SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_010442890.1 NCBI__GCF_000192475.1:WP_010442890.1 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 MC58) (see 2 papers)
50% identity, 95% coverage: 4:500/522 of query aligns to 1:502/517 of Q9JZG1

query
sites
Q9JZG1

V

M

T

T

D

Q

Q

T

D

N

R

R

V

V

V

I

I

I

F

F

D

D

T

T

L

L

R

R

D
|
D

G

G

E

E

Q

Q

S

S

P

P

G

G

A

A

T

A

M

M

T

T

H

K

D

E

E

E

K

K

L

I

E

R

I

V

A

A

E

R

L

Q

L

L

D

E

E

K

M

L

G

G

V

V

D

D

I

I

E

E

A

A

G

G

F

F

P

A

I

A

A

A

S

S

E

P

G

G

D

D

F

F

K

E

A

A

V

V

S

N

E

A

I

I

A

A

E

K

R

T

S

I

K

T

N

K

S

S

R

T

I

V

C

C

G

S

L

L

A

S

R

R

A

A

N

I

F

E

A

R

D

D

I

I

D

R

R

Q

C

A

W

G

E

E

A

A

V

V

K

A

H

P

A

A

E

P

K

K

N

K

R

R

I

I

H

H

T

T

F

F

I

I

G

A

T

T

S

S

P

P

L

I

H

H

R

M

A

E

I

Y

P

K

-

L

N

K

L

M

T

K

M

P

D

K

E

Q

M

V

A

I

D

E

K

A

I

A

H

V

E

K

T

A

V

V

T

K

H

I

A

A

R

R

N

E

L

Y

C

T

E

D

N

D

V

V

Q

E

W

F

S

S

P

C

M

E

D

D

A

A

T

L

R

R

T

S

E

E

W

I

D

D

Y

F

L

L

C

A

R

E

V

I

I

C

E

G

I

A

A

V

I

I

K

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

A

I

P

P

V

Y

E

K

S

T

A

E

D

E

L

F

I

F

K

R

R

E

L

L

I

I

E

A

T

K

V

T

P

P

G

N

A

G

D

G

E

K

V

V

F

W

A

S

T

A

H
|
H

C

C

H
|
H

N

N

D

D

L

L

G

G

M

L

A

A

T

V

A

A

N

N

S

S

L

L

A

A

V

L

A

K

G

G

A

A

R

R

Q

Q

I

V

E

E

C

C

T

T

I

V

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N
|
N

T

A

A

S

L

V

E

E

V

I

V

V

M

M

A

A

L

L

R

K

T

V

R

R

N

H

D

D

I

L

M

F

P

G

W

L

H

E

T

T

G

G

I

I

D

D

T

T

K

Q

I

I

M

V

H

P

I

S

S

S

R

K

R

L

V

V

A

S

T

T

V

I

A

T

G

G

F

Y

P

P

V

V

Q

Q

F

P

N

N

K

K

A

A

I

I

V

V

G

G

K

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

M

V

L

L

K

K

N

H

R

R

E

E

N

T

F

Y

E

E

I

I

M

M

R

S

P

A

E

E

D

S

I

V

G

G

L

W

S

A

G

T

T

N

S

R

L

L

P

S

L

L

G

G

K

K

H

L

S

S

G

G

R

R

A

N

A

A

L

F

R

K

D

T

K

K

L

L

E

A

T

D

L

L

G

G

F

I

E

E

V

L

-

E

G

S

D

E

N

E

Q

A

L

L

K

N

D

A

I

A

F

F

V

A

R

R

F

F

K

K

D

E

L
|
L

A
|
A

D
|
D

R
x
K

K
|
K

K
x
R

E
|
E

V
x
I

F
|
F

D
|
D

D
x
E

D
|
D

L
|
L

I
x
H

A
|
A

L
|
L

M
x
V

S
|
S

L

-

D
|
D

D
x
E

-
x
M

-
x
G

-
x
S

-
x
M

D
x
N

D
x
A

D
x
E

R
x
S

L
x
Y

Q
x
K

L
x
F

V
x
I

S
|
S

M
x
Q

K
|
K

V
x
I

T
x
S

C
x
T

G
x
E

T
|
T

G
|
G

G
x
E

Q
x
E

A
x
P

E
x
R

S
x
A

T
x
D

V
x
I

E
x
V

L
x
F

E
x
S

F
x
I

D
x
K

G
|
G

K
x
E

D
x
E

V
x
K

I
x
R

A
|
A

T
x
S

E
x
A

H
x
T

G
|
G

D
x
S

G
|
G

P
|
P

V
|
V

D
|
D

A
|
A

T
x
I

F
|
F

K
|
K

A
|
A

I
|
I

R
x
E

A
x
S

I
x
V

Y
x
A

P
x
Q

N
x
S

K
x
G

A
|
A

H
x
A

L
|
L

Q
|
Q

L
x
I

Y
|
Y

Q
x
S

V
|
V

H
x
N

A
|
A

V
|
V

T
|
T

E
x
Q

G
|
G

T
|
T

D
x
E

A
x
S

Q
|
Q

A
x
G

T
x
E

V
x
T

S
|
S

V
|
V

R
|
R

L
|
L

E
x
A

E
x
R

D
x
G

G
x
N

M
x
R

I
x
V

A
x
V

T
x
N

G
|
G

Q
|
Q

S
x
G

A
|
A

N
x
D

T
|
T

D
|
D

T
x
V

V
x
L

V
|
V

A
|
A

S
x
T

A
|
A

K
|
K

A
|
A

Y
|
Y

I
x
L

H
x
S

A
|
A

L
|
L

N
x
S

R
x
K

L
|
L

D16 (= D19) binding Mn(2+)
H204 (= H206) binding Mn(2+)
H206 (= H208) binding Mn(2+)
N240 (= N242) 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)
46% identity, 73% coverage: 3:384/522 of query aligns to 11:408/409 of 6e1jA

