SitesBLAST

S102 (≠ A36) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ E206) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

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)
37% identity, 94% coverage: 19:384/391 of query aligns to 7:383/517 of Q9JZG1

query
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S

D16 (= D28) 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

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
39% identity, 81% coverage: 19:335/391 of query aligns to 22:341/399 of 6ktqA

query
sites
6ktqA

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binding 2-oxoglutaric acid: R30 (= R27), R154 (≠ S147), T156 (≠ G149), E158 (= E151), S184 (≠ R177), T188 (= T181), H216 (= H208), H218 (= H210)
binding coenzyme a: V67 (≠ M64), R96 (= R89), A97 (≠ L90), F116 (≠ G109), H128 (≠ L121), E158 (= E151)
binding zinc ion: E31 (≠ D28), H216 (= H208), H218 (= H210)

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)
34% identity, 95% coverage: 19:390/391 of query aligns to 85:481/503 of Q9FN52

query
sites
Q9FN52

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G263 (= G183) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
34% identity, 94% coverage: 19:385/391 of query aligns to 18:409/409 of 6e1jA

query
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6e1jA

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H

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A

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I

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-

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x
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x
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A

K

K

K

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A

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L

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K

A

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C

binding coenzyme a: Q30 (= Q31), F60 (≠ V61), S63 (≠ M64), I95 (vs. gap), R97 (= R89), F121 (≠ G109), K132 (= K120), L133 (= L121), S322 (≠ C299), G323 (= G300), I324 (= I301), D327 (= D304), K331 (= K308), L359 (≠ H334), R362 (≠ A337), H363 (≠ A338)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ S179), T194 (= T181), H225 (= H208), H227 (= H210)
binding manganese (ii) ion: D27 (= D28), V82 (vs. gap), E84 (vs. gap), H225 (= H208), H227 (= H210)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
31% identity, 94% coverage: 19:384/391 of query aligns to 8:381/516 of Q8F3Q1

query
sites
Q8F3Q1

V

L

A

E

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A

R16 (= R27) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 27:28) binding pyruvate
D17 (= D28) 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 (≠ E93) 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 (≠ L95) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ G109) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ G149) 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 (= E151) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T181) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H302) mutation H->A,N: Loss of activity.
D304 (= D304) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ T312) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ Y313) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ E314) mutation to A: Loss of activity.

Sites not aligning to the query:

430 Y→L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
431 D→A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
451 L→V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
454 Y→A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
458 I→A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
464 T→A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
468 V→A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
493 P→A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
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)
37% identity, 72% coverage: 19:298/391 of query aligns to 4:295/308 of 3rmjB

query
sites
3rmjB

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active site: Q16 (= Q31)
binding manganese (ii) ion: D13 (= D28), H201 (= H208), H203 (= H210), N237 (= N244)

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
30% identity, 83% coverage: 8:332/391 of query aligns to 21:344/400 of 3ivtB

query
sites
3ivtB

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P

D

V

I

E

E

F

C

H
|
H

G

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

A

L

R

E

A

A

G

G

A

A

S

T

H

H

L

I

S

D

V

T

T

S

V

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

E

A

V

L

A

L

A

A

A

R

L

M

E

Y

A

V

A

T

G

D

R

R

-

E

-

Y

-

I

A

T

T

H

G

K

V

Y

A

K

L

L

G

N

Q

Q

L

L

C

R

A

E

L

L

S

E

E

N

L

L

V

V

A

A

R

D

A

A

S

V

G

E

R

V

P

Q

L

I

S

P

P

F

Q

N

K

N

P

Y

I

I

V

T

G

G

E

M

G

C

V

A

F

F

T

T

H

H

E

K

C

A

G

G

I

I

H

H

V

A

D

K

G

A

L

I

M

L

K

A

D

N

R

P

A

S

T

T

Y

Y

E

E

S

I

A

-

D

-

L

L

R

K

P

P

E

E

R

D

F

F

G

G

R

M

S

S

H

R

R

Y

I

V

A

H

I

V

G

G

active site: Q42 (= Q31)
binding 2-oxoglutaric acid: R38 (= R27), H98 (≠ W87), R158 (≠ S147), S160 (≠ G149), T192 (= T181), H219 (= H208), H221 (= H210)
binding zinc ion: E39 (≠ D28), 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)
30% identity, 83% coverage: 8:332/391 of query aligns to 26:349/418 of Q9Y823

