SitesBLAST

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
29% identity, 70% coverage: 3:365/522 of query aligns to 21:370/399 of 6ktqA

query
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6ktqA

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binding 2-oxoglutaric acid: R30 (= R12), R154 (≠ I141), T156 (≠ D143), E158 (= E145), S184 (≠ V174), T188 (= T178), H216 (= H206), H218 (= H208)
binding coenzyme a: V67 (≠ S49), R96 (≠ S75), A97 (≠ T76), F116 (= F103), H128 (≠ L115), E158 (= E145)
binding zinc ion: E31 (≠ D13), H216 (= H206), H218 (= H208)

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)
28% identity, 85% coverage: 2:445/522 of query aligns to 5:439/517 of Q9JZG1

query
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Q9JZG1

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D16 (= D13) 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

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)
30% identity, 72% coverage: 4:378/522 of query aligns to 85:469/503 of Q9FN52

query
sites
Q9FN52

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G263 (= G180) 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)
30% identity, 66% coverage: 4:350/522 of query aligns to 85:443/506 of Q9FG67

query
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Q9FG67

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D

T

T

L

L

R

R

D

D

G

G

A

E

Q

Q

T

S

E

P

G

G

I

G

S
|
S

F

L

S

T

V

P

A

P

D

Q

K

K

L

L

K

E

I

I

A

A

R

R

R

Q

L

L

V

A

E

K

M

L

G

R

F

V

D

D

Y

I

V

M

E

E

G

V

G

G

W

F

P

P

G

G

S

S

N

S

P

E

K

E

D

E

L

L

E

E

F

T

F

I

G

K

Q

T

V

I

A

A

R

K

-

T

-

V

-

G

D

N

P

E

V

V

L

D

R

E

E

E

K

T

-

G

-

Y

-

V

-

P

-

V

V

I

T

C

A

A

F

I

G

A

S

R

T

C

R

K

R

H

K

R

N

D

T

I

R

-

P

-

A

-

D

-

D

E

E

A

N

T

L

W

Q

E

R

A

L

L

C

K

S

Y

C

A

G

K

V

R

K

P

T

R

V

I

T

L

L

V

F

F

G

T

K

S

T

T

W

S

D

D

L

I

H

H

V

M

T

K

R

Y

A

K

L

L

N

K

T

K

T

T

L

Q

E

E

N

V

L

I

A

E

M

M

I

A

R

V

E

S

S

S

V

I

A

R

Y

F

L

A

K

K

E

S

Q

L

G

G

L

F

-

N

E

D

V

I

I

Q

Y

F

D

G

A

C

E

E

H

-

F

-

D

D

G

G

Y

G

K

R

E

S

N

D

P

K

D

D

Y

F

A

L

L

C

A

K

T

I

L

L

E

G

A

E

A

A

V

I

S

K

A

A

G

G

A

V

S

T

T

V

L

V

V

T

L

I

C

G

D

D

T

T

N

V

G

G

G

I

S

N

M

M

P

P

W

H

E

E

V

Y

E

G

A

E

A

L

V

V

R

T

R

Y

V

L

V

K

E

A

K

N

F

T

P

P

-

G

-

I

-

D

R

D

V

V

T

V

V

V

G
x
A

I

V

H

H

A

C

H

H

N

N

D

D

T

L

G

G

M

L

A

A

V

T

A

A

N

N

T

S

V

I

V

A

A

G

V

I

K

R

A

A

G

G

A

A

R

R

H

Q

V

V

Q

E

G

V

T

T

V

I

N

N

G

G

Y

I

G

G

E

E

R

R

C

S

G

G

N

N

A

A

D

S

L

L

C

E

A

E

V

V

L

V

P

-

N

-

L

M

T

A

F

L

K

K

C

C

G

R

F

G

T

A

T

Y

L

V

P

I

R

N

E

G

S

V

F

Y

S

T

R

K

-

I

-

D

-

T

-

R

-

Q

L

I

V

M

E

A

L

T

S

S

R

K

Y

M

V

V

S

Q

E

E

V

Y

A

T

N

G

V

L

H

Y

P

V

Y

Q

P

A

Q

H

Q

K

P

P

Y

I

V

V

G

G

M

A

S

N

A

C

F

F

A

V

H

H

K

E

G

S

G

G

V

I

H

H

V

Q

S

D

A

G

I

I

M

L

K

K

E

N

P

R

R

S

C

T

Y

Y

E

E

H

I

I

L

D

S

P

P

S

E

L

D

V

I

G

G

-

I

-

V

-

K

-

S

N

Q

R

N

R

S

R

G

V

L

L

V

V

L

S

G

E

K

L

L

A

S

G

G

Q

R

S

H

N

A

L

V

L

K

Y

D

K

R

L

L

R

K

E

E

L

L

N

G

L

Y

D

E

L

L

S102 (= S21) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ G204) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
27% identity, 95% coverage: 6:500/522 of query aligns to 10:494/516 of Q8F3Q1