query
sites
6e1jA

N

K

V

L

T

P

D

D

Q

K

D

N

R

Y

V

V

V

R

I

V

F

F

D

D

T

T

L

L

R

R

D
|
D

G

G

E

E

Q
|
Q

S

S

P

P

G

G

A

A

T

A

M

L

T

T

H

P

D

P

E

Q

K

K

L

I

E

E

I

I

A

A

E

R

L

Q

L

L

D

A

E

K

M

L

G

R

V

V

D

D

I

I

I

M

E

E

A

V

G

G

F
|
F

P

P

I

V

A
x
S

S

S

E

E

G

E

D

E

F

F

K

E

A

T

V

I

S

Q

E

T

I

I

A

A

E

K

R

T

S

V

K

G

N

N

S

E

R
x
V

-

D

-
x
E

-

E

-

T

-

G

-

Y

-

I

-

P

-

V

I

I

C

C

G

V

L
x
I

A

A

R
|
R

A

S

N

K

F

E

A

R

D

D

I

I

D

K

R

A

C

A

W

W

E

E

A

S

V

V

K

K

H

Y

A

A

E

K

K

R

N

P

R

R

I

I

H

V

T

I

F
|
F

I

T

G

S

T

T

S

S

P

D

L

I

H

H

-

L

R

K

A

Y

I
x
K

P
x
L

N

K

L

M

T

T

M

R

D

E

E

E

M

V

A

V

D

D

K

M

I

V

H

A

E

S

T

S

V

I

T

R

H

F

A

A

R

K

N

S

L

L

-

G

C

F

E

E

N

D

V

I

Q

E

W

F

S

G

P

C

M

E

D

D

A

G

T

G

R

R

T

S

E

D

W

K

D

D

Y

Y

L

I

C

C

R

T

V

V

I

F

E

E

I

E

A

A

I

I

K

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

A

M

P

P

V

H

E

E

S

Y

A

G

D

K

L

L

I

V

K

R

R

Y

L

I

I

K

E

A

T

N

V

T

P

P

G

G

A

I

D

D

E

D

V

V

V

I

F

F

A

S

T

A

H
|
H

C

C

H
|
H

N

N

D

D

L

L

G

G

M

V

A

A

T

T

A

A

N

N

S

T

L

I

A

A

A

G

V

I

A

C

G

A

G

G

A

A

R

R

Q

Q

I

V

E

E

C

V

T

T

I

I

N

N

G

G

L

I

G

G

E

E

R

R

A

S

G

G

N

N

T

A

A

P

L

L

E

E

V

V

M

M

A

A

L

L

R

K

T

C

R

R

N

G

D

A

I

F

M

V

-

M

-

G

P

G

W

V

H

Y

T

T

G

R

I

I

D

D

T

T

T

R

K

Q

I

I

M

M

H

A

I

T

S

S

R

K

R

M

V

V

A

Q

T

E

V

Y

A

T

G

G

F

L

P

Y

V

V

Q

Q

F

P

N

H

K

K

A

P

I

I

V

V

G

G

K

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

M

I

L

L

K
|
K

N

N

R

R

E

S

N

T

F

Y

E

E

I

I

M

I

R

S

P

P

E

E

D

D

I

V

G

G

L

V

-

V

-

K

-

S

S

Q

G

N

T

S

S

G

L

I

P

V

L

L

G

G

K

K

H
x
L

S

S

G

G

R
|
R

A
x
H

A

A

L

V

R

K

D

G

K

R

L

L

E

K

T

E

L

L

G

G

F

Y

E

E

V

I

G

S

D

D

N

E

Q

K

L

L

K

N

D

E

I

V

F

F

V

S

R

R

F

F

K

R

D

D

L

L

A

T

D

K

R

Q

K

K

E

R

V

V

F

T

D

D

L

L

I

K

A

A

L

L

M

V

S

T

binding coenzyme a: Q30 (= Q22), F60 (= F52), S63 (≠ A55), I95 (≠ L78), R97 (= R80), F121 (= F104), K132 (≠ I114), L133 (≠ P115), S322 (= S301), G323 (= G302), I324 (= I303), D327 (= D306), K331 (= K310), L359 (≠ H335), R362 (= R338), H363 (≠ A339)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P173), T194 (= T175), H225 (= H206), H227 (= H208)
binding manganese (ii) ion: D27 (= D19), V82 (≠ R74), E84 (vs. gap), H225 (= H206), H227 (= H208)

