|
|
1)
|
chain |
B |
residue |
82 |
type |
catalytic |
sequence |
G
|
description |
653
|
source |
MCSA : MCSA2
|
|
2)
|
chain |
B |
residue |
146 |
type |
catalytic |
sequence |
R
|
description |
653
|
source |
MCSA : MCSA2
|
|
3)
|
chain |
B |
residue |
177 |
type |
catalytic |
sequence |
D
|
description |
653
|
source |
MCSA : MCSA2
|
|
4)
|
chain |
B |
residue |
203 |
type |
catalytic |
sequence |
K
|
description |
653
|
source |
MCSA : MCSA2
|
|
5)
|
chain |
B |
residue |
204 |
type |
catalytic |
sequence |
T
|
description |
653
|
source |
MCSA : MCSA2
|
|
6)
|
chain |
B |
residue |
206 |
type |
catalytic |
sequence |
D
|
description |
653
|
source |
MCSA : MCSA2
|
|
7)
|
chain |
B |
residue |
206 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_01980
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
8)
|
chain |
B |
residue |
82 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
9)
|
chain |
B |
residue |
243 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
10)
|
chain |
B |
residue |
146 |
type |
BINDING |
sequence |
R
|
description |
in other chain => ECO:0000269|Ref.5
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
11)
|
chain |
B |
residue |
176 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_01980
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
12)
|
chain |
B |
residue |
204 |
type |
BINDING |
sequence |
T
|
description |
in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
13)
|
chain |
B |
residue |
251 |
type |
BINDING |
sequence |
M
|
description |
in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
14)
|
chain |
B |
residue |
312 |
type |
BINDING |
sequence |
E
|
description |
in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
15)
|
chain |
B |
residue |
428 |
type |
BINDING |
sequence |
Y
|
description |
in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
16)
|
chain |
B |
residue |
177 |
type |
SITE |
sequence |
D
|
description |
Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000305|PubMed:12015149
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
17)
|
chain |
B |
residue |
203 |
type |
SITE |
sequence |
K
|
description |
Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000305|PubMed:12015149
|
source |
Swiss-Prot : SWS_FT_FI7
|
|