SitesBLAST

3tcyA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site (see paper)
44% identity, 86% coverage: 17:242/264 of query aligns to 22:247/277 of 3tcyA

query
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3tcyA

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active site: H132 (= H127), H137 (= H132), E178 (= E174), S197 (= S193)
binding cobalt (ii) ion: H132 (= H127), H137 (= H132), E178 (= E174)
binding phenylalanine: A152 (≠ D147), Y153 (≠ L148), K159 (≠ A152), L169 (= L165)

Sites not aligning to the query:

binding phenylalanine: 248, 250, 251, 252

1ltvA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized fe(iii) (see paper)
44% identity, 86% coverage: 17:242/264 of query aligns to 20:245/275 of 1ltvA

query
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1ltvA

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active site: H130 (= H127), H135 (= H132), E176 (= E174), S195 (= S193)
binding fe (iii) ion: H130 (= H127), H135 (= H132), E176 (= E174)

1ltzA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin (see paper)
44% identity, 86% coverage: 17:242/264 of query aligns to 22:247/274 of 1ltzA

query
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1ltzA

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active site: H132 (= H127), H137 (= H132), E178 (= E174), S197 (= S193)
binding fe (iii) ion: H132 (= H127), H137 (= H132), E178 (= E174)
binding 7,8-dihydrobiopterin: I96 (= I91), D98 (= D93), F101 (= F96), Y173 (= Y169)

2v27B Structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34h (see paper)
40% identity, 81% coverage: 26:239/264 of query aligns to 19:230/272 of 2v27B

query
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2v27B

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active site: H119 (= H127), H124 (= H132), E164 (= E174), S183 (= S193)
binding fe (iii) ion: H119 (= H127), H124 (= H132), E164 (= E174)

P04177 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Rattus norvegicus (Rat) (see 7 papers)
34% identity, 85% coverage: 25:248/264 of query aligns to 225:454/498 of P04177

query
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P04177

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Q310 (≠ P106) mutation to H: Does not affect Vmax for phenylalanine. Increases KM for phenylalanine.
H323 (≠ Y119) mutation to Y: Does not affect Vmax for phenylalaninet. Increases KM for phenylalanine.
H331 (= H127) binding
H336 (= H132) binding
W372 (= W170) mutation to F: Does not affect substrate specificity.
E376 (= E174) binding
D425 (≠ K223) 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

P90986 Tyrosine 3-monooxygenase; Abnormal catecholamine distribution protein 2; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Caenorhabditis elegans (see 4 papers)
35% identity, 81% coverage: 22:235/264 of query aligns to 238:453/519 of P90986

query
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P90986

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S

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.

2tohA Tyrosine hydroxylase catalytic and tetramerization domains from rat (see paper)
34% identity, 85% coverage: 25:248/264 of query aligns to 63:292/336 of 2tohA

query
sites
2tohA

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active site: H169 (= H127), H174 (= H132), E214 (= E174), S233 (= S193)
binding fe (iii) ion: H169 (= H127), H174 (= H132), E214 (= E174)
binding 7,8-dihydrobiopterin: V129 (= V87), L132 (= L90), L133 (≠ I91), Y138 (≠ F96), P165 (= P123), E170 (≠ D128), Y209 (= Y169)

P17289 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Bos taurus (Bovine) (see 2 papers)
34% identity, 80% coverage: 25:236/264 of query aligns to 218:431/491 of P17289

query
sites
P17289

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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

P07101 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Homo sapiens (Human) (see 32 papers)
33% identity, 80% coverage: 25:236/264 of query aligns to 255:468/528 of P07101

query
sites
P07101

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Y

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x
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E259 (≠ N29) to G: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T276 (≠ N46) to P: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs28934581
P301 (≠ A67) to A: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
F309 (≠ I75) to S: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T314 (= T80) to M: in ARSEGS; parkinsonian symptoms in infancy; loss of about 80% of tyrosine 3-monooxygenase activity; dbSNP:rs121917764
R319 (≠ Q85) to P: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
R328 (≠ D94) to W: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs1428589694
R337 (≠ K103) to H: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs28934580
C359 (≠ M125) to F: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs121917765
F375 (≠ Y141) 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 (≠ V142) to V: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
L387 (= L153) to M: in ARSEGS; no effect on tyrosine 3-monooxygenase activity
I394 (= I162) to T: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
T399 (≠ R167) to M: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs1057520384
Q412 (≠ E180) to K: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; reduced affinity for L-tyrosine; dbSNP:rs121917762
G414 (= G182) to R: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs370962049
G428 (= G196) to R: in ARSEGS; phenotype with prominent levodopa-responsive myoconus-dystonia (M-D); dbSNP:rs1264884607
R441 (= R209) to P: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs367874223
S467 (= S235) to G: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity