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)
46% identity, 72% coverage: 7:383/522 of query aligns to 82:474/503 of Q9FN52

query
sites
Q9FN52

Q

K

D

N

R

Y

V

V

V

R

I

V

F

L

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

S

S

P

P

G

G

A

A

T

A

M

L

T

T

H

P

D

P

E

Q

K

K

L

L

E

E

I

I

A

A

E

R

L

Q

L

L

D

A

E

K

M

L

G

R

V

V

D

D

I

I

I

M

E

E

A

V

G

G

F

F

P

P

I

V

A

S

S

S

E

E

G

E

D

E

F

F

K

E

A

A

V

I

S

K

E

T

I

I

A

A

E

K

R

T

S

V

K

G

N

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

V

S

P

R

V

I

I

C

C

G

G

L

I

A

A

R

R

A

C

N

K

F

K

A

R

D

D

I

I

D

E

R

A

C

T

W

W

E

E

A

A

V

L

K

K

H

Y

A

A

E

K

K

R

N

P

R

R

I

V

H

M

T

L

F

F

I

T

G

S

T

T

S

S

P

E

L

I

H

H

R

M

A

K

I

Y

P

K

-

L

N

K

L

K

T

T

M

K

D

E

E

E

M

V

A

I

D

E

K

M

I

A

H

V

E

N

T

S

V

V

T

K

H

Y

A

A

R

K

N

S

L

L

-

G

C

F

E

K

N

D

V

I

Q

Q

W

F

S

G

P

C

M

E

D

D

A

G

T

G

R

R

T

T

E

E

W

K

D

D

Y

F

L

I

C

C

R

K

V

I

I

L

E

G

I

E

A

S

I

I

K

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

A

M

P

P

V

Q

E

E

S

F

A

G

D

E

L

L

I

V

K

A

R

Y

L

V

I

I

E

E

T

N

V

T

P

P

G

G

A

A

D

D

E

D

V

I

V

V

F

F

A

A

T

I

H

H

C

C

H

H

N

N

D

D

L

L

G

G

M

V

A

A

T

T

A

A

N

N

S

T

L

I

A

S

A

G

V

I

A

C

G

A

G

G

A

A

R

R

Q

Q

I

V

E

E

C

V

T

T

I

I

N

N

G

G

L

I

G

G

E

E

R

R

A

S

G

G

N

N

T

A

A

P

L

L

E

E

V

V

M

M

A

A

L

L

R

K

T

C

R

R

N

G

D

E

I

S

M

L

-

M

-

D

P

G

W

V

H

Y

T

T

G

K

I

I

D

D

T

S

T

R

K

Q

I

I

M

M

H

A

I

T

S

S

R

K

R

M

V

V

A

Q

T

E

V

H

A

T

G

G

F

M

P

Y

V

V

Q

Q

F

P

N

H

K

K

A

P

I

I

V

V

G

G

K

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

M

I

L

L

K

K

N

N

R

R

E

S

N

T

F

Y

E

E

I

I

M

L

R

S

P

P

E

E

D

D

I

V

G

G

L

I

-

V

-

K

-

S

S

E

G

N

T

S

S

G

L

I

P

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

A

H

A

A

L

V

R

K

D

D

K

R

L

L

E

K

T

E

L

L

G

G

F

Y

E

E

V

I

G

S

D

D

N

E

Q

K

L

F

K

N

D

D

I

I

F

F

V

S

R

R

F

Y

K

R

D

E

L

L

A

T

D

K

R

D

K

K

E

R

V

I

F

T

D

D

D

A

D

D

L

L

I

K

A

A

L

L

M

V

G263 (= G177) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 73% coverage: 6:388/522 of query aligns to 81:479/506 of Q9FG67

