SitesBLAST

K47 (= K47) mutation to M: 17-fold increase in Km for acetyl-CoA and 14-fold decrease in catalytic activity.; mutation to R: 7-fold increase in Km for acetyl-CoA.
E111 (= E111) mutation to G: No activity with acetyl-CoA but catalyzes an acyltransferase reaction using succinyl-CoA and homoserine.
C142 (= C142) mutation C->A,S: Lack of activity.
K163 (= K163) binding ; mutation to M: 13-fold increase in Km for homoserine.
S192 (= S192) binding ; mutation to A: 5-fold increase in Km for homoserine.
H235 (= H235) mutation H->A,N,Q: Lack of activity.
E237 (= E237) mutation to A: 65-fold decrease in catalytic activity.; mutation to D: 6-fold decrease in catalytic activity.; mutation to Q: 19-fold decrease in catalytic activity.
R249 (= R249) binding ; mutation to M: 64-fold increase in Km for homoserine and 10-fold decrease in catalytic activity.

P07623 Homoserine O-succinyltransferase; HST; Homoserine transsuccinylase; HTS; EC 2.3.1.46 from Escherichia coli (strain K12) (see 4 papers)
42% identity, 100% coverage: 1:304/305 of query aligns to 1:305/309 of P07623

query
sites
P07623

M
|
M

P

P

I

I

K

R

I

V

P

P

E

D

T

E

L

L

P

P

A

A

F

V

D

N

V

F

L

L

S

R

S

E

E

E

G

N

V

V

M

F

V

V

M

M

G

T

Q

T

G

S

R

R

A

A

D

S

R

G

Q

Q

D

E

I

I

R

R

P

P

L

L

Q

K

I

V

G

L

L

I

L

L

N

N

L

L

M

M

P

P

K
|
K

I

I

Q

E

T

T

E

E

T

N

Q

Q

F

F

A

L

R

R

L

L

I

L

G

S

A

N

T

S

P

P

L

L

Q

Q

I

V

D

D

L

I

T

Q

L

L

I

L

R

R

M

I

T

D

E

S

H

R

Q

E

S

S

K

R

H

N

T

T

S

P

A

A

A

E

H

H

M

L

E

N

A

N

F

F

Y

Y

R
x
C

P

N

F

F

A

E

E

D

V

I

R

Q

D

D

R

Q

K

N

F

F

D

D

G

G

L

L

I

I

I

V

T

T

G

G

A

A

P

P

I

L

E

G

H

L

L

V

E

E

F

F

A

N

D

D

V

V

T

A

Y

Y

W

W

D

P

E

Q

L

I

R

K

E

Q

V

V

F

L

A

E

W

W

T

S

Q

K

T

D

N

H

V

V

H

T

A

S

T

T

F

L

G

F

V

V

C
|
C

W

W

G

A

G

V

M

Q

A

A

M

A

I

L

N

N

H

I

F

L

H

Y

G

G

V

I

Q

P

K
|
K

H

Q

I

T

L

R

P

T

A

E

K

K

A

L

F

S

G

G

C

V

F

Y

R

E

H

H

R

H

N

I

L

L

A

H

P

P

A

H

S

A

P

L

Y

L

L

T

R

R

G

G

F

F

S

D

D

D

D

S

C

F

V

L

I

A

P

P

V

H

S

S

R
|
R

W

Y

T

A

E

D

M

F

K

P

Q

A

S

A

E

L

I

I

D

R

A

D

V

Y

P

T

G

D

L

L

T

E

T

I

L

L

L

A

G

E

S

T

P

E

E

E

V

G

G

D

P

A

C

Y

L

L

V

F

E

A

D

S

P

K

G

D

H

K

R

R

A

I

L

A

Y

F

I

V

F

T

N

G

H
|
H

F

P

E
|
E

Y
|
Y

D

D

T

A

G

Q

T

T

L

L

K

A

E

Q

E
|
E

Y

F

D

F

R
|
R

D

D

V

V

E

E

N

A

G

G

T

L

P

D

I

P

N

D

V

V

P

P

T

Y

N

N

Y

Y

Y

F

P

P

D

H

D

N

D

D

P

P

A

Q

R

N

A

T

P

P

L

R

N

A

R

S

W

W

R

R

S

S

H

H

A

G

H

N

L

L

Y

F

G

T

N

N

W

W

L

L

N

N

-

Y

E

Y

I

V

Y

Y

Q

Q

T

I

T

T

E

P

Y

Y

D

D

L

L

E

R

K

H

I

M

G

N

M1 (= M1) modified: Initiator methionine, Removed
K46 (= K46) mutation to A: 16-fold decrease in Km for L-homoserine. 32-fold decrease in catalytic activity.; mutation to L: 6-fold increase in Km for L-homoserine and in Km for succinyl-CoA. Slight increase in catalytic activity.; mutation to R: Slight decrease in catalytic activity.
KK 46:47 (= KK 46:47) mutation to AA: Lack of activity.
