643
67 S → P: in PKU; haplotype 4; dbSNP:rs5030842
68 R → S: in PKU; haplotype 1; dbSNP:rs76394784
76 E → G: in non-PKU HPA; dbSNP:rs62507347
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
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

6pahA Human phenylalanine hydroxylase catalytic domain dimer with bound l- dopa (3,4-dihydroxyphenylalanine) inhibitor (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 63:277/308 of 6pahA

query
sites
6pahA

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I

L

P

S

E

S

V

R

P

D

F

F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y
|
Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H169 (= H147), H174 (= H152), E214 (= E193), S233 (= S212)
binding 3,4-dihydroxyphenylalanine: H169 (= H147), H174 (= H152), Y209 (= Y188), E214 (= E193)
binding fe (iii) ion: H169 (= H147), H174 (= H152), E214 (= E193)

5pahA Human phenylalanine hydroxylase catalytic domain dimer with bound dopamine inhibitor (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 63:277/308 of 5pahA

query
sites
5pahA

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I

L

P

S

E

S

V

R

P

D

F

F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y
|
Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H169 (= H147), H174 (= H152), E214 (= E193), S233 (= S212)
binding fe (iii) ion: H169 (= H147), H174 (= H152), E214 (= E193)
binding l-dopamine: H169 (= H147), H174 (= H152), Y209 (= Y188), E214 (= E193)

4pahA Human phenylalanine hydroxylase catalytic domain dimer with bound nor- adrenaline inhibitor (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 63:277/308 of 4pahA

query
sites
4pahA

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I

L

P

S

E

S

V

R

P

D

F
|
F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y
|
Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H169 (= H147), H174 (= H152), E214 (= E193), S233 (= S212)
binding fe (iii) ion: H169 (= H147), H174 (= H152), E214 (= E193)
binding l-norepinephrine: F138 (= F116), H169 (= H147), H174 (= H152), Y209 (= Y188), E214 (= E193)

3pahA Human phenylalanine hydroxylase catalytic domain dimer with bound adrenaline inhibitor (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 63:277/308 of 3pahA

query
sites
3pahA

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L
|
L

I

L

P

S

E

S

V

R

P

D

F

F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y
|
Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H169 (= H147), H174 (= H152), E214 (= E193), S233 (= S212)
binding fe (iii) ion: H169 (= H147), H174 (= H152), E214 (= E193)
binding 4-[(1S)-1-hydroxy-2-(methylamino)ethyl]benzene-1,2-diol: L132 (= L110), H174 (= H152), Y209 (= Y188), E214 (= E193)

1mmtA Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (fe(ii)) complexed with tetrahydrobiopterin and norleucine (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 63:277/308 of 1mmtA

query
sites
1mmtA

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G
|
G

L
|
L

I
x
L

P

S

E
x
S

V

R

P

D

F
|
F

F
x
L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P
x
H

V

C

T

T

D

Q

W

Y

I

I

R
|
R

K

H

P

G

E

S

E

K

F

P

E

M

Y
|
Y

I
x
T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D
x
E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y
|
Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H169 (= H147), H174 (= H152), E214 (= E193), S233 (= S212)
binding fe (ii) ion: H169 (= H147), H174 (= H152), E214 (= E193)
binding 5,6,7,8-tetrahydrobiopterin: G131 (= G109), L132 (= L110), L133 (≠ I111), S135 (≠ E113), F138 (= F116), L139 (≠ F117), H148 (≠ P126), E170 (≠ D148), Y209 (= Y188), E214 (= E193)
binding norleucine: R154 (= R132), Y161 (= Y139), T162 (≠ I140), H169 (= H147), S233 (= S212), S234 (= S213)

4anpA Crystal structure of human phenylalanine hydroxylase in complex with a pharmacological chaperone (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 63:277/309 of 4anpA

query
sites
4anpA

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I

L

P

S

E

S

V

R

P

D

F
|
F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V
x
P

E

E

P
|
P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y

Y

W
|
W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H169 (= H147), H174 (= H152), E214 (= E193), S233 (= S212)
binding 5,6-dimethyl-3-(4-methyl-2-pyridinyl)-2-thioxo-2,3-dihydrothieno[2,3- d]pyrimidin-4(1h)-one: F138 (= F116), P163 (≠ V141), P165 (= P143), H169 (= H147), W210 (= W189), E214 (= E193)
binding fe (iii) ion: H169 (= H147), H174 (= H152), E214 (= E193)