query
sites
Q9FG67

D

D

Q

G

D

N

R

Y

V

V

V

R

I

V

F

F

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

S

S

P

P

G

G

A

G

T
x
S

M

L

T

T

H

P

D

P

E

Q

K

K

L

L

E

E

I

I

A

A

E

R

L

Q

L

L

D

A

E

K

M

L

G

R

V

V

D

D

I

I

I

M

E

E

A

V

G

G

F

F

P

P

I

G

A

S

S

S

E

E

G

E

D

E

F

L

K

E

A

T

V

I

S

K

E

T

I

I

A

A

E

K

R

T

S

V

K

G

N

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

V

S

P

R

V

I

I

C

C

G

A

L

I

A

A

R

R

A

C

N

K

F

H

A

R

D

D

I

I

D

E

R

A

C

T

W

W

E

E

A

A

V

L

K

K

H

Y

A

A

E

K

K

R

N

P

R

R

I

I

H

L

T

V

F

F

I

T

G

S

T

T

S

S

P

D

L

I

H

H

R

M

A

K

I

Y

P

K

-

L

N

K

L

K

T

T

M

Q

D

E

E

E

M

V

A

I

D

E

K

M

I

A

H

V

E

S

T

S

V

I

T

R

H

F

A

A

R

K

N

S

L

L

C

G

E

F

N

N

-

D

V

I

Q

Q

W

F

S

G

P

C

M

E

D

D

A

G

T

G

R

R

T

S

E

D

W

K

D

D

Y

F

L

L

C

C

R

K

V

I

I

L

E

G

I

E

A

A

I

I

K

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

A

M

P

P

V

H

E

E

S

Y

A

G

D

E

L

L

I

V

K

T

R

Y

L

L

I

K

E

A

T

N

V

T

P

P

G

G

A

I

D

D

E

D

V

V

F

V

A
|
A

T

V

H

H

C

C

H

H

N

N

D

D

L

L

G

G

M

L

A

A

T

T

A

A

N

N

S

S

L

I

A

A

A

G

V

I

A

R

G

A

G

G

A

A

R

R

Q

Q

I

V

E

E

C

V

T

T

I

I

N

N

G

G

L

I

G

G

E

E

R

R

A

S

G

G

N

N

T

A

A

S

L

L

E

E

V

V

M

M

A

A

L

L

R

K

T

C

R

R

N

G

D

A

-

Y

-

V

I

I

M

N

P

G

W

V

H

Y

T

T

G

K

I

I

D

D

T

T

T

R

K

Q

I

I

M

M

H

A

I

T

S

S

R

K

R

M

V

V

A

Q

T

E

V

Y

A

T

G

G

F

L

P

Y

V

V

Q

Q

F

A

N

H

K

K

A

P

I

I

V

V

G

G

K

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

M

I

L

L

K

K

N

N

R

R

E

S

N

T

F

Y

E

E

I

I

M

L

R

S

P

P

E

E

D

D

I

I

G

G

L

I

-

V

-

K

-

S

S

Q

G

N

T

S

S

G

L

L

P

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

A

H

A

A

L

V

R

K

D

D

K

R

L

L

E

K

T

E

L

L

G

G

F

Y

E

E

V

L

G

D

D

D

N

E

Q

K

L

L

K

N

D

A

I

V

F

F

V

S

R

L

F

F

K

R

D

D

L

L

A

T

D

K

R

N

K

K

E

R

V

I

F

T

D

D

D

A

D

D

L

L

I

K

A

A

L

L

M

V

S

T

L

S

D

S

D

D

D

E

S102 (≠ T27) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (= A204) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
52% identity, 61% coverage: 8:324/522 of query aligns to 2:306/308 of 3rmjB

query
sites
3rmjB

D

N

R

R

V

V

V

I

I

I

F

F

D

D

T

T

L

L

R

R

D
|
D

G

G

E

E

Q
|
Q

S

S

P

P

G

G

A

A

T

A

M

M

T

T

H

K

D

E

E

E

K

K

L

I

E

R

I

V

A

A

E

R

L

Q

L

L

D

E

E

K

M

L

G

G

V

V

D

D

I

I

E

E

A

A

G

G

F

F

P

A

I

A

A

A

S

S

E

P

G

G

D

D

F

F

K

E

A

A

V

V

S

N

E

A

I

I

A

A

E

K

R

T

S

I

K

T

N

K

S

S

R

T

I

V

C

C

G

S

L

L

A

S

R

R

A

A

N

I

F

E

A

R

D

D

I

I

D

R

R

Q

C

A

W

G

E

E

A

A

V

V

K

A

H

P

A

A

E

P

K

K

N

K

R

R

I

I

H

H

T

T

F

F

I

I

G

A

T

T

S

S

P

P

L

I

H

H

R

M

A

E

I

Y

P

K

-

L

N

K

L

M

T

K

M

P

D

K

E

Q

M

V

A

I

D

E

K

A

I

A

H

V

E

K

T

A

V

V

T

K

H

I

A

A

R

R

N

E

L

Y

C

T

E

D

N

D

V

V

Q

E

W

F

S

S

P

C

M

E

D

D

A

A

T

L

R

R

T

S

E

E

W

I

D

D

Y

F

L

L

C

A

R

E

V

I

I

C

E

G

I

A

A

V

I

I

K

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

A

I

P

P

V

Y

E

K

S

T

A

E

D

E

L

F

I

F

K

R

R

E

L

L

I

I

E

A

T

K

V

T

P

P

G

N

A

G

D

G

E

K

V

V

F

W

A

S

T

A

H
|
H

C

C

H
|
H

N

N

D

D

L

L

G

G

M

L

A

A

T

V

A

A

N

N

S

S

L

L

A

A

V

L

A

K

G

G

A

A

R

R

Q

Q

I

V

E

E

C

C

T

T

I

V

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N
|
N

T

A

A

S

L

V

E

E

V

I

V

V

M

M

A

A

L

L

R

K

T

V

R

R

N

H

D

D

I

L

M

F

P

G

W

L

H

E

T

T

G

G

I

I

D

D

T

T

K

Q

I

I

M

V

H

P

I

S

S

S

R

K

R

L

V

V

A

S

T

T

V

I

A

T

G

G

F

Y

P

P

V

V

Q

Q

F

P

N

N

K

K

A

A

I

I

V

V

G

G

K

A

N

N

A

A

F

F

A

S

H

H

E

E

S

T

G

-

I

-

H

-

Q

-

D

-

G

-

M

-

L

-

K

-

N

-

R

-

E

-

N

-

F

Y

E

E

I

I

M

M

R

S

P

A

E

E

D

S

I

V

G

G

active site: Q16 (= Q22)
binding manganese (ii) ion: D13 (= D19), H201 (= H206), H203 (= H208), N237 (= N242)

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
35% identity, 68% coverage: 9:365/522 of query aligns to 21:370/399 of 6ktqA