query
sites
Q9Y823

A

S

S

D

F

F

L

L

P

-

E

-

S

S

P

R

L

V

A

N

P

N

V

F

A

S

L

I

C

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

T

F

A

A

G

N

V

A

A

F

F

F

T

D

R

T

A

E

E

K

K

K

R

I

A

Q

I

I

A

A

E

K

A

A

L

L

Q

D

A

N

A

F

G

G

V

V

A

D

E

Y

V

I

E
|
E

V

L

G

T

V

S

P

P

A

V

M

A

G

S

E

E

E

Q

E

S

R

R

A

Q

D

D

I

C

R

E

A

A

V

I

A

C

A

K

V

L

L

G

K

L

T

K

A

C

A

K

P

I

V

L

V

T

W
x
H

C

I

R

R

L

C

R

H

A

M

E

D

D

D

L

A

A

R

A

V

A

A

Q

V

R

E

T

T

G

G

V

V

V

D

R

G

L

V

H
x
D

I

V

G

V

V

I

P

G

V

T

S

S

E

Q

R

Y

Q

L

I

R

S

K

A

Y

K

S

L

H

G

G

K

K

D

D

A

M

A

T

W

Y

V

I

R

I

D

D

K

S

V

A

E

T

K

E

L

V

V

I

R

N

A

F

A

V

S

K

W

S

A

K

G

G

H

I

K

E

V

V

S
x
R

V

F

G
x
S

A

S

E
|
E

D

D

A

S

S

F

R

R

A

S

D

D

P

L

F

V

F

D

L

L

A

L

E

S

I

L

A

Y

H

K

V

A

A

V

A

D

E

K

A

I

G

G

A

V

I

N

R

R

F

V

R

G

I

I

S

A

D

D

T
|
T

L

V

G

G

V

C

L

A

D

T

P

P

F

R

A

Q

A

V

H

Y

E

D

L

L

V

I

G

R

R

T

V

L

V

R

T

G

R

V

C

V

P

S

L

C

P

D

V

I

E
|
E

F

C

H
|
H

G

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

A

L

R

E

A

A

G

G

A

A

S

T

H

H

L

I

S

D

V

T

T

S

V

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

E

A

V

L

A

L

A

A

A

R

L

M

E

Y

A

V

A

T

G

D

R

R

A

E

T

Y

-

I

-

T

-

H

G

K

V

Y

A

K

L

L

G

N

Q

Q

L

L

C
x
R

A

E

L

L

S

E

E

N

L

L

V

V

A

A

R

D

A

A

S

V

G

E

R

V

P

Q

L

I

S

P

P

F

Q

N

K

N

P

Y

I

I

V

T

G

G

E

M

G

C

V

A

F

F

T

T

H

H

E

K

C

A

G

G

I

I

H

H

V

A

D

K

G

A

L

I

M

L

K

A

D

N

R

P

A

S

T

T

Y
|
Y

E

E

S

I

A

-

D

-

L

L

R

K

P

P

E

E

R

D

F

F

G

G

R

M

S

S

H

R

R

Y

I

V

A

H

I

V

G

G

R43 (= R27) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D28) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q31) mutation to A: Abolishes the catalytic activity.
E74 (= E58) 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 (≠ W87) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ H107) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ S147) 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 (≠ G149) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E151) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T181) 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 (= E206) 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 (≠ C269) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y313) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.

Sites not aligning to the query:

364 Q→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, 79% coverage: 19:325/391 of query aligns to 2:309/311 of 3bliA

