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)
41% identity, 99% coverage: 1:304/307 of query aligns to 1:305/309 of P07623

query
sites
P07623

M
|
M

P

P

I

I

R

R

I

V

P

P

N

D

D

E

L

L

P

P

A

A

F

V

T

N

A

F

L

L

Q

R

T

E

E

E

G

N

V

V

M

F

V

V

M

M

Q

T

E

T

A

S

D

R

A

A

I

S

R

G

Q

Q

D

E

I

I

R

R

P

P

L

L

R

K

F

V

G

L

L

I

L

L

N

N

L

L

M

M

P

P

D
x
K

K
|
K

I

I

R

E

T

T

E

E

T

N

Q

Q

I

F

A

L

R

R

L

L

G

S

N

N

T

S

P

P

L

L

Q

Q

V

V

E

D

L

I

S

Q

L

L

I

L

R

R

I

I

T

D

N

S

H

R

V

E

P

S

R

R

N

N

T

T

A

P

A

A

D

E

H

H

M

L

S

N

A

N

F

F

Y

Y

R
x
C

S

N

W

F

E

E

D

D

A

I

R

Q

R

D

E

Q

T

N

F

F

D

D

G

G

F

L

I

I

I

V

T

T

G

G

A

A

P

P

V

L

E

G

T

L

M

V

P

E

F

F

E

N

E

D

V

V

S

A

Y

Y

W

W

D

P

E

Q

L

I

C

K

S

Q

V

V

F

L

D

E

W

W

T

S

Q

K

S

D

H

H

V

V

H

T

A

S

C

T

L

L

N

F

I

V

C
|
C

W

W

A

A

A

V

Q

Q

A

A

V

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

R

E

K

K

A

L

S

S

G

G

V

V

F

Y

R

E

H

H

R

H

N

I

R

L

A

H

P

P

A

H

S

A

P

L

Y

L

L

T

C

R

G

G

L

F

S

D

D

D

G

S

V

F

P

L

I

A

P

P

V

H

S

S

R
|
R

W

Y

T

A

E

D

V

F

R

P

E

A

D

A

D

L

L

I

P

R

P

D

E

Y

S

T

G

D

L

L

R

E

V

I

L

L

L

A

D

E

S

T

P

E

E

E

T

G

G

D

P

A

C

Y

L

L

L

F

E

A

D

S

A

K

A

D

H

K

R

R

S

I

L

A

H

F

M

V

F

T

N

G

H
|
H

I

P

E
|
E

Y
|
Y

D

D

T

A

D

Q

T

T

L

L

R

A

N

Q

E
|
E

Y

F

V

F

R
|
R

D

D

V

V

A

E

K

A

D

G

A

L

A

D

T

P

P

D

V

V

P

P

H

Y

G

N

Y

Y

F

F

P

P

D

H

D

N

D

D

P

P

S

Q

Q

N

P

T

P

P

E

R

N

A

R

S

W

W

R

R

S

S

H

H

A

G

H

N

L

L

F

F

A

T

N

N

W

W

I

L

N

N

-

Y

Q

Y

I

V

Y

Y

Q

Q

T

I

T

T

P

P

F

Y

E

D

L

L

S

R

R

H

I

M

G

N

M1 (= M1) modified: Initiator methionine, Removed
K46 (≠ D46) 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 (≠ DK 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)
43% identity, 90% coverage: 18:294/307 of query aligns to 2:267/268 of 2vdjA

query
sites
2vdjA

E

E

G

N

V

I

M

F

V

V

M

M

Q

T

E

K

A

E

D

R

A

A

I

E

R

T

Q

Q

D

D

I

I

R

R

P

A

L

L

R

K

F

I

G

A

L

I

L

L

N

N

L

L

M

M

P

P

D

T

K

K

I

Q

R

E

T

T

E

E

T

A

Q

Q

I

L

A

L

R

R

L

L

L

I

G

G

N

N

T

T

P

P

L

L

Q

Q

V

L

E

D

L

V

S

H

L

L

I

L

R

-

I

-

T

-

N

-

H

-

V

-

P

-

R

-

N

-

T

-

A

-

D

-

H

H

M

M

-

E

S

S

A

S

F

F

Y

Y

R

K

S

T

W

F

E

R

D

D

A

I

R

E

R

N

E

E

T

K

F

F

D

D

G

G

F

L

I

I

T

T

G

G

A

A

P

P

V

V

E

E

T

T

M

L

P

S

F

F

E

E

V

V

S

D

Y

Y

W

W

D

E

E

E

L

L

C

K

S

R

V

I

F

M

D

E

W

Y

T

S

Q

K

S

T

H

N

V

V

H

T

A

S

C

T

L

L

N

H

I

I

C

C

W

W

A

G

A

A

Q

Q

A

A

A

G

V

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

R

E

K

K

A

M

S

F

G

G

V

V

F

F

R

E

H

H

R

E

N

V

R

R

A

E

P

Q

A

H

S

V

P

K

Y

L

L

L

C

Q

G

G

L

F

S

D

D

E

G

L

V

F

P

F

I

A

P

V

V

H

S
|
S

R

R

W

H

T

T

E

E

V

V

R

R

E

E

D

S

D

D

L

I

P

R

P

E

E

V

S

K

G

E

L

L

R

T

V

L

L

L

L

A

D

N

S

S

P

E

E

E

T

A

G

G

P

V

C

H

L

L

L

V

E

I

D

G

A

Q

A

E

H

G

R

R

S

Q

L

V

H

F

M

A

F

L

N

G

H
|
H

I

S

E

E

Y

Y

D

S

T

C

D

D

T

T

L

L

R

K

N

Q

E
|
E

Y

Y

V

E

R
|
R

D

D

V

R

A

D

K

K

D

G

A

L

A

N

T

I

P

D

V

V

P

P

H

K

G

N

Y

Y

F

F

P

K

D

H

D

D

D

N

P

P

S

N

Q

E

P

K

P

P

E

L

N

V

R

R

W

W

R

R

S

S

H

H

A

G

H

N

L

L

F

F

A

S

N

N

W

W

I

L

N

N

-

Y

Q

Y

I

V

Y

Y

Q

Q

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

Query Sequence

>AZOBR_RS14010 FitnessBrowser__azobra:AZOBR_RS14010
MPIRIPNDLPAFTALQTEGVMVMQEADAIRQDIRPLRFGLLNLMPDKIRTETQIARLLGN
TPLQVELSLIRITNHVPRNTAADHMSAFYRSWEDARRETFDGFIITGAPVETMPFEEVSY
WDELCSVFDWTQSHVHACLNICWAAQAAVHHFHGVPKHLLPRKASGVFRHRNRAPASPYL
CGLSDGVPIPVSRWTEVREDDLPPESGLRVLLDSPETGPCLLEDAAHRSLHMFNHIEYDT
DTLRNEYVRDVAKDAATPVPHGYFPDDDPSQPPENRWRSHAHLLFANWINQIYQTTPFEL
SRIGTAA

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