Sites not aligning to the query:

19 modified: Phosphoserine; by CaMK2; S → C: found in a patient with ARSEGS; uncertain 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
246 H → Y: in ARSEGS; loss of about 40% of tyrosine 3-monooxygenase activity
247 G → S: in ARSEGS; loss of about 50% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs762304556
492 P → L: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs767635052
494 T → M: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs45471299
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

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)
33% identity, 80% coverage: 25:236/264 of query aligns to 185:398/458 of 6zvpD

query
sites
6zvpD

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D

D

L

I

S

G

G

L

I

A

A

S

L

L

K

G

Y

A

I

S

D

D

D

E

K

E

W

-

A

-

I

I

H

E

L

K

L

L

S

S

R

T

I

L

Y
|
Y

W

W

F

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

N

N

G

G

A

E

L

V

K

K

I

A

Y

Y

G

G

A
|
A

G

G

I

L

L

L

S

S

A

Y

G

G

E

E

T

L

K

L

F

H

S

C

L

L

S

S

D

E

P

P

E

E

H

I

R

R

D

A

Y

F

D

D

V

P

R

E

S

A

I

A

M

A

Q

V

T

Q

P

P

Y

Y

W

Q

K

D

D

Q

K

T

F

Y

Q

Q

D

S

K

V

Y

Y

Y

F

V

V

I

S

E

E

S

S

Y

F

binding fe (iii) ion: H291 (= H127), H296 (= H132), E336 (= E174), A351 (= A189)
binding l-dopamine: P287 (= P123), H291 (= H127), H296 (= H132), Y331 (= Y169), E336 (= E174)

Sites not aligning to the query:

binding l-dopamine: 2

2xsnA Crystal structure of human tyrosine hydroxylase catalytic domain
33% identity, 80% coverage: 25:236/264 of query aligns to 63:276/335 of 2xsnA

query
sites
2xsnA

Y

Y

T

T

E

A

E

E

N

E

F

I

A

A

V

T

W

W

K

K

T

E

L

V

Y

Y

E

T

R

T

Q

L

I

K

V

G

N

L

L

Y

P

A

N

T

A

H

A

A

S

C

K

G

A

E

Y

H

L

L

E

E

G

A

I

F

K

A

E

L

I

L

-

E

-

R

-

F

-

S

N

G

F

Y

T

R

A

E

D

D

R

N

I

I

A

P

N

Q

F

L

S

E

E

D

V

V

N

S

Q

R

I

F

L

L

S

K

K

E

S

R

T

T

G

G

W

F

G

Q

V

L

Q

R

V

P

V

V

P

A

G

G

L

L

I

L

D

S

D

A

D

R

L

D

F

F

F

L

G

A

L

S

L

L

N

A

H

F

K

R

R

V

F

F

P

Q

S

C

S

T

T

Q

W

Y

L

I

R

R

K

H

M

A

E

S

Q

S

L

P

D

M

Y

H

L

S

E

P

E

E

P

P

D

D

M

C

F

C

H
|
H

D

E

A

L

F

L

A

G

H
|
H

M

V

P

P

M

M

L

L

T

A

N

D

Q

R

P

T

Y

F

V

A

D

Q

F

F

L

S

Q

Q

D

D

L

I

S

G

G

L

I

A

A

S

L

L

K

G

Y

A

I

S

D

D

D

E

K

E

W

-

A

-

I

I

H

E

L

K

L

L

S

S

R

T

I

L

Y

Y

W

W

F

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

N

N

G

G

A

E

L

V

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

A

Y

G

G

E

E

T

L

K

L

F

H

S

C

L

L

S

S

D

E

P

P

E

E

H

I

R

R

D

A

Y

F

D

D

V

P

R

E

S

A

I

A

M

A

Q

V

T

Q

P

P

Y

Y

W

Q

K

D

D

Q

K

T

F

Y

Q

Q

D

S

K

V

Y

Y

Y

F

V

V

I

S

E

E

S

S

Y

F

active site: H169 (= H127), H174 (= H132), E214 (= E174), S233 (= S193)
binding zinc ion: H169 (= H127), H174 (= H132), E214 (= E174)

