SitesBLAST

K46 (≠ D34) 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 (≠ DA 34:35) mutation to AA: Lack of activity.
K47 (≠ A35) 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 (≠ A77) mutation C->A,S: No change in activity.
C142 (= C129) mutation C->A,S: Lack of activity.
K157 (≠ R144) mutation to L: Lack of activity.
R193 (= R179) 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 (= H221) mutation H->A,N: Lack of activity.
E237 (= E223) mutation to A: 32-fold decrease in catalytic activity.; mutation to D: 3-fold decrease in catalytic activity.
Y238 (= Y224) mutation to F: 5-fold increase in Km for L-homoserine.
E246 (= E232) mutation to A: 150-fold increase in Km for L-homoserine.; mutation to D: 24-fold increase in Km for L-homoserine.
R249 (= R235) mutation to K: 4-fold increase in Km for L-homoserine.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

Q72X44 Homoserine O-acetyltransferase; HAT; Homoserine transacetylase; HTA; EC 2.3.1.31 from Bacillus cereus (strain ATCC 10987 / NRS 248) (see paper)
27% identity, 88% coverage: 24:299/315 of query aligns to 36:290/301 of Q72X44

query
sites
Q72X44

L

L

T

K

V

I

G

A

L

I

L

L

N

N

N

L

M

M

P

P

D

T

A
x
K

A

Q

L

-

A

-

A

E

T

T

D

E

R

A

Q

Q

F

L

S

L

A

R

L

L

L

I

G

G

R

N

E

T

V

P

R

L

L

Q

L

L

R

D

F

V

H

H

L

L

-

L

-

H

-

M

-

E

P

S

E

H

I

L

A

S

R

R

G

N

P

V

E

-

A

A

R

Q

D

E

M

H

L

L

A

T

P

S

L

F

S

Y

A

K

P

T

A

F

D

R

A

D

L

I

E

E

G

N

A

E

G

K

L

F

D

D

A

G

L

L

I

I

V

I

T

T

G

G

C

A

E

P

P

V

R
x
E

A

T

A

L

D

S

L

F

R

E

D

E

E

V

P

D

Y

Y

W

W

P

E

A

E

L

L

A

K

G

R

V

I

I

M

D

E

W

Y

A

S

R

K

D

T

H

N

T

V

V

T

S

S

T

T

L

L

F

H

S

I

C
|
C

L

W

A

G

A

A

H

Q

A

A

A

G

V

L

L

Y

H

H

L

H

D

Y

G

G

I

V

A

Q

R

K

R

Y

R

P

M

L

A

K

R

E

K
|
K

R

M

S

F

G

G

I

V

F

F

A

E

C

H

R

E

P

V

V

R

A

E

A

Q

H

H

-

V

P

K

L

L

A

Q

G

G

M

F

P

D

A

E

V

L

L

F

P

F

V

A

P

P

H

H

S
|
S

R

R

W

H

N

T

D

E

L

V

A

R

E

E

A

S

D

D

L

I

-

R

A

E

A

V

S

K

G

E

Y

L

H

T

V

L

L

L

T

A

R

N

S

S

D

E

E

E

A

A

G

G

V

V

D

H

L

L

F

V

V

I

K

G

P

Q

E

E

R

-

S

G

L

R

L

Q

V

V

F

F

L

A

Q

L

G

G

H
|
H

P

S

E
|
E

Y

Y

D

S

P

C

D

D

S

T

L

L

A

K

R

Q

E

E

Y

Y

R

E

R
|
R

D

D

L

-

K

-

R

-

F

-

G

-

R

-

G

R

E

D

R

K

A

G

E

L

P

N

P

I

D

D

R

V

P

P

V

K

H

N

Y

Y

F

F

D

K

P

H

E

D

I

-

E

-

A

-

L

-

D

-

H

-

A

-

R

-

G

-

W

-

A

-

G

-

E

N

P

P

S

N

C

E

A

K

P

P

P

L

A

V

A

-

P

-

A

R

W

W

P

R

P

S

V

H

A

G

A

N

Q

L

L

L

F

F

R

S

N

N

W

W

L

L

S

N

K47 (≠ A35) 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 (≠ R98) mutation to G: No activity with acetyl-CoA but catalyzes an acyltransferase reaction using succinyl-CoA and homoserine.
C142 (= C129) mutation C->A,S: Lack of activity.
K163 (= K150) binding ; mutation to M: 13-fold increase in Km for homoserine.
S192 (= S178) binding ; mutation to A: 5-fold increase in Km for homoserine.
H235 (= H221) mutation H->A,N,Q: Lack of activity.
E237 (= E223) 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 (= R235) binding ; mutation to M: 64-fold increase in Km for homoserine and 10-fold decrease in catalytic activity.