query
sites
6ktqA

R

K

V

V

V

G

I

I

F

L

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

S

T

P

P

G

G

A

V

T

V

M

F

T

T

H

T

D

D

E

Q

K

R

L

V

E

E

I

I

A

A

E

K

L

A

L

L

D

S

E

D

M

I

G

G

V

V

D

Q

I

M

I

I

E

E

A

A

G

G

F

H

P

P

I

A

A
x
V

S

S

E

P

G

D

D

I

F

Y

K

E

A

G

V

I

S

R

E

R

I

I

A

I

E

K

R

L

S

K

K

R

N

E

S

G

R

V

I

I

C

K

G

S

L

E

A

I

R

V

A

A

N

H

F

S

A
x
R

D
x
A

I

V

D

K

R

R

C

D

W

I

E

E

A

V

V

G

K

A

H

E

A

I

E

E

K

A

N

D

R

R

I

I

H

A

T

I

F
|
F

I

Y

G

G

T

I

S

S

P

D

L

T

H

H

-

L

R

K

A

A

I

K

P
x
H

N

H

L

T

T

T

M

R

D

D

E

E

M

A

A

L

D

R

K

S

I

I

H

A

E

E

T

T

V

V

T

S

H

Y

A

A

R

K

N

S

L

H

C

G

E

V

N

K

V

V

Q
x
R

W

F

S
x
T

P

A

M
x
E

D

D

A

A

T

T

R

R

T

A

E

D

W

Y

D

Q

Y

Y

L

L

C

L

R

E

V

V

I

I

E

K

I

T

A

V

I

R

K

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

A

Y

P

P

V

S

E

R

S

T

A

R

D

E

L

L

I

F

K

K

R

D

L

L

I

T

E

S

T

R

V

F

P

P

G

-

A

-

D

-

E

D

V

I

V

E

F

F

A

D

T

I

H
|
H

C

A

H
|
H

N

N

D

D

L

L

G

G

M

M

A

A

T

V

A

A

N

N

S

V

L

L

A

A

V

A

A

E

G

G

A

A

R

T

Q

I

I

I

E

H

C

T

T

T

I

L

N

N

G

G

L

L

G

G

E

E

R

R

A

V

G

G

N

I

T

A

A

P

L

L

E

Q

E

V

V

V

V

A

M

A

A

A

L

L

R

K

T

-

R

-

N

-

D

-

I

-

M

-

P

-

W

Y

H

H

T

F

G

G

I

I

-

E

-

V

D

D

T

L

T

K

K

K

I

L

M

S

H

E

I

V

S

A

R

S

R

L

V

V

A

E

T

K

V

Y

A

S

G

G

F

I

P

A

V

L

Q

P

F

P

N

N

K

F

A

P

I

I

V

T

G

G

K

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

M

V

L

L

K

N

N

D

R

P

E

K

N

T

F

Y

E

E

I

F

M

L

R

P

P

P

E

E

D

T

I

F

G

G

L

R

S

S

G

R

T

D

S

Y

L

V

P

-

L

I

G

D

K

K

H

Y

S

T

G

G

R

K

A

H

A

A

L

V

R

K

D

D

K

R

L

F

E

D

T

R

L

L

G

G

F

V

E

K

V

L

G

T

D

D

N

S

Q

E

L

I

K

D

D

Q

I

V

F

L

V

A

R

K

F

I

K

K

binding 2-oxoglutaric acid: R30 (= R18), R154 (≠ Q141), T156 (≠ S143), E158 (≠ M145), S184 (≠ N171), T188 (= T175), H216 (= H206), H218 (= H208)
binding coenzyme a: V67 (≠ A55), R96 (≠ A84), A97 (≠ D85), F116 (= F104), H128 (≠ P115), E158 (≠ M145)
binding zinc ion: E31 (≠ D19), H216 (= H206), H218 (= H208)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
32% identity, 71% coverage: 12:382/522 of query aligns to 6:379/380 of 4ov9A