query
sites
3bliA

V

L

A

E

L

I

C

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q
|
Q

T

T

A

R

G

G

V

V

A

S

F

F

T

S

R

T

A

S

E

E

K

K

R

L

A

N

I

I

A

A

E

K

A

F

L

L

-

L

Q

Q

A

K

A

L

G

N

V

V

A

D

E

R

V

V

E

E

V

I

G

-

V

-

P

-

A

A

M

S

G

A

E
x
R

E
x
V

E

S

R

K

A

G

D

E

I

L

R

E

A

T

V

V

A

Q

A

K

V

I

L

M

K

E

T

W

A

A

P

T

V

E

V

Q

W

L

C

T

-

E

R

R

L

I

R

E

A

I

E

L

D

G

L

F

A

V

A

D

A

G

Q

N

R

K

T

T

-

V

-

D

-

W

-

I

-

K

-

D

-

S

G

G

V

A

V

K

R

V

L

L

H

N

I

L

G

L

V

T

P

K

V

G

S

S

E

L

R

H

Q

H

I

L

S

E

A

K

K

Q

L

L

G

G

K

K

D

T

A

P

A

K

W

E

V

F

R

F

D

T

K

D

V

V

E

S

K

F

L

V

V

I

R

E

A

Y

A

A

S

I

W

K

A

S

G

G

H

L

K

K

V

I

S

N

V

V

G
x
Y

A

L

E
|
E

D

D

A

W

S

S

-

N

-

G

-

F

R

R

A

N

D

S

P

P

F

D

F

Y

L

V

A

K

E

S

I

L

A

V

H

E

V

H

A

L

A

S

E

K

A

E

G

H

A

I

I

E

R

R

F

I

R

F

I

L

S
x
P

D

D

T
|
T

L

L

G

G

V

V

L

L

D

S

P

P

F

E

A

E

A

T

H

F

E

Q

L

G

V

V

G

D

R

S

V

L

V

I

T

Q

R

K

C

Y

P

P

-

D

L

I

P

H

V

F

E

E

F

F

H
|
H

G

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

A

I

R

R

A

A

G

G

A

V

S

K

H

G

L

L

S

H

V

A

T

S

V

I

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

P

L

L

E

E

E

A

V

L

A

V

A

T

L

I

-

H

E

D

A

K

A

S

G

N

R

S

A

K

T

T

G

N

V

I

A

N

L

E

G

I

Q

A

L

I

C

T

A

E

L

A

S

S

E

R

L

L

V

V

A

E

R

V

A

F

S

S

G

G

R

K

P

R

L

I

S

S

P

A

Q

N

K

R

P

P

I

I

V

V

G

G

E

E

G

D

V

V

F

F

T

T

H

Q

E

T

C

A

G

G

I

V

H

N

V

L

D

-

G

-

L

-

M

-

K

-

D

-

R

-

A

-

T

-

Y

Y

E

A

S

N

A

P

D

I

L

L

R

-

P

P

E

E

R

R

F

F

G

G

R

R

active site: Q14 (= Q31)
binding acetyl coenzyme *a: Q14 (= Q31), R47 (≠ E66), V48 (≠ E67), E140 (= E151)
binding pyruvic acid: R10 (= R27), Y138 (≠ G149), P171 (≠ S179), T173 (= T181)
binding zinc ion: D11 (= D28), H201 (= H208), H203 (= H210)

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
30% identity, 83% coverage: 8:332/391 of query aligns to 3:315/370 of 3mi3A

query
sites
3mi3A

A

S

S

D

F

F

L

L

P

-

E

-

S

S

P

R

L

V

A

N

P

N

V

F

A

S

L

I

C

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

T

F

A

A

G

N

V

A

A

F

F

F

T

D

R

T

A

E

E

K

K

K

R

I

A

Q

I

I

A

A

E

K

A

A

L

L

Q

D

A

N

A

F

G

G

V

V

A

D

E

Y

V

I

E

E

V

L

G

T

V

S

P

P

A

V

M

A

G

S

E

E

E

Q

E

S

R

R

A

Q

D

D

I

C

R

E

A

A

V

I

A

C

A

K

V

L

L

G

K

L

T

K

A

C

A

K

P

I

V

L

V

T

W

H

C

I

R

R

L

C

R

H

A

M

E

D

D

D

L

A

A

R

A

V

A

A

Q

V

R

E

T

T

G

G

V

V

V

D

R

-

L

-

H

-

I

-

G

G

V

V

P
x
D

V

V

S

V

E

-

R

-

Q

-

I

-

S

-

A

-

K

-

L

I

G

G

K

T

D

S

A

M

A

T

W

Y

V

I

R

I

D

D

K

S

V

A

E

T

K

E

L

V

V

I

R

N

A

F

A

V

S

K

W

S

A

K

G

G

H

I

K

E

V

V

S

R

V

F

G

S

A

S

E

E

D

D

A

S

S

F

R

R

A

S

D

D

P

L

F

V

F

D

L

L

A

L

E

S

I

L

A

Y

H

K

V

A

A

V

A

D

E

K

A

I

G

G

A

V

I

N

R

R

F

V

R

G

I

I

S

A

D

D

T
|
T

L

V

G

G

V

C

L

A

D

T

P

P

F

R

A

Q

A

V

H

Y

E

D

L

L

V

I

G

R

R

T

V

L

V

R

T

G

R

V

C

V

P

S

L

C

P

D

V

I

E

E

F

C

H
|
H

G

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

A

L

R

E

A

A

G

G

A

A

S

T

H

H

L

I

S

D

V

T

T

S

V

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

E

A

V

L

A

L

A

A

A

R

L

M

E

Y

A

V

A

T

G

D

R

R

A

E

T

Y

-

I

-

T

-

H

G

K

V

Y

A

K

L

L

G

N

Q

Q

L

L

C

R

A

E

L

L

S

E

E

N

L

L

V

V

A

A

R

D

A

A

S

V

G

E

R

V

P

Q

L

I

S

P

P

F

Q

N

K

N

P

Y

I

I

V

T

G

G

E

M

G

C

V

A

F

F

T

T

H

H

E

K

C

A

G

G

I

I

H

H

V

A

D

K

G

A

L

I

M

L

K

A

D

N

R

P

A

S

T

T

Y

Y

E

E

S

I

A

-

D

-

L

L

R

K

P

P

E

E

R

D

F

F

G

G

R

M

S

S

H

R

R

Y

I

V

A

H

I

V

G

G

active site: Q24 (= Q31)
binding lysine: R20 (= R27), D100 (≠ P111), T163 (= T181), H190 (= H208), H192 (= H210)
binding zinc ion: E21 (≠ D28), H190 (= H208), H192 (= H210)

