SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011318900.1 NCBI__GCF_000204075.1:WP_011318900.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58) (see 2 papers)
53% identity, 97% coverage: 3:516/531 of query aligns to 2:502/517 of Q9JZG1

query
sites
Q9JZG1

T

T

K

Q

P

T

E

N

R

R

I

V

I

I

F

F

D

D

T

T

L

L

R

R

D
|
D

G

G

E

E

Q

Q

C

S

P

P

G

G

A

A

T

A

L

M

N

T

I

K

D

E

E

E

K

K

L

I

A

R

I

V

A

A

K

R

Q

Q

L

L

A

E

R

K

L

L

G

G

V

V

D

D

I

I

E

E

A

A

G

G

F

F

A

A

F

A

A

A

S

S

P

P

G

G

D

D

F

F

E

E

A

A

V

V

H

N

K

A

I

I

A

A

Q

K

T

T

V

I

G

-

T

-

E

-

N

T

G

K

P

S

V

T

I

V

C

C

S

S

L

L

A

S

R

R

A

A

R

I

H

E

D

R

D

D

I

I

K

R

A

Q

A

A

A

G

E

E

A

A

I

V

K

A

P

P

A

A

A

P

K

K

G

K

R

R

I

I

H

H

T

T

F

F

I

I

A

A

T

T

S

S

D

P

I

I

H

H

L

M

Q

E

Y

Y

K

K

L

L

K

K

K

M

T

K

R

P

P

K

E

Q

V

V

I

I

A

E

I

A

A

A

E

V

E

K

M

A

V

V

A

K

Y

I

A

A

K

R

S

E

F

Y

T

T

D

D

V

V

E

E

F

F

S

S

P

C

E

E

D

D

A

A

G

L

R

R

S

S

D

E

P

I

E

D

F

F

L

L

Y

A

Q

E

V

I

L

C

E

G

R

A

A

V

I

I

A

E

A

A

G

G

A

A

T

T

I

I

N

N

I

I

P

P

D

D

T

T

V

V

G

G

Y

Y

T

S

T

I

P

P

S

Y

E

K

F

T

G

E

A

E

I

F

K

R

G

E

I

L

K

I

E

A

N

K

V

T

P

P

N

N

I

G

D

G

Q

K

A

V

I

V

I

W

S

S

V

A

H
|
H

G

C

H
|
H

N

N

D

D

L

L

G

G

L

L

A

A

V

V

A

A

N

N

F

S

L

L

E

A

A

A

V

L

K

K

N

G

G

G

A

A

R

R

Q

Q

L

V

E

E

C

C

T

T

I

V

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N
|
N

A

A

A

S

L

V

E

E

L

I

V

V

M

M

A

A

M

L

H

K

V

V

R

R

R

H

Q

D

Y

L

F

F

N

G

P

L

F

E

L

T

G

G

R

-

H

-

P

-

D

-

S

-

E

-

P

-

L

-

T

-

N

-

I

I

D

D

T

T

K

T

Q

Q

I

I

Y

V

K

P

T

S

S

S

R

K

L

L

V

V

S

S

N

T

L

I

T

T

G

G

M

Y

L

P

V

V

Q

Q

P

P

N

N

K

K

A

A

I

I

V

V

G

G

A

A

N

N

A

A

F

F

A

S

H

H

E

E

S

S

G

G

I

I

H

H

Q

Q

D

D

G

G

V

V

L

L

K

K

N

H

K

R

L

E

T

T

Y

Y

E

E

I

I

M

M

D

S

A

A

Q

E

L

S

I

V

G

G

L

W

T

A

D

T

N

N

Q

R

I

L

V

S

L

L

G

G

K

K

H

L

S

S

G

G

R

R

N

N

A

A

F

F

R

K

T

T

R

K

L

L

K

A

E

D

L

L

G

G

F

I

E

E

L

L

-

E

S

S

E

E

T

E

E

A

L

L

N

N

K

A

A

A

F

F

V

A

K

R

F

F

K

K

E

E

V
x
L

A
|
A

D
|
D

K
|
K

K
x
R

E
|
E

I
|
I

S
x
F

D
|
D

W
x
E

D
|
D

L
|
L

E
x
H

A
|
A

I
x
L

V
|
V

N
x
S

D
|
D

E
|
E

I
x
M

-
x
G

Q
x
S

Q
x
M

A
x
N

P
x
A

D
x
E

L
x
S

F
x
Y

R
x
K

V
x
F

E
x
I

L
x
S

V
x
Q

Q
x
K

V
x
I

S
|
S

C
x
T

G
x
E

S
x
T

N
x
G

A
x
E

R
x
E

P
|
P

T
x
R

A
|
A

T
x
D

V
x
I

T
x
V

L
x
F

R

-

T
x
S

P
x
I

D
x
K

G
|
G

E
|
E

L
x
K

T
x
R

D
x
A

A
x
S

A
|
A

I
x
T

G
|
G

T
x
S

G
|
G

P
|
P

V
|
V

D
|
D

A
|
A

V
x
I

Y
x
F

K
|
K

A
|
A

I
|
I

N
x
E

R
x
S

V
|
V

V
x
A

N
x
Q

V
x
S

P
x
G

N
x
A

Q
x
A

L
|
L

I
x
Q

E
x
I

F
x
Y

S
|
S

V
|
V

Q
x
N

S
x
A

V
|
V

T
|
T

A
x
Q

G
|
G

I
x
T

D
x
E

A
x
S

I
x
Q

G
|
G

E
|
E

V
x
T

T
x
S

I
x
V

R
|
R

L
|
L

R
x
A

Y
x
R

E
x
G

S
x
N

R
|
R

V
|
V

F
x
V

S
x
N

G
|
G

H
x
Q

A
x
G

A
|
A

N
x
D

T
|
T

D
|
D

I
x
V

I
x
L

V
|
V

A
|
A

S
x
T

A
|
A

Q
x
K

A
|
A

Y
|
Y

V
x
L

N
x
S

A
|
A

L
|
L

N
x
S

R
x
K

L
|
L

D16 (= D17) binding Mn(2+)
H204 (= H208) binding Mn(2+)
H206 (= H210) binding Mn(2+)
N240 (= N244) binding Mn(2+)

Sites not aligning to the query:

366:517 Required for the condensation reaction. Not required to bind substrate

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
51% identity, 73% coverage: 10:396/531 of query aligns to 20:407/409 of 6e1jA

query
sites
6e1jA

I

V

F

F

D

D

T

T

L

L

R

R

D
|
D

G

G

E

E

Q
|
Q

C

S

P

P

G

G

A

A

T

A

L

L

N

T

I

P

D

P

E

Q

K

K

L

I

A

E

I

I

A

A

K

R

Q

Q

L

L

A

A

R

K

L

L

G

R

V

V

D

D

I

I

I

M

E

E

A

V

G

G

F
|
F

A

P

F

V

A
x
S

S

S

P

E

G

E

D

E

F

F

E

E

A

T

V

I

H

Q

K

T

I

I

A

A

Q

K

T

T

V

V

G

G

T

N

E

E

N
x
V

G

D

-
x
E

-

E

-

T

-

G

-

Y

-

I

P

P

V

V

I

I

C

C

S

V

L
x
I

A

A

R
|
R

A

S

R

K

H

E

D

R

D

D

I

I

K

K

A

A

A

W

E

E

A

S

I

V

K

K

P

Y

A

A

A

K

K

R

G

P

R

R

I

I

H

V

T

I

F
|
F

I

T

A

S

T

T

S

S

D

D

I

I

H

H

L

L

Q

K

Y

Y

K
|
K

L
|
L

K

K

K

M

T

T

R

R

P

E

E

E

V

V

I

V

A

D

I

M

A

V

E

A

E

S

M

S

V

I

A

R

Y

F

A

A

K

K

S

S

F

L

T

G

-

F

D

E

D

D

V

I

E

E

F

F

S

G

P

C

E

E

D

D

A

G

G

G

R

R

S

S

D

D

P

K

E

D

F

Y

L

I

Y

C

Q

T

V

V

L

F

E

E

R

E

A

A

I

I

A

K

A

A

G

G

A

A

T

T

I

L

N

A

I

C

P
|
P

D

D

T
|
T

V

V

G

G

Y

I

T

N

T

M

P

P

S

H

E

E

F

Y

G

G

A

K

I

L

I

V

K

R

G

Y

I

I

K

K

E

A

N

N

V

T

P

P

N

G

I

I

D

D

Q

D

A

V

I

I

I

F

S

S

V

A

H
|
H

G

C

H
|
H

N

N

D

D

L

L

G

G

L

V

A

A

V

T

A

A

N

N

F

T

L

I

E

A

A

G

V

I

K

C

N

A

G

G

A

A

R

R

Q

Q

L

V

E

E

C

V

T

T

I

I

N

N

G

G

I

I

G

G

E

E

R

R

A

S

G

G

N

N

A

A

A

P

L

L

E

E

L

V

V

V

M

M

A

A

M

L

H

K

V

C

R

R

R

G

Q

A

Y

F

F

V

N

M

P

G

F

G

L

V

G

-

R

-

H

-

P

-

D

-

S

-

E

-

P

-

L

Y

T

T

N

R

I

I

D

D

T

T

K

R

Q

Q

I

I

Y

M

K

A

T

T

S

S

R

K

L

M

V

V

S

Q

N

E

L

Y

T

T

G

G

M

L

L

Y

V

V

Q

Q

P

P

N

H

K

K

A

P

I

I

V

V

G

G

A

A

N

N

A

C

F

F

A

V

H

H

E

E

S
|
S

G
|
G

I
|
I

H

H

Q

Q

D
|
D

G

G

V

I

L

L

K
|
K

N

N

K

R

L

S

T

T

Y

Y

E

E

I

I

M

I

D

S

A

P

Q

E

L

D

I

V

G

G

L

V

T

V

D

K

N

S

Q

Q

-

N

-

S

-

G

I

I

V

V

L

L

G

G

K

K

H
x
L

S

S

G

G

R
|
R

N
x
H

A

A

F

V

R

K

T

G

R

R

L

L

K

K

E

E

L

L

G

G

F

Y

E

E

L

I

S

S

E

D

T

E

E

K

L

L

N

N

K

E

A

V

F

F

V

S

K

R

F

F

K

R

E

D

V

L

A

T

D

K

K

Q

K

K

E

R

I

V

S

T

D

D

W

D

D

D

L

L

E

K

A

A

I

L

V

V

binding coenzyme a: Q30 (= Q20), F60 (= F50), S63 (≠ A53), I95 (≠ L79), R97 (= R81), F121 (= F105), K132 (= K116), L133 (= L117), S322 (= S314), G323 (= G315), I324 (= I316), D327 (= D319), K331 (= K323), L359 (≠ H348), R362 (= R351), H363 (≠ N352)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P175), T194 (= T177), H225 (= H208), H227 (= H210)
binding manganese (ii) ion: D27 (= D17), V82 (≠ N72), E84 (vs. gap), H225 (= H208), H227 (= H210)