query
sites
4ov9A

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

S

A

P

L

G

K

A

R

T

P

M

W

T

T

H

I

D

D

E

E

K

K

L

I

E

E

I

V

A

F

E

D

L

L

D

V

E

E

M

L

G

N

V

V

D

D

I

G

I

I

E

E

A

V

G

G

F

F

P

P

I

S

A

S

S

N

E

E

G

T

D

E

F

F

K

H

A

T

V

C

S

Q

E

V

I

L

A

S

E

K

R

R

S

A

-

P

K

K

N

G

S

K

R

P

I

I

C

A

G

A

L
|
L

A

S

R

R

A

A

N

N

F

Q

A

N

D

E

I

I

D

A

R

V

C

T

W

W

E

E

A

A

V

I

K

Q

H

K

A

A

E

D

K

C

N

P

R

R

I

M

H

H

T

I

F

V

I

Y

G

P

T

V

S

S

P

D

L

F

H

S

-

I

R

K

A

H

I

V

P

L

N

K

L

I

T

S

M

E

D

K

E

E

M

V

A

L

D

Q

K

K

I

I

H

R

E

N

T

S

V

I

T

S

H

F

A

A

R

R

N

S

L

I

C

V

E

G

-

P

-

G

-

I

N

E

V

I

Q

Q

W

F

S

S

P

G

M

E

-

H

-

F

-

G

D

D

A

A

T

I

R

E

T

N

E

-

W

F

D

A

Y

F

L

T

C

K

R

E

V

A

I

F

E

L

I

T

A

A

I

I

K

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

A

R

P

P

V

M

E

V

S

F

A

V

D

N

L

M

I

V

K

K

R

E

L

I

I

K

E

D

T

V

V

V

P

-

G

-

A

K

D

D

E

K

V

A

V

I

F

I

A

S

T

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

M

M

A

A

T

T

A

A

N

T

S

S

L

V

A

E

A

S

V

V

A

Y

G

V

G

G

A

A

R

E

Q

Q

I

I

E

E

C

V

T

A

I

L

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

T

T

A

N

L

L

E

Y

E

E

V

T

V

A

M

I

A

A

L

L

R

H

T

Q

R

N

N

G

D

E

I

-

M

-

P

-

W

-

H

N

T

L

G

N

I

I

D

N

T

F

T

Q

K

R

I

I

M

Y

H

P

I

T

S

A

R

K

R

R

V

I

A

S

T

E

V

L

A

T

G

G

F

I

P

P

V

I

Q

G

F

E

N

K

K

T

A

P

I

I

V

I

G

G

K

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

-

M

L

L

H

K

Q

N

S

R

K

E

G

N

A

F

Y

E

R

I

T

M

F

R

S

P

P

E

E

D

F

I

V

G

G

-

R

L

M

S

D

G

K

T

E

S

T

L

I

P

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

A

K

A

A

L

I

R

E

D

F

K

L

L

L

E

H

T

Q

L

R

G

G

F

I

E

Q

V

V

G

S

D

K

N

E

Q

G

L

I

K

H

D

H

I

L

F

F

V

S

R

L

F

A

K

K

D

S

L

I

A

S

D

S

R

R

K

E

-

N

K

R

E

E

V

I

F

T

D

E

D

A

D

E

L

L

I

V

A

A

L

L

active site: Q16 (= Q22)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R18), L73 (= L78), T176 (= T175), H205 (= H206), H207 (= H208)
binding zinc ion: D13 (= D19), H205 (= H206), H207 (= H208)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
32% identity, 71% coverage: 12:382/522 of query aligns to 6:377/379 of 4ov4A

query
sites
4ov4A

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

S

A

P

L

G

K

A

R

T

P

M

W

T

T

H

I

D

D

E

E

K

K

L

I

E

E

I

V

A

F

E

D

L

L

D

V

E

E

M

L

G

N

V

V

D

D

I

G

I

I

E

E

A

V

G

G

F

F

P

P

I

S

A

S

S

N

E

E

G

T

D

E

F

F

K

H

A

T

V

C

S

Q

E

V

I

L

A

S

E

K

R

R

S

A

-

P

K

K

N

G

S

K

R

P

I

I

C

A

G

A

L

L

A

S

R

R

A

A

N

N

F

Q

A

N

D

E

I

I

D

A

R

V

C

T

W

W

E

E

A

A

V

I

K

Q

H

K

A

A

E

D

K

C

N

P

R

R

I

M

H

H

T

I

F

V

I

Y

G

P

T

V

S

S

P

D

L

F

H

S

-

I

R

K

A

H

I

V

P

L

N

K

L

I

T

S

M

E

D

K

E

E

M

V

A

L

D

Q

K

K

I

I

H

R

E

N

T

S

V

I

T

S

H

F

A

A

R

R

N

S

L

I

C

V

E

G

-

P

-

G

-

I

N

E

V

I

Q

Q

W

F

S

S

P

G

M

E

-

H

-

F

-

G

D

D

A

A

T

I

R

E

T

N

E

-

W

F

D

A

Y

F

L

T

C

K

R

E

V

A

I

F

E

L

I

T

A

A

I

I

K

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

A

R

P

P

V

M

E

V

S

F

A

V

D

N

L

M

I

V

K

K

R

E

L

I

I

K

E

D

T

V

V

V

P

-

G

-

A

K

D

D

E

K

V

A

V

I

F

I

A

S

T

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

M

M

A

A

T

T

A

A

N

T

S

S

L

V

A

E

A

S

V

V

A

Y

G

V

G

G

A

A

R

E

Q

Q

I

I

E

E

C

V

T

A

I

L

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

T

T

A

N

L

L

E

Y

E

E

V

T

V

A

M

I

A

A

L

L

R

H

T

Q

R

N

N

G

D

E

I

-

M

-

P

-

W

-

H

N

T

L

G

N

I

I

D

N

T

F

T

Q

K

R

I

I

M

Y

H

P

I

T

S

A

R

K

R

R

V

I

A

S

T

E

V

L

A

T

G

G

F

I

P

P

V

I

Q

G

F

E

N

K

K

T

A

P

I

I

V

I

G

G

K

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

-

M

-

L

-

K

Q

N

S

R

K

E

G

N

A

F

Y

E

R

I

T

M

F

R

S

P

P

E

E

D

F

I

V

G

G

-

R

L

M

S

D

G

K

T

E

S

T

L

I

P

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

A

K

A

A

L

I

R

E

D

F

K

L

L

L

E

H

T

Q

L

R

G

G

F

I

E

Q

V

V

G

S

D

K

N

E

Q

G

L

I

K

H

D

H

I

L

F

F

V

S

R

L

F

A

K

K

D

S

L

I

A

S

D

S

R

R

K

E

-

N

K

R

E

E

V

I

F

T

D

E

D

A

D

E

L

L

I

V

A

A

L

L

active site: Q16 (= Q22)
binding 3-methyl-2-oxobutanoic acid: R12 (= R18), P174 (= P173), T176 (= T175), H205 (= H206), H207 (= H208)
binding zinc ion: D13 (= D19), H205 (= H206), H207 (= H208)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
30% identity, 96% coverage: 1:501/522 of query aligns to 1:511/516 of Q8F3Q1

