SitesBLAST

3tcyA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site (see paper)
48% identity, 80% coverage: 23:238/271 of query aligns to 29:244/277 of 3tcyA

query
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3tcyA

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active site: H132 (= H126), H137 (= H131), E178 (= E171), S197 (= S191)
binding cobalt (ii) ion: H132 (= H126), H137 (= H131), E178 (= E171)
binding phenylalanine: A152 (≠ I146), Y153 (= Y147), G156 (≠ L150), K159 (≠ N153), L169 (= L162), L172 (= L165)

Sites not aligning to the query:

binding phenylalanine: 248, 249, 250, 251, 252

1ltvA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized fe(iii) (see paper)
48% identity, 80% coverage: 23:238/271 of query aligns to 27:242/275 of 1ltvA

query
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1ltvA

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active site: H130 (= H126), H135 (= H131), E176 (= E171), S195 (= S191)
binding fe (iii) ion: H130 (= H126), H135 (= H131), E176 (= E171)

1ltzA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin (see paper)
48% identity, 80% coverage: 23:238/271 of query aligns to 29:244/274 of 1ltzA

query
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1ltzA

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active site: H132 (= H126), H137 (= H131), E178 (= E171), S197 (= S191)
binding fe (iii) ion: H132 (= H126), H137 (= H131), E178 (= E171)
binding 7,8-dihydrobiopterin: G94 (≠ A88), L95 (= L89), I96 (= I90), D98 (≠ F92), F101 (= F95), A170 (= A163), Y173 (= Y166)

P90986 Tyrosine 3-monooxygenase; Abnormal catecholamine distribution protein 2; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Caenorhabditis elegans (see 4 papers)
36% identity, 85% coverage: 16:244/271 of query aligns to 233:461/519 of P90986

query
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P90986

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Sites not aligning to the query:

35 modified: Phosphoserine; by PKA
276:519 mutation Missing: In e1112; spontaneously induces activation of the crh-1/CREB1 transcription factor in cholinergic SIA neurons in the absence and presence of food. Reduces swimming-induced paralysis in response to amphetamine. Defective male mating behavior.

5jk8A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
38% identity, 85% coverage: 3:233/271 of query aligns to 124:355/390 of 5jk8A

query
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5jk8A

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E

active site: H250 (= H126), H255 (= H131), E295 (= E171), S314 (= S191)
binding fe (iii) ion: H250 (= H126), H255 (= H131), E295 (= E171)
binding 7,8-dihydrobiopterin: G212 (≠ A88), L213 (= L89), L214 (≠ I90), A216 (≠ F92), F219 (= F95), S287 (≠ A163), Y290 (= Y166)
binding norleucine: R235 (= R111), Y242 (= Y118), T243 (≠ L119), H250 (= H126), E295 (= E171), G311 (= G188), S314 (= S191), S315 (= S192)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): C202 (≠ T78), T203 (= T79), R226 (≠ K102), P262 (= P138), D266 (≠ H142)

Sites not aligning to the query:

binding piperazine-n,n'-bis(2-ethanesulfonic acid): 44, 361, 365, 380, 382

5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
38% identity, 85% coverage: 3:233/271 of query aligns to 133:364/400 of 5jk5A

