SitesBLAST

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 (= C90) 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.

Q72X44 Homoserine O-acetyltransferase; HAT; Homoserine transacetylase; HTA; EC 2.3.1.31 from Bacillus cereus (strain ATCC 10987 / NRS 248) (see paper)
51% identity, 97% coverage: 1:301/309 of query aligns to 1:301/301 of Q72X44

query
sites
Q72X44

M

M

P

P

I

I

R

I

V

I

P

D

D

K

E

D

L

L

P

P

A

A

V

R

N

K

F

V

L

L

R

Q

E

E

N

N

V

I

F

F

V

V

M

M

T

T

T

K

S

E

R

R

A

A

S

E

G

T

Q

Q

E

D

I

I

R

R

P

A

L

L

K

K

V

I

L

A

I

I

L

L

N

N

L

L

M

M

P

P

K

T

K
|
K

I

Q

E

E

T

T

E

E

N

A

Q

Q

F

L

L

L

R

R

L

L

L

I

S

G

N

N

S

T

P

P

L

L

Q

Q

V

L

D

D

I

V

Q

H

L

L

R

H

I

M

D

E

S

S

R

H

E

L

S

S

R

R

N

N

T

V

P

A

A

Q

E

E

H

H

L

L

N

T

N

S

F

F

Y

Y

C

K

N

T

F

F

E

R

D

D

I

I

Q

E

D

N

Q

E

N

K

F

F

D

D

G

G

L

L

I

I

V

I

T

T

G

G

A

A

P

P

L

V

G
x
E

L

T

V

L

E

S

F

F

N

E

D

E

V

V

A

D

Y

Y

W

W

P

E

Q

E

I

L

K

K

Q

R

V

I

L

M

E

E

W

Y

S

S

K

K

D

T

H

N

V

V

T

T

S

S

T

T

L

L

F

H

V

I

C
|
C

W

W

A

G

V

A

Q

Q

A

A

A

G

L

L

N

Y

I

H

L

H

Y

Y

G

G

I

V

P

Q

K

K

Q

Y

T

P

R

L

T

K

E

E

K
|
K

L

M

S

F

G

G

V

V

Y

F

E

E

H

H

H

E

I

V

L

R

H

E

P

Q

H

H

A

V

L

K

L

L

T

L

R

Q

G

G

F

F

D

D

D

E

S

L

F

F

L

F

A

A

P

P

H

H

S
|
S

R

R

Y

H

A

T

D

E

F

V

P

R

A

E

A

S

L

D

I

I

R

R

D

E

Y

V

T

K

D

E

L

L

E

T

I

L

L

L

A

A

E

N

T

S

E

E

G

A

D

G

A

V

Y

H

L

L

F

V

A

I

S

G

K

Q

D

E

K

G

R

R

I

Q

A

V

F

F

V

A

T

L

G

G

H
|
H

P

S

E
|
E

Y

Y

D

S

A

C

Q

D

T

T

L

L

A

K

Q

Q

E

E

F

Y

F

E

R
|
R

D

D

V

R

E

D

A

K

G

G

L

L

D

N

P

I

D

D

V

V

P

P

Y

K

N

N

Y

Y

F

F

P

K

H

H

N

D

D

N

P

P

Q

N

N

E

T

K

P

P

R

L

A

V

S

R

W

W

R

R

S

S

H

H

G

G

N

N

L

L

F

F

T

S

N

N

W

W

L

L

N

N

Y

Y

V

V

Y

Y

Q

Q

I

E

T

T

P

P

Y

Y

D

V

L

L

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 (≠ G111) 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.

2vdjA Crystal structure of homoserine o-acetyltransferase (meta) from bacillus cereus with homoserine (see paper)
49% identity, 90% coverage: 17:295/309 of query aligns to 1:267/268 of 2vdjA

query
sites
2vdjA

E

E

N

N

V

I

F

F

V

V

M

M

T

T

T

K

S

E

R

R

A

A

S

E

G

T

Q

Q

E

D

I

I

R

R

P

A

L

L

K

K

V

I

L

A

I

I

L

L

N

N

L

L

M

M

P

P

K

T

K

K

I

Q

E

E

T

T

E

E

N

A

Q

Q

F

L

L

L

R

R

L

L

L

I

S

G

N

N

S

T

P

P

L

L

Q

Q

V

L

D

D

I

V

Q

H

L

L

R

H

I

M

D

E

S

S

R

-

E

-

S

-

R

-

N

-

T

-

P

-

A

-

E

-

H

-

L

-

N

-

N

S

F

F

Y

Y

C

K

N

T

F

F

E

R

D

D

I

I

Q

E

D

N

Q

E

N

K

F

F

D

D

G

G

L

L

I

I

V

I

T

T

G

G

A

A

P

P

L

V

G

E

L

T

V

L

E

S

F

F

N

E

D

E

V

V

A

D

Y

Y

W

W

P

E

Q

E

I

L

K

K

Q

R

V

I

L

M

E

E

W

Y

S

S

K

K

D

T

H

N

V

V

T

T

S

S

T

T

L

L

F

H

V

I

C

C

W

W

A

G

V

A

Q

Q

A

A

A

G

L

L

N

Y

I

H

L

H

Y

Y

G

G

I

V

P

Q

K

K

Q

Y

T

P

R

L

T

K

E

E

K

K

L

M

S

F

G

G

V

V

Y

F

E

E

H

H

H

E

I

V

L

R

H

E

P

Q

H

H

A

V

L

K

L

L

T

L

R

Q

G

G

F

F

D

D

D

E

S

L

F

F

L

F

A

A

P

V

H

H

S
|
S

R

R

Y

H

A

T

D

E

F

V

P

R

A

E

A

S

L

D

I

I

R

R

D

E

Y

V

T

K

D

E

L

L

E

T

I

L

L

L

A

A

E

N

T

S

E

E

G

A

D

G

A

V

Y

H

L

L

F

V

A

I

S

G

K

Q

D

E

K

G

R

R

I

Q

A

V

F

F

V

A

T

L

G

G

H
|
H

P

S

E

E

Y

Y

D

S

A

C

Q

D

T

T

L

L

A

K

Q

Q

E
|
E

F

Y

F

E

R
|
R

D

D

V

R

E

D

A

K

G

G

L

L

D

N

P

I

D

D

V

V

P

P

Y

K

N

N

Y

Y

F

F

P

K

H

H

N

D

D

N

P

P

Q

N

N

E

T

K

P

P

R

L

A

V

S

R

W

W

R

R

S

S

H

H

G

G

N

N

L

L

F

F

T

S

N

N

W

W

L

L

N

N

Y

Y

V

V

Y

Y

Q

Q

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

Query Sequence

>18041 FitnessBrowser__Keio:18041
MPIRVPDELPAVNFLREENVFVMTTSRASGQEIRPLKVLILNLMPKKIETENQFLRLLSN
SPLQVDIQLLRIDSRESRNTPAEHLNNFYCNFEDIQDQNFDGLIVTGAPLGLVEFNDVAY
WPQIKQVLEWSKDHVTSTLFVCWAVQAALNILYGIPKQTRTEKLSGVYEHHILHPHALLT
RGFDDSFLAPHSRYADFPAALIRDYTDLEILAETEEGDAYLFASKDKRIAFVTGHPEYDA
QTLAQEFFRDVEAGLDPDVPYNYFPHNDPQNTPRASWRSHGNLLFTNWLNYYVYQITPYD
LRHMNPTLD

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