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 substrate; mutation to M: 13-fold increase in Km for homoserine.
S192 (= S192) binding substrate; 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 substrate; 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, 93% coverage: 1:296/317 of query aligns to 1:301/309 of P07623

query
sites
P07623

M
|
M

P

P

I

I

K

R

I

V

P

P

D

D

D

E

L

L

P

P

A

A

R

V

P

N

I

F

L

L

E

R

Q

E

E

E

G

N

V

V

V

F

V

V

M

M

R

T

T

S

D

R

A

A

V

S

R

G

Q

Q

D

E

I

I

R

R

P

P

L

L

R

K

I

V

G

L

L

I

L

L

N

N

L

L

M

M

P

P

N
x
K

K
|
K

I

I

S

E

T

T

E

E

T

N

Q

Q

L

F

A

L

R

R

L

L

G

S

A

N

T

S

P

P

L

L

Q

Q

V

V

E

D

L

I

T

Q

L

L

V

L

R

R

M

I

T

D

D

S

H

R

V

E

A

S

R

R

H

N

T

T

P

P

A

A

D

E

H

H

M

L

A

N

F

F

Y

Y

R
x
C

P

N

W

F

A

E

E

D

V

I

R

Q

D

D

E

Q

R

N

F

F

D

D

G

G

F

L

V

I

I

V

T

T

G

G

A

A

P

P

V

L

E

G

H

L

L

V

P

E

F

F

E

N

E

D

V

V

G

A

Y

Y

W

W

P

P

E

Q

L

I

C

K

R

Q

V

V

L

L

D

E

W

W

T

S

Q

K

T

D

H

H

V

V

H

T

S

S

S

T

F

L

T

F

I

V

C
|
C

W

W

A

A

A

V

Q

Q

A

A

L

L

H

N

H

I

F

L

H

Y

G

G

V

I

P

P

K
|
K

H

Q

L

T

L

R

P

T

A

E

K

K

A

L

F

S

G

G

L

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

P

F

H

L

I

A

P

P

V

H

S

S

R
|
R

W

Y

A

A

E

D

I

F

R

P

Q

A

A

A

D

L

I

I

P

R

A

D

G

Y

S

T

G

D

L

L

E

E

T

I

L

L

L

A

D

E

S

T

A

E

E

E

T

G

G

D

P

A

C

Y

L

L

L

F

D

A

D

S

P

K

A

D

H

K

R

R

S

I

L

A

H

F

M

V

F

T

N

G

H
|
H

V

P

E
|
E

Y
|
Y

D

D

T

A

R

Q

S

T

L

L

A

A

D

Q

E
|
E

Y

F

F

F

R
|
R

D

D

G

V

Q

E

G

A

P

G

L

L

-

D

-

P

-

D

-

V

P

P

A

Y

G

N

Y

Y

F

F

P

P

G

H

D

N

D

D

P

P

A

Q

R

N

P

T

P

P

E

R

N

A

R

S

W

W

R

R

G

S

H

H

A

G

H

N

L

L

F

F

G

T

N

N

W

W

I

L

N

N

-

Y

E

Y

I

V

Y

Y

R

Q

T

I

T

T

P

P

F

Y

D

D

I

L

M1 (= M1) modified: Initiator methionine, Removed
K46 (≠ N46) 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 (≠ NK 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)
41% identity, 85% coverage: 17:286/317 of query aligns to 1:262/268 of 2vdjA

query
sites
2vdjA

Q

E

E

E

G

N

V

I

V

F

V

V

M

M

R

T

R

K

T

E

D

R

A

A

V

E

R

T

Q

Q

D

D

I

I

R

R

P

A

L

L

R

K

I

I

G

A

L

I

L

L

N

N

L

L

M

M

P

P

N

T

K

K

I

Q

S

E

T

T

E

E

T

A

Q

Q

L

L

A

L

R

R

L

L

L

I

G

G

A

N

T

T

P

P

L

L

Q

Q

V

L

E

D

L

V

T

H

L

L

V

L

R

H

M

M

T

E

D

-

H

-

V

-

A

-

R

-

H

-

T

-

P

-

A

-

D

-

H

-

M

-

A

S

F

F

Y

Y

R

K

P

T

W

F

A

R

E

D

V

I

R

E

D

N

E

E

R

K

F

F

D

D

G

G

F

L

V

I

I

I

T

T

G

G

A

A

P

P

V

V

E

E

H

T

L

L

P

S

F

F

E

E

V

V

G

D

Y

Y

W

W

P

E

E

E

L

L

C

K

R

R

V

I

L

M

D

E

W

Y

T

S

Q

K

T

T

H

N

V

V

H

T

S

S

S

T

F

L

T

H

I

I

C

C

W

W

A

G

A

A

Q

Q

A

A

A

G

L

L

H

Y

H

H

F

H

H

Y

G

G

V

V

P

Q

K

K

H

Y

L

P

L

L

P

K

A

E

K

K

A

M

F

F

G

G

L

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

P

F

H

F

I

A

P

V

V

H

S
|
S

R

R

W

H

A

T

E

E

I

V

R

R

Q

E

A

S

D

D

I

I

P

R

A

E

G

V

S

K

G

E

L

L

E

T

T

L

L

L

L

A

D

N

S

S

A

E

E

E

T

A

G

G

P

V

C

H

L

L

L

V

D

I

D

G

P

Q

A

E

H

G

R

R

S

Q

L

V

H

F

M

A

F

L

N

G

H
|
H

V

S

E

E

Y

Y

D

S

T

C

R

D

S

T

L

L

A

K

D

Q

E
|
E

Y

Y

F

E

R
|
R

D

D

G

R

Q

D

G

K

P

G

L

L

-

N

-

I

-

D

-

V

P

P

A

K

G

N

Y

Y

F

F

P

K

G

H

D

D

D

N

P

P

A

N

R

E

P

K

P

P

E

L

N

V

R

R

W

W

R

R

G

S

H

H

A

G

H

N

L

L

F

F

G

S

N

N

W

W

I

L

N

N

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

Query Sequence

>WP_011951434.1 NCBI__GCF_000016765.1:WP_011951434.1
MPIKIPDDLPARPILEQEGVVVMRRTDAVRQDIRPLRIGLLNLMPNKISTETQLARLLGA
TPLQVELTLVRMTDHVARHTPADHMAAFYRPWAEVRDERFDGFVITGAPVEHLPFEEVGY
WPELCRVLDWTQTHVHSSFTICWAAQAALHHFHGVPKHLLPAKAFGLFRHRNLAPASPYL
RGFSDDPHIPVSRWAEIRQADIPAGSGLETLLDSAETGPCLLDDPAHRSLHMFNHVEYDT
RSLADEYFRDGQGPLPAGYFPGDDPARPPENRWRGHAHLLFGNWINEIYRTTPFDIAAIG
GGRPPANDAGPIEAAAG

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