3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 83% coverage: 8:332/391 of query aligns to 3:313/364 of 3ivsA

query
sites
3ivsA

A

S

S

D

F

F

L

L

P

-

E

-

S

S

P

R

L

V

A

N

P

N

V

F

A

S

L

I

C

I

D

E

T

S

T

T

L

L

R

R

D
x
E

G

G

E

E

Q
|
Q

T

F

A

A

G

N

V

A

A

F

F

F

T

D

R

T

A

E

E

K

K

K

R

I

A

Q

I

I

A

A

E

K

A

A

L

L

Q

D

A

N

A

F

G

G

V

V

A

D

E

Y

V

I

E

E

V

L

G

T

V

S

P

P

A

V

M

A

G

S

E

E

E

Q

E

S

R

R

A

Q

D

D

I

C

R

E

A

A

V

I

A

C

A

K

V

L

L

G

K

L

T

K

A

C

A

K

P

I

V

L

V

T

W

H

C

I

R

R

L

C

R

H

A

M

E

D

D

D

L

A

A

R

A

V

A

A

Q

V

R

E

T

T

G

G

V

V

-

D

-

G

V

V

R

D

L

V

H

V

I

I

G

G

V

-

P

-

V

-

S

-

E

-

R

-

Q

-

I

-

S

-

A

-

K

-

L

-

G

-

K

-

D

-

A

T

W

Y

V

I

R

I

D

D

K

S

V

A

E

T

K

E

L

V

V

I

R

N

A

F

A

V

S

K

W

S

A

K

G

G

H

I

K

E

V

V

S

R

V

F

G

S

A

S

E

E

D

D

A

S

S

F

R

R

A

S

D

D

P

L

F

V

F

D

L

L

A

L

E

S

I

L

A

Y

H

K

V

A

A

V

A

D

E

K

A

I

G

G

A

V

I

N

R

R

F

V

R

G

I

I

S

A

D

D

T

T

L

V

G

G

V

C

L

A

D

T

P

P

F

R

A

Q

A

V

H

Y

E

D

L

L

V

I

G

R

R

T

V

L

V

R

T

G

R

V

C

V

P

S

L

C

P

D

V

I

E

E

F

C

H
|
H

G

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

A

L

R

E

A

A

G

G

A

A

S

T

H

H

L

I

S

D

V

T

T

S

V

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

E

A

V

L

A

L

A

A

A

R

L

M

E

Y

A

V

A

T

G

D

R

R

A

E

T

Y

-

I

-

T

-

H

G

K

V

Y

A

K

L

L

G

N

Q

Q

L

L

C

R

A

E

L

L

S

E

E

N

L

L

V

V

A

A

R

D

A

A

S

V

G

E

R

V

P

Q

L

I

S

P

P

F

Q

N

K

N

P

Y

I

I

V

T

G

G

E

M

G

C

V

A

F

F

T

T

H

H

E

K

C

A

G

G

I

I

H

H

V

A

D

K

G

A

L

I

M

L

K

A

D

N

R

P

A

S

T

T

Y

Y

E

E

S

I

A

-

D

-

L

L

R

K

P

P

E

E

R

D

F

F

G

G

R

M

S

S

H

R

R

Y

I

V

A

H

I

V

G

G

active site: Q24 (= Q31)
binding cobalt (ii) ion: E21 (≠ D28), H188 (= H208), H190 (= H210)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
28% identity, 85% coverage: 19:349/391 of query aligns to 4:345/380 of 4ov9A