query
sites
Q8F3Q1

V

I

Y

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

A

E

Q

Q

T

T

E

R

G

G

I

V

S

S

F

F

S

S

V

T

A

S

D

E

K

K

L

L

K

N

I

I

A

A

R

K

R

F

L

L

V

L

E

Q

-

K

M

L

G

N

F

V

D

D

Y

R

V

V

E

E

G

I

G

A

W

S

P

A

G

R

S

V

N

S

P

K

K

G

D

E

L

L

E

E

F

T

F

V

G

Q

Q

K

V

I

-

M

-

E

-

W

A

A

R

A

D

T

P

E

V

Q

L

L

R

T

E

E

K

R

V

I

T

E

A

I

F
x
L

G

G

S
x
F

T

V

R

D

R

G

K

N

N

K

T

T

R

-

P

-

A

-

D

-

E

-

N

-

L

V

Q

D

R

W

L

I

C

K

S

D

C

S

G

G

V

A

K

K

T

V

V

L

T

N

L

L

F
x
L

G

T

K

K

T

G

W

S

D

L

L

H

H

H

V

L

T

E

R

K

A

Q

L

L

N

G

T

K

T

T

L

P

E

K

E

E

N

F

L

F

A

T

M

D

I

V

R

S

E

F

S

V

V

I

A

E

Y

Y

L

A

K

I

E

K

Q

S

G

G

L

L

E

K

V

I

I

N

Y

V

D
x
Y

A

L

E
|
E

H

D

F

W

F

S

D

N

G

G

Y

F

K

R

E

N

N

S

P

P

D

D

Y

Y

A

V

L

K

A

S

T

L

L

V

E

E

A

H

A

L

V

S

S

K

A

E

G

H

A

I

S

E

T

R

L

I

V

F

L

L

C

P

D

D

T
|
T

N

L

G

G

G

V

S

L

M

S

P

P

W

E

E

E

V

T

E

F

A

Q

A

G

V

V

R

D

R

S

V

L

V

I

E

Q

K

K

F

Y

P

P

R

D

V

I

T

H

V

F

G

E

I

F

H

H

A

G

H

H

N

N

D

D

T

Y

G

D

M

L

A

S

V

V

A

A

N

N

T

S

V

L

V

Q

A

A

V

I

K

R

A

A

G

G

A

V

R

K

H

G

V

L

Q

H

G

A

T

S

V

I

N

N

G

G

Y

L

G

G

E

E

R

R

C

A

G

G

N

N

A

T

D

P

L

L

C

E

A

A

V

L

L

V

P

T

N

T

L

I

T

H

F

D

K

K

C

S

G

N

F

S

T

K

T

T

L

N

P

I

R

N

E

E

S

-

F

-

S

I

R

A

L

I

V

T

E

E

L

A

S

S

R

R

Y

L

V

V

S

E

E

V

V

F

A

S

N

G

V

K

H

R

P

I

Y

S

P

A

Q

N

Q

R

P

P

Y

I

V

V

G

G

M

E

S

D

A

V

F

F

A

T

H

Q

K

T

G

A

G

G

V

V

H
|
H

V

A

S
x
D

A

G

I

D

M

K

K

K

E

G

P
x
N

R
x
L

C
x
Y

Y

A

E

N

H

P

I

I

D

L

P

P

S

E

L

R

V

F

G

G

N

R

R

K

R

R

R

S

V

Y

L

A

V

L

S

G

E

K

L

L

A

A

G

G

Q

K

S

A

N

S

L

I

L

S

Y

E

K

N

L

V

R

K

E

Q

L

L

N

G

L

M

D

V

L

L

P

S

S

E

Q

V

G

-

E

-

V

V

A

L

R

Q

Q

K

I

V

L

L

A

E

E

R

L

V

K

I

E

E

L

L

E

G

R

D

Q

Q

G

N

F

K

Q

L

F

V

E

T

S

P

A

E

E

D

A

L

S

P

F

F

E

-

L

I

V

A

R

D

R

V

A

S

A

G

N

R

G

T

Y

G

E

E

R

K

P

V

F

L

V

T

L

I

E

K

S

S

L

C

R

N

I

I

L

-

T

-

E

-

L

-

K

H

E

S

G

G

G

I

A

G

V

I

H

R

A

P

E

H

A

A

T

Q

I

I

K

E

L

L

R

E

V

Y

G

Q

D

G

K

K

V

I

V

H

H

K

T

E

A

I

A

S

E

E

G

G

N

D

G

G

P

G

V
x
Y

N
x
D

A

A

L

F

D

M

N

N

A

A

L

L

R

T

K

K

A

I

L

T

E

N

Q

R

F

L

Y

G

P

I

A

S

I

I

K

P

R

-

M

-

R

K

L
|
L

V

I

D

D

Y
|
Y

K

E

V

V

R

R

V
x
I

L

P

D

P

G

G

T

-

A

G

G

K

T
|
T

G

D

A

A

V

L

V
|
V

R

E

V

T

L

R

I

I

E

T

T

W

G

N

-

K

-

S

-

L

-

D

-

L

D

E

G

E

Q

D

R

Q

T

T

W

F

V

K

T

T

V

M

G

G

V

V

S

H

P
|
P

N

D

R16 (= R12) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 12:13) binding pyruvate
D17 (= D13) 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 (≠ F73) 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 (≠ S75) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ F103) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ D143) 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 (= E145) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T178) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H303) mutation H->A,N: Loss of activity.
D304 (≠ S305) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ P311) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ R312) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ C313) mutation to A: Loss of activity.
Y430 (≠ V438) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (≠ N439) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L461) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y464) 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 (≠ V468) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (= T475) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (= V479) 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 (= P499) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.

Sites not aligning to the query:

495 Q→A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
29% identity, 57% coverage: 2:299/522 of query aligns to 2:295/308 of 3rmjB