2vdjA Crystal structure of homoserine o-acetyltransferase (meta) from bacillus cereus with homoserine (see paper)
27% identity, 88% coverage: 24:299/315 of query aligns to 20:262/268 of 2vdjA

query
sites
2vdjA

L

L

T

K

V

I

G

A

L

I

L

L

N

N

N

L

M

M

P

P

D

T

A

K

A

Q

L

-

A

-

A

E

T

T

D

E

R

A

Q

Q

F

L

S

L

A

R

L

L

L

I

G

G

R

N

E

T

V

P

R

L

L

Q

L

L

R

D

F

V

H

H

L

L

P

L

E

H

I

-

A

-

R

-

G

-

P

-

E

-

A

-

R

-

D

-

M

M

L

E

A

S

P

S

L

F

S

Y

A

K

P

T

A

F

D

R

A

D

L

I

E

E

G

N

A

E

G

K

L

F

D

D

A

G

L

L

I

I

V

I

T

T

G

G

C

A

E

P

P

V

R

E

A

T

A

L

D

S

L

F

R

E

D

E

E

V

P

D

Y

Y

W

W

P

E

A

E

L

L

A

K

G

R

V

I

I

M

D

E

W

Y

A

S

R

K

D

T

H

N

T

V

V

T

S

S

T

T

L

L

F

H

S

I

C

C

L

W

A

G

A

A

H

Q

A

A

A

G

V

L

L

Y

H

H

L

H

D

Y

G

G

I

V

A

Q

R

K

R

Y

R

P

M

L

A

K

R

E

K

K

R

M

S

F

G

G

I

V

F

F

A

E

C

H

R

E

P

V

V

R

A

E

A

Q

H

H

-

V

P

K

L

L

A

Q

G

G

M

F

P

D

A

E

V

L

L

F

P

F

V

A

P

V

H

H

S
|
S

R

R

W

H

N

T

D

E

L

V

A

R

E

E

A

S

D

D

L

I

-

R

A

E

A

V

S

K

G

E

Y

L

H

T

V

L

L

L

T

A

R

N

S

S

D

E

E

E

A

A

G

G

V

V

D

H

L

L

F

V

V

I

K

G

P

Q

E

E

R

-

S

G

L

R

L

Q

V

V

F

F

L

A

Q

L

G

G

H
|
H

P

S

E

E

Y

Y

D

S

P

C

D

D

S

T

L

L

A

K

R

Q

E
|
E

Y

Y

R

E

R
|
R

D

D

L

-

K

-

R

-

F

-

G

-

R

-

G

R

E

D

R

K

A

G

E

L

P

N

P

I

D

D

R

V

P

P

V

K

H

N

Y

Y

F

F

D

K

P

H

E

D

I

-

E

-

A

-

L

-

D

-

H

-

A

-

R

-

G

-

W

-

A

-

G

-

E

N

P

P

S

N

C

E

A

K

P

P

P

L

A

V

A

-

P

-

A

R

W

W

P

R

P

S

V

H

A

G

A

N

Q

L

L

L

F

F

R

S

N

N

W

W

L

L

S

N

binding l-homoserine: S164 (= S178), H207 (= H221), E218 (= E232), R221 (= R235)

Query Sequence

>WP_012334052.1 NCBI__GCF_000019365.1:WP_012334052.1
MLKPATPPLARAGRPRPAAPRDRLTVGLLNNMPDAALAATDRQFSALLGREVRLLRFHLP
EIARGPEARDMLAPLSAPADALEGAGLDALIVTGCEPRAADLRDEPYWPALAGVIDWARD
HTVSTLFSCLAAHAAVLHLDGIARRRMARKRSGIFACRPVAAHPLLAGMPAVLPVPHSRW
NDLAEADLAASGYHVLTRSDEAGVDLFVKPERSLLVFLQGHPEYDPDSLAREYRRDLKRF
GRGERAEPPDRPVHYFDPEIEAALDDHARGGWAGEPSCAPPAAPAWPPVAAQLFRNWLSL
VATRRGARAGAAAAP

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