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)
33% identity, 80% coverage: 25:236/264 of query aligns to 62:275/335 of 6zn2A

query
sites
6zn2A

Y

Y

T

T

E

A

E

E

N

E

F

I

A

A

V

T

W

W

K

K

T

E

L

V

Y

Y

E

T

R

T

Q

L

I

K

V

G

N

L

L

Y

P

A

N

T

A

H

A

A

S

C

K

G

A

E

Y

H

L

L

E

E

G

A

I

F

K

A

E

L

I

L

-

E

-

R

-

F

-

S

N

G

F

Y

T

R

A

E

D

D

R

N

I

I

A

P

N

Q

F

L

S

E

E

D

V

V

N

S

Q

R

I

F

L

L

S

K

K

E

S

R

T

T

G

G

W

F

G

Q

V

L

Q

R

V

P

V

V

P

A

G

G

L

L

I

L

D

S

D
x
A

D

R

L

D

F

F

F

L

G

A

L

S

L

L

N

A

H

F

K

R

R

V

F

F

P

Q

S

C

S

T

T

Q

W

Y

L

I

R

R

K

H

M

A

E

S

Q

S

L

P

D

M

Y

H

L

S

E

P

E

E

P
|
P

D

D

M

C

F

C

H
|
H

D

E

A

L

F

L

A

G

H
|
H

M

V

P

P

M

M

L

L

T

A

N

D

Q

R

P

T

Y

F

V

A

D

Q

F

F

L

S

Q

Q

D

D

L

I

S

G

G

L

I

A

A

S

L

L

K

G

Y

A

I

S

D

D

D

E

K

E

W

-

A

-

I

I

H
x
E

L

K

L

L

S
|
S

R

T

I

L

Y
|
Y

W
|
W

F

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

Q

N

N

G

G

A

E

L

V

K

K

I

A

Y

Y

G

G

A

A

G

G

I

L

L

L

S

S

A

Y

G

G

E

E

T

L

K

L

F

H

S

C

L

L

S

S

D

E

P

P

E

E

H

I

R

R

D

A

Y

F

D

D

V

P

R

E

S

A

I

A

M

A

Q

V

T

Q

P

P

Y
|
Y

W

Q

K

D

D

Q

K

T

F

Y

Q

Q

D

S

K

V

Y

Y

Y

F

V

V

I

S

E

E

S

S

Y

F

binding fe (iii) ion: H168 (= H127), H173 (= H132), E213 (= E174)
binding l-dopamine: P164 (= P123), H173 (= H132), E213 (= E174)
binding : A134 (≠ D93), E202 (≠ H163), S205 (= S166), Y208 (= Y169), W209 (= W170), Y260 (= Y221)

5jk8A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
33% identity, 81% coverage: 25:238/264 of query aligns to 144:359/390 of 5jk8A