query
sites
Q8F3Q1

M

M

T

T

N

K

V

V

T

-

D

-

Q

E

D

T

R

R

V

L

V

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

S

T

P

R

G

G

A

V

T

S

M

F

T

S

H

T

D

S

E

E

K

K

L

L

E

N

I

I

A

A

E

K

-

F

L

L

D

Q

E

K

M

L

G

N

V

V

D

D

I

R

I

V

E

E

A

I

G

A

F

S

P

A

I

R

A

V

S

S

E

K

G

G

D

E

F

L

K

E

A

T

V

V

S

Q

E

K

I

I

A

M

E

E

R

W

S

A

K

A

N

T

S

E

R

Q

I

L

C

T

G

E

-

R

L

I

A

E

R

I

A
x
L

N

G

F
|
F

A

V

D

D

I

G

D

N

R

K

C

T

W

V

E

D

A

W

V

I

K

K

H

D

A

S

E

G

K

A

N

-

R

K

I

V

H

L

T

N

F

L

I
x
L

G

T

T

K

S

G

P

S

L

L

H

H

R

H

A

L

I

E

P

K

N

Q

L

L

-

G

-

K

T

T

M

P

D

K

E

E

M

F

A

F

D

T

K

D

I

V

H

S

E

F

T

V

V

I

T

E

H

Y

A

A

-

I

-

K

R

S

N

G

L

L

C

K

E

I

N

N

V

V

Q
x
Y

-

L

-
x
E

-

D

W

W

S

S

P

-

M

-

D

N

A

G

T

F

R

R

T

N

E

S

W

P

D

D

Y

Y

L

V

C

K

R

S

V

L

I

V

E

E

I

H

A

L

I

S

K

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

A

S

P

P

V

E

E

E

S

T

A

F

D

Q

L

G

I

V

K

D

R

S

L

L

I

I

E

Q

T

K

V

Y

P

P

G

-

A

-

D

-

E

D

V

I

V

H

F

F

A

E

T

F

H

H

C

G

H

H

N

N

D

D

L

Y

G

D

M

L

A

S

T

V

A

A

N

N

S

S

L

L

A

Q

A

A

V

I

A

R

G

A

G

G

A

V

R

K

Q

G

I

L

E

H

C

A

T

S

I

I

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

T

T

A

P

L

L

E

E

E

A

V

L

V

V

M

T

A

T

L

I

R

H

T

D

R

K

N

S

D

N

I

S

M

-

P

-

W

-

H

K

T

T

G

N

I

I

D

N

T

E

T

I

K

A

I

I

M

T

H

E

I

A

S

S

R

R

R

L

V

V

A

E

T

V

V

F

A

S

G

G

F

K

P

R

V

I

Q

S

F

A

N

N

K

R

A

P

I

I

V

V

G

G

K

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

M

D

L

K

K

K

N

G

R
x
N

E
x
L

N
x
Y

F

A

E

N

I

P

M

I

R

L

P

P

E

E

D

R

I

F

G

G

L

-

S

R

G

K

T

R

S

S

L

Y

P

A

L

L

G

G

K

K

H

L

S

A

G

G

R

K

A

A

A

S

L

I

R

S

D

E

K

N

L

V

E

K

T

Q

L

L

G

G

F

M

E

V

V

L

G

S

D

E

N

V

Q

V

L

L

K

Q

D

K

I

V

F

L

V

E

R

R

F

V

K

I

D

E

L

L

A

G

D

D

R

Q

K

N

K

K

E

L

V

V

F

T

D

P

D

E

D

D

L

L

-

P

-

F

-

I

I

I

A

A

L

D

M

V

S

S

L

G

D

R

D

T

D

G

D

E

D

K

R

V

L

L

Q

T

L

I

V

K

S

S

M

C

K

N

V

I

T

H

C

S

G

G

T

I

G

G

G

I

Q

R

A

P

E

H

S

A

T

Q

V

I

E

E

L

L

E

E

F

Y

D

Q

G

G

K

K

D

I

V

H

I

K

A

E

T

I

E

S

H

E

G

G

D

D

G

G

P

G

V
x
Y

D
|
D

A

A

T

F

F

M

K

N

A

A

I

L

R

T

A

K

I

I

Y

-

P

T

N

N

K

R

A

L

H

G

L

I

Q

S

L

I

-

P

-

K

-
x
L

-

I

-

D

Y
|
Y

Q

E

V

V

H

R

A

-

V
x
I

T

P

E

P

G

G

T

G

D

K

A
x
T

Q

D

A

A

T

L

V
|
V

S

E

V

T

R

R

-

I

-

T

-

W

-

N

-

K

-

S

-

L

-

D

L

L

E

E

D

D

G

Q

M

T

I

F

A

K

T

T

G

-

Q

M

S

G

A

V

N

H

T
x
P

D

D

T
x
Q

V

T

V

V

A

A

S

A

A

V

K

H

A

A

Y

T

I

E

H

K

A

M

L

L

N

N

R

Q

L

I

I

L

R16 (= R18) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 18:19) binding pyruvate
D17 (= D19) 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 (≠ A81) 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 (= F83) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ I105) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ Q141) 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 (vs. gap) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T175) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H304) mutation H->A,N: Loss of activity.
D304 (= D306) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ R312) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ E313) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ N314) mutation to A: Loss of activity.
Y430 (≠ V430) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (= D431) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (vs. gap) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y450) 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 (≠ V455) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (≠ A461) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (= V465) 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 (≠ T483) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
Q495 (≠ T485) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
30% identity, 70% coverage: 12:377/522 of query aligns to 37:394/418 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