K47 (= K47) mutation to A: 22-fold decrease in Km for L-homoserine. Almost loss of catalytic activity.; mutation to L: 8-fold decrease in Km for L-homoserine and 10-fold increase in Km for succinyl-CoA. 20-fold decrease in catalytic activity.; mutation to R: 14-fold decrease in Km for L-homoserine. 72-fold decrease in catalytic activity.
C90 (≠ R90) mutation C->A,S: No change in activity.
C142 (= C142) mutation C->A,S: Lack of activity.
K157 (= K157) mutation to L: Lack of activity.
R193 (= R193) mutation to A: 3-fold increase in Km for L-homoserine. 8-fold decrease in catalytic activity.; mutation to K: 8-fold decrease in catalytic activity.
H235 (= H235) mutation H->A,N: Lack of activity.
E237 (= E237) mutation to A: 32-fold decrease in catalytic activity.; mutation to D: 3-fold decrease in catalytic activity.
Y238 (= Y238) mutation to F: 5-fold increase in Km for L-homoserine.
E246 (= E246) mutation to A: 150-fold increase in Km for L-homoserine.; mutation to D: 24-fold increase in Km for L-homoserine.
R249 (= R249) mutation to K: 4-fold increase in Km for L-homoserine.

2vdjA Crystal structure of homoserine o-acetyltransferase (meta) from bacillus cereus with homoserine (see paper)
45% identity, 91% coverage: 17:294/305 of query aligns to 1:267/268 of 2vdjA

query
sites
2vdjA

S

E

E

E

G

N

V

I

M

F

V

V

M

M

G

T

Q

K

G

E

R

R

A

A

D

E

R

T

Q

Q

D

D

I

I

R

R

P

A

L

L

Q

K

I

I

G

A

L

I

L

L

N

N

L

L

M

M

P

P

K

T

K

K

I

Q

Q

E

T

T

E

E

T

A

Q

Q

F

L

A

L

R

R

L

L

I

I

G

G

A

N

T

T

P

P

L

L

Q

Q

I

L

D

D

L

V

T

H

L

L

I

L

R

-

M

-

T

-

E

-

H

-

Q

-

S

-

K

-

H

-

T

-

S

-

A

-

H

H

M

M

E

E

A

S

-

S

F

F

Y

Y

R

K

P

T

F

F

A

R

E

D

V

I

R

E

D

N

R

E

K

K

F

F

D

D

G

G

L

L

I

I

T

T

G

G

A

A

P

P

I

V

E

E

H

T

L

L

E

S

F

F

A

E

D

E

V

V

T

D

Y

Y

W

W

D

E

E

E

L

L

R

K

E

R

V

I

F

M

A

E

W

Y

T

S

Q

K

T

T

N

N

V

V

H

T

A

S

T

T

F

L

G

H

V

I

C

C

W

W

G

G

G

A

M

Q

A

A

M

G

I

L

N

Y

H

H

F

H

H

Y

G

G

V

V

Q

Q

K

K

H

Y

I

P

L

L

P

K

A

E

K

K

A

M

F

F

G

G

C

V

F

F

R

E

H

H

R

E

N

V

L

R

A

E

P

Q

A

H

S

V

P

K

Y

L

L

L

R

Q

G

G

F

F

S

D

D

E

D

L

C

F

V

F

I

A

P

V

V

H

S
|
S

R

R

W

H

T

T

E

E

M

V

K

R

Q

E

S

S

E

D

I

I

D

R

A

E

V

V

P

K

G

E

L

L

T

T

T

L

L

L

L

A

G

N

S

S

P

E

E

E

V

A

G

G

P

V

C

H

L

L

V

V

E

I

D

G

P

Q

G

E

H

G

R

R

A

Q

L

V

Y

F

I

A

F

L

N

G

H
|
H

F

S

E

E

Y

Y

D

S

T

C

G

D

T

T

L

L

K

K

E

Q

E
|
E

Y

Y

D

E

R
|
R

D

D

V

R

E

D

N

K

G

G

T

L

P

N

I

I

N

D

V

V

P

P

T

K

N

N

Y

Y

Y

F

P

K

D

H

D

D

D

N

P

P

A

N

R

E

A

K

P

P

L

L

N

V

R

R

W

W

R

R

S

S

H

H

A

G

H

N

L

L

Y

F

G

S

N

N

W

W

L

L

N

N

-

Y

E

Y

I

V

Y

Y

Q

Q

binding l-homoserine: S164 (= S192), H207 (= H235), E218 (= E246), R221 (= R249)

Query Sequence

>3608188 FitnessBrowser__Dino:3608188
MPIKIPETLPAFDVLSSEGVMVMGQGRADRQDIRPLQIGLLNLMPKKIQTETQFARLIGA
TPLQIDLTLIRMTEHQSKHTSAAHMEAFYRPFAEVRDRKFDGLIITGAPIEHLEFADVTY
WDELREVFAWTQTNVHATFGVCWGGMAMINHFHGVQKHILPAKAFGCFRHRNLAPASPYL
RGFSDDCVIPVSRWTEMKQSEIDAVPGLTTLLGSPEVGPCLVEDPGHRALYIFNHFEYDT
GTLKEEYDRDVENGTPINVPTNYYPDDDPARAPLNRWRSHAHLLYGNWLNEIYQTTEYDL
EKIGT

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