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
51% identity, 74% coverage: 10:400/531 of query aligns to 87:480/506 of Q9FG67

query
sites
Q9FG67

I

V

F

F

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

C

S

P

P

G

G

A

G

T
x
S

L

L

N

T

I

P

D

P

E

Q

K

K

L

L

A

E

I

I

A

A

K

R

Q

Q

L

L

A

A

R

K

L

L

G

R

V

V

D

D

I

I

I

M

E

E

A

V

G

G

F

F

A

P

F

G

A

S

S

S

P

E

G

E

D

E

F

L

E

E

A

T

V

I

H

K

K

T

I

I

A

A

Q

K

T

T

V

V

G

G

T

N

E

E

N

V

G

D

-

E

-

T

-

G

-

Y

-

V

P

P

V

V

I

I

C

C

S

A

L

I

A

A

R

R

A

C

R

K

H

H

D

R

D

D

I

I

K

E

A

A

A

T

A

W

E

E

A

A

I

L

K

K

P

Y

A

A

A

K

K

R

G

P

R

R

I

I

H

L

T

V

F

F

I

T

A

S

T

T

S

S

D

D

I

I

H

H

L

M

Q

K

Y

Y

K

K

L

L

K

K

T

T

R

Q

P

E

E

E

V

V

I

I

A

E

I

M

A

A

E

V

E

S

M

S

V

I

A

R

Y

F

A

A

K

K

S

S

F

L

T

G

-

F

D

N

D

D

V

I

E

Q

F

F

S

G

P

C

E

E

D

D

A

G

G

G

R

R

S

S

D

D

P

K

E

D

F

F

L

L

Y

C

Q

K

V

I

L

L

E

G

R

E

A

A

I

I

A

K

A

A

G

G

A

V

T

T

T

V

I

V

N

T

I

I

P

G

D

D

T

T

V

V

G

G

Y

I

T

N

T

M

P

P

S

H

E

E

F

Y

G

G

A

E

I

L

I

V

K

T

G

Y

I

L

K

K

E

A

N

N

V

T

P

P

N

G

I

I

D

D

Q

D

A

V

I

V

S
x
A

V

V

H

H

G

C

H

H

N

N

D

D

L

L

G

G

L

L

A

A

V

T

A

A

N

N

F

S

L

I

E

A

A

G

V

I

K

R

N

A

G

G

A

A

R

R

Q

Q

L

V

E

E

C

V

T

T

I

I

N

N

G

G

I

I

G

G

E

E

R

R

A

S

G

G

N

N

A

A

A

S

L

L

E

E

L

V

V

V

M

M

A

A

M

L

H

K

V

C

R

R

R

G

Q

A

Y

Y

F

V

N

I

P

N

F

G

L

V

G

-

R

-

H

-

P

-

D

-

S

-

E

-

P

-

L

Y

T

T

N

K

I

I

D

D

T

T

K

R

Q

Q

I

I

Y

M

K

A

T

T

S

S

R

K

L

M

V

V

S

Q

N

E

L

Y

T

T

G

G

M

L

L

Y

V

V

Q

Q

P

A

N

H

K

K

A

P

I

I

V

V

G

G

A

A

N

N

A

C

F

F

A

V

H

H

E

E

S

S

G

G

I

I

H

H

Q

Q

D

D

G

G

V

I

L

L

K

K

N

N

K

R

L

S

T

T

Y

Y

E

E

I

I

M

L

D

S

A

P

Q

E

L

D

I

I

G

G

L

I

T

V

D

K

N

S

Q

Q

-

N

-

S

-

G

I

L

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

N

H

A

A

F

V

R

K

T

D

R

R

L

L

K

K

E

E

L

L

G

G

F

Y

E

E

L

L

S

D

E

D

T

E

E

K

L

L

N

N

K

A

A

V

F

F

V

S

K

L

F

F

K

R

E

D

V

L

A

T

D

K

K

N

K

K

E

R

I

I

S

T

D

D

W

A

D

D

L

L

E

K

A

A

I

L

V

V

-

T

-

S

N

S

D

D

E

E

I

I

S102 (≠ T25) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ S206) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
50% identity, 73% coverage: 10:396/531 of query aligns to 87:474/503 of P0DO78

query
sites
P0DO78

I

V

F

F

D

D

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

C

A

P

P

G

G

A

G

T

A

L

L

N

T

I

P

D

P

E

Q

K

K

L

L

A

E

I

I

A

A

K

R

Q

K

L

L

A

A

R

K

L

L

G

R

V

V

D

D

I

V

I

M

E

E

A

V

G

G

F

F

A

P

F

G

A

S

S

S

P

E

G

E

D

E

F

F

E

E

A

T

V

V

H

K

K

T

I

I

A

A

Q

K

T

T

V

V

G

G

T

N

E

E

N

V

G

D

-

E

-

T

-

G

-

Y

-

I

P

P

V

V

I

I

C

C

S

A

L

I

A

A

R

R

A

S

R

K

H

Q

D

R

D

D

I

I

K

E

A

A

A

W

E

E

A

A

I

V

K

K

P

Y

A

A

A

K

K

R

G

P

R

K

I

I

H

L

T

I

F

F

I

T

A

S

T

T

S

S

D

D

I

I

H

H

L

M

Q

K

Y

Y

K

K

L

L

K

K

T

T

R

K

P

E

E

E

V

V

I

I

A

E

I

M

A

A

E

T

E

S

M

S

V

I

A

R

Y

F

A

A

K

K

S

S

F

L

T

G

-

F

D

I

D

D

V

V

E

Q

F

L

S

G

P

C

E

E

D

D

A

G

G

G

R

R

S

S

D

E

P

K

E

E

F

F

L

L

Y

C

Q

K

V

I

L

L

E

G

R

E

A

A

I

I

A

K

A

A

G

G

A

A

T

T

T

A

I

V

N

N

I

V

P

A

D

D

T

T

V

V

G

G

Y

I

T

N

T

M

P

P

S

E

E

E

F

Y

G

G

A

E

I

L

I

V

K

R

G

Y

I

L

K

K

E

A

N

N

V

T

P

P

N

G

I

I

D

D

Q

D

A

I

I

V

I

F

S

S

V

V

H
|
H

G

C

H
|
H

N

N

D

D

L

L

G

G

L

V

A

A

V

T

A

A

N

N

F

T

L

I

E

A

A

G

V

V

K

C

N

A

G

G

A

A

R

R

Q

Q

L

V

E

E

C

V

T

T

I

V

N

N

G

G

I

I

G

G

E

E

R

R

A

S

G

G

N

N

A

A

A

P

L

L

E

E

L

V

V

V

M

M

A

A

M

L

H

K

V

C

R

R

R

G

Q

A

Y

Y

F

V

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

-

D

-

S

M

E

D

E

G

P

V

L

Y

T

T

N

R

I

I

D

D

T

T

K

R

Q

Q

I

I

Y

M

K

A

T

T

S

S

R

K

L

M

V

V

S

Q

N

E

L

Y

T

T

G

G

M

L

L

Y

V

V

Q

Q

P

P

N

H

K

K

A

P

I

I

V

V

G

G

A

A

N

N

A

C

F

F

A

V

H

H

E

E

S

S

G

G

I

V

H
|
H

Q

Q

D

D

G

G

V

I

L

L

K

K

N

N

K

R

L

S

T

T

Y

Y

E

E

I

I

M

L

D

S

A

P

Q

E

L

D

I

V

G

G

L

V

T

V

D

K

N

S

Q

Q

-

N

-

S

-

G

I

I

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

N

H

A

A

F

V

R

K

T

D

R

R

L

L

K

K

E

E

L

L

G

G

F

Y

E

E

L

L

S

D

E

D

T

E

E

K

L

F

N

N

K

D

A

I

F

F

V

S

K

R

F

F

K

R

E

D

V

L

A

T

D

K

K

Q

K

K

E

R

I

I

S

T

D

D

W

A

D

D

L

L

E

K

A

A

I

L

V

V

R93 (= R16) mutation to A: Lost catalytic activity.
D94 (= D17) mutation to A: Lost catalytic activity.
H292 (= H208) mutation to A: Lost catalytic activity.
H294 (= H210) mutation to A: Lost catalytic activity.
H392 (= H317) mutation to A: Lost catalytic activity.

Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
49% identity, 73% coverage: 10:396/531 of query aligns to 87:474/503 of Q9FN52

