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)
47% identity, 99% coverage: 1:295/299 of query aligns to 1:295/309 of P07623

query
sites
P07623

M
|
M

P

P

I

I

I

R

I

V

P

P

Q

D

D

E

L

L

P

P

A

A

R

V

R

N

I

F

L

L

D

R

A

E

E

E

S

N

V

V

F

F

T

V

L

M

G

T

D

T

A

S

D

R

A

A

R

S

R

G

Q

Q

D

E

I

I

R

R

A

P

L

L

Q

K

V

V

V

L

V

I

L

L

N

N

L

L

M

M

P

P

T
x
K

K
|
K

V

I

T

E

T

T

E

E

T

N

Q

Q

I

F

A

L

R

R

V

L

L

L

A

S

N

N

T

S

P

P

L

L

Q

Q

V

V

E

D

L

I

T

Q

L

L

I

L

H

R

T

I

A

D

S

S

Y

R

Q

E

P

S

T

R

H

N

T

T

D

P

P

A

E

E

H

H

L

L

R

N

N

N

F

F

Y

Y

S
x
C

T

N

F

F

D

E

Q

D

I

I

R

Q

D

D

R

Q

Q

N

F

F

D

D

G

G

L

L

I

I

V

V

T

T

G

G

A

A

P

P

V

L

E

G

T

L

L

V

P

E

W

F

L

N

A

D

V

V

D

A

Y

Y

W

W

S

P

E

Q

L

I

T

K

T

Q

I

V

L

L

D

E

W

W

S

S

R

K

E

D

A

H

V

V

R

T

S

S

S

T

L

L

F

F

I

V

C
|
C

W

W

G

A

A

V

Q

Q

A

A

L

L

Q

N

H

I

F

L

H

Y

G

G

I

I

E

P

K
|
K

Q

Q

T

T

L

R

P

T

A

E

K

K

R

L

F

S

G

G

V

V

F

Y

W

E

H

H

L

I

R

L

D

H

R

P

S

H

S

A

P

L

L

L

V

T

R

R

G

G

H

F

D

D

D

S

F

F

L

L

V

A

P

P

V

H

S

S

R
|
R

H

Y

T

A

E

D

V

F

I

P

A

A

E

L

V

I

L

R

A

D

Q

Y

S

T

Q

D

L

L

Q

E

I

I

L

L

A

A

E

E

S

T

S

E

E

E

A

G

G

D

L

A

H

Y

L

L

L

F

W

A

D

S

A

K

D

D

Q

K

H

R

R

I

T

A

Y

F

L

V

F

T

N

G

H
|
H

P

P

E
|
E

Y
|
Y

D

D

A

A

D

Q

T

T

L

L

D

A

R

Q

E
|
E

Y

F

R

F

R
|
R

D

D

R

V

E

E

K

A

G

G

L

L

P

D

I

P

Q

D

L

V

P

P

L

Y

N

N

Y

Y

Y

F

P

P

N

H

D

N

D

D

P

P

N

Q

Q

N

V

T

P

P

R

R

V

A

R

S

W

W

R

R

S

S

H

H

A

G

Q

N

L

L

Y

F

T

T

N

N

W

W

L

L

N

N

Y

Y

E

Y

V

V

Y

Y

Q

Q

M1 (= M1) modified: Initiator methionine, Removed
K46 (≠ T46) 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 (≠ TK 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 (≠ S90) 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)
48% identity, 93% coverage: 18:295/299 of query aligns to 2:267/268 of 2vdjA

query
sites
2vdjA

E

E

S

N

V

I

F

F

T

V

L

M

G

T

D

K

A

E

D

R

A

A

R

E

R

T

Q

Q

D

D

I

I

R

R

A

A

L

L

Q

K

V

I

V

A

V

I

L

L

N

N

L

L

M

M

P

P

T

T

K

K

V

Q

T

E

T

T

E

E

T

A

Q

Q

I

L

A

L

R

R

V

L

L

I

A

G

N

N

T

T

P

P

L

L

Q

Q

V

L

E

D

L

V

T

H

L

L

I

L

H

H

T

M

A

E

S

S

Y

-

Q

-

P

-

T

-

H

-

T

-

D

-

P

-

E

-

H

-

L

-

R

-

N

S

F

F

Y

Y

S

K

T

T

F

F

D

R

Q

D

I

I

R

E

D

N

R

E

Q

K

F

F

D

D

G

G

L

L

I

I

V

I

T

T

G

G

A

A

P

P

V

V

E

E

T

T

L

L

P

S

W

F

L

E

A

E

V

V

D

D

Y

Y

W

W

S

E

E

E

L

L

T

K

T

R

I

I

L

M

D

E

W

Y

S

S

R

K

E

T

A

N

V

V

R

T

S

S

S

T

L

L

F

H

I

I

C

C

W

W

G

G

A

A

Q

Q

A

A

A

G

L

L

Q

Y

H

H

F

H

H

Y

G

G

I

V

E

Q

K

K

Q

Y

T

P

L

L

P

K

A

E

K

K

R

M

F

F

G

G

V

V

F

F

W

E

H

H

H

E

L

V

R

R

D

E

R

Q

S

H

S

V

P

K

L

L

V

L

R

Q

G

G

H

F

D

D

D

E

D

L

F

F

L

F

V

A

P

V

V

H

S
|
S

R

R

H

H

T

T

E

E

V

V

I

R

A

E

A

S

E

D

V

I

L

R

A

E

Q

V

S

K

Q

E

L

L

Q

T

I

L

L

L

A

A

E

N

S

S

S

E

E

E

A

A

G

G

L

V

H

H

L

L

L

V

W

I

D

G

A

Q

D

E

Q

G

H

R

R

Q

T

V

Y

F

L

A

F

L

N

G

H
|
H

P

S

E

E

Y

Y

D

S

A

C

D

D

T

T

L

L

D

K

R

Q

E
|
E

Y

Y

R

E

R
|
R

D

D

R

R

E

D

K

K

G

G

L

L

P

N

I

I

Q

D

L

V

P

P

L

K

N

N

Y

Y

Y

F

P

K

N

H

D

D

D

N

P

P

N

N

Q

E

V

K

P

P

R

L

V

V

R

R

W

W

R

R

S

S

H

H

A

G

Q

N

L

L

Y

F

T

S

N

N

W

W

L

L

N

N

Y

Y

E

Y

V

V

Y

Y

Q

Q

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

Query Sequence

>Synpcc7942_0371 FitnessBrowser__SynE:Synpcc7942_0371
MPIIIPQDLPARRILDAESVFTLGDADARRQDIRALQVVVLNLMPTKVTTETQIARVLAN
TPLQVELTLIHTASYQPTHTDPEHLRNFYSTFDQIRDRQFDGLIVTGAPVETLPWLAVDY
WSELTTILDWSREAVRSSLFICWGAQAALQHFHGIEKQTLPAKRFGVFWHHLRDRSSPLV
RGHDDDFLVPVSRHTEVIAAEVLAQSQLQILAESSEAGLHLLWDADQHRTYLFNHPEYDA
DTLDREYRRDREKGLPIQLPLNYYPNDDPNQVPRVRWRSHAQLLYTNWLNYEVYQPLSR

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