query
sites
3rmjB

D

N

K

R

V

V

V

I

Y

F

D

D

T

T

L

L

R

R

D
|
D

G

G

A

E

Q
|
Q

T

S

E

P

G

G

I

A

S

A

F

M

S

T

V

K

A

E

D

E

K

K

L

I

K

R

I

V

A

A

R

R

R

Q

L

L

V

E

E

K

M

L

G

G

F

V

D

D

Y

I

V

I

E

E

G

A

G

G

W

F

P

A

G

A

S

A

N

S

P

P

K

G

D

D

L

F

E

E

F

A

F

V

G

N

Q

A

V

I

A

A

R

K

D

T

P

-

V

I

L

T

R

K

E

S

K

T

V

V

T

C

A

S

F

L

G

S

S

R

T

A

R

I

R

E

K

R

N

D

T

I

R

R

P

Q

A

A

D

G

D

-

E

-

N

-

L

-

Q

E

R

A

L

V

C

A

S

P

C

A

G

P

V

K

K

K

T

R

V

I

T

H

L

T

F

F

G

I

K

A

T

T

W

S

D

P

L

I

H

H

V

M

T

E

R

Y

A

K

L

L

N

K

T

M

T

K

L

P

E

K

E

Q

N

V

L

I

A

E

M

A

I

A

R

V

E

K

S

A

V

V

A

K

Y

I

L

A

K

R

E

E

Q

Y

G

T

L

D

E

D

V

V

I

E

Y

F

D

S

A

C

E

E

H

-

F

-

D

D

G

A

Y

L

K

R

E

S

N

E

P

I

D

D

Y

F

A

L

L

A

A

E

T

I

L

C

E

G

A

A

A

V

V

I

S

E

A

A

G

G

A

A

S

T

T

T

L

I

V

N

L

I

C

P

D

D

T

T

N

V

G

G

G

Y

S

S

M

I

P

P

W

Y

E

K

V

T

E

E

A

E

A

F

V

F

R

R

R

E

V

L

V

I

E

A

K

K

F

T

P

P

-

N

-

G

R

K

V

V

T

V

V

W

G

S

I

A

H
|
H

A

C

H
|
H

N

N

D

D

T

L

G

G

M

L

A

A

V

V

A

A

N

N

T

S

V

L

V

A

A

A

V

L

K

K

A

G

G

G

A

A

R

R

H

Q

V

V

Q

E

G

C

T

T

V

V

N

N

G

G

Y

L

G

G

E

E

R

R

C

A

G

G

N
|
N

A

A

D

S

L

V

C

E

A

E

V

I

L

V

P

M

N

A

L

L

T

K

F

V

K

R

C

H

G

D

F

L

T

F

T

G

L

L

P

E

R

T

E

G

-

I

S

D

F

T

S

T

R

Q

L

I

V

V

E

P

L

S

S

S

R

K

Y

L

V

V

S

S

E

T

V

I

A

T

N

G

V

Y

H

P

P

V

Y

Q

P

P

Q

N

Q

K

P

A

Y

I

V

V

G

G

M

A

S

N

A

A

F

F

A

S

H

H

K

E

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

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
33% identity, 66% coverage: 6:348/522 of query aligns to 6:338/376 of O87198

query
sites
O87198

V

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x
E

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x
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-

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x
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H

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A

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N

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L

L

R12 (= R12) binding 2-oxoglutarate
E13 (≠ D13) binding Mg(2+)
H72 (≠ F73) 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 (≠ K98) binding L-lysine
R133 (≠ I141) binding 2-oxoglutarate
S135 (≠ D143) binding L-lysine
T166 (= T178) binding 2-oxoglutarate; binding L-lysine
H195 (= H206) binding Mg(2+)
H197 (= H208) binding Mg(2+)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
33% identity, 62% coverage: 6:331/522 of query aligns to 6:314/314 of 2zyfA

query
sites
2zyfA

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P

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K

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|
L

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A

active site: Q16 (= Q16)
binding 2-oxoglutaric acid: R12 (= R12), H72 (≠ F73), L94 (= L102), R127 (≠ I141), T160 (= T178), H189 (= H206)
binding magnesium ion: E13 (≠ D13), H189 (= H206), H191 (= H208)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
33% identity, 62% coverage: 6:331/522 of query aligns to 6:312/312 of 2ztjA

query
sites
2ztjA

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x
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L

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x
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|
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|
H

N

N

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T

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C

A

A

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I

A

A

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T

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A

A

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E

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G

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A

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I

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I

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A

A

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H

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A

A

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A

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Y

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P

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A

active site: Q16 (= Q16)
binding 2-oxoglutaric acid: R12 (= R12), H72 (≠ F73), L94 (≠ F103), R125 (≠ I141), A156 (≠ C176), T158 (= T178), H187 (= H206), H189 (= H208)
binding copper (ii) ion: E13 (≠ D13), H187 (= H206), H189 (= H208)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
34% identity, 61% coverage: 6:323/522 of query aligns to 5:305/347 of 3a9iA

query
sites
3a9iA

V

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A

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L

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x
D

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L

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K

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-

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x
S

A

A

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H

-

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Y

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L

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Y

A

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A

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|
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A

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G

E

I

F

H
|
H

A

G

H
|
H

N

N

D

D

T

T

G

G

M

C

A

A

V

I

A

A

N

N

T

A

V

Y

V

E

A

A

V

I

K

E

A

A

G

G

A

A

R

T

H

H

V

V

Q

D

G

T

T

T

V

I

N

L

G

G

Y

I

G

G

E

E

R

R

C

N

G

G

N

I

A

T

D

P

L

L

C

G

A

G

V

F

L

L

P

A

N

R

L

M

T

-

F

-

K

-

C

-

G

-

F

Y

T

T

T

L

L

Q

P

P

-

E

-

Y

-

V

-

R

R

K

E

Y

S

K

F

L

S

E

R

M

L

L

V

P

E

E

L

L

S

D

R

R

Y

M

V

V

S

A

E

R

V

M

A

V

N

G

V

V

H

E

P

-

Y

I

P

P

Q

F

Q

N

P

N

Y

Y

V

I

-

T

G

G

M

E

S

T

A

A

F

F

A

S

H

H

K

K

G

A

G

G

V

M

H

H

V

L

S

K

A

A

I

I

M

Y

K

I

E

N

P

P

R

E

C

A

Y

Y

E

E

H

P

I

Y

D

P

P

P

S

E

L

V

V

F

G

G

binding cobalt (ii) ion: E12 (≠ D13), H188 (= H206), H190 (= H208)
binding lysine: R11 (= R12), D91 (≠ K98), S128 (≠ D143), T159 (= T178), H188 (= H206), H190 (= H208)