query
sites
Q9FN52

I

V

F

L

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

C

S

P

P

G

G

A

A

T

A

L

L

N

T

I

P

D

P

E

Q

K

K

L

L

A

E

I

I

A

A

K

R

Q

Q

L

L

A

A

R

K

L

L

G

R

V

V

D

D

I

I

I

M

E

E

A

V

G

G

F

F

A

P

F

V

A

S

S

S

P

E

G

E

D

E

F

F

E

E

A

A

V

I

H

K

K

T

I

I

A

A

Q

K

T

T

V

V

G

G

T

N

E

E

N

V

G

D

-

E

-

T

-

G

-

Y

-

V

P

P

V

V

I

I

C

C

S

G

L

I

A

A

R

R

A

C

R

K

H

K

D

R

D

D

I

I

K

E

A

A

A

T

A

W

E

E

A

A

I

L

K

K

P

Y

A

A

A

K

K

R

G

P

R

R

I

V

H

M

T

L

F

F

I

T

A

S

T

T

S

S

D

E

I

I

H

H

L

M

Q

K

Y

Y

K

K

L

L

K

K

T

T

R

K

P

E

E

E

V

V

I

I

A

E

I

M

A

A

E

V

E

N

M

S

V

V

A

K

Y

Y

A

A

K

K

S

S

F

L

T

G

-

F

D

K

D

D

V

I

E

Q

F

F

S

G

P

C

E

E

D

D

A

G

G

G

R

R

S

T

D

E

P

K

E

D

F

F

L

I

Y

C

Q

K

V

I

L

L

E

G

R

E

A

S

I

I

A

K

A

A

G

G

A

A

T

T

I

V

N

G

I

F

P

A

D

D

T

T

V

V

G
|
G

Y

I

T

N

T

M

P

P

S

Q

E

E

F

F

G

G

A

E

I

L

I

V

K

A

G

Y

I

V

K

I

E

E

N

N

V

T

P

P

N

G

I

A

D

D

Q

D

A

I

I

V

I

F

S

A

V

I

H

H

G

C

H

H

N

N

D

D

L

L

G

G

L

V

A

A

V

T

A

A

N

N

F

T

L

I

E

S

A

G

V

I

K

C

N

A

G

G

A

A

R

R

Q

Q

L

V

E

E

C

V

T

T

I

I

N

N

G

G

I

I

G

G

E

E

R

R

A

S

G

G

N

N

A

A

A

P

L

L

E

E

L

V

V

V

M

M

A

A

M

L

H

K

V

C

R

R

R

G

Q

E

Y

S

F

L

N

M

P

D

F

G

L

V

G

-

R

-

H

-

P

-

D

-

S

-

E

-

P

-

L

Y

T

T

N

K

I

I

D

D

T

S

K

R

Q

Q

I

I

Y

M

K

A

T

T

S

S

R

K

L

M

V

V

S

Q

N

E

L

H

T

T

G

G

M

M

L

Y

V

V

Q

Q

P

P

N

H

K

K

A

P

I

I

V

V

G

G

A

D

N

N

A

C

F

F

A

V

H

H

E

E

S

S

G

G

I

I

H

H

Q

Q

D

D

G

G

V

I

L

L

K

K

N

N

K

R

L

S

T

T

Y

Y

E

E

I

I

M

L

D

S

A

P

Q

E

L

D

I

V

G

G

L

I

T

V

D

K

N

S

Q

E

-

N

-

S

-

G

I

I

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

N

H

A

A

F

V

R

K

T

D

R

R

L

L

K

K

E

E

L

L

G

G

F

Y

E

E

L

I

S

S

E

D

T

E

E

K

L

F

N

N

K

D

A

I

F

F

V

S

K

R

F

Y

K

R

E

E

V

L

A

T

D

K

K

D

K

K

E

R

I

I

S

T

D

D

W

A

D

D

L

L

E

K

A

A

I

L

V

V

G263 (= G179) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
55% identity, 63% coverage: 7:338/531 of query aligns to 3:307/308 of 3rmjB

query
sites
3rmjB

R

R

I

V

I

I

F

F

D

D

T

T

L

L

R

R

D
|
D

G

G

E

E

Q
|
Q

C

S

P

P

G

G

A

A

T

A

L

M

N

T

I

K

D

E

E

E

K

K

L

I

A

R

I

V

A

A

K

R

Q

Q

L

L

A

E

R

K

L

L

G

G

V

V

D

D

I

I

E

E

A

A

G

G

F

F

A

A

F

A

A

A

S

S

P

P

G

G

D

D

F

F

E

E

A

A

V

V

H

N

K

A

I

I

A

A

Q

K

T

T

V

I

G

-

T

-

E

-

N

T

G

K

P

S

V

T

I

V

C

C

S

S

L

L

A

S

R

R

A

A

R

I

H

E

D

R

D

D

I

I

K

R

A

Q

A

A

A

G

E

E

A

A

I

V

K

A

P

P

A

A

A

P

K

K

G

K

R

R

I

I

H

H

T

T

F

F

I

I

A

A

T

T

S

S

D

P

I

I

H

H

L

M

Q

E

Y

Y

K

K

L

L

K

K

K

M

T

K

R

P

P

K

E

Q

V

V

I

I

A

E

I

A

A

A

E

V

E

K

M

A

V

V

A

K

Y

I

A

A

K

R

S

E

F

Y

T

T

D

D

V

V

E

E

F

F

S

S

P

C

E

E

D

D

A

A

G

L

R

R

S

S

D

E

P

I

E

D

F

F

L

L

Y

A

Q

E

V

I

L

C

E

G

R

A

A

V

I

I

A

E

A

A

G

G

A

A

T

T

I

I

N

N

I

I

P

P

D

D

T

T

V

V

G

G

Y

Y

T

S

T

I

P

P

S

Y

E

K

F

T

G

E

A

E

I

F

K

R

G

E

I

L

K

I

E

A

N

K

V

T

P

P

N

N

I

G

D

G

Q

K

A

V

I

V

I

W

S

S

V

A

H
|
H

G

C

H
|
H

N

N

D

D

L

L

G

G

L

L

A

A

V

V

A

A

N

N

F

S

L

L

E

A

A

A

V

L

K

K

N

G

G

G

A

A

R

R

Q

Q

L

V

E

E

C

C

T

T

I

V

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N
|
N

A

A

A

S

L

V

E

E

L

I

V

V

M

M

A

A

M

L

H

K

V

V

R

R

R

H

Q

D

Y

L

F

F

N

G

P

L

F

E

L

T

G

G

R

-

H

-

P

-

D

-

S

-

E

-

P

-

L

-

T

-

N

-

I

I

D

D

T

T

K

T

Q

Q

I

I

Y

V

K

P

T

S

S

S

R

K

L

L

V

V

S

S

N

T

L

I

T

T

G

G

M

Y

L

P

V

V

Q

Q

P

P

N

N

K

K

A

A

I

I

V

V

G

G

A

A

N

N

A

A

F

F

A

S

H

H

E

E

S

-

G

-

I

-

H

-

Q

-

D

-

G

-

V

-

L

-

K

-

N

-

K

-

L

-

T

T

Y

Y

E

E

I

I

M

M

D

S

A

A

Q

E

L

S

I

V

G

G

L

W

active site: Q16 (= Q20)
binding manganese (ii) ion: D13 (= D17), H201 (= H208), H203 (= H210), N237 (= N244)

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
34% identity, 70% coverage: 7:378/531 of query aligns to 21:370/399 of 6ktqA

query
sites
6ktqA

R

K

I

V

I

G

I

I

F

L

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

C

T

P

P

G

G

A

V

T

V

L

F

N

T

I

T

D

D

E

Q

K

R

L

V

A

E

I

I

A

A

K

K

Q

A

L

L

A

S

R

D

L

I

G

G

V

V

D

Q

I

M

I

I

E

E

A

A

G

G

F

H

A

P

F

A

A
x
V

S

S

P

P

G

D

D

I

F

Y

E

E

A

G

V

I

H

R

K

R

I

I

A

I

Q

K

T

L

V

-

G

-

T

K

E

R

N

E

G

G

P

V

V

I

-

K

-

S

-

E

I

I

C

V

S

A

L

H

A

S

R
|
R

A
|
A

R

V

H

K

D

R

D

D

I

I

K

E

A

V

A

G

A

A

E

E

A

I

I

-

K

-

P

-

A

-

A

E

K

A

G

D

R

R

I

I

H

A

T

I

F
|
F

I

Y

A

G

T

I

S

S

D

D

I

T

H

H

L

L

Q

K

Y

A

K

K

L
x
H

K

H

K

T

T

T

R

R

P

D

E

E

V

A

I

L

A

R

I

S

A

I

E

A

E

E

M

T

V

V

A

S

Y

Y

A

A

K

K

S

S

F

H

T

G

D

V

D

K

V

V

E
x
R

F

F

S
x
T

P

A

E
|
E

D

D

A

A

G

T

R

R

S

A

D

D

P

Y

E

Q

F

Y

L

L

Y

L

Q

E

V

V

L

I

E

K

R

T

A

V

I

R

A

D

A

A

G

G

A

A

T

D

T

R

I

V

N
x
S

I

I

P

A

D

D

T
|
T

V

V

G

G

Y

V

T

L

T

Y

P

P

S

S

E

R

F

T

G

R

A

E

I

L

I

F

K

K

G

D

I

L

K

T

E

S

N

R

V

F

P

P

N

D

I

I

D

E

Q

-

A

-

I

-

I

F

S

D

V

I

H
|
H

G

A

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

V

A

A

N

N

F

V

L

L

E

A

A

A

V

A

K

E

N

G

G

G

A

A

R

T

Q

I

L

I

E

H

C

T

T

T

I

L

N

N

G

G

I

L

G

G

E

E

R

R

A

V

G

G

N

I

A

A

A

P

L

L

E

Q

E

V

L

V

V

A

M

A

A

A

M

L

H

-

V

-

R

-

R

K

Q

Y

Y

H

F

F

N

G

P

-

F

-

L

-

G

-

R

-

H

-

P

-

D

-

S

-

E

-

P

-

L

I

T

E

N

V

I

V

D

D

T

L

K

K

Q

K

I

L

Y

S

K

E

T

V

S

A

R

S

L

L

V

V

S

E

N

K

L

Y

T

S

G

G

M

I

L

A

V

L

Q

P

P

P

N

N

K

F

A

P

I

I

V

T

G

G

A

D

N

Y

A

A

F

F

A

V

H

H

E

K

S

A

G

G

I

V

H

H

Q

V

D

A

G

G

V

V

L

L

K

N

N

D

K

P

L

K

T

T

Y

Y

E

E

I

F

M

L

D

P

A

P

Q

E

L

T

I

F

G

G

L

R

T

S

D

R

N

D

Q

Y

I

-

V

V

L

I

G

D

K

K

H

Y

S

T

G

G

R

K

N

H

A

A

F

V

R

K

T

D

R

R

L

F

K

D

E

R

L

L

G

G

F

V

E

K

L

L

S

T

E

D

T

S

E

E

L

I

N

D

K

Q

A

V

F

L

V

A

K

K

F

I

K

K

binding 2-oxoglutaric acid: R30 (= R16), R154 (≠ E143), T156 (≠ S145), E158 (= E147), S184 (≠ N173), T188 (= T177), H216 (= H208), H218 (= H210)
binding coenzyme a: V67 (≠ A53), R96 (= R81), A97 (= A82), F116 (= F105), H128 (≠ L117), E158 (= E147)
binding zinc ion: E31 (≠ D17), H216 (= H208), H218 (= H210)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
33% identity, 74% coverage: 5:395/531 of query aligns to 1:377/379 of 4ov4A