query
sites
4ov9A

V

I

A

H

L

I

C

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

T

A

A

L

G

K

V

R

A

P

F

W

T

T

R

I

A

D

E

E

K

K

R

I

A

E

I

V

A

F

E

D

A

L

L

L

Q

V

A

E

A

L

G

N

V

V

A

D

E

G

V

I

E

E

V

V

G

G

V

F

P

P

A

S

M

S

G

N

E

E

E

T

E

E

R

F

A

H

D

T

I

C

R

Q

A

V

V

L

A

S

A

K

V

R

L

A

K

P

T

K

A

G

A

K

P

P

V

I

V

A

-

A

W
x
L

C

S

R

R

L

A

R

N

A

Q

E

N

D

E

L

I

A

A

-

V

-

T

-

W

-

E

A

A

A

I

Q

Q

R

K

T

A

G

D

V

C

V

P

R

R

L

M

H

H

I

I

G

V

V

Y

P

P

V

V

S

S

E

D

R

F

Q

S

I

I

S

K

A

H

K

V

L

L

G

K

K

I

D

S

A

E

A

-

W

-

V

-

R

K

D

E

K

V

V

L

E

Q

K

K

L

I

V

R

R

N

A

S

A

I

S

S

W

F

A

A

G

R

H

S

K

I

V

V

S

G

V

P

G

G

A

I

E

E

D

I

A

Q

S

F

R

S

A

G

D

E

P

H

F

F

-

G

-

D

-

A

-

I

-

E

-

N

-

F

-

A

F

F

L

T

A

K

E

E

I

A

A

F

H

L

V

T

A

A

A

I

E

E

A

A

G

G

A

A

I

N

R

I

F

I

R

N

I

L

S

P

D

N

T
|
T

L

V

G

E

V

R

L

Y

D

R

P

P

F

M

A

V

A

F

H

V

E

N

L

M

V

V

G

K

R

E

V

I

-

K

-

D

V

V

T

V

R

K

C

D

P

K

L

A

P

I

V

I

E

S

F

I

H
|
H

G

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

A

V

R

Y

A

V

G

G

A

A

S

E

H

Q

L

I

S

E

V

V

T

A

V

L

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

N

L

L

E

Y

E

E

V

T

A

A

A

I

A

A

L

L

E

H

A

Q

A

N

G

G

R

E

A

N

T

L

G

N

V

I

A

N

L

F

G

Q

Q

R

L

I

C

Y

A

P

L

T

S

A

E

K

L

R

V

I

A

S

R

E

A

L

S

T

G

G

R

I

P

P

L

I

S

G

P

E

Q

K

K

T

P

P

I

I

V

I

G

G

E

E

G

D

V

I

F

F

T

S

H

H

E

R

C

S

G

G

I

I

H

H

V

-

D

Q

G

T

L

L

M

H

K

Q

D

S

R

K

A

G

T

A

Y

Y

E

R

S

T

A

-

D

-

L

F

R

S

P

P

E

E

R

F

F

V

G

G

R

R

S

M

H

D

R

K

-

E

-

T

I

I

A

S

I

F

G

T

K

N

H

Q

S

S

S

G

A

H

A

K

G

A

L

I

A

E

R

F

A

L

L

L

A

H

E

Q

A

R

G

G

L

I

active site: Q16 (= Q31)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R27), L73 (≠ W87), T176 (= T181), H205 (= H208), H207 (= H210)
binding zinc ion: D13 (= D28), H205 (= H208), H207 (= H210)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
28% identity, 85% coverage: 19:349/391 of query aligns to 4:343/379 of 4ov4A

