Uniprot ID | O66883 |
Uniprot Name | THYX_AQUAE |
Taxonomy ID | 224324 |
Sequence |
M
M
K
I
Y
L
M
G
S
D
Q
R
I
V
R
C
A
R
V
S
F
A
K
D
S
Y
V
D
E
K
R
D
K
R
L
I
R
Y
L
F
K
H
R
H
A
S
P
F
E
H
N
I
I
A
F
E
W
K
K
E
K
W
I
E
L
L
S
K
L
E
N
P
T
V
Q
V
Y
Y
S
N
G
F
V
F
L
N
L
R
N
A
I
N
V
W
E
L
L
P
D
A
V
K
E
R
I
K
E
A
F
P
T
T
Y
G
V
I
Q
R
R
G
E
I
E
D
E
E
L
Y
S
L
P
Y
T
K
D
K
A
Y
V
K
E
K
I
E
T
S
S
G
W
I
G
L
V
D
K
L
E
L
E
T
D
M
D
F
Y
T
F
V
V
E
C
P
L
F
V
A
R
Q
W
M
R
H
R
F
G
S
Y
N
E
V
S
K
R
Y
V
G
K
E
F
L
E
F
Y
L
P
K
Y
I
R
K
Q
A
E
K
N
K
Q
A
S
V
D
E
P
I
S
E
S
E
V
F
I
K
K
I
E
N
L
I
S
K
S
V
K
L
Y
E
E
I
I
E
K
G
G
A
K
E
L
A
R
G
V
L
P
Q
F
M
K
T
R
F
Y
W
T
V
P
R
I
S
L
D
N
F
I
T
L
R
T
H
E
G
A
Q
K
E
I
R
E
F
A
E
A
I
K
E
M
V
G
Y
R
G
T
D
K
K
N
V
I
|
Cofactor |
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q9WYT0}; Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers. {ECO:0000250|UniProtKB:Q9WYT0}; |
Active site |
ACT_SITE 286 286 Involved in ionization of N3 of dUMP, leading to its activation. {ECO:0000250|UniProtKB:Q9WYT0}. |
Pfam |
PF02511
|
InterPro |
IPR003669
IPR036098
|