query
sites
4ov4A

P

P

E

K

R

T

I

I

I

H

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

C

A

P

L

G

K

A

R

T

P

L

W

N

T

I

I

D

D

E

E

K

K

L

I

A

E

I

V

A

F

K

D

Q

L

L

L

A

V

R

E

L

L

G

N

V

V

D

D

I

G

I

I

E

E

A

V

G

G

F

F

A

P

F

S

A

S

S

N

P

E

G

T

D

E

F

F

E

H

A

T

V

C

H

Q

K

V

I

L

A

S

Q

K

T

R

V

-

G

-

T

A

E

P

N

K

G

G

P

K

V

P

I

I

C

A

S

A

L

L

A

S

R

R

A

A

R

N

H

Q

D

N

D

E

I

I

K

A

A

V

A

T

A

W

E

E

A

A

I

I

K

Q

P

K

A

A

A

D

K

C

G

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

D

D

I

F

H

S

L

I

Q

K

Y

H

K

V

L

L

K

K

K

I

T

S

R

E

P

K

E

E

V

V

I

L

A

Q

I

K

A

I

E

R

E

N

M

S

V

I

A

S

Y

F

A

A

K

R

S

S

F

I

T

V

D

G

-

P

-

G

-

I

D

E

V

I

E

Q

F

F

S

S

P

G

E

E

D

H

A

F

G

G

R

D

S

A

D

I

P

E

E

N

F

F

L

A

Y

F

-

T

-

K

Q

E

V

A

L

F

E

L

R

T

A

A

I

I

A

E

A

A

G

G

A

A

T

N

T

I

I

I

N

N

I

L

P
|
P

D

N

T
|
T

V

V

G

E

Y

R

T

Y

T

R

P

P

S

M

E

V

F

F

G

V

A

N

I

M

I

V

K

K

G

E

I

I

K

K

E

D

N

V

V

V

P

K

N

-

I

-

D

D

Q

K

A

A

I

I

S

S

V

I

H
|
H

G

T

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

T

A

A

N

T

F

S

L

V

E

E

A

S

V

V

K

Y

N

V

G

G

A

A

R

E

Q

Q

L

I

E

E

C

V

T

A

I

L

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

N

L

L

E

Y

E

E

L

T

V

A

M

I

A

A

M

L

H

H

V

Q

R

N

R

G

Q

E

Y

N

F

L

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

-

D

-

S

-

E

-

P

-

L

-

T

-

N

N

I

I

D

N

T

F

K

Q

Q

R

I

I

Y

Y

K

P

T

T

S

A

R

K

L

R

V

I

S

S

N

E

L

L

T

T

G

G

M

I

L

P

V

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

A

E

N

D

A

I

F

F

A

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

D

H

G

-

V

-

L

-

K

Q

N

S

K

K

L

G

T

A

Y

Y

E

R

I

T

M

F

D

S

A

P

Q

E

L

F

I

V

G

G

L

R

T

M

D

D

N

K

Q

E

-

T

I

I

V

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

N

K

A

A

F

I

R

E

T

F

R

L

L

L

K

H

E

Q

L

R

G

G

F

I

E

Q

L

V

S

S

E

K

T

E

E

G

L

I

N

H

K

H

A

L

F

F

V

S

K

L

F

A

K

K

E

S

V

I

A

S

D

S

K

R

K

E

-

N

K

R

E

E

I

I

S

T

D

E

W

A

D

E

L

L

E

V

A

A

I

L

active site: Q16 (= Q20)
binding 3-methyl-2-oxobutanoic acid: R12 (= R16), P174 (= P175), T176 (= T177), H205 (= H208), H207 (= H210)
binding zinc ion: D13 (= D17), H205 (= H208), H207 (= H210)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
33% identity, 74% coverage: 5:395/531 of query aligns to 1:379/380 of 4ov9A

query
sites
4ov9A

P

P

E

K

R

T

I

I

I

H

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

C

A

P

L

G

K

A

R

T

P

L

W

N

T

I

I

D

D

E

E

K

K

L

I

A

E

I

V

A

F

K

D

Q

L

L

L

A

V

R

E

L

L

G

N

V

V

D

D

I

G

I

I

E

E

A

V

G

G

F

F

A

P

F

S

A

S

S

N

P

E

G

T

D

E

F

F

E

H

A

T

V

C

H

Q

K

V

I

L

A

S

Q

K

T

R

V

-

G

-

T

A

E

P

N

K

G

G

P

K

V

P

I

I

C

A

S

A

L
|
L

A

S

R

R

A

A

R

N

H

Q

D

N

D

E

I

I

K

A

A

V

A

T

A

W

E

E

A

A

I

I

K

Q

P

K

A

A

A

D

K

C

G

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

D

D

I

F

H

S

L

I

Q

K

Y

H

K

V

L

L

K

K

K

I

T

S

R

E

P

K

E

E

V

V

I

L

A

Q

I

K

A

I

E

R

E

N

M

S

V

I

A

S

Y

F

A

A

K

R

S

S

F

I

T

V

D

G

-

P

-

G

-

I

D

E

V

I

E

Q

F

F

S

S

P

G

E

E

D

H

A

F

G

G

R

D

S

A

D

I

P

E

E

N

F

F

L

A

Y

F

-

T

-

K

Q

E

V

A

L

F

E

L

R

T

A

A

I

I

A

E

A

A

G

G

A

A

T

N

T

I

I

I

N

N

I

L

P

P

D

N

T
|
T

V

V

G

E

Y

R

T

Y

T

R

P

P

S

M

E

V

F

F

G

V

A

N

I

M

I

V

K

K

G

E

I

I

K

K

E

D

N

V

V

V

P

K

N

-

I

-

D

D

Q

K

A

A

I

I

S

S

V

I

H
|
H

G

T

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

T

A

A

N

T

F

S

L

V

E

E

A

S

V

V

K

Y

N

V

G

G

A

A

R

E

Q

Q

L

I

E

E

C

V

T

A

I

L

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

N

L

L

E

Y

E

E

L

T

V

A

M

I

A

A

M

L

H

H

V

Q

R

N

R

G

Q

E

Y

N

F

L

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

-

D

-

S

-

E

-

P

-

L

-

T

-

N

N

I

I

D

N

T

F

K

Q

Q

R

I

I

Y

Y

K

P

T

T

S

A

R

K

L

R

V

I

S

S

N

E

L

L

T

T

G

G

M

I

L

P

V

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

A

E

N

D

A

I

F

F

A

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

D

T

G

-

V

L

L

H

K

Q

N

S

K

K

L

G

T

A

Y

Y

E

R

I

T

M

F

D

S

A

P

Q

E

L

F

I

V

G

G

L

R

T

M

D

D

N

K

Q

E

-

T

I

I

V

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

N

K

A

A

F

I

R

E

T

F

R

L

L

L

K

H

E

Q

L

R

G

G

F

I

E

Q

L

V

S

S

E

K

T

E

E

G

L

I

N

H

K

H

A

L

F

F

V

S

K

L

F

A

K

K

E

S

V

I

A

S

D

S

K

R

K

E

-

N

K

R

E

E

I

I

S

T

D

E

W

A

D

E

L

L

E

V

A

A

I

L

active site: Q16 (= Q20)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R16), L73 (= L79), T176 (= T177), H205 (= H208), H207 (= H210)
binding zinc ion: D13 (= D17), H205 (= H208), H207 (= H210)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
29% identity, 98% coverage: 1:521/531 of query aligns to 1:515/516 of Q8F3Q1