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
28% identity, 58% coverage: 6:306/522 of query aligns to 4:299/311 of 3bliA

query
sites
3bliA

V

I

Y

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

A

E

Q
|
Q

T

T

E

R

G

G

I

V

S

S

F

F

S

S

V

T

A

S

D

E

K

K

L

L

K

N

I

I

A

A

R

K

R

F

L

L

V

L

E

Q

-

K

M

L

G

N

F

V

D

D

Y

R

V

V

E

E

G

I

G

A

W

S

P

A

G
x
R

S
x
V

N

S

P

K

K

G

D

E

L

L

E

E

F

T

F

V

G

Q

Q

K

V

I

-

M

-

E

-

W

A

A

R

A

D

T

P

E

V

Q

L

L

R

T

E

E

K

R

V

I

T

E

A

I

F

L

G

G

S

F

T

V

R

D

R

G

K

N

N

K

T

T

R

-

P

-

A

-

D

-

E

-

N

-

L

V

Q

D

R

W

L

I

C

K

S

D

C

S

G

G

V

A

K

K

T

V

V

L

T

N

L

L

F

L

G

T

K

K

T

G

W

S

D

L

L

H

H

H

V

L

T

E

R

K

A

Q

L

L

N

G

T

K

T

T

L

P

E

K

E

E

N

F

L

F

A

T

M

D

I

V

R

S

E

F

S

V

V

I

A

E

Y

Y

L

A

K

I

E

K

Q

S

G

G

L

L

E

K

V

I

I

N

Y

V

D
x
Y

A

L

E
|
E

H

D

F

W

F

S

D

N

G

G

Y

F

K

R

E

N

N

S

P

P

D

D

Y

Y

A

V

L

K

A

S

T

L

L

V

E

E

A

H

A

L

V

S

S

K

A

E

G

H

A

I

S

E

T

R

L

I

V

F

L

L

C
x
P

D

D

T
|
T

N

L

G

G

G

V

S

L

M

S

P

P

W

E

E

E

V

T

E

F

A

Q

A

G

V

V

R

D

R

S

V

L

V

I

E

Q

K

K

F

Y

P

P

R

D

V

I

T

H

V

F

G

E

I

F

H
|
H

A

G

H
|
H

N

N

D

D

T

Y

G

D

M

L

A

S

V

V

A

A

N

N

T

S

V

L

V

Q

A

A

V

I

K

R

A

A

G

G

A

V

R

K

H

G

V

L

Q

H

G

A

T

S

V

I

N

N

G

G

Y

L

G

G

E

E

R

R

C

A

G

G

N

N

A

T

D

P

L

L

C

E

A

A

V

L

L

V

P

T

N

T

L

I

T

H

F

D

K

K

C

S

G

N

F

S

T

K

T

T

L

N

P

I

R

N

E

E

S

-

F

-

S

I

R

A

L

I

V

T

E

E

L

A

S

S

R

R

Y

L

V

V

S

E

E

V

V

F

A

S

N

G

V

K

H

R

P

I

Y

S

P

A

Q

N

Q

R

P

P

Y

I

V

V

G

G

M

E

S

D

A

V

F

F

A

T

H

Q

K

T

G

A

G

G

V

V

H

N

V

L

S

Y

A

A

active site: Q14 (= Q16)
binding acetyl coenzyme *a: Q14 (= Q16), R47 (≠ G48), V48 (≠ S49), E140 (= E145)
binding pyruvic acid: R10 (= R12), Y138 (≠ D143), P171 (≠ C176), T173 (= T178)
binding zinc ion: D11 (= D13), H201 (= H206), H203 (= H208)

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
27% identity, 69% coverage: 6:367/522 of query aligns to 14:350/370 of 3mi3A