S

F

P

A

G

N

A

A

T

F

M

F

T

D

H

T

D

E

E

K

K

K

L

I

E

Q

I

I

A

A

E

K

L

A

L

L

D

D

E

N

M

F

G

G

V

V

D

D

I

Y

I

I

E
|
E

A

L

G

T

F

S

P

P

I

V

A

A

S

S

E

E

G

Q

D

S

F

R

K

Q

A

D

V

C

S

E

E

A

I

I

A

C

E

K

R

L

S

G

K

L

N

K

S

C

R

K

I

I

C

L

G

T

L
x
H

A

I

R

R

A

C

N

H

F

M

A

D

D

D

I

A

D

R

R

V

C

A

W

V

E

E

A

T

V

-

K

-

H

-

A

-

E

G

K

V

N

D

R

G

I

V

H
x
D

T

V

F

V

I

I

G

G

T

T

S

S

P

Q

L

Y

H

L

R

R

A

K

I

Y

P

S

N

H

-

G

L

K

T

D

M

M

D

T

E

Y

M

I

A

I

D

D

K

S

I

A

H

T

E

E

T

V

V

I

T

N

H

F

A

V

R

K

N

S

L

K

C

G

E

I

N

E

V

V

Q
x
R

W

F

S
|
S

P

S

M
x
E

D

D

A

S

T

F

R

R

T

S

E

D

W

L

D

V

Y

D

L

L

C

L

R

S

V

L

I

Y

E

K

I

A

A

V

I

D

K

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

A

T

P

P

V

R

E

Q

S

V

A

Y

D

D

L

L

I

I

K

R

R

-

L

-

I

-

E

-

T

T

V

L

P

R

G

G

A

V

D

V

E

S

V

C

V

D

F

I

A
x
E

T

C

H
|
H

C

F

H
|
H

N

N

D

D

L

T

G

G

M

M

A

A

T

I

A

A

N

N

S

A

L

Y

A

C

A

A

V

L

A

E

G

A

G

G

A

A

R

T

Q

H

I

I

E

D

C

T

T

S

I

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

T

T

A

P

L

L

E

G

E

A

V

L

M

A

A

R

L

M

R

Y

T

V

R

T

N

D

D

R

I

E

M

Y

P

I

W

T

H

H

T

K

G

-

I

Y

D

K

T

L

T

N

K

Q

I

L

M
x
R

H

E

I

L

S

E

R

N

R

L

V

V

A

A

T

D

V

A

A

V

G

E

F

V

P

Q

V

I

Q

P

F

F

N

N

K

N

A

Y

I

I

V

T

G

G

K

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

M

I

L

L

K

A

N

N

R

P

E

S

N

T

F
x
Y

E

E

I

I

M

L

R

K

P

P

E

E

D

D

I

F

G

G

L

M

S

S

G

R

T

Y

S

V

L

H

P

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

A

N

A

A

L

I

R

K

D

S

K

R

L

A

E

E

T
x
Q

L

L

G

N

F

L

E

H

V

L

G

T

D

D

N

A

Q

Q

L

A

K

K

D

E

I

L

F

T

V

V

R

R

F

I

K

K

D

K

L

L

A

A

D

D

R

V

K

R

K

T

E

L

V

A

F

M

D

D

R43 (= R18) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D19) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q22) mutation to A: Abolishes the catalytic activity.
E74 (= E49) 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 (≠ L78) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ H102) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ Q141) 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 (= S143) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (≠ M145) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T175) 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 (≠ A204) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H206) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H208) binding 2-oxoglutarate; binding Zn(2+)
R288 (≠ M271) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (≠ F315) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ T347) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
30% identity, 70% coverage: 12:377/522 of query aligns to 32:389/400 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

S

F

P

A

G

N

A

A

T

F

M

F

T

D

H

T

D

E

E

K

K

K

L

I

E

Q

I

I

A

A

E

K

L

A

L

L

D

D

E

N

M

F

G

G

V

V

D

D

I

Y

I

I

E

E

A

L

G

T

F

S

P

P

I

V

A

A

S

S

E

E

G

Q

D

S

F

R

K

Q

A

D

V

C

S

E

E

A

I

I

A

C

E

K

R

L

S

G

K

L

N

K

S

C

R

K

I

I

C

L

G

T

L
x
H

A

I

R

R

A

C

N

H

F

M

A

D

D

D

I

A

D

R

R

V

C

A

W

V

E

E

A

T

V

-

K

-

H

-

A

-

E

G

K

V

N

D

R

G

I

V

H

D

T

V

F

V

I

I

G

G

T

T

S

S

P

Q

L

Y

H

L

R

R

A

K

I

Y

P

S

N

H

-

G

L

K

T

D

M

M

D

T

E

Y

M

I

A

I

D

D

K

S

I

A

H

T

E

E

T

V

V

I

T

N

H

F

A

V

R

K

N

S

L

K

C

G

E

I

N

E

V

V

Q
x
R

W

F

S
|
S

P

S

M

E

D

D

A

S

T

F

R

R

T

S

E

D

W

L

D

V

Y

D

L

L

C

L

R

S

V

L

I

Y

E

K

I

A

A

V

I

D

K

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

A

T

P

P

V

R

E

Q

S

V

A

Y

D

D

L

L

I

I

K

R

R

-

L

-

I

-

E

-

T

T

V

L

P

R

G

G

A

V

D

V

E

S

V

C

V

D

F

I

A

E

T

C

H
|
H

C

F

H
|
H

N

N

D

D

L

T

G

G

M

M

A

A

T

I

A

A

N

N

S

A

L

Y

A

C

A

A

V

L

A

E

G

A

G

G

A

A

R

T

Q

H

I

I

E

D

C

T

T

S

I

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

T

T

A

P

L

L

E

G

E

A

V

L

M

A

A

R

L

M

R

Y

T

V

R

T

N

D

D

R

I

E

M

Y

P

I

W

T

H

H

T

K

G

-

I

Y

D

K

T

L

T

N

K

Q

I

L

M

R

H

E

I

L

S

E

R

N

R

L

V

V

A

A

T

D

V

A

A

V

G

E

F

V

P

Q

V

I

Q

P

F

F

N

N

K

N

A

Y

I

I

V

T

G

G

K

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

M

I

L

L

K

A

N

N

R

P

E

S

N

T

F

Y

E

E

I

I

M

L

R

K

P

P

E

E

D

D

I

F

G

G

L

M