query
sites
Q8F3Q1

M

M

T

T

T

K

K

V

P

E

E

T

R

R

I

L

I

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

C

T

P

R

G

G

A

V

T

S

L

F

N

S

I

T

D

S

E

E

K

K

L

L

A

N

I

I

A

A

K

K

-

F

Q

L

L

L

A

Q

R

K

L

L

G

N

V

V

D

D

I

R

I

V

E

E

A

I

G

A

F

S

A

A

F

R

A

V

S

S

P

K

G

G

D

E

F

L

E

E

A

T

V

V

H

Q

K

K

I

I

A

M

Q

E

T

W

V

A

G

A

T

T

E

E

N

Q

G

L

P

T

V

E

I

R

C

I

S

E

L

I

-
x
L

-

G

-
x
F

-

V

-

D

A

G

R

N

A

K

R

T

H

V

D

D

D

W

I

I

K

K

-

D

A

S

A

G

A

A

E

K

A

V

I

L

K

N

P

L

A
x
L

A

T

K

K

G

G

R

S

I

L

H

H

T

-

F

-

I

-

A

-

T

-

S

-

D

-

I

-

H

H

L

L

Q

E

Y

K

K

Q

L

L

K

G

K

K

T

T

R

P

P

K

E

E

V

F

I

F

A

T

I

D

A

V

E

S

E

F

M

V

V

I

A

E

Y

Y

A

A

K

I

S

K

F

S

T

G

D

L

D

K

V

I

E

N

F

V

S
x
Y

P

L

E
|
E

D

D

A

W

G

S

-

N

-

G

-

F

R

R

S

N

D

S

P

P

E

D

F

Y

L

V

Y

K

Q

S

V

L

L

V

E

E

R

H

A

L

I

S

A

K

A

E

G

H

A

I

T

E

T

R

I

I

N

F

I

L

P

P

D

D

T
|
T

V

L

G

G

Y

V

T

L

T

S

P

P

S

E

E

E

F

T

G

F

A

Q

I

G

I

V

K

D

G

S

I

L

K

I

E

Q

N

K

V

Y

P

P

N

D

I

I

D

H

Q

-

A

-

I

-

I

F

S

E

V

F

H

H

G

G

H

H

N

N

D

D

L

Y

G

D

L

L

A

S

V

V

A

A

N

N

F

S

L

L

E

Q

A

A

V

I

K

R

N

A

G

G

A

V

R

K

Q

G

L

L

E

H

C

A

T

S

I

I

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

P

L

L

E

E

E

A

L

L

V

V

M

T

A

T

M

I

H

H

V

-

R

-

Q

-

Y

-

F

-

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

-

D

D

S

K

E

S

E

N

P

S

L

K

T

T

N

N

I

I

D

N

T

E

K

I

Q

A

I

I

Y

T

K

E

T

A

S

S

R

R

L

L

V

V

S

E

N

V

L

F

T

S

G

G

M

K

L

R

V

I

Q

S

P

A

N

N

K

R

A

P

I

I

V

V

G

G

A

E

N

D

A

V

F

F

A

T

H

Q

E

T

S

A

G

G

I

V

H
|
H

Q

A

D
|
D

G

G

V

D

L

K

K

K

N

G

K
x
N

L
|
L

T
x
Y

Y

A

E

N

I

P

M

I

D

L

A

P

Q

E

L

R

I

F

G

G

L

-

T

R

D

K

N

R

Q

S

I

Y

V

A

L

L

G

G

K

K

H

L

S

A

G

G

R

K

N

A

A

S

F

I

R

S

T

E

R

N

L

V

K

K

E

Q

L

L

G

G

F

M

E

V

L

L

S

S

E

E

T

V

E

V

L

L

N

Q

K

K

A

V

F

L

V

E

K

R

F

V

K

I

E

E

V

L

A

G

D

D

K

Q

K

N

K

K

E

L

I

V

S

T

D

P

W

E

D

D

L

L

E

P

A

F

I

I

V

I

N

A

D

D

-

V

E

S

I

G

Q

R

Q

T

A

G

P

E

D

K

L

V

F

L

R

T

V

I

E

K

L

S

V

C

Q

N

V

I

S

H

C

S

G

G

S

I

N

G

A

I

R

R

P

P

T

H

A

A

T

Q

V

I

T

E

L

L

R

E

T

Y

P

-

D

Q

G

G

E

K

E

I

L

H

T

K

D

E

A

I

A

S

I

E

G

G

T

D

G

G

P

G

V
x
Y

D
|
D

A

A

V

F

Y

M

K

N

A

A

I

L

N

T

R

K

V

I

V

T

N

N

-

R

-

L

-

G

-

I

-

S

V

I

P

P

N

-

Q

K

L
|
L

I

I

E

D

F
x
Y

S

E

V

V

Q

R

S
x
I

V

P

T

P

A

G

G

G

-

K

I
x
T

D

D

A

A

I

L

G
x
V

E

E

V

T

T

R

I

I

R

T

L

W

R

N

Y

K

-

S

-

L

-

D

-

L

-

E

E

E

S

D

R

Q

V

T

F

F

S

K

G

T

H

M

A

G

A

V

N

H

T
x
P

D

D

I
x
Q

I

T

V

V

A

A

S

A

A

V

Q

H

A

A

Y

T

V

E

N

K

A

M

L

L

N

N

R

Q

L

I

Y

L

A

Q

S

P

L

W

Q

Q

R16 (= R16) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 16:17) binding pyruvate
D17 (= D17) mutation to A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat.; mutation to N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat.
L81 (vs. gap) mutation to A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat.; mutation to V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat.
F83 (vs. gap) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ A97) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ S145) binding pyruvate; mutation to L: 259-fold increase in Km for pyruvate and 76-fold decrease in kcat.; mutation to V: 114-fold increase in Km for pyruvate and 5.3-fold decrease in kcat.
E146 (= E147) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T177) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H317) mutation H->A,N: Loss of activity.
D304 (= D319) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ K325) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (= L326) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ T327) mutation to A: Loss of activity.
Y430 (≠ V446) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (= D447) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L463) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (≠ F466) mutation to A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
I458 (≠ S470) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (≠ I475) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (≠ G479) mutation to A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
P493 (≠ T499) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
Q495 (≠ I501) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
32% identity, 70% coverage: 10:383/531 of query aligns to 6:358/376 of O87198

query
sites
O87198

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

C

F

P

E

G

K

A

A

T

N

L

F

N

S

I

T

D

Q

E

D

K

K

L

V

A

E

I

I

A

A

K

K

Q

A

L

L

A

D

R

E

L

F

G

G

V

I

D

E

I

Y

I

I

E

E

A

V

G

T

F

T

A

P

F

V

A

A

S

S

P

P

G

Q

D

S

F

R

E

K

A

D

V

A

H

E

K

V

I

L

A

A

Q

-

T

S

V

L

G

G

T

L

E

K

N

A

G

K

P

V

V

V

I

T

C
x
H

S

I

L

Q

A

C

R

R

A

-

R

-

H

-

D

-

I

L

K

D

A

A

A

K

E

V

A

A

I

V

K

E

P

T

A

G

A

V

K

Q

G

G

R

-

I

I

H
x
D

T

L

F

L

I

F

A

G

T

T

S

S

D

K

I

-

H

Y

L

L

Q

R

Y

A

K

A

L

H

K

G

K

R

T

D

R

I

P

P

E

R

V

I

I

I

A

E

I

E

A

A

E

K

E

E

M

V

V

I

A

A

Y

Y

A

I

K

R

S

E

F

A

T

A

D

P

D

H

V

V

E

E

-

V

-
x
R

F

F

S
|
S

P

A

E

E

D

D

A

T

G

F

R

R

S

S

D

E

P

E

E

Q

F

D

L

L

Y

L

Q

A

V

V

L

Y

E

E

R

-

A

A

I

V

A

A

A

P

G

Y

A

V

T

D

T

R

I

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

T

A

T

T

P

P

S

R

E

Q

F

V

G

Y

A

A

I

L

I

V

K

R

G

E

I

V

K

R

E

R

N

V

V

V

-

G

P

P

N

R

I

V

D

D

Q

-

A

-

I

-

I

I

S

E

V

F

H
|
H

G

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

A

A

N

N

F

A

L

Y

E

E

A

A

V

I

K

E

N

A

G

G

A

A

R

T

Q

H

L

V

E

D

C

T

T

T

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

L

F

V

L

M

A

A

R

M

M

H

Y

V

T

R

-

Q

-

Y

-

F

L

N

Q

P

P

F

E

L

Y

G

V

R

R

H

R

P

K

D

Y

S

K

E

L

E

E

P

M

L

L

T

P

N

E

I

L

D

D

T

-

K

-

Q

-

I

-

Y

-

K

-

T

-

S

-

R

R

L

M

V

V

S

A

N

R

L

M

T

V

G

G

M

V

L

E

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

E

N

T

A

A

F

F

A

S

H

H

E

K

S

A

G

G

I

M

H

H

Q

L

D

K

G

A

V

I

L

Y

K

I

N

N

K

P

L

E

T

A

Y

Y

E

E

I

P

M

Y

D

P

A

P

Q

E

L

V

I

F

G

G

L

V

T

K

D

R

N

K

Q

L

I

I

V

I

L

A

G

S

K

R

H

L

S

T

G

G

R

R

N

H

A

A

F

I

R

K

T

A

R

R

L

A

K

E

E

E

L

L

G

G

F

L

E

H

L

Y

S

G

E

E

T

E

E

E

L

L

N

H

K

R

A

V

F

T

V

Q

K

H

F

I

K

K

E

A

V

L

A

A

D

D

K

R

R12 (= R16) binding 2-oxoglutarate
E13 (≠ D17) binding Mg(2+)
H72 (≠ C77) binding 2-oxoglutarate; mutation to L: Significant decrease in sensitivity to lysine inhibition. Large decrease in affinity for 2-oxoglutarate. Almost no effect on affinity for acetyl-CoA and on turnover number.
D92 (≠ H103) binding L-lysine
R133 (vs. gap) binding 2-oxoglutarate
S135 (= S145) binding L-lysine
T166 (= T177) binding 2-oxoglutarate; binding L-lysine
H195 (= H208) binding Mg(2+)
H197 (= H210) binding Mg(2+)

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
31% identity, 70% coverage: 10:382/531 of query aligns to 32:381/400 of 3ivtB

query
sites
3ivtB

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

C

F

P

A

G

N

A

A

T

F

L

F

N

D

I

T

D

E

E

K

K

K

L

I

A

Q

I

I

A

A

K

K

Q

A

L

L

A

D

R

N

L

F

G

G

V

V

D

D

I

Y

I

I

E

E

A

L

G

T

F

S

A

P

F

V

A

A

S

S

P

E

G

Q

-

S

-

R

-

Q

D

D

F

C

E

E

A

A

V

I

H

C

K

K

I

L

A

G

Q

L

T

K

V

C

G

K

T

-

E

-

N

-

G

-

P

-

V

-

I

I

C

L

S

T

L
x
H

A

I

R

R

A

C

R

H

H

M

D

D

I

A

K

R

A

V

A

A

A

V

E

E

A

T

I

-

K

-

P

-

A

G

A

V

K

D

G

G

R

-

I

V

H

D

T

V

F

V

I

I

A

G

T

T

S

S

D

Q

I

Y

H

L

L

R

Q

K

Y

Y

K

S

L

H

K

G

K

K

T

D

R

M

P

T

E

Y

V

I

I

I

A

D

I

S

A

A

E

T

E

E

M

V

V

I

A

N

Y

F

A

V

K

K

S

S

F

K

T

G

D

I

D

E

V

V

E
x
R

F

F

S
|
S

P

S

E

E

D

D

A

S

G

F

R

R

S

S

D

D

P

L

E

V

F

D

L

L

Y

L

Q

S

V

L

L

Y

E

K

R

A

A

V

I

D

A

K

A

I

G

G

A

V

T

N

T

R

I

V

N

G

I

I

P

A

D

D

T
|
T

V

V

G

G

Y

C

T

A

T

T

P

P

S

R

E

Q

F

V

G

Y

A

D

I

L

I

I

K

R

G

T

I

L

K

R

E

-

N

G

V

V

P

V

N

S

I

C

D

D

Q

-

A

-

I

-

I

I

S

E

V

C

H
|
H

G

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

A

A

N

N

F

A

L

Y

E

C

A

A

V

L

K

E

N

A

G

G

A

A

R

T

Q

H

L

I

E

D

C

T

T

S

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

E

A

L

L

V

L

M

A

A

R

M

M

H

Y

V

V

R

-

Q

-

Y

-

F

-

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

T

D

D

S

R

E

E

E

Y

P

I

L

T

T

H

N

K

I

Y

D

K

T

L

K

N

Q

Q

I

L

Y

R

K

E

T

L

S

E

R

N

L

L

V

V

S

A

N

D

L

A

T

V

G

E

M

V

L

Q

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

M

N

C

A

A

F

F

A

T

H

H

E

K

S

A

G

G

I

I

H

H

Q

A

D

K

G

A

V

I

L

L

K

A

N

N

K

P

L

S

T

T

Y

Y

E

E

I

I

M

L

D

K

A

P

Q

E

L

D

I

F

G

G

L

M

T

S

D

R

N

Y

Q

V

I

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

R

K

T

S

R

R

L

A

K

E

E

Q

L

L

G

N

F

L

E

H

L

L

S

T

E

D

T

A

E

Q

L

A

N

K

K

E

A

L

F

T

V

V

K

R

F

I

K

K

E

K

V

L

A

A

D

D

active site: Q42 (= Q20)
binding 2-oxoglutaric acid: R38 (= R16), H98 (≠ L79), R158 (≠ E143), S160 (= S145), T192 (= T177), H219 (= H208), H221 (= H210)
binding zinc ion: E39 (≠ D17), H219 (= H208), H221 (= H210)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
31% identity, 70% coverage: 10:382/531 of query aligns to 37:386/418 of Q9Y823