query
sites
4ov4A

V

I

A

H

L

I

C

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

T

A

A

L

G

K

V

R

A

P

F

W

T

T

R

I

A

D

E

E

K

K

R

I

A

E

I

V

A

F

E

D

A

L

L

L

Q

V

A

E

A

L

G

N

V

V

A

D

E

G

V

I

E

E

V

V

G

G

V

F

P

P

A

S

M

S

G

N

E

E

E

T

E

E

R

F

A

H

D

T

I

C

R

Q

A

V

V

L

A

S

A

K

V

R

L

A

K

P

T

K

A

G

A

K

P

P

V

I

V

A

-

A

W

L

C

S

R

R

L

A

R

N

A

Q

E

N

D

E

L

I

A

A

-

V

-

T

-

W

-

E

A

A

A

I

Q

Q

R

K

T

A

G

D

V

C

V

P

R

R

L

M

H

H

I

I

G

V

V

Y

P

P

V

V

S

S

E

D

R

F

Q

S

I

I

S

K

A

H

K

V

L

L

G

K

K

I

D

S

A

E

A

-

W

-

V

-

R

K

D

E

K

V

V

L

E

Q

K

K

L

I

V

R

R

N

A

S

A

I

S

S

W

F

A

A

G

R

H

S

K

I

V

V

S

G

V

P

G

G

A

I

E

E

D

I

A

Q

S

F

R

S

A

G

D

E

P

H

F

F

-

G

-

D

-

A

-

I

-

E

-

N

-

F

-

A

F

F

L

T

A

K

E

E

I

A

A

F

H

L

V

T

A

A

A

I

E

E

A

A

G

G

A

A

I

N

R

I

F

I

R

N

I

L

S
x
P

D

N

T
|
T

L

V

G

E

V

R

L

Y

D

R

P

P

F

M

A

V

A

F

H

V

E

N

L

M

V

V

G

K

R

E

V

I

-

K

-

D

V

V

T

V

R

K

C

D

P

K

L

A

P

I

V

I

E

S

F

I

H
|
H

G

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

A

V

R

Y

A

V

G

G

A

A

S

E

H

Q

L

I

S

E

V

V

T

A

V

L

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

N

L

L

E

Y

E

E

V

T

A

A

A

I

A

A

L

L

E

H

A

Q

A

N

G

G

R

E

A

N

T

L

G

N

V

I

A

N

L

F

G

Q

Q

R

L

I

C

Y

A

P

L

T

S

A

E

K

L

R

V

I

A

S

R

E

A

L

S

T

G

G

R

I

P

P

L

I

S

G

P

E

Q

K

K

T

P

P

I

I

V

I

G

G

E

E

G

D

V

I

F

F

T

S

H

H

E

R

C

S

G

G

I

I

H

H

V

Q

D

H

G

-

L

-

M

-

K

Q

D

S

R

K

A

G

T

A

Y

Y

E

R

S

T

A

-

D

-

L

F

R

S

P

P

E

E

R

F

F

V

G

G

R

R

S

M

H

D

R

K

-

E

-

T

I

I

A

S

I

F

G

T

K

N

H

Q

S

S

S

G

A

H

A

K

G

A

L

I

A

E

R

F

A

L

L

L

A

H

E

Q

A

R

G

G

L

I

active site: Q16 (= Q31)
binding 3-methyl-2-oxobutanoic acid: R12 (= R27), P174 (≠ S179), T176 (= T181), H205 (= H208), H207 (= H210)
binding zinc ion: D13 (= D28), H205 (= H208), H207 (= H210)

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 88% coverage: 21:366/391 of query aligns to 6:373/376 of O87198

