Uniprot ID | Q9YA75 |
Uniprot Name | THYX_AERPE |
Taxonomy ID | 272557 |
Sequence |
M
A
A
S
L
E
K
A
G
L
G
I
S
V
R
L
L
E
Y
T
G
D
G
E
R
I
V
A
V
A
S
K
V
S
L
S
R
S
P
A
E
R
L
L
A
I
G
E
D
E
V
E
T
W
I
L
E
T
F
R
R
Q
H
F
S
P
W
E
H
S
V
Y
T
F
M
V
E
G
L
S
R
V
A
S
H
Q
L
V
R
H
R
V
A
S
Y
T
Q
L
S
H
R
Y
S
E
G
Y
L
R
E
A
A
L
K
A
C
E
S
I
G
L
D
C
P
S
K
P
A
E
T
E
G
G
R
K
A
A
Y
R
L
Y
S
Q
A
L
E
R
A
A
R
D
F
G
A
S
E
R
F
A
I
A
A
K
A
F
V
I
P
P
T
I
L
A
R
G
D
G
G
D
G
V
V
E
A
Y
L
R
S
A
A
I
Y
Y
S
L
L
S
R
G
A
R
R
E
D
A
R
Y
I
L
P
D
A
L
R
T
R
I
V
V
T
M
N
A
R
E
L
I
Q
V
F
F
P
L
R
M
C
T
R
A
Q
W
E
I
R
H
I
A
W
L
L
W
R
E
L
S
R
V
H
P
R
L
F
R
W
A
G
P
S
C
V
L
R
E
N
T
L
R
T
T
P
A
S
L
Y
S
Y
L
E
G
V
E
R
F
T
Q
P
R
C
P
E
L
V
E
N
K
A
I
P
G
C
L
R
Q
A
A
S
V
A
P
P
G
D
G
E
Y
E
|
Cofactor |
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_01408}; Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers. {ECO:0000255|HAMAP-Rule:MF_01408}; |
Active site |
ACT_SITE 233 233 Involved in ionization of N3 of dUMP, leading to its activation. {ECO:0000255|HAMAP-Rule:MF_01408}. |
Pfam |
PF02511
|
InterPro |
IPR003669
IPR036098
|