query
sites
Q9Y823

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

C

F

P

A

G

N

A

A

T

F

L

F

N

D

I

T

D

E

E

K

K

K

L

I

A

Q

I

I

A

A

K

K

Q

A

L

L

A

D

R

N

L

F

G

G

V

V

D

D

I

Y

I

I

E
|
E

A

L

G

T

F

S

A

P

F

V

A

A

S

S

P

E

G

Q

-

S

-

R

-

Q

D

D

F

C

E

E

A

A

V

I

H

C

K

K

I

L

A

G

Q

L

T

K

V

C

G

K

T

-

E

-

N

-

G

-

P

-

V

-

I

I

C

L

S

T

L
x
H

A

I

R

R

A

C

R

H

H

M

D

D

I

A

K

R

A

V

A

A

A

V

E

E

A

T

I

-

K

-

P

-

A

G

A

V

K

D

G

G

R

-

I

V

H
x
D

T

V

F

V

I

I

A

G

T

T

S

S

D

Q

I

Y

H

L

L

R

Q

K

Y

Y

K

S

L

H

K

G

K

K

T

D

R

M

P

T

E

Y

V

I

I

I

A

D

I

S

A

A

E

T

E

E

M

V

V

I

A

N

Y

F

A

V

K

K

S

S

F

K

T

G

D

I

D

E

V

V

E
x
R

F

F

S
|
S

P

S

E
|
E

D

D

A

S

G

F

R

R

S

S

D

D

P

L

E

V

F

D

L

L

Y

L

Q

S

V

L

L

Y

E

K

R

A

A

V

I

D

A

K

A

I

G

G

A

V

T

N

T

R

I

V

N

G

I

I

P

A

D

D

T
|
T

V

V

G

G

Y

C

T

A

T

T

P

P

S

R

E

Q

F

V

G

Y

A

D

I

L

I

I

K

R

G

T

I

L

K

R

E

-

N

G

V

V

P

V

N

S

I

C

D

D

Q

-

A

-

I

-

I

I

S
x
E

V

C

H
|
H

G

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

A

A

N

N

F

A

L

Y

E

C

A

A

V

L

K

E

N

A

G

G

A

A

R

T

Q

H

L

I

E

D

C

T

T

S

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

E

A

L

L

V

L

M

A

A

R

M

M

H

Y

V

V

R

-

Q

-

Y

-

F

-

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

T

D

D

S

R

E

E

E

Y

P

I

L

T

T

H

N

K

I

Y

D

K

T

L

K

N

Q

Q

I

L

Y
x
R

K

E

T

L

S

E

R

N

L

L

V

V

S

A

N

D

L

A

T

V

G

E

M

V

L

Q

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

M

N

C

A

A

F

F

A

T

H

H

E

K

S

A

G

G

I

I

H

H

Q

A

D

K

G

A

V

I

L

L

K

A

N

N

K

P

L

S

T

T

Y
|
Y

E

E

I

I

M

L

D

K

A

P

Q

E

L

D

I

F

G

G

L

M

T

S

D

R

N

Y

Q

V

I

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

R

K

T

S

R

R

L

A

K

E

E
x
Q

L

L

G

N

F

L

E

H

L

L

S

T

E

D

T

A

E

Q

L

A

N

K

K

E

A

L

F

T

V

V

K

R

F

I

K

K

E

K

V

L

A

A

D

D

R43 (= R16) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D17) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q20) mutation to A: Abolishes the catalytic activity.
E74 (= E47) mutation to A: Abolishes the catalytic activity.; mutation to Q: Results in a moderate decrease in the turnover number and a slight increase in the Km value for each substrate.
H103 (≠ L79) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ H103) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ E143) binding 2-oxoglutarate; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
S165 (= S145) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E147) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T177) binding 2-oxoglutarate; binding L-lysine; mutation to A: Exhibits a 25-fold decrease in catalytic efficiency.; mutation to S: Results in a modest decrease in catalytic efficiency.; mutation to V: Abolishes the catalytic activity.
E222 (≠ S206) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H208) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H210) binding 2-oxoglutarate; binding Zn(2+)
R288 (≠ Y284) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y328) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ E360) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
32% identity, 59% coverage: 7:317/531 of query aligns to 1:296/311 of 3bliA

query
sites
3bliA

R

R

I

L

I

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q
|
Q

C

T

P

R

G

G

A

V

T

S

L

F

N

S

I

T

D

S

E

E

K

K

L

L

A

N

I

I

A

A

K

K

-

F

Q

L

L

L

A

Q

R

K

L

L

G

N

V

V

D

D

I

R

I

V

E

E

A

I

G

A

F

S

A

A

F
x
R

A
x
V

S

S

P

K

G

G

D

E

F

L

E

E

A

T

V

V

H

Q

K

K

I

I

A

M

Q

E

T

W

V

A

G

A

T

T

E

E

N

Q

G

L

P

T

V

E

I

R

C

I

S

E

L

I

-

L

-

G

-

F

-

V

-

D

A

G

R

N

A

K

R

T

H

V

D

D

D

W

I

I

K

K

-

D

A

S

A

G

A

A

E

K

A

V

I

L

K

N

P

L

A

L

A

T

K

K

G

G

R

S

I

L

H

H

T

-

F

-

I

-

A

-

T

-

S

-

D

-

I

-

H

H

L

L

Q

E

Y

K

K

Q

L

L

K

G

K

K

T

T

R

P

P

K

E

E

V

F

I

F

A

T

I

D

A

V

E

S

E

F

M

V

V

I

A

E

Y

Y

A

A

K

I

S

K

F

S

T

G

D

L

D

K

V

I

E

N

F

V

S
x
Y

P

L

E
|
E

D

D

A

W

G

S

-

N

-

G

-

F

R

R

S

N

D

S

P

P

E

D

F

Y

L

V

Y

K

Q

S

V

L

L

V

E

E

R

H

A

L

I

S

A

K

A

E

G

H

A

I

T

E

T

R

I

I

N

F

I

L

P
|
P

D

D

T
|
T

V

L

G

G

Y

V

T

L

T

S

P

P

S

E

E

E

F

T

G

F

A

Q

I

G

I

V

K

D

G

S

I

L

K

I

E

Q

N

K

V

Y

P

P

N

D

I

I

D

H

Q

-

A

-

I

-

I

F

S

E

V

F

H
|
H

G

G

H
|
H

N

N

D

D

L

Y

G

D

L

L

A

S

V

V

A

A

N

N

F

S

L

L

E

Q

A

A

V

I

K

R

N

A

G

G

A

V

R

K

Q

G

L

L

E

H

C

A

T

S

I

I

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

P

L

L

E

E

E

A

L

L

V

V

M

T

A

T

M

I

H

H

V

-

R

-

Q

-

Y

-

F

-

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

-

D

D

S

K

E

S

E

N

P

S

L

K

T

T

N

N

I

I

D

N

T

E

K

I

Q

A

I

I

Y

T

K

E

T

A

S

S

R

R

L

L

V

V

S

E

N

V

L

F

T

S

G

G

M

K

L

R

V

I

Q

S

P

A

N

N

K

R

A

P

I

I

V

V

G

G

A

E

N

D

A

V

F

F

A

T

H

Q

E

T

S

A

G

G

I

V

H

N

active site: Q14 (= Q20)
binding acetyl coenzyme *a: Q14 (= Q20), R47 (≠ F52), V48 (≠ A53), E140 (= E147)
binding pyruvic acid: R10 (= R16), Y138 (≠ S145), P171 (= P175), T173 (= T177)
binding zinc ion: D11 (= D17), H201 (= H208), H203 (= H210)

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
30% identity, 71% coverage: 10:384/531 of query aligns to 14:354/370 of 3mi3A

query
sites
3mi3A

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

C

F

P

A

G

N

A

A

T

F

L

F

N

D

I

T

D

E

E

K

K

K

L

I

A

Q

I

I

A

A

K

K

Q

A

L

L

A

D

R

N

L

F

G

G

V

V

D

D

I

Y

I

I

E

E

A

L

G

T

F

S

A

P

F

V

A

A

S

S

P

E

G

Q

-

S

-

R

-

Q

D

D

F

C

E

E

A

A

V

I

H

C

K

K

I

L

A

G

Q

L

T

K

V

C

G

K

T

-

E

-

N

-

G

-

P

-

V

-

I

I

C

L

S

T

L

H

A

I

R

R

A

C

R

H

H

M

D

D

I

A

K

R

A

V

A

A

A

V

E

E

A

T

I

-

K

-

P

-

A

G

A

V

K

D

G

G

R

-

I

V

H
x
D

T

V

F

V

I

I

A

G

T

T

S

S

D

-

I

-

H

-

L

M

Q

T

Y

Y

K

-

L

-

K

-

T

-

R

-

P

-

E

-

V

I

I

I

A

D

I

S

A

A

E

T

E

E

M

V

V

I

A

N

Y

F

A

V

K

K

S

S

F

K

T

G

D

I

D

E

V

V

E

R

F

F

S

S

P

S

E

E

D

D

A

S

G

F

R

R

S

S

D

D

P

L

E

V

F

D

L

L

Y

L

Q

S

V

L

L

Y

E

K

R

A

A

V

I

D

A

K

A

I

G

G

A

V

T

N

T

R

I

V

N

G

I

I

P

A

D

D

T
|
T

V

V

G

G

Y

C

T

A

T

T

P

P

S

R

E

Q

F

V

G

Y

A

D

I

L

I

I

K

R

G

T

I

L

K

R

E

-

N

G

V

V

P

V

N

S

I

C

D

D

Q

-

A

-

I

-

I

I

S

E

V

C

H
|
H

G

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

A

A

N

N

F

A

L

Y

E

C

A

A

V

L

K

E

N

A

G

G

A

A

R

T

Q

H

L

I

E

D

C

T

T

S

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

E

A

L

L

V

L

M

A

A

R

M

M

H

Y

V

V

R

-

Q

-

Y

-

F

-

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

T

D

D

S

R

E

E

E

Y

P

I

L

T

T

H

N

K

I

Y

D

K

T

L

K

N

Q

Q

I

L

Y

R

K

E

T

L

S

E

R

N

L

L

V

V

S

A

N

D

L

A

T

V

G

E

M

V

L

Q

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

M

N

C

A

A

F

F

A

T

H

H

E

K

S

A

G

G

I

I

H

H

Q

A

D

K

G

A

V

I

L

L

K

A

N

N

K

P

L

S

T

T

Y

Y

E

E

I

I

M

L

D

K

A

P

Q

E

L

D

I

F

G

G

L

M

T

S

D

R

N

Y

Q

V

I

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

R

K

T

S

R

R

L

A

K

E

E

Q

L

L

G

N

F

L

E

H

L

L

S

T

E

D

T

A

E

Q

L

A

N

K

K

E

A

L

F

T

V

V

K

R

F

I

K

K

E

K

V

L

A

A

D

D

K

V

K

R

active site: Q24 (= Q20)
binding lysine: R20 (= R16), D100 (≠ H103), T163 (= T177), H190 (= H208), H192 (= H210)
binding zinc ion: E21 (≠ D17), H190 (= H208), H192 (= H210)