query
sites
5jk8A

Y

Y

T

T

E

E

N

E

F

I

A

K

V

T

W

W

K

G

T

V

L

V

Y

Y

E

N

R

R

Q

L

I

K

V

E

N

L

L

F

P

P

N

T

A

N

A

A

S

C

K

H

-

Q

-

H

A

A

Y

Y

L

I

E

F

G

P

I

L

K

L

E

E

I

Q

N

N

-

C

-

G

F

Y

T

S

A

P

D

D

R

N

I

I

A

P

N

Q

F

L

S

Q

E

D

V

I

N

S

Q

N

I

F

L

L

S

Q

K

E

S

C

T
|
T

G

G

W

W

G

R

V

I

Q

R

V

P

V

V

P

Q

G

G

L

L

I
x
L

D

S

D
x
A

D

R

L

D

F
|
F

F

L

G

N

L

G

L

L

N

A

H

F

K
x
R

R

V

F

F

P

H

S

A

S

T

T

Q

W

Y

L

I

R

R

K

H

M

P

E

S

Q

V

L

P

D

L

Y
|
Y

L
x
T

E

P

E

E

P

P

D

D

M

C

F

C

H
|
H

D

E

A

L

F

L

A

G

H
|
H

M

V

P

P

M

L

L

L

T

A

N

D

Q

P

P

D

Y

F

V

A

D
|
D

F

F

L

S

Q

Q

D

E

L

I

S

G

G

L

I

A

A

S

L

I

K

G

Y

A

I

S

D

D

D

E

K

D

W

-

A

-

I

I

H

Q

L

L

S
|
S

R

T

I

C

Y
|
Y

W

W

F

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

E

N

G

G

D

A

T

L

I

K

R

I

A

Y

Y

G

G

A

A

G

G

I

I

L

L

S
|
S

A

T

G

G

E

E

T

M

K

E

F

H

S

F

L

L

S

T

D

D

D

K

P

A

E

K

H

K

R

L

D

P

Y

F

D

N

V

P

R

F

S

D

I

A

M

C

Q

N

T

T

P

E

Y

Y

W

P

K

I

D

T

K

T

F

F

Q

Q

D

P

K

L

Y

Y

V

V

I

A

E

E

S

S

Y

F

E

Q

Q

K

active site: H250 (= H127), H255 (= H132), E295 (= E174), S314 (= S193)
binding fe (iii) ion: H250 (= H127), H255 (= H132), E295 (= E174)
binding 7,8-dihydrobiopterin: L214 (≠ I91), A216 (≠ D93), F219 (= F96), S287 (= S166), Y290 (= Y169)
binding norleucine: Y242 (= Y119), T243 (≠ L120), H250 (= H127), S314 (= S193), S315 (= S194)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T203 (= T80), R226 (≠ K103), D266 (= D143)

Sites not aligning to the query:

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

5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
33% identity, 81% coverage: 25:238/264 of query aligns to 153:368/400 of 5jk5A

query
sites
5jk5A

Y

Y

T

T

E

E

N

E

F

I

A

K

V

T

W

W

K

G

T

V

L

V

Y

Y

E

N

R

R

Q

L

I

K

V

E

N

L

L

F

P

P

N

T

A

N

A

A

S

C

K

H

-

Q

-

H

A

A

Y

Y

L

I

E

F

G

P

I

L

K

L

E

E

I

Q

N

N

-

C

-

G

F

Y

T

S

A

P

D

D

R

N

I

I

A

P

N

Q

F

L

S

Q

E

D

V

I

N

S

Q

N

I

F

L

L

S

Q

K

E

S

C

T
|
T

G

G

W

W

G

R

V

I

Q

R

V

P

V

V

P

Q

G
|
G

L
|
L

I
x
L

D

S

D

A

D

R

L

D

F
|
F

F
x
L

G

N

L

G

L

L

N

A

H

F

K

R

R

V

F

F

P

H

S

A

S

T

T

Q

W

Y

L

I

R

R

K

H

M

P

E

S

Q

V

L

P

D

L

Y

Y

L

T

E

P

E

E

P

P

D

D

M

C

F

C

H
|
H

D

E

A

L

F

L

A

G

H
|
H

M

V

P

P

M

L

L

L

T

A

N

D

Q
x
P

P

D

Y

F

V

A

D
|
D

F

F

L

S

Q

Q

D

E

L

I

S

G

G

L

I

A

A

S

L

I

K

G

Y

A

I

S

D

D

D

E

K

D

W

-

A

-

I

I

H

Q

L

L

S
|
S

R

T

I

C

Y
|
Y

W

W

F

F

T

T

I

V

E
|
E

F

F

G

G

L

L

I

C

R

K

E

E

N

G

G

D

A

T

L

I

K

R

I

A

Y

Y

G

G

A

A

G

G

I

I

L

L

S
|
S

S

S

A

T

G

G

E

E

T

M

K

E

F

H

S

F

L

L

S

T

D

D

D

K

P

A

E

K

H

K

R

L

D

P

Y

F

D

N

V

P

R

F

S

D

I

A

M

C

Q

N

T

T

P

E

Y

Y

W

P

K

I

D

T

K

T

F

F

Q

Q

D

P

K

L

Y

Y

V

V

I

A

E

E

S

S

Y

F

E

Q

Q

K

active site: H259 (= H127), H264 (= H132), E304 (= E174), S323 (= S193)
binding fe (iii) ion: H259 (= H127), H264 (= H132), E304 (= E174)
binding 7,8-dihydrobiopterin: G221 (= G89), L222 (= L90), L223 (≠ I91), F228 (= F96), L229 (≠ F97), S296 (= S166), Y299 (= Y169)
binding piperazine-n,n'-bis(2-ethanesulfonic acid): T212 (= T80), P271 (≠ Q139), D275 (= D143)

Sites not aligning to the query:

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

3e2tA The catalytic domain of chicken tryptophan hydroxylase 1 with bound tryptophan (see paper)
29% identity, 89% coverage: 25:260/264 of query aligns to 63:300/307 of 3e2tA