query
sites
3mi3A

V

I

Y

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

T

F

E

A

G

N

I

A

S

F

F

F

S

D

V

T

A

E

D

K

K

K

L

I

K

Q

I

I

A

A

R

K

R

A

L

L

V

D

E

N

M

F

G

G

F

V

D

D

Y

Y

V

I

E

E

G

L

G

T

W

S

P

P

G

V

S

A

N

S

P

E

K

Q

-

S

-

R

-

Q

D

D

L

C

E

E

F

A

F

I

G

C

Q

K

V

L

A

G

R

-

D

-

P

-

V

-

L

L

R

K

E

C

K

K

V

I

T

L

A

T

F

H

G

I

S

R

T

C

R

H

R

M

K

D

N

D

T

A

R

R

P

V

A

A

D

V

D

E

E

T

N

G

L

V

Q

D

R

-

L

-

C

-

S

-

C

-

G

G

V

V

K
x
D

T

V

V

V

T

-

L

-

F

-

G

-

K

-

T

-

W

-

D

-

L

-

H

-

V

-

T

-

R

-

A

-

L

I

N

G

T

T

T

S

L

M

E

T

E

Y

N

I

L

I

A

D

M

S

I

A

R

T

E

E

S

V

V

I

A

N

Y

F

L

V

K

K

E

S

Q

K

G

G

L

I

E

E

V

V

I

R

Y

F

D

S

A

S

E

E

H

-

F

-

D

D

G

S

Y

F

K

R

E

S

N

D

P

L

D

V

Y

D

A

L

L

L

A

S

T

L

L

Y

E

K

A

A

A

V

V

D

S

K

A

I

G

G

A

V

S

N

T

R

L

V

V

G

L

I

C

A

D

D

T
|
T

N

V

G

G

G

C

S

A

M

T

P

P

W

R

E

Q

V

V

E

Y

A

D

A

L

V

I

R

R

R

-

V

T

V

L

E

R

K

G

F

V

P

V

R

S

V

C

T

D

V

I

G

E

I

C

H
|
H

A

F

H
|
H

N

N

D

D

T

T

G

G

M

M

A

A

V

I

A

A

N

N

T

A

V

Y

V

C

A

A

V

L

K

E

A

A

G

G

A

A

R

T

H

H

V

I

Q

D

G

T

T

S

V

I

N

L

G

G

Y

I

G

G

E

E

R

R

C

N

G

G

N

I

A

T

D

P

L

L

C

G

A

A

V

L

L

L

P

A

N

R

L

M

T

Y

F

V

K

T

C

D

G

R

F

E

T

Y

T

I

L

T

P

H

R

K

E

Y

S

K

F

L

S

N

R

Q

L

L

V

R

E

E

L

L

S

E

R

N

Y

L

V

V

S

A

E

D

V

A

A

V

N

E

V

V

H

Q

P

-

Y

I

P

P

Q

F

Q

N

P

N

Y

Y

V

I

-

T

G

G

M

M

S

C

A

A

F

F

A

T

H

H

K

K

G

A

G

G

V

I

H

H

V

A

S

K

A

A

I

I

M

L

K

A

E

N

P

P

R

S

C

T

Y

Y

E

E

H

I

I

L

D

K

P

P

S

E

L

D

V

F

G

G

N

M

R

S

R

R

R

Y

V

V

L

H

V

V

-

G

S

S

E

R

L

L

A

T

G

G

Q

W

S

N

N

A

L

I

L

K

Y

S

K

R

L

A

R

E

E

Q

L

L

N

N

L

L

D

H

L

L

P

T

S

D

Q

A

G

Q

E

-

V

-

A

A

R

K

Q

E

I

L

L

T

A

V

E

R

L

I

K

K

E

K

L

L

active site: Q24 (= Q16)
binding lysine: R20 (= R12), D100 (≠ K98), T163 (= T178), H190 (= H206), H192 (= H208)
binding zinc ion: E21 (≠ D13), H190 (= H206), H192 (= H208)

3ivsA Homocitrate synthase lys4 (see paper)
27% identity, 69% coverage: 6:367/522 of query aligns to 14:345/364 of 3ivsA

query
sites
3ivsA

V

I

Y

I

D

E

T

S

T

T

L

L

R

R

D
x
E

G

G

A

E

Q
|
Q

T

F

E

A

G

N

I

A

S

F

F

F

S

D

V

T

A

E

D

K

K

K

L

I

K

Q

I

I

A

A

R

K

R

A

L

L

V

D

E

N

M

F

G

G

F

V

D

D

Y

Y

V

I

E

E

G

L

G

T

W

S

P

P

G

V

S

A

N

S

P

E

K

Q

-

S

-

R

-

Q

D

D

L

C

E

E

F

A

F

I

G

C

Q

K

V

L

A

G

R

-

D

-

P

-

V

-

L

L

R

K

E

C

K

K

V

I

T

L

A

T

F

H

G

I

S

R

T

C

R

H

R

M

K

D

N

D

T

A

R

R

P

V

A

A

D

V

D

E

E

T

N

G

L

V

Q

D

R

-

L

-

C

-

S

-

C

-

G

G

V

V

K

D

T

V

V

V

T

-

L

-

F

I

G

G

K

T

T

T

W

Y

D

I

L

I

H

D

V

S

T

A

R

T

A

-

L

-

N

-

T

-

L

-

E

-

N

-

L

-

A

-

M

-

I

-

R

-

E

E

S

V

V

I

A

N

Y

F

L

V

K

K

E

S

Q

K

G

G

L

I

E

E

V

V

I

R

Y

F

D

S

A

S

E

E

H

-

F

-

D

D

G

S

Y

F

K

R

E

S

N

D

P

L

D

V

Y

D

A

L

L

L

A

S

T

L

L

Y

E

K

A

A

A

V

V

D

S

K

A

I

G

G

A

V

S

N

T

R

L

V

V

G

L

I

C

A

D

D

T

T

N

V

G

G

G

C

S

A

M

T

P

P

W

R

E

Q

V

V

E

Y

A

D

A

L

V

I

R

R

R

-

V

T

V

L

E

R

K

G

F

V

P

V

R

S

V

C

T

D

V

I

G

E

I

C

H
|
H

A

F

H
|
H

N

N

D

D

T

T

G

G

M

M

A

A

V

I

A

A

N

N

T

A

V

Y

V

C

A

A

V

L

K

E

A

A

G

G

A

A

R

T

H

H

V

I

Q

D

G

T

T

S

V

I

N

L

G

G

Y

I

G

G

E

E

R

R

C

N

G

G

N

I

A

T

D

P

L

L

C

G

A

A

V

L

L

L

P

A

N

R

L

M

T

Y

F

V

K

T

C

D

G

R

F

E

T

Y

T

I

L

T

P

H

R

K

E

Y

S

K

F

L

S

N

R

Q

L

L

V

R

E

E

L

L

S

E

R

N

Y

L

V

V

S

A

E

D

V

A

A

V

N

E

V

V

H

Q

P

-

Y

I

P

P

Q

F

Q

N

P

N

Y

Y

V

I

-

T

G

G

M

M

S

C

A

A

F

F

A

T

H

H

K

K

G

A

G

G

V

I

H

H

V

A

S

K

A

A

I

I

M

L

K

A

E

N

P

P

R

S

C

T

Y

Y

E

E

H

I

I

L

D

K

P

P

S

E

L

D

V

F

G

G

N

M

R

S

R

R

R

Y

V

V

L

H

V

V

-

G

S

S

E

R

L

L

A

T

G

G

Q

W

S

N

N

A

L

I

L

K

Y

S

K

R

L

A

R

E

E

Q

L

L

N

N

L

L

D

H

L

L

P

Q

S

-

Q

-

G

-

E

-

V

-

A

A

R

K

Q

E

I

L

L

T

A

V

E

R

L

I

K

K

E

K

L

L

active site: Q24 (= Q16)
binding cobalt (ii) ion: E21 (≠ D13), H188 (= H206), H190 (= H208)