3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 72% coverage: 10:391/531 of query aligns to 14:356/364 of 3ivsA

query
sites
3ivsA

I

I

F

I

D

E

T

S

T

T

L

L

R

R

D
x
E

G

G

E

E

Q
|
Q

C

F

P

A

G

N

A

A

T

F

L

F

N

D

I

T

D

E

E

K

K

K

L

I

A

Q

I

I

A

A

K

K

Q

A

L

L

A

D

R

N

L

F

G

G

V

V

D

D

I

Y

I

I

E

E

A

L

G

T

F

S

A

P

F

V

A

A

S

S

P

E

G

Q

-

S

-

R

-

Q

D

D

F

C

E

E

A

A

V

I

H

C

K

K

I

L

A

G

Q

L

T

K

V

C

G

K

T

-

E

-

N

-

G

-

P

-

V

-

I

I

C

L

S

T

L

H

A

I

R

R

A

C

R

H

H

M

D

D

I

A

K

R

A

V

A

A

A

V

E

E

A

T

I

-

K

-

P

-

A

G

A

V

K

D

G

G

R

-

I

V

H

D

T

V

F

V

I

I

A

G

T

T

S

T

D

Y

I

I

H

-

L

-

Q

-

Y

-

K

-

L

-

K

-

T

-

R

-

P

-

E

-

V

-

I

I

A

D

I

S

A

A

E

T

E

E

M

V

V

I

A

N

Y

F

A

V

K

K

S

S

F

K

T

G

D

I

D

E

V

V

E

R

F

F

S

S

P

S

E

E

D

D

A

S

G

F

R

R

S

S

D

D

P

L

E

V

F

D

L

L

Y

L

Q

S

V

L

L

Y

E

K

R

A

A

V

I

D

A

K

A

I

G

G

A

V

T

N

T

R

I

V

N

G

I

I

P

A

D

D

T

T

V

V

G

G

Y

C

T

A

T

T

P

P

S

R

E

Q

F

V

G

Y

A

D

I

L

I

I

K

R

G

T

I

L

K

R

E

-

N

G

V

V

P

V

N

S

I

C

D

D

Q

-

A

-

I

-

I

I

S

E

V

C

H
|
H

G

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

A

A

N

N

F

A

L

Y

E

C

A

A

V

L

K

E

N

A

G

G

A

A

R

T

Q

H

L

I

E

D

C

T

T

S

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

E

A

L

L

V

L

M

A

A

R

M

M

H

Y

V

V

R

-

Q

-

Y

-

F

-

N

-

P

-

F

-

L

-

G

-

R

-

H

-

P

T

D

D

S

R

E

E

E

Y

P

I

L

T

T

H

N

K

I

Y

D

K

T

L

K

N

Q

Q

I

L

Y

R

K

E

T

L

S

E

R

N

L

L

V

V

S

A

N

D

L

A

T

V

G

E

M

V

L

Q

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

M

N

C

A

A

F

F

A

T

H

H

E

K

S

A

G

G

I

I

H

H

Q

A

D

K

G

A

V

I

L

L

K

A

N

N

K

P

L

S

T

T

Y

Y

E

E

I

I

M

L

D

K

A

P

Q

E

L

D

I

F

G

G

L

M

T

S

D

R

N

Y

Q

V

I

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

R

K

T

S

R

R

L

A

K

E

E

Q

L

L

G

N

F

L

E

H

L

L

S

Q

E

A

T

K

E

E

L

L

N

T

K

-

A

-

F

-

V

V

K

R

F

I

K

K

E

K

V

L

A

A

D

V

K

R

K

T

K

L

E

A

I

M

S

D

D

D

W

V

D

D

active site: Q24 (= Q20)
binding cobalt (ii) ion: E21 (≠ D17), H188 (= H208), H190 (= H210)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
31% identity, 63% coverage: 10:344/531 of query aligns to 6:313/314 of 2zyfA

query
sites
2zyfA

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

C

F

P

E

G

K

A

A

T

N

L

F

N

S

I

T

D

Q

E

D

K

K

L

V

A

E

I

I

A

A

K

K

Q

A

L

L

A

D

R

E

L

F

G

G

V

I

D

E

I

Y

I

I

E

E

A

V

G

T

F

T

A

P

F

V

A

A

S

S

P

P

G

Q

D

S

F

R

E

K

A

D

V

A

H

E

K

V

I

L

A

A

Q

-

T

S

V

L

G

G

T

L

E

K

N

A

G

K

P

-

V

-

I

V

C

V

S

T

L
x
H

A

I

R

Q

A

C

R

R

H

L

D

D

D

A

I

A

K

K

A

V

A

A

A

V

E

E

A

T

I

-

K

-

P

-

A

-

K

-

G

-

R

-

I

-

H

-

T

-

F

-

I

-

A

G

T

V

S

Q

D

G

I

I

H

D

L

L

Q
x
L

Y

F

K

G

L

T

K

S

K

K

T

G

R

R

-

D

-

I

P

P

E

R

V

I

I

I

A

E

I

E

A

A

E

K

E

E

M

V

V

I

A

A

Y

Y

A

I

K

R

S

E

F

A

T

A

D

P

D

H

V

V

E

E

-

V

-
x
R

F

F

S

S

P

A

E

E

D

D

A

T

G

F

R

R

S

S

D

E

P

E

E

Q

F

D

L

L

Y

L

Q

A

V

V

L

Y

E

E

R

-

A

A

I

V

A

A

A

P

G

Y

A

V

T

D

T

R

I

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

T

A

T

T

P

P

S

R

E

Q

F

V

G

Y

A

A

I

L

I

V

K

R

G

E

I

V

K

R

E

R

N

V

V

V

-

G

P

P

N

R

I

V

D

D

Q

-

A

-

I

-

I

I

S

E

V

F

H
|
H

G

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

A

A

N

N

F

A

L

Y

E

E

A

A

V

I

K

E

N

A

G

G

A

A

R

T

Q

H

L

V

E

D

C

T

T

T

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

L

F

V

L

M

A

A

R

M

M

H

Y

V

T

R

-

Q

-

Y

-

F

L

N

Q

P

P

F

E

L

Y

G

V

R

R

H

R

P

K

D

Y

S

K

E

L

E

E

P

M

L

L

T

P

N

E

I

L

D

D

T

-

K

-

Q

-

I

-

Y

-

K

-

T

-

S

-

R

R

L

M

V

V

S

A

N

R

L

M

T

V

G

G

M

V

L

E

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

E

N

T

A

A

F

F

A

S

H

H

E

K

S

A

G

G

I

M

H

H

Q

L

D

K

G

A

V

I

L

Y

K

I

N

N

K

P

L

E

T

A

Y

Y

E

E

I

P

M

Y

D

P

A

P

Q

E

L

V

I

F

G

G

L

V

T

K

D

R

N

K

Q

L

I

I

V

I

active site: Q16 (= Q20)
binding 2-oxoglutaric acid: R12 (= R16), H72 (≠ L79), L94 (≠ Q114), R127 (vs. gap), T160 (= T177), H189 (= H208)
binding magnesium ion: E13 (≠ D17), H189 (= H208), H191 (= H210)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
30% identity, 63% coverage: 10:344/531 of query aligns to 6:311/312 of 2ztjA

query
sites
2ztjA

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

C

F

P

E

G

K

A

A

T

N

L

F

N

S

I

T

D

Q

E

D

K

K

L

V

A

E

I

I

A

A

K

K

Q

A

L

L

A

D

R

E

L

F

G

G

V

I

D

E

I

Y

I

I

E

E

A

V

G

T

F

T

A

P

F

V

A

A

S

S

P

P

G

Q

D

S

F

R

E

K

A

D

V

A

H

E

K

V

I

L

A

A

Q

-

T

S

V

L

G

G

T

L

E

K

N

A

G

K

P

-

V

-

I

V

C

V

S

T

L
x
H

A

I

R

Q

A

C

R

R

H

L

D

D

D

A

I

A

K

K

A

V

A

A

A

V

E

E

A

T

I

-

K

-

P

-

A

-

K

-

G

-

R

-

I

-

H

-

T

-

F

-

I

-

A

G

T

V

S

Q

D

G

I

I

H

D

L

L

Q
x
L

Y

F

K

G

L

T

K

G

K

R

T

D

R

I

P

P

E

R

V

I

I

I

A

E

I

E

A

A

E

K

E

E

M

V

V

I

A

A

Y

Y

A

I

K

R

S

E

F

A

T

A

D

P

D

H

V

V

E

E

-

V

-
x
R

F

F

S

S

P

A

E

E

D

D

A

T

G

F

R

R

S

S

D

E

P

E

E

Q

F

D

L

L

Y

L

Q

A

V

V

L

Y

E

E

R

-

A

A

I

V

A

A

A

P

G

Y

A

V

T

D

T

R

I

V

N

G

I

L

P
x
A

D

D

T
|
T

V

V

G

G

Y

V

T

A

T

T

P

P

S

R

E

Q

F

V

G

Y

A

A

I

L

I

V

K

R

G

E

I

V

K

R

E

R

N

V

V

V

-

G

P

P

N

R

I

V

D

D

Q

-

A

-

I

-

I

I

S

E

V

F

H
|
H

G

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

A

A

N

N

F

A

L

Y

E

E

A

A

V

I

K

E

N

A

G

G

A

A

R

T

Q

H

L

V

E

D

C

T

T

T

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

L

F

V

L

M

A

A

R

M

M

H

Y

V

T

R

-

Q

-

Y

-

F

L

N

Q

P

P

F

E

L

Y

G

V

R

R

H

R

P

K

D

Y

S

K

E

L

E

E

P

M

L

L

T

P

N

E

I

L

D

D

T

-

K

-

Q

-

I

-

Y

-

K

-

T

-

S

-

R

R

L

M

V

V

S

A

N

R

L

M

T

V

G

G

M

V

L

E

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

E

N

T

A

A

F

F

A

S

H

H

E

K

S

A

G

G

I

M

H

H

Q

L

D

K

G

A

V

I

L

Y

K

I

N

N

K

P

L

E

T

A

Y

Y

E

E

I

P

M

Y

D

P

A

P

Q

E

L

V

I

F

G

G

L

V

T

K

D

R

N

K

Q

L

I

I

V

I

active site: Q16 (= Q20)
binding 2-oxoglutaric acid: R12 (= R16), H72 (≠ L79), L94 (≠ Q114), R125 (vs. gap), A156 (≠ P175), T158 (= T177), H187 (= H208), H189 (= H210)
binding copper (ii) ion: E13 (≠ D17), H187 (= H208), H189 (= H210)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
32% identity, 64% coverage: 10:350/531 of query aligns to 5:312/347 of 3a9iA