query
sites
5jk5A

K

R

E

E

I

I

A

A

H

K

T

I

A

A

P

S

Y

-

V

T

A

Y

R

K

S

H

A

G

D

D

D

E

S

I

G

P

Y

R

I

I

H

D

Y

Y

P

T

Q

E

E

E

H

I

D

K

I

T

W

W

S

G

Q

V

L

V

Y

Y

A

N

R

R

Q

L

A

K

V

E

K

L

L

F

P

P

G

T

R

N

A

A

C

C

K

H

E

Q

Y

H

L

A

Q

Y

G

I

L

F

A

P

A

L

L

L

-

E

-

Q

-

N

-

C

A

G

M

Y

P

S

K

P

D

D

R

N

I

I

P

P

Q

Q

L

L

A

Q

E

D

I

I

D

S

K

N

V

F

L

L

Q

Q

A

E

T

C

T
|
T

G

G

W

W

K

R

T

I

A

R

A

P

V
|
V

P

Q

A
x
G

L
|
L

I
x
L

S
|
S

F
x
A

G

R

R

D

F
|
F

F
x
L

E

N

L

G

L

L

A

A

N

F

K
x
R

E

V

F

F

P

H

V

A

A

T

T

Q

F

Y

I

I

R

R

R

H

K

P

E

S

E

V

F

P

D

L

Y

Y

L

T

Q

P

E

E

P

P

D

D

I

C

F

C

H
|
H

E

E

I

L

F

L

G

G

H
|
H

C

V

P

P

L

L

T

A

N

D

P
|
P

S

D

F

F

A

A

H
x
D

F

F

S

S

H

Q

I

E

Y

I

G

G

Q

L

L

A

G

S

L

I

N

G

A

A

S

S

K

D

E

E

D

D

R

I

V

Q

F

L

L

L

A
x
S

R

T

L

C

Y
|
Y

W

W

F

F

T

T

V

V

E
|
E

F

F

G

G

L

L

L

C

K

K

P

E

Q

G

D

D

G

T

E

-

L

I

C

R

I

A

Y

Y

G

G

G

A

G

G

I

I

L

L

S
|
S

S

S

P

T

G

G

E

E

T

M

L

E

Y

H

A

F

M

L

E

T

S

D

Q

K

V

A

P

-

E

K

R

K

K

L

P

P

F

F

D

N

L

P

L

F

D

D

V

A

L

C

R

N

T

T

P

E

Y

Y

R

P

I

I

D

T

I

T

M

F

Q

Q

P

P

I

L

Y

Y

V

V

I

A

E

E

active site: H259 (= H126), H264 (= H131), E304 (= E171), S323 (= S191)
binding fe (iii) ion: H259 (= H126), H264 (= H131), E304 (= E171)
binding 7,8-dihydrobiopterin: V219 (= V86), G221 (≠ A88), L222 (= L89), L223 (≠ I90), S224 (= S91), A225 (≠ F92), F228 (= F95), L229 (≠ F96), S296 (≠ A163), Y299 (= Y166)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T212 (= T79), R235 (≠ K102), P271 (= P138), D275 (≠ H142)

Sites not aligning to the query:

binding piperazine-n,n'-bis(2-ethanesulfonic acid): 44, 374, 391

P04177 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Rattus norvegicus (Rat) (see 7 papers)
35% identity, 91% coverage: 21:267/271 of query aligns to 222:464/498 of P04177