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
27% identity, 69% coverage: 6:367/522 of query aligns to 32:379/400 of 3ivtB

query
sites
3ivtB

V

I

Y

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

T

F

E

A

G

N

I

A

S

F

F

F

S

D

V

T

A

E

D

K

K

K

L

I

K

Q

I

I

A

A

R

K

R

A

L

L

V

D

E

N

M

F

G

G

F

V

D

D

Y

Y

V

I

E

E

G

L

G

T

W

S

P

P

G

V

S

A

N

S

P

E

K

Q

-

S

-

R

-

Q

D

D

L

C

E

E

F

A

F

I

G

C

Q

K

V

L

A

G

R

-

D

-

P

-

V

-

L

L

R

K

E

C

K

K

V

I

T

L

A

T

F
x
H

G

I

S

R

T

C

R

H

R

M

K

D

N

D

T

A

R

R

P

V

A

A

D

-

E

-

N

-

L

-

Q

-

R

-

L

-

C

V

S

E

C

T

G

G

V

V

K

D

T

G

V

V

T

D

L

V

F

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S

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-

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-

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Y

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A

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L

L

Y

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A

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K

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I

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G

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H

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H

N

N

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M

A

A

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I

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A

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N

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A

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active site: Q42 (= Q16)
binding 2-oxoglutaric acid: R38 (= R12), H98 (≠ F73), R158 (≠ I141), S160 (≠ D143), T192 (= T178), H219 (= H206), H221 (= H208)
binding zinc ion: E39 (≠ D13), H219 (= H206), H221 (= H208)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
27% identity, 69% coverage: 6:367/522 of query aligns to 37:384/418 of Q9Y823

query
sites
Q9Y823

V

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R43 (= R12) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D13) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q16) mutation to A: Abolishes the catalytic activity.
E74 (= E43) 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 (≠ F73) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ T101) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ I141) 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 (≠ D143) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E145) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T178) 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 (≠ G204) 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 (≠ V270) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y314) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ E345) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
25% identity, 67% coverage: 6:354/522 of query aligns to 6:351/380 of 4ov9A

query
sites
4ov9A

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active site: Q16 (= Q16)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R12), L73 (≠ G74), T176 (= T178), H205 (= H206), H207 (= H208)
binding zinc ion: D13 (= D13), H205 (= H206), H207 (= H208)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
25% identity, 67% coverage: 6:354/522 of query aligns to 6:349/379 of 4ov4A

query
sites
4ov4A

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S

I

I

H
|
H

A

T

H
|
H

N

N

D

D

T

L

G

G

M

M

A

A

V

T

A

A

N

T

T

S

V

V

V

E

A

S

V

V

K

Y

A

V

G

G

A

A

R

E

H

Q

V

I

Q

E

G

V

T

A

V

L

N

N

G

G

Y

L

G

G

E

E

R

R

C

A

G

G

N

N

A

T

D

N

L

L

C

Y

A

E

V

T

L

A

P

I

N

A

L

L

T

H

F

Q

K

N

C

G

G

E

F

N

T

L

T

N

L

I

P

-

R

-

E

-

S

N

F

F

S

Q

R

R

L

I

V

Y

E

P

L

T

S

A

R

K

Y

R

V

I

S

S

E

E

V

L

A

T

N

G

V

I

H

P

P

I

Y

G

P

E

Q

K

Q

T

P

P

Y

I

V

I

G

G

M

E

S

D

A

I

F

F

A

S

H

H

K

R

G

S

G

G

V

I

H

H

V

Q

S

H

A

-

I

-

M

-

K

Q

E

S

P

K

R

G

C

A

Y

Y

E

R

H

T

I

F

D

S

P

P

S

E

L

F

V

V

G

G

-

R

-

M

N

D

R

K

R

E

R

T

V

I

L

S

V

F

S

T

E

N

L

Q

A

S

G

G

Q

H

S

K

N

A

L

I

L

E

Y

F

K

L

L

L

R

H

E

Q

L

R

N

G

L

I

D

Q

L

V

P

S

S

K

Q

E

G

G

active site: Q16 (= Q16)
binding 3-methyl-2-oxobutanoic acid: R12 (= R12), P174 (≠ C176), T176 (= T178), H205 (= H206), H207 (= H208)
binding zinc ion: D13 (= D13), H205 (= H206), H207 (= H208)

Q53WI0 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39; EC 4.1.3.43 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
27% identity, 65% coverage: 5:343/522 of query aligns to 12:333/347 of Q53WI0