1kw0A Catalytic domain of human phenylalanine hydroxylase (fe(ii)) in complex with tetrahydrobiopterin and thienylalanine (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 62:276/307 of 1kw0A

query
sites
1kw0A

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L
|
L

I
x
L

P

S

E
x
S

V

R

P

D

F
|
F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P
x
H

V

C

T

T

D

Q

W

Y

I

I

R
|
R

K

H

P

G

E

S

E

K

F

P

E

M

Y
|
Y

I
x
T

V

P

E
|
E

P
|
P

D

D

I

I

F

C

H
|
H

D
x
E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

I

V

E
|
E

F
|
F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H168 (= H147), H173 (= H152), E213 (= E193), S232 (= S212)
binding fe (ii) ion: H168 (= H147), H173 (= H152), E213 (= E193)
binding 5,6,7,8-tetrahydrobiopterin: L131 (= L110), L132 (≠ I111), S134 (≠ E113), F137 (= F116), H147 (≠ P126), E169 (≠ D148), E213 (= E193)
binding beta(2-thienyl)alanine: R153 (= R132), Y160 (= Y139), T161 (≠ I140), E163 (= E142), P164 (= P143), H168 (= H147), F214 (= F194), S232 (= S212), S233 (= S213)

1j8uA Catalytic domain of human phenylalanine hydroxylase fe(ii) in complex with tetrahydrobiopterin (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 62:276/307 of 1j8uA

query
sites
1j8uA

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I
x
L

P

S

E
x
S

V

R

P

D

F
|
F

F
x
L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S
x
A

R

T

L

I

Y

Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H168 (= H147), H173 (= H152), E213 (= E193), S232 (= S212)
binding fe (ii) ion: H168 (= H147), H173 (= H152), E213 (= E193)
binding 5,6,7,8-tetrahydrobiopterin: L132 (≠ I111), S134 (≠ E113), F137 (= F116), L138 (≠ F117), A205 (≠ S185)

1j8tA Catalytic domain of human phenylalanine hydroxylase fe(ii) (see paper)
36% identity, 73% coverage: 46:257/290 of query aligns to 62:276/307 of 1j8tA

query
sites
1j8tA

Y

Y

T

M

D

E

A

E

D

E

H

K

D

K

T

T

Y

W

R

G

R

T

L

V

Y

F

E

K

R

T

Q

L

R

K

A

S

L

L

L

Y

P

K

G

T

L

H

A

A

S

C

Q

Y

A

E

F

Y

I

N

D

H

A

I

L

F

P

P

S

L

L

L

G

E

A

K

-

Y

-

C

-

G

-

F

-

H

S

E

D

D

Q

N

I

I

P

P

R

Q

F

L

E

E

E

D

V

V

N

S

E

Q

R

F

L

L

Y

Q

K

T

A

C

T

T

G

G

W

F

E

R

L

L

V

R

G

P

V

V

P

A

G

G

L

L

I

L

P

S

E

S

V

R

P

D

F

F

F

L

T

G

L

G

L

L

A

A

N

F

R

R

Q

V

F

F

P

H

V

C

T

T

D

Q

W

Y

I

I

R

R

K

H

P

G

E

S

E

K

F

P

E

M

Y

Y

I

T

V

P

E

E

P

P

D

D

I

I

F

C

H
|
H

D

E

L

L

F

L

G

G

H
|
H

V

V

P

P

L

L

L

F

F

S

N

D

P

R

V

S

F

F

A

A

D

Q

Y

F

V

S

Q

Q

R

E

Y

I

G

G

Q

L

G

A

G

S

L

L

K

G

A

A

Q

P

G

D

L

-

G

E

S

Y

C

I

E

E

M

K

L

L

S

A

R

T

L

I

Y

Y

W

W

Y

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

A

G

G

D

E

S

L

I

R

K

A

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

S

F

G

G

E

E

L

L

A

Q

Y

Y

S

C

V

L

Q

-

S

S

P

E

E

K

P

P

Q

K

R

L

I

L

P

P

L

L

A

E

L

L

E

E

R

K

T

T

M

A

R

I

T

Q

R

N

Y

Y

K

T

I

V

D

T

T

E

Y

F

Q

Q

Q

P

T

L

Y

Y

F

Y

V

V

I

A

D

E

S

S

F

F

E

N

active site: H168 (= H147), H173 (= H152), E213 (= E193), S232 (= S212)
binding fe (ii) ion: H168 (= H147), H173 (= H152), E213 (= E193)

Query Sequence

>Ac3H11_1847 FitnessBrowser__acidovorax_3H11:Ac3H11_1847
VRKVMAAKEKKMGQAPVVYGQSTRPPRGDYSRANADYTCPQDYAAYTDADHDTYRRLYER
QRALLPGLASQAFIDALPSLGASDQIPRFEEVNERLYKATGWELVGVPGLIPEVPFFTLL
ANRQFPVTDWIRKPEEFEYIVEPDIFHDLFGHVPLLFNPVFADYVQRYGQGGLKAQGLGS
CEMLSRLYWYTIEFGLIREAGELRAYGAGILSSSGELAYSVQSPEPQRIPLALERTMRTR
YKIDTYQQTYFVIDSFEQLFEMTAADFAPIYERLRGLPEFAADEREAVAA

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