query
sites
P04177

Y

H

I

V

H

E

Y

Y

P

T

Q

A

E

E

H

I

D

A

I

T

W

W

S

K

Q

E

L

V

Y

Y

A

V

R

T

Q

L

A

K

V

G

K

L

L

Y

P

A

G

T

R

H

A

A

C

C

K

R

E

E

Y

H

L

L

Q

E

G

G

L

F

A

Q

A

L

L

L

-

E

-

R

-

Y

-

C

A

G

M

Y

P

R

K

E

D

D

R

S

I

I

P

P

Q

Q

L

L

A

E

E

D

I

V

D

S

K

R

V

F

L

L

Q

K

A

E

T

R

T

T

G

G

W

F

K

Q

T

L

A

R

A

P

V

V

P

A

A

G

L

L

I

L

S

S

F

A

G

R

R

D

F

F

F

L

E

A

L

S

L

L

A

A

N

F

K

R

E

V

F

F

P
x
Q

V

C

A

T

T

Q

F

Y

I

I

R

R

R

H

K

A

E

S

F

P

D

M

Y
x
H

L

S

Q

P

E

E

P

P

D

D

I

C

F

C

H
|
H

E

E

I

L

F

L

G

G

H
|
H

C

V

P

P

L

M

L

L

T

A

N

D

P

R

S

T

F

F

A

A

H

Q

F

F

S

S

H

Q

I

D

Y

I

G

G

Q

L

L

A

G

S

L

L

N

G

A

A

S

S

K

D

E

E

D

E

R

I

V

E

F

K

L

L

A

S

R

T

L

V

Y

Y

W
|
W

F

F

T

T

V

V

E
|
E

F

F

G

G

L

L

L

C

K

K

P

-

Q

Q

D

N

G

G

E

E

L

L

C

K

I

A

Y

Y

G

G

G

A

G

G

I

L

L

L

S

S

P

Y

G

G

E

E

T

L

L

L

Y

H

A

S

M

L

E

-

S

S

Q

E

V

E

P

P

E

E

R

V

K

R

P

A

F

F

D

D

L

P

L

D

D

T

V

A

L

A

R

V

T

Q

P

P

Y

Y

R

Q

I
x
D

D

Q

I

T

M

Y

Q

Q

P

P

I

V

Y

Y

Y

F

V

V

I

S

E

E

H

S

I

F

D

N

M

-

L

-

D

-

E

-

I

D

A

A

K

K

M

D

D

K

I

L

M

R

A

N

Y

Y

V

A

A

S

K

R

A

I

R

Q

Q

R

L

-

G

-

L

P

F

F

A

S

P

V

K

K

Y

F

P

D

P

P

K

Y

T

T

Q310 (≠ P105) mutation to H: Does not affect Vmax for phenylalanine. Increases KM for phenylalanine.
H323 (≠ Y118) mutation to Y: Does not affect Vmax for phenylalaninet. Increases KM for phenylalanine.
H331 (= H126) binding
H336 (= H131) binding
W372 (= W167) mutation to F: Does not affect substrate specificity.
E376 (= E171) binding
D425 (≠ I222) Important for substrate specificity; mutation to V: Shifts substrate specificity from tyrosine to phenylalanine.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
19 modified: Phosphoserine; by CaMK2
31 modified: Phosphoserine
40 modified: Phosphoserine; by CaMK2 and PKA

P17289 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Bos taurus (Bovine) (see 2 papers)
34% identity, 94% coverage: 14:267/271 of query aligns to 208:457/491 of P17289

query
sites
P17289

R

K

S

Q

A

G

D

D

D

P

S

I

G

P

Y

H

I

V

H

E

Y

Y

P

T

Q

A

E

E

H

T

D

A

I

T

W

W

S

K

Q

E

L

V

Y

Y

A

S

R

T

Q

L

A

R

V

G

K

L

L

Y

P

P

G

T

R

H

A

A

C

C

K

R

E

E

Y

H

L

L

Q

E

G

A

L

F

A

E

A

L

L

L

-

E

-

R

-

F

-

C

A

G

M

Y

P

R

K

E

D

D

R

R

I

I

P

P

Q

Q

L

L

A

E

E

D

I

V

D

S

K

R

V

F

L

L

Q

K

A

E

T

R

T

T

G

G

W

F

K

Q

T

L

A

R

A

P

V

A

P

A

A

G

L

L

I

L

S

S

F

A

G

R

R

D

F

F

F

L

E

A

L

S

L

L

A

A

N

F

K

R

E

V

F

F

P

Q

V

C

A

T

T

Q

F

Y

I

I

R

R

R

H

K

A

E

S

F

P

D

M

Y

H

L

S

Q

P

E

E

P

P

D

E

I

C

F

C

H

H

E

E

I

L

F

L

G

G

H

H

C

V

P

P

L

M

L

L

T

A

N

D

P

R

S

T

F

F

A

A

H

Q

F

F

S

S

H

Q

I

D

Y

I

G

G

Q

L

L

A

G

S

L

L

N

G

A

V

S

S

K

D

E

E

D

E

R

I

V

E

F

K

L

L

A

S

R

T

L

L

Y

Y

W

W

F

F

T

T

V

V

E

E

F

F

G

G

L

L

L

C

K

K

P

-

Q

Q

D

N

G

G

E

E

L

V

C

K

I

A

Y

Y

G

G

G

A

G

G

I

L

L

L

S

S

P

Y

G

G

E

E

T

L

L

L

Y

H

A

S

M

L

E

-

S

S

Q

E

V

E

P

P

E

E

R

I

K

R

P

A

F

F

D

D

L

P

L

D

D

A

V

A

L

A

R

V

T

Q

P

P

Y

Y

R

Q

I

D

D

Q

I

T

M

Y

Q

Q

P

P

I

V

Y

Y

Y

F

V

V

I

S

E

E

H

S

I

F

D

S

M

-

L

-

D

-

E

-

I

D

A

A

K

K

M

D

D

K

I

L

M

R

A

S

Y

Y

V

A

A

S

K

R

A

I

R

Q

Q

R

L

-

G

-

L

P

F

F

A

S

P

V

K

K

Y

F

P

D

P

P

K

Y

T

T

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
19 modified: Phosphoserine; by CaMK2
31 modified: Phosphoserine
40 modified: Phosphoserine; by CaMK2 and PKA