query
sites
O87198

L

I

C

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

T

F

A

E

G

K

V

A

A

N

F

F

T

S

R

T

A

Q

E

D

K

K

R

V

A

E

I

I

A

A

E

K

A

A

L

L

Q

D

A

E

A

F

G

G

V

I

A

E

E

Y

V

I

E

E

V

V

G

T

V

T

P

P

A

V

M

A

G

S

E

P

E

Q

E

S

R

R

A

K

D

D

I

A

R

E

A

V

V

L

A

A

A

S

V

L

L

G

K

L

T

K

A

A

A

K

P

V

V

V

-

T

-
x
H

V

I

W

Q

C

C

R

R

L

L

R

D

A

A

E

A

D

K

L

V

A

A

A

V

A

E

Q

T

R

G

T

V

G

Q

V

G

V

I

R
x
D

L

L

H

L

I

F

G

G

V

-

P

-

V

-

S

T

E

S

R

K

Q

Y

I

L

S

R

A

A

K

A

L

H

G

G

K

R

D

D

A

I

A

P

W

R

V

I

R

I

D

E

K

E

V

A

E

K

K

E

L

V

V

I

R

A

A

Y

A

I

S

R

W

E

A

A

G

A

H

P

K

H

V

V

S

E

V

V

-
x
R

-

F

G
x
S

A

A

E

E

D

D

A

T

S

F

R

R

A

S

D

E

P

E

F

Q

F

D

L

L

A

L

E

A

I

V

A

Y

H

E

V

A

A

V

A

A

E

P

A

Y

G

-

A

V

I

D

R

R

F

V

R

G

I

L

S

A

D

D

T
|
T

L

V

G

G

V

V

L

A

D

T

P

P

F

R

A

Q

A

V

H

Y

E

A

L

L

V

V

G

-

R

R

V

E

V

V

T

R

R

R

C

V

P

V

L

G

P

P

-

R

-

V

-

D

V

I

E

E

F

F

H
|
H

G

G

H
|
H

N

N

D

D

L

T

G

G

M

C

A

A

T

I

A

A

N

N

S

A

L

Y

A

E

A

A

A

I

R

E

A

A

G

G

A

A

S

T

H

H

L

V

S

D

V

T

T

T

V

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

V

F

A

L

A

A

-

R

-

M

-

Y

A

T

L

L

E

Q

A

P

A

E

G

Y

R

V

A

R

T

R

G

K

V

Y

A

K

L

L

G

E

Q

M

L

L

C

P

A

E

L

L

S

D

E

R

L

M

V

V

A

A

R

R

A

M

S

V

G

G

R

V

P

E

L

I

S

P

P

F

Q

N

K

N

P

Y

I

I

V

T

G

G

E

E

G

T

V

A

F

F

T

S

H

H

E

K

C

A

G

G

I

M

H

H

V

L

D

K

G

A

L

I

M

Y

K

I

D

N

R

P

A

E

T

A

Y

Y

E

E

S

P

A

Y

D

P

L

-

R

-

P

P

E

E

R

V

F

F

G

G

R

V

S

K

H

R

R

K

I

L

A

I

I

I

-

A

-

S

-

R

-

L

-

T

G

G

K

R

H

H

S

A

S

I

A

K

A

A

-

R

-

A

-

E

-

L

G

G

L

L

-

H

-

Y

-

G

-

E

-

L

-

H

-

R

-

V

-

T

-

Q

-

H

A

I

R

K

A

A

L

L

A

A

E

D

A

R

G

G

L

-

P

-

A

-

D

-

A

Q

A

L

T

T

L

L

A

E

L

L

M

D

P

R

A

I

L

L

R

R

D

E

W

W

R12 (= R27) binding 2-oxoglutarate
E13 (≠ D28) binding Mg(2+)
H72 (vs. gap) 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 (≠ R105) binding L-lysine
R133 (vs. gap) binding 2-oxoglutarate
S135 (≠ G149) binding L-lysine
T166 (= T181) binding 2-oxoglutarate; binding L-lysine
H195 (= H208) binding Mg(2+)
H197 (= H210) binding Mg(2+)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
32% identity, 88% coverage: 21:366/391 of query aligns to 5:344/347 of 3a9iA

query
sites
3a9iA

L

I

C

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

T

F

A

E

G

K

V

A

A

N

F

F

T

S

R

T

A

Q

E

D

K

K

R

V

A

E

I

I

A

A

E

K

A

A

L

L

Q

D

A

E

A

F

G

G

V

I

A

E

E

Y

V

I

E

E

V

V

G

T

V

T

P

P

A

V

M

A

G

S

E

P

E

Q

E

S

R

R

A

K

D

D

I

A

R

E

A

V

V

L

A

A

A

S

V

L

L

G

K

L

T

K

A

A

A

K

P

V

V

V

-

T

-

H

V

I

W

Q

C

C

R

R

L

L

R

D

A

A

E

A

D

K

L

V

A

A

A

V

A

-

Q

-

R

E

T

T

G

G

V

V

V

Q

R

G

L

I

H
x
D

I

L

G

L

V

F

P

G

V

T

S

S

E

K

R

Y

Q

L

I

D

S

I

A

P

K

R

L

I

G

I

K

E

D

E

A

A

A

K

W

-

V

-

R

-

D

-

K

E

V

V

E

I

K

A

L

Y

V

I

R

R

A

E

A

A

S

-

W

-

A

A

G

P

H

H

-

V

K

E

V

V

S

R

V

F

G
x
S

A

A

E

E

D

D

A

T

S

F

R

R

A

S

D

E

P

E

F

Q

F

D

L

L

A

L

E

A

I

V

A

Y

H

E

V

A

A

V

A

A

E

P

A

Y

G

-

A

V

I

D

R

R

F

V

R

G

I

L

S

A

D

D

T
|
T

L

V

G

G

V

V

L

A

D

T

P

P

F

R

A

Q

A

V

H

Y

E

A

L

L

V

V

G

-

R

R

V

E

V

V

T

R

R

R

C

V

P

V

L

G

P

P

-

R

-

V

-

D

V

I

E

E

F

F

H
|
H

G

G

H
|
H

N

N

D

D

L

T

G

G

M

C

A

A

T

I

A

A

N

N

S

A

L

Y

A

E

A

A

A

I

R

E

A

A

G

G

A

A

S

T

H

H

L

V

S

D

V

T

T

T

V

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

V

F

A

L

A

A

-

R

-

M

-

Y

A

T

L

L

E

Q

A

P

A

E

G

Y

R

V

A

R

T

R

G

K

V

Y

A

K

L

L

G

E

Q

M

L

L

C

P

A

E

L

L

S

D

E

R

L

M

V

V

A

A

R

R

A

M

S

V

G

G

R

V

P

E

L

I

S

P

P

F

Q

N

K

N

P

Y

I

I

V

T

G

G

E

E

G

T

V

A

F

F

T

S

H

H

E

K

C

A

G

G

I

M

H

H

V

L

D

K

G

A

L

I

M

Y

K

I

D

N

R

P

A

E

T

A

Y

Y

E

E

S

P

A

Y

D

P

L

-

R

-

P

P

E

E

R

V

F

F

G

G

R

V

S

K

H

-

R

-

I

-

A

-

I

-

G

G

K

L

H

H

S

Y

S

G

A

E

G

E

L

L

A

H

R

R

A

V

L

T

A

Q

E

H

A

I

G

K

L

A

P

L

A

A

D

D

-

R

-

G

A

Q

A

L

T

T

L

L

A

E

L

L

M

D

P

R

A

I

L

L

R

R

D

E

W

W

binding cobalt (ii) ion: E12 (≠ D28), H188 (= H208), H190 (= H210)
binding lysine: R11 (= R27), D91 (≠ H107), S128 (≠ G149), T159 (= T181), H188 (= H208), H190 (= H210)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
31% identity, 80% coverage: 21:331/391 of query aligns to 6:313/314 of 2zyfA