query
sites
3a9iA

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

C

F

P

E

G

K

A

A

T

N

L

F

N

S

I

T

D

Q

E

D

K

K

L

V

A

E

I

I

A

A

K

K

Q

A

L

L

A

D

R

E

L

F

G

G

V

I

D

E

I

Y

I

I

E

E

A

V

G

T

F

T

A

P

F

V

A

A

S

S

P

P

G

Q

D

S

F

R

E

K

A

D

V

A

H

E

K

V

I

L

A

A

Q

-

T

S

V

L

G

G

T

L

E

K

N

A

G

K

P

V

V

V

I

T

C

H

S

I

L

Q

A

C

R

R

A

-

R

-

H

-

D

-

I

L

K

D

A

A

A

K

E

V

A

A

I

V

K

E

P

T

A

G

A

V

K

Q

G

G

R

-

I

I

H
x
D

T

L

F

L

I

F

A

G

T

T

S

S

-

K

-

Y

-

L

D

D

I

I

H

-

L

-

Q

-

Y

-

K

-

L

-

K

-

T

-

R

-

P

P

E

R

V

I

I

I

A

E

I

E

A

A

E

K

E

E

M

V

V

I

A

A

Y

Y

A

I

K

R

S

E

F

A

T

A

D

P

D

H

V

V

E

E

-

V

-

R

F

F

S
|
S

P

A

E

E

D

D

A

T

G

F

R

R

S

S

D

E

P

E

E

Q

F

D

L

L

Y

L

Q

A

V

V

L

Y

E

E

R

-

A

A

I

V

A

A

A

P

G

Y

A

V

T

D

T

R

I

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

T

A

T

T

P

P

S

R

E

Q

F

V

G

Y

A

A

I

L

I

V

K

R

G

E

I

V

K

R

E

R

N

V

V

V

-

G

P

P

N

R

I

V

D

D

Q

-

A

-

I

-

I

I

S

E

V

F

H
|
H

G

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

A

A

N

N

F

A

L

Y

E

E

A

A

V

I

K

E

N

A

G

G

A

A

R

T

Q

H

L

V

E

D

C

T

T

T

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

L

F

V

L

M

A

A

R

M

M

H

Y

V

T

R

-

Q

-

Y

-

F

L

N

Q

P

P

F

E

L

Y

G

V

R

R

H

R

P

K

D

Y

S

K

E

L

E

E

P

M

L

L

T

P

N

E

I

L

D

D

T

-

K

-

Q

-

I

-

Y

-

K

-

T

-

S

-

R

R

L

M

V

V

S

A

N

R

L

M

T

V

G

G

M

V

L

E

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

E

N

T

A

A

F

F

A

S

H

H

E

K

S

A

G

G

I

M

H

H

Q

L

D

K

G

A

V

I

L

Y

K

I

N

N

K

P

L

E

T

A

Y

Y

E

E

I

P

M

Y

D

P

A

P

Q

E

L

V

I

F

G

G

L

-

T

-

D

-

N

-

Q

-

I

-

V

V

L

K

G

G

K

L

H

H

S

Y

G

G

binding cobalt (ii) ion: E12 (≠ D17), H188 (= H208), H190 (= H210)
binding lysine: R11 (= R16), D91 (≠ H103), S128 (= S145), T159 (= T177), H188 (= H208), H190 (= H210)

3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
25% identity, 97% coverage: 3:515/531 of query aligns to 45:574/576 of 3hpzB

query
sites
3hpzB

T

T

K

W

P

P

E

D

R

R

I

V

I

I

-

D

-

R

-

A

-

P

-

L

I

W

F

C

D

A

T

V

T

D

L

L

R

R

D
|
D

G

G

E

N

Q

Q

C

A

P

L

G

I

A

D

T

P

L

M

N

S

I

P

D

A

E

R

K

K

L

R

A

R

I

M

A

F

K

D

Q

L

L

L

A

V

R

R

L

M

G

G

V

Y

D

K

I

E

I

I

E

E

A

V

G

G

F

F

A

P

F

S

A

A

S

S

P

Q

G

T

D

D

F

F

E

D

A

F

V

V

H

R

K

E

I

I

A

I

Q

E

T

Q

V

G

G

A

T

I

E

P

N

D

G

D

P

V

V

T

I

I

C

Q

S

V

L

L

A

T

R

Q

A

C

R

R

H

P

D

E

D

L

I

I

K

E

A

R

A

T

A

F

E

Q

A

A

I

C

K

S

P

G

A

A

A

P

K

R

G

A

R

I

I

V

H

H

T

F

F

Y

I

N

A

S

T

T

S

S

D

I

I

L

H

Q

L

R

Q

R

Y

V

K

V

L

F

K

R

K

A

T

N

R

R

P

A

E

E

V

V

I

Q

A

A

I

I

A

A

E

T

-

D

-

G

-

A

-

R

-

K

-

C

-

V

E

E

M

Q

V

A

A

A

Y

K

A

Y

K

P

S

G

F

T

T

Q

D

W

D

R

V

F

E

E

F

Y

S

S

P

P

E
|
E

D

S

A

Y

G

T

R

G

S

T

D

E

P

L

E

E

F

Y

L

A

Y

K

Q

Q

V

V

L

C

E

D

R

A

A

V

I

G

A

E

A

V

G

I

A

A

T

P

T

T

-

P

-

E

-

R

-

P

-

I

I

F

N

N

I

L

P
|
P

D

A

T
|
T

V

V

G

E

Y

M

T

T

P

P

S

N

E

V

F

Y

G

A

A

D

I

S

I

I

K

E

G

W

I

M

K

S

E

R

N

N

V

L

P

A

N

N

I

R

D

E

Q

S

A

V

I

I

I

L

S

S

V

L

H
|
H

G

P

H
|
H

N

N

D

D

L

R

G

G

L

T

A

A

V

V

A

A

N

A

F

A

L

E

E

L

A

G

V

F

K

A

N

A

G

G

A

A

R

D

Q

R

L

I

E

E

C

G

T

C

I

L

N

F

G

G

I

N

G

G

E

E

R

R

A

T

G

G

N

N

A

V

A

C

L

L

E

V

E

T

L

L

V

G

M

L

A

N

M

L

H

-

V

-

R

-

Q

-

Y

-

F

-

N

-

P

-

F

-

L

F

G

S

R

R

H

G

P

V

D

D

S

P

E

Q

E

I

P

D

L

F

T

S

N

N

I

I

D

D

T

-

K

-

Q

E

I

I

Y

R

K

R

T

T

S

V

R

E

L

Y

V

C

S

N

N

Q

L

L

T

P

G

V

M

H

L

E

V

R

Q

H

P

P

N

Y

K

G

A

G

I

D

V

L

G

V

A

Y

N

T

A

A

F

F

A

-

H

-

E

-

S

S

G

G

I

S

H

H

Q

Q

D

D

G

A

V

I

L

N

K

K

N

G

-

L

-

D

-

A

-

M

-

K

-

L

-

D

-

A

-

D

-

A

-

D

-

C

-

D

-

V

-

D

-

M

-

L

-

W

K

Q

L

V

T

P

Y

Y

E

L

I

P

M

I

D

D

A

P

Q

R

L

D

I

V

G

G

L

R

T

T

D

-

N

Y

Q

E

I

A

V

V

L

I

G

R

K

V

H

N

S

K

G

G

R

G

N

V

A

A

F

Y

R

I

T

M

R

K

L

-

K

T

E

D

L

H

G

G

F

L

E

S

L

L

S

P

E

R

T

-

E

-

L

-

N

-

K

R

A

L

F

Q

V

I

K

E

F

F

K

S

E

Q

V

V

A

I

D

Q

K

K

K

V

K

S

E

P

I

K

S

E

D

M

W

W

D

D

L

-

E

-

A

A

I

F

V

A

N

E

D

E

E

Y

I

L

Q

A

Q

P

A

V

P

R

D

P

L

L

F

E

R

R

V

I

-

R

E

Q

L

H

V

V

Q

D

V

A

S

A

C

D

G

D

S

D

N

G

A

G

R

T

P

T

T

S

A

I

T

T

V

A

T

T

L

V

R

K

T

I

P

-

D

N

G

G

E

V

E

E

L

T

T

E

D

I

A

S

A

G

I

S

G

G

T

N

G

G

P

P

V

L

D

A

A

A

V

F

Y

V

K

H

A

A

I

L

N

A

R

D

V

-

V

V

N

G

V

F

P

D

N

V

Q

A

L

V

I

L

E

D

F

Y

S

Y

V

E

Q

H

S

A

V

M

T

S

A

A

G

G

I

D

D

D

A

A

I

Q

G

A

E

A

V

A

T

Y

I

V

R

E

L

A

R

S

Y

V

-

T

-

I

-

A

E

T

S

S

R

K

V

T

F

V

S

W

G

G

H

V

A

G

A

I

N

A

T

P

D

S

I

I

I

T

V

T

A

A

S

S

A

L

Q

R

A

A

Y

V

V

V

N

S

A

A

L

V

N

N

R

R

binding Bromopyruvate: E201 (= E147), P235 (= P175), T237 (= T177), H268 (= H208), H270 (= H210)
binding zinc ion: D64 (= D17), H268 (= H208), H270 (= H210)

Query Sequence

>WP_011318900.1 NCBI__GCF_000204075.1:WP_011318900.1
MTTKPERIIIFDTTLRDGEQCPGATLNIDEKLAIAKQLARLGVDIIEAGFAFASPGDFEA
VHKIAQTVGTENGPVICSLARARHDDIKAAAEAIKPAAKGRIHTFIATSDIHLQYKLKKT
RPEVIAIAEEMVAYAKSFTDDVEFSPEDAGRSDPEFLYQVLERAIAAGATTINIPDTVGY
TTPSEFGAIIKGIKENVPNIDQAIISVHGHNDLGLAVANFLEAVKNGARQLECTINGIGE
RAGNAALEELVMAMHVRRQYFNPFLGRHPDSEEPLTNIDTKQIYKTSRLVSNLTGMLVQP
NKAIVGANAFAHESGIHQDGVLKNKLTYEIMDAQLIGLTDNQIVLGKHSGRNAFRTRLKE
LGFELSETELNKAFVKFKEVADKKKEISDWDLEAIVNDEIQQAPDLFRVELVQVSCGSNA
RPTATVTLRTPDGEELTDAAIGTGPVDAVYKAINRVVNVPNQLIEFSVQSVTAGIDAIGE
VTIRLRYESRVFSGHAANTDIIVASAQAYVNALNRLYASLQTQDKQTEVTA

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