2tohA Tyrosine hydroxylase catalytic and tetramerization domains from rat (see paper)
35% identity, 91% coverage: 21:267/271 of query aligns to 60:302/336 of 2tohA

query
sites
2tohA

Y

H

I

V

H

E

Y

Y

P

T

Q

A

E

E

H

I

D

A

I

T

W

W

S

K

Q

E

L

V

Y

Y

A

V

R

T

Q

L

A

K

V

G

K

L

L

Y

P

A

G

T

R

H

A

A

C

C

K

R

E

E

Y

H

L

L

Q

E

G

G

L

F

A

Q

A

L

L

L

-

E

-

R

-

Y

-

C

A

G

M

Y

P

R

K

E

D

D

R

S

I

I

P

P

Q

Q

L

L

A

E

E

D

I

V

D

S

K

R

V

F

L

L

Q

K

A

E

T

R

T

T

G

G

W

F

K

Q

T

L

A

R

A

P

V
|
V

P

A

A

G

L
|
L

I
x
L

S

S

F

A

G

R

R

D

F
x
Y

F

L

E

A

L

S

L

L

A

A

N

F

K

R

E

V

F

F

P
x
Q

V

C

A
x
T

T

Q

F

Y

I

I

R

R

R

H

K

A

E

S

F

P

D

M

Y

H

L

S

Q

P

E

E

P
|
P

D

D

I

C

F

C

H
|
H

E
|
E

I

L

F

L

G

G

H
|
H

C

V

P

P

L

M

L

L

T

A

N

D

P

R

S

T

F

F

A

A

H

Q

F

F

S

S

H

Q

I

D

Y

I

G

G

Q

L

L

A

G

S

L

L

N

G

A

A

S

S

K

D

E

E

D

E

R

I

V

E

F

K

L

L

A
x
S

R

T

L

V

Y
|
Y

W

W

F

F

T

T

V

V

E
|
E

F

F

G

G

L

L

L

C

K

K

P

-

Q

Q

D

N

G

G

E

E

L

L

C

K

I

A

Y

Y

G

G

G

A

G

G

I

L

L

L

S
|
S

S

S

P

Y

G

G

E

E

T

L

L

L

Y

H

A

S

M

L

E

-

S

S

Q

E

V

E

P

P

E

E

R

V

K

R

P

A

F

F

D

D

L

P

L

D

D

T

V

A

L

A

R

V

T

Q

P

P

Y

Y

R

Q

I

D

D

Q

I

T

M

Y

Q

Q

P

P

I

V

Y

Y

Y

F

V

V

I

S

E

E

H

S

I

F

D

N

M

-

L

-

D

-

E

-

I

D

A

A

K

K

M

D

D

K

I

L

M

R

A

N

Y

Y

V

A

A

S

K

R

A

I

R

Q

Q

R

L

-

G

-

L

P

F

F

A

S

P

V

K

K

Y

F

P

D

P

P

K

Y

T

T

active site: H169 (= H126), H174 (= H131), E214 (= E171), S233 (= S191)
binding fe (iii) ion: H169 (= H126), H174 (= H131), E214 (= E171)
binding 7,8-dihydrobiopterin: V129 (= V86), L132 (= L89), L133 (≠ I90), Y138 (≠ F95), Q148 (≠ P105), T150 (≠ A107), P165 (= P122), E170 (= E127), S206 (≠ A163), Y209 (= Y166), E214 (= E171)

2xsnA Crystal structure of human tyrosine hydroxylase catalytic domain
35% identity, 94% coverage: 14:267/271 of query aligns to 53:302/335 of 2xsnA