query
sites
3e2tA

Y

F

T

T

E

E

N

E

F

I

A

K

V

T

W

W

K

G

T

T

L

V

Y

Y

E

-

R

R

Q

E

I

L

V

N

N

K

L

L

-

Y

P

P

N

T

A

H

A

A

S

C

K

R

A

E

Y

Y

L

L

E

K

G

N

I

L

-

P

-

L

-

T

K

K

E

Y

I

C

N

G

F

Y

T

R

A

E

D

D

R

N

I

I

A

P

N

Q

F

L

S

E

E

D

V

V

N

S

Q

R

I

F

L

L

S

K

K

E

S

R

T

T

G

G

W

F

G

T

V

I

Q

R

V

P

V

V

P

A

G

G

L

Y

I

L

D

S

D

P

D

R

L

D

F

F

F

L

G

A

L

G

L

L

N

A

H

F

K

R

R

V

F

F

P

H

S

C

S

T

T

Q

W

Y

L

V

R
|
R

K

H

M

S

E

S

Q

D

L

P

D

L

Y
|
Y

L
x
T

E

P

E
|
E

P
|
P

D

D

M

T

F

C

H
|
H

D

E

A

L

F

L

A

G

H
|
H

M

V

P

P

M

L

L

L

T

A

N

E

Q

P

P

S

Y

F

V

A

D

Q

F

F

L

S

Q

Q

D

E

L

I

S

G

G

L

I

A

A

S

L

L

K

G

Y

A

I

S

D

D

D

E

K

-

W

-

A

A

I

V

H

Q

L

K

L

L

S

A

R

T

I

C

Y

Y

W

F

F

F

T

T

I

V

E
|
E

F
|
F

G

G

L

L

I

C

R

K

E

Q

N

E

G

G

A

Q

L

L

K

R

I

V

Y

Y

G

G

A

A

G

G

I

L

L

L

S
|
S

S

S

A

I

G

S

E

E

T

L

K

K

F

H

S

S

L

L

S

S

D

G

D

S

P

A

E

K

H

V

R

K

D

P

Y

F

D

D

V

P

R

K

S

V

I

T

M

C

Q

K

T

Q

P

E

Y

C

W

L

K
x
I

D

T

K

T

F

F

Q

Q

D

E

K

V

Y

Y

Y

F

V

V

I

S

E

E

S

S

Y

F

E

E

Q

E

L

A

Y

K

N

E

S

K

I

M

P

R

E

E

I

F

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active site: H169 (= H127), H174 (= H132), E214 (= E174), S233 (= S193)
binding fe (iii) ion: H169 (= H127), H174 (= H132), E214 (= E174)
binding imidazole: H169 (= H127), H174 (= H132), E214 (= E174)
binding tryptophan: R154 (= R112), Y161 (= Y119), T162 (≠ L120), E164 (= E122), P165 (= P123), H169 (= H127), F215 (= F175), S233 (= S193), I263 (≠ K223)

P70080 Tryptophan 5-hydroxylase 1; Tryptophan 5-monooxygenase 1; EC 1.14.16.4 from Gallus gallus (Chicken) (see paper)
29% identity, 89% coverage: 25:260/264 of query aligns to 167:404/445 of P70080

query
sites
P70080

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Y236 (≠ L90) binding
R258 (= R112) binding
T266 (≠ L120) binding
H273 (= H127) binding
H278 (= H132) binding
E318 (= E174) binding
S337 (= S193) binding
I367 (≠ K223) binding

P16331 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Mus musculus (Mouse) (see paper)
33% identity, 80% coverage: 25:236/264 of query aligns to 179:392/453 of P16331

query
sites
P16331

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F263 (= F105) 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.

5fgjA Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453 (see paper)
33% identity, 80% coverage: 25:236/264 of query aligns to 157:370/428 of 5fgjA

query
sites
5fgjA

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active site: H263 (= H127), H268 (= H132), E308 (= E174), S327 (= S193)
binding fe (iii) ion: H263 (= H127), H268 (= H132), E308 (= E174)

P04176 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Rattus norvegicus (Rat) (see 2 papers)
33% identity, 80% coverage: 25:236/264 of query aligns to 179:392/453 of P04176

query
sites
P04176

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H285 (= H127) binding
H290 (= H132) binding
E330 (= E174) binding

Sites not aligning to the query:

16 modified: Phosphoserine; by PKA

Query Sequence

>Echvi_2513 FitnessBrowser__Cola:Echvi_2513
MAGKSAEWVFEDPRLKAMHQDYDAYTEENFAVWKTLYERQIVNLPNAASKAYLEGIKEIN
FTADRIANFSEVNQILSKSTGWGVQVVPGLIDDDLFFGLLNHKRFPSSTWLRKMEQLDYL
EEPDMFHDAFAHMPMLTNQPYVDFLQDLSGIALKYIDDKWAIHLLSRIYWFTIEFGLIRE
NGALKIYGAGILSSAGETKFSLSDDPEHRDYDVRSIMQTPYWKDKFQDKYYVIESYEQLY
NSIPEIERVLAEELIANEDPEKEP

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