query
sites
Q53WI0

V

V

Y

V

D

D

T

T

L

L

R

R

D

D

G

G

A

S

Q

H

T

A

E

H

G

R

I

H

S

Q

F

Y

S

T

V

V

A

E

D

E

K

A

L

R

K

A

I

I

A

A

R

Q

R

A

L

L

V

D

E

E

M

A

G

G

F

V

D

Y

Y

A

V

I

E

E

-

V

-

S

-

H

-

G

-

D

-

G

-

L

G

G

-

S

-

L

-

Q

W

Y

P

G

G

F

S

S

N

R

P

T

K

D

D

E

L

M

E

E

F

L

F

I

G

R

Q

A

V

V

A

-

R

R

D

E

P

T

V

V

L

R

R

R

E

A

K

K

V

V

T

A

A

A

F

L

-

L

-

P

G

G

S

I

T

G

R

T

R

R

K

K

N

E

T

L

R

K

P

E

A

A

D

-

E

-

N

-

L

-

Q

-

R

-

L

-

C

V

S

E

C

A

G

G

V

I

K

Q

T

M

V

V

T

R

L

I

F

A

G

T

K

Q

T

C

W

T

D

E

L

A

H

D

V

I

T

S

R

-

A

-

L

-

N

-

T

-

L

-

E

E

E

Q

N

H

L

F

A

G

M

M

I

A

R

-

E

-

S

-

V

-

A

-

Y

-

L

-

K

K

E

E

Q

M

G

G

L

L

E

E

V

A

I

V

Y

-

D

-

A

-

E

G

H

F

F

L

F

M

D

M

G

S

Y

H

K

M

E

R

N

P

P

P

D

E

Y

F

A

L

L

A

A

E

T

Q

L

A

E

R

A

L

A

M

V

E

S

G

A

Y

G

G

A

A

S

D

T

V

L

V

V

Y

L

I

C

V

D

D

T

S

N

A

G

G

G

A

S

M

M

L

P

P

W

E

E

D

V

A

E

Y

A

A

A

R

V

V

R

K

R

A

V

L

V

K

E

E

K

A

F

L

P

S

R

R

V

A

T

K

V

V

G

G

I

F

H

H

A

A

H

H

N

N

D

N

T

L

G

G

M

L

A

A

V

I

A

G

N

N

T

T

V

L

V

A

A

A

V

L

K

A

A

A

G

G

A

A

R

D

H

W

V

V

Q

D

G

A

T

T

V

L

N

R

G

G

Y

Y

G

G

E

A

R

G

C

A

G

G

N

N

A

A

D

P

L

L

C

-

A

E

V

V

L

L

P

A

N

A

L

V

T

L

F

D

K

K

C

A

G

G

F

L

T

N

T

-

L

-

P

P

R

G

E

L

S

D

F

V

S

F

R

K

L

L

V

L

E

D

L

A

S

A

R

E

Y

Y

V

V

-

M

S

G

E

P

V

I

A

L

N

H

V

F

H

Q

P

P

Y

Y

P

P

Q

D

Q

R

P

D

Y

S

V

V

G

A

M

I

S

G

A

-

F

-

A

-

H

-

K

Y

G

A

G

G

V

V

H

Y

V

S

S

T

A

F

I

L

M

L

K

H

E

A

P

K

R

R

C

I

Y

G

E

K

H

E

-

L

-

G

I

V

D

D

P

P

S

L

L

A

V

I

-

L

-

E

-

L

G

G

N

R

R

R

R

Q

R

A

V

V

L

-

V

-

S

-

E

-

L

-

A
|
A

G

G

Q

Q

S

E

N

D

L

W

L

I

Y

L

K

R

L

V

A324 (= A334) mutation to G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.

P9WQB3 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
25% identity, 83% coverage: 11:445/522 of query aligns to 79:542/644 of P9WQB3