query
sites
2xsnA

R

R

S

H

A

G

D

D

D

P

S

I

G

P

Y

R

I

V

H

E

Y

Y

P

T

Q

A

E

E

H

I

D

A

I

T

W

W

S

K

Q

E

L

V

Y

Y

A

T

R

T

Q

L

A

K

V

G

K

L

L

Y

P

A

G

T

R

H

A

A

C

C

K

G

E

E

Y

H

L

L

Q

E

G

A

L

F

A

A

A

L

L

L

-

E

-

R

-

F

-

S

A

G

M

Y

P

R

K

E

D

D

R

N

I

I

P

P

Q

Q

L

L

A

E

E

D

I

V

D

S

K

R

V

F

L

L

Q

K

A

E

T

R

T

T

G

G

W

F

K

Q

T

L

A

R

A

P

V

V

P

A

A

G

L

L

I

L

S

S

F

A

G

R

R

D

F

F

F

L

E

A

L

S

L

L

A

A

N

F

K

R

E

V

F

F

P

Q

V

C

A

T

T

Q

F

Y

I

I

R

R

R

H

K

A

E

S

F

P

D

M

Y

H

L

S

Q

P

E

E

P

P

D

D

I

C

F

C

H
|
H

E

E

I

L

F

L

G

G

H
|
H

C

V

P

P

L

M

L

L

T

A

N

D

P

R

S

T

F

F

A

A

H

Q

F

F

S

S

H

Q

I

D

Y

I

G

G

Q

L

L

A

G

S

L

L

N

G

A

A

S

S

K

D

E

E

D

E

R

I

V

E

F

K

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active site: H169 (= H126), H174 (= H131), E214 (= E171), S233 (= S191)
binding zinc ion: H169 (= H126), H174 (= H131), E214 (= E171)

6zvpD Atomic model of the em-based structure of the full-length tyrosine hydroxylase in complex with dopamine (residues 40-497) in which the regulatory domain (residues 40-165) has been included only with the backbone atoms (see paper)
35% identity, 94% coverage: 14:267/271 of query aligns to 175:424/458 of 6zvpD

query
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binding fe (iii) ion: H291 (= H126), H296 (= H131), E336 (= E171), A351 (≠ G187)
binding l-dopamine: F260 (= F95), F269 (= F104), P287 (= P122), H291 (= H126), H296 (= H131), Y331 (= Y166), E336 (= E171)

Sites not aligning to the query:

binding l-dopamine: 2

6zn2A Partial structure of tyrosine hydroxylase in complex with dopamine showing the catalytic domain and an alpha-helix from the regulatory domain involved in dopamine binding. (see paper)
35% identity, 94% coverage: 14:267/271 of query aligns to 52:301/335 of 6zn2A

query
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6zn2A

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binding fe (iii) ion: H168 (= H126), H173 (= H131), E213 (= E171)
binding l-dopamine: L132 (≠ I90), P164 (= P122), H168 (= H126), H173 (= H131), Y208 (= Y166), E213 (= E171)
binding : L132 (≠ I90), S133 (= S91), A134 (≠ F92), D198 (≠ K156), E199 (= E157), I201 (≠ R159), E202 (≠ V160), S205 (≠ A163), T206 (≠ R164), Y208 (= Y166), W209 (= W167), Y260 (= Y220), D262 (≠ I222)

P07101 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Homo sapiens (Human) (see 32 papers)
35% identity, 94% coverage: 14:267/271 of query aligns to 245:494/528 of P07101

query
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P07101

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H246 (≠ S15) to Y: in ARSEGS; loss of about 40% of tyrosine 3-monooxygenase activity
G247 (≠ A16) to S: in ARSEGS; loss of about 50% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs762304556
E259 (= E28) to G: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T276 (≠ G45) to P: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs28934581
P301 (= P66) to A: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
F309 (≠ V74) to S: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T314 (= T79) to M: in ARSEGS; parkinsonian symptoms in infancy; loss of about 80% of tyrosine 3-monooxygenase activity; dbSNP:rs121917764
R319 (≠ A84) to P: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
R328 (≠ G93) to W: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs1428589694
R337 (≠ K102) to H: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs28934580
C359 (≠ I124) to F: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs121917765
F375 (= F140) to L: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs763198914
A376 (= A141) to V: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
L387 (= L152) to M: in ARSEGS; no effect on tyrosine 3-monooxygenase activity
I394 (≠ R159) to T: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T399 (≠ R164) to M: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs1057520384
Q412 (= Q178) to K: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; reduced affinity for L-tyrosine; dbSNP:rs121917762
G414 (= G180) to R: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs370962049
G428 (= G194) to R: in ARSEGS; phenotype with prominent levodopa-responsive myoconus-dystonia (M-D); dbSNP:rs1264884607
R441 (≠ K208) to P: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs367874223
S467 (≠ H234) to G: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
P492 (= P265) to L: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs767635052
T494 (= T267) to M: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs45471299

Sites not aligning to the query:

19 modified: Phosphoserine; by CaMK2; S → C: found in a patient with ARSEGS; unknown pathological significance; dbSNP:rs766704202
62 modified: Phosphoserine; S→A: Affects subcellular localization. Accumulates mainly in the soma of the neuroblastoma cells.; S→E: Does not affect subcellular localization. Distributed throughout the soma and neurites.
71 modified: Phosphoserine; by CaMK2 and PKA; S→E: Suppresses feedback inhibition induced by dopamine. Suppresses feedback inhibition induced by dopamine; when associated with A-207.
112 V → M: in dbSNP:rs6356
207 C → Y: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; C→A: Suppresses the decrease in tyrosine 3-monooxygenase activity induced by NEM modification. Suppresses feedback inhibition induced by dopamine; when associated with E-71.
227 D → G: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
233 R → H: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs80338892
236 L → P: in ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and tyrosine 3-monooxygenase activity; rare mutation; dbSNP:rs121917763
241 A → T: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs1260455415
498 D → G: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs771351747
499 V → M: in dbSNP:rs1800033
510 L → Q: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity

P17752 Tryptophan 5-hydroxylase 1; Tryptophan 5-monooxygenase 1; EC 1.14.16.4 from Homo sapiens (Human) (see paper)
35% identity, 91% coverage: 22:268/271 of query aligns to 164:406/444 of P17752

query
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L

N

G

A

A

S

S

K

E

E

E

D

A

R

V

V

Q

F

K

L

L

A

A

R

T

L

C

Y

Y

W

F

F

F

T

T

V

V

E
|
E

F

F

G

G

L

L

L

C

K

K

P

-

Q

Q

D

D

G

G

E

Q

L

L

C

R

I

V

Y

F

G

G

G

A

G

G

I

L

L

L

S

S

P

I

G

S

E

E

T

L

L

K

Y

H

A

A

M

L

E

S

S

G

Q

H

V

A

P

-

E

K

R

V

K

K

P

P

F

F

D

D

L

P

L

K

D

I

V

T

L

C

R

K

T

Q

P

E

Y

C

R

L

I

I

D

T

I

T

M

F

Q

Q

P

D

I

V

Y

Y

Y

F

V

V

I

S

E

E

H

S

I

F

D

-

M

-

L

-

D

-

E

E

I

D

A

A

K

K

M

E

D

K

I

M

M

R

A

E

Y

F

V

T

A

K

K

T

A

I

R

K

Q

R

L

-

G

-

L

P

F

F

A

G

P

V

K

K

Y

Y

P

N

P

P

K

Y

T

T

K

R

H272 (= H126) binding
H277 (= H131) binding
E317 (= E171) binding

3e2tA The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan (see paper)
37% identity, 91% coverage: 22:268/271 of query aligns to 61:303/307 of 3e2tA

query
sites
3e2tA

I

I

H

E

Y

F

P

T

Q

E

E

E

H

I

D

K

I

T

W

W

S

G

Q

T

L

V

Y

Y

A

R

R

E

Q

L

A

N

V

K

K

L

L

Y

P

P

G

T

R

H

A

A

C

C

K

R

E

E

Y

Y

L

L

Q

K

G

N

L

L

A

P

A

L

L

L

-

T

-

K

-

Y

-

C

A

G

M

Y

P

R

K

E

D

D

R

N

I

I

P

P

Q

Q

L

L

A

E

E

D

I

V

D

S

K

R

V

F

L

L

Q

K

A

E

T

R

T

T

G

G

W

F

K

T

T

I

A

R

A

P

V

V

P

A

A

G

L
x
Y

I

L

S

S

F

P

G

R

R

D

F
|
F

F

L

E

A

L

G

L

L

A

A

N

F

K

R

E

V

F

F

P

H

V

C

A

T

T

Q

F

Y

I

V

R
|
R

R

H

K

S

E

S

E

D

F

P

D

L

Y
|
Y

L
x
T

Q
x
P

E
|
E

P
|
P

D

D

I

T

F

C

H
|
H

E
|
E

I

L

F

L

G

G

H
|
H

C

V

P

P

L

L

T

A

N

E

P

P

S

S

F

F

A

A

H

Q

F

F

S

S

H

Q

I

E

Y

I

G

G

Q

L

L

A

G

S

L

L

N

G

A

A

S

S

K

D

E

E

D

A

R

V

V

Q

F

K

L

L

A

A

R

T

L

C

Y

Y

W
x
F

F

F

T

T

V

V

E
|
E

F
|
F

G

G

L

L

L

C

K

K

P

-

Q

Q

D

E

G

G

E

Q

L

L

C

R

I

V

Y

Y

G

G

G

A

G
|
G

I

L

L

L

S
|
S

P

I

G

S

E

E

T

L

L

K

Y

H

A

S

M

L

E

-

S

S

Q

G

V

S

P

A

E

K

R

V

K

K