query
sites
P9WQB3

L
|
L

R
|
R

D
|
D

G
|
G

A
x
N

Q
|
Q

T
x
A

E
x
L

G
x
I

I
x
D

S
x
P

F
x
M

S
|
S

V
x
P

A
|
A

D
x
R

K
|
K

L
x
R

K
x
R

I
x
M

A
x
F

R
x
D

R
x
L

L
|
L

V
|
V

E
x
R

M
|
M

G
|
G

F
x
Y

D
x
K

Y
x
E

V
x
I

E
|
E

G
x
V

G
|
G

W
x
F

P
|
P

G
x
S

S
x
A

N
x
S

P
x
Q

K
x
T

D
|
D

L
x
F

E
x
D

F
|
F

F
x
V

G
x
R

Q
x
E

V
x
I

A
x
I

R
x
E

D
x
Q

P
x
G

V
x
A

L
x
I

R
x
P

E
x
D

K
x
D

V
|
V

T
|
T

A
x
I

F
x
Q

G
x
V

S
x
L

T
|
T

R
x
Q

R

-

K

-

N

-

T
x
C

R
|
R

P
|
P

A
x
E

D
x
L

D
x
I

E
|
E

N
x
R

L
x
T

Q
x
F

R
x
Q

L
x
A

C
|
C

S
|
S

C
x
G

G
x
A

V
x
P

K
x
R

T
x
A

V
x
I

T
x
V

L
x
H

F
|
F

G
x
Y

K
x
N

T
x
S

W
x
T

D
x
S

L
x
I

H
x
L

V
x
Q

T
x
R

R
|
R

A
x
V

L
x
V

-
x
F

N
x
R

T
x
A

T
x
N

L
x
R

E
x
A

E
|
E

N
x
V

L
x
Q

A
|
A

M
x
I

I
x
A

R
x
T

E
x
D

S
x
G

V
x
A

A
x
R

Y
x
K

L
x
C

K
x
V

E
|
E

Q
|
Q

G
x
A

L
x
A

E
x
K

V

-

I

-

Y
|
Y

D
x
P

A
x
G

E
x
T

H
x
Q

F
x
W

F
x
R

D
x
F

G
x
E

Y
|
Y

K
x
S

E
x
P

N
x
E

P

-

D
x
S

Y
|
Y

A
x
T

L
x
G

A
x
T

T
x
E

L
|
L

E
|
E

A
x
Y

A
|
A

V
x
K

S
x
Q

A

-

G

-

A

-

S

-

T

-

L

-

V

-

L
x
V

C
|
C

D
|
D

T
x
A

N
x
V

G
|
G

G
x
E

-
x
V

-
x
I

-
x
A

-
x
P

-
x
T

-
x
P

-
x
E

-
x
R

-
x
P

-
x
I

-
x
F

S
x
N

M
x
L

P
|
P

W
x
A

E
x
T

V
|
V

E
|
E

A
x
M

A
x
T

V
x
T

R
x
P

R
x
N

V
|
V

-
x
Y

-
x
A

-
x
D

-
x
S

V
x
I

E
|
E

K
x
W

F
x
M

P
x
S

R
|
R

-
x
N

-
x
L

-
x
A

-
x
N

-
x
R

-
x
E

-
x
S

V
|
V

T
x
I

V
x
L

G
x
S

I
x
L

H
|
H

A
x
P

H
|
H

N
|
N

D
|
D

T
x
R

G
|
G

M
x
T

A
|
A

V
|
V

A
|
A

N
x
A

T
x
A

V
x
E

V
x
L

A
x
G

V
x
F

K
x
A

A
|
A

G
|
G

A
|
A

R
x
D

H
x
R

V
x
I

Q
x
E

G
|
G

T
x
C

V
x
L

N
x
F

G
|
G

Y
x
N

G
|
G

E
|
E

R
|
R

C
x
T

G
|
G

N
|
N

A
x
V

D
x
C

L
|
L

C
x
V

A
x
T

V
x
L

L
x
G

P
x
L

N
|
N

L
|
L

T

-

F
|
F

K
x
S

C
x
R

G
|
G

F
x
V

T
x
D

T

-

L

-

P
|
P

R
x
Q

E
x
I

S
x
D

F
|
F

S
|
S

R
x
N

L
x
I

V
x
D

E
|
E

L
x
I

S
x
R

R
|
R

Y
x
T

V
|
V

S
x
E

E
x
Y

V
x
C

A
x
N

N
x
Q

V
x
L

H
x
P

P
x
V

Y
x
H

P
x
E

Q
x
R

Q
x
H

P
|
P

Y
|
Y

V
x
G

G
|
G

M
x
D

S
x
L

A
x
V

F
x
Y

A
x
T

H
x
A

K
x
F

G
x
S

G
|
G

V
x
S

H
|
H

V
x
Q

S
x
D

A
|
A

I
|
I

M
x
N

K
|
K

E
x
G

P
x
L

R
x
D

C
x
A

-
x
M

-
x
K

-
x
L

-
x
D

-
x
A

-
x
D

-
x
A

-
x
D

-
x
C

-
x
D

-
x
V

-
x
D

-
x
M

-
x
L

-
x
W

-
x
Q

-
x
V

-
x
P

Y
|
Y

E
x
L

H
x
P

I
|
I

D
|
D

P
|
P

S
x
R

L
x
D

V
|
V

G
|
G

N
x
R

R
x
T

R
x
Y

R
x
E

-
x
A

-
x
V

V
x
I

L
x
R

V
|
V

S
x
N

E
x
S

L
x
Q

A
x
S

G
|
G

Q
x
K

S
x
G

N
x
G

L
x
V

L
x
A

Y
|
Y

K
x
I

L
x
M

R
x
K

-
x
T

E
x
D

L
x
H

N
x
G

L
|
L

D
x
S

L
|
L

P
|
P

S
x
R

Q
x
R

G
x
L

E
x
Q

V
x
I

A
x
E

-
x
F

R
x
S

Q
|
Q

I
x
V

L
x
I

A
x
Q

E
x
K

L
x
I

K
x
A

E
|
E

L

-

E

-

R

-

Q

-

G
|
G

F
x
T

Q
x
A

F
x
G

E
|
E

S
x
G

A
x
G

E
|
E

A
x
V

S
|
S

F
x
P

E
x
K

L
x
E

L
x
M

V
x
W

R
x
D

R
x
A

A
x
F

A
|
A

N
x
E

G
x
E

Y
|
Y

E
x
L

R
x
A

P
|
P

F
x
V

-
x
R

V
x
P

L
|
L

E
|
E

S
x
R

L
x
I

R
|
R

I
x
Q

L
x
H

T
x
V

E
x
D

L
x
A

-
x
A

-
x
D

K
x
D

E
x
D

G
|
G

A
x
T

V
x
T

H
x
S

A
x
I

E
x
T

A
|
A

T
|
T

I
x
V

K
|
K

L
x
I

R
x
N

V
x
G

G
x
V

D
x
E

K
x
T

V
x
E

V
x
I

H

-

T

-

A
x
S

A
x
G

E
x
S

G
|
G

N
|
N

G
|
G

P
|
P

V
x
L

N
x
A

A
|
A

L
x
F

D
x
V

N
x
H

A
|
A

L
|
L

R80 (= R12) binding 3-methyl-2-oxobutanoate
T254 (≠ E186) binding 3-methyl-2-oxobutanoate
H285 (= H206) binding 3-methyl-2-oxobutanoate
H287 (= H208) binding 3-methyl-2-oxobutanoate
369:424 (vs. 293:327, 20% identical) Subdomain I
425:433 (vs. 328:335, 22% identical) Linker
434:490 (vs. 336:394, 20% identical) Subdomain II
N532 (= N435) binding L-leucine
A536 (≠ N439) binding L-leucine

Sites not aligning to the query:

51:368 N-terminal domain
426:644 Required for the condensation reaction. Not required to bind substrate
491:644 Regulatory domain
563 binding L-leucine
565 binding L-leucine
625 binding L-leucine
627 binding L-leucine

Query Sequence

>WP_015738277.1 NCBI__GCF_000024605.1:WP_015738277.1
MDKVVVYDTTLRDGAQTEGISFSVADKLKIARRLVEMGFDYVEGGWPGSNPKDLEFFGQV
ARDPVLREKVTAFGSTRRKNTRPADDENLQRLCSCGVKTVTLFGKTWDLHVTRALNTTLE
ENLAMIRESVAYLKEQGLEVIYDAEHFFDGYKENPDYALATLEAAVSAGASTLVLCDTNG
GSMPWEVEAAVRRVVEKFPRVTVGIHAHNDTGMAVANTVVAVKAGARHVQGTVNGYGERC
GNADLCAVLPNLTFKCGFTTLPRESFSRLVELSRYVSEVANVHPYPQQPYVGMSAFAHKG
GVHVSAIMKEPRCYEHIDPSLVGNRRRVLVSELAGQSNLLYKLRELNLDLPSQGEVARQI
LAELKELERQGFQFESAEASFELLVRRAANGYERPFVLESLRILTELKEGGAVHAEATIK
LRVGDKVVHTAAEGNGPVNALDNALRKALEQFYPAIKRMRLVDYKVRVLDGTAGTGAVVR
VLIETGDGQRTWVTVGVSPNIIEASWQALADSFTYGLLKQAE

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