query
sites
2zyfA

L

I

C

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

T

F

A

E

G

K

V

A

A

N

F

F

T

S

R

T

A

Q

E

D

K

K

R

V

A

E

I

I

A

A

E

K

A

A

L

L

Q

D

A

E

A

F

G

G

V

I

A

E

E

Y

V

I

E

E

V

V

G

T

V

T

P

P

A

V

M

A

G

S

E

P

E

Q

E

S

R

R

A

K

D

D

I

A

R

E

A

V

V

L

A

A

A

S

V

L

L

G

K

L

T

K

A

A

A

K

P

V

V

V

-

T

-
x
H

V

I

W

Q

C

C

R

R

L

L

R

D

A

A

E

A

D

K

L

V

A

A

A

V

A

-

Q

-

R

E

T

T

G

G

V

V

V

Q

R

G

L

I

H

D

I

L

G
x
L

V

F

P

G

V

T

S

S

E

K

R

-

Q

-

I

-

S

-

A

-

K

-

L

-

G

G

K

R

D

D

A

I

A

P

W

R

V

I

R

I

D

E

K

E

V

A

E

K

K

E

L

V

V

I

R

A

A

Y

A

I

S

R

W

E

A

A

G

A

H

P

K

H

V

V

S

E

V

V

-
x
R

-

F

G

S

A

A

E

E

D

D

A

T

S

F

R

R

A

S

D

E

P

E

F

Q

F

D

L

L

A

L

E

A

I

V

A

Y

H

E

V

A

A

V

A

A

E

P

A

Y

G

-

A

V

I

D

R

R

F

V

R

G

I

L

S

A

D

D

T
|
T

L

V

G

G

V

V

L

A

D

T

P

P

F

R

A

Q

A

V

H

Y

E

A

L

L

V

V

G

-

R

R

V

E

V

V

T

R

R

R

C

V

P

V

L

G

P

P

-

R

-

V

-

D

V

I

E

E

F

F

H
|
H

G

G

H
|
H

N

N

D

D

L

T

G

G

M

C

A

A

T

I

A

A

N

N

S

A

L

Y

A

E

A

A

A

I

R

E

A

A

G

G

A

A

S

T

H

H

L

V

S

D

V

T

T

T

V

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

V

F

A

L

A

A

-

R

-

M

-

Y

A

T

L

L

E

Q

A

P

A

E

G

Y

R

V

A

R

T

R

G

K

V

Y

A

K

L

L

G

E

Q

M

L

L

C

P

A

E

L

L

S

D

E

R

L

M

V

V

A

A

R

R

A

M

S

V

G

G

R

V

P

E

L

I

S

P

P

F

Q

N

K

N

P

Y

I

I

V

T

G

G

E

E

G

T

V

A

F

F

T

S

H

H

E

K

C

A

G

G

I

M

H

H

V

L

D

K

G

A

L

I

M

Y

K

I

D

N

R

P

A

E

T

A

Y

Y

E

E

S

P

A

Y

D

P

L

-

R

-

P

P

E

E

R

V

F

F

G

G

R

V

S

K

H

R

R

K

I

L

A

I

I

I

active site: Q16 (= Q31)
binding 2-oxoglutaric acid: R12 (= R27), H72 (vs. gap), L94 (≠ G109), R127 (vs. gap), T160 (= T181), H189 (= H208)
binding magnesium ion: E13 (≠ D28), H189 (= H208), H191 (= H210)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
31% identity, 80% coverage: 21:331/391 of query aligns to 6:311/312 of 2ztjA

query
sites
2ztjA

L

I

C

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

T

F

A

E

G

K

V

A

A

N

F

F

T

S

R

T

A

Q

E

D

K

K

R

V

A

E

I

I

A

A

E

K

A

A

L

L

Q

D

A

E

A

F

G

G

V

I

A

E

E

Y

V

I

E

E

V

V

G

T

V

T

P

P

A

V

M

A

G

S

E

P

E

Q

E

S

R

R

A

K

D

D

I

A

R

E

A

V

V

L

A

A

A

S

V

L

L

G

K

L

T

K

A

A

A

K

P

V

V

V

-

T

-
x
H

V

I

W

Q

C

C

R

R

L

L

R

D

A

A

E

A

D

K

L

V

A

A

A

V

A

E

Q

T

R

G

T

V

G

Q

V

G

V

I

R

D

L

L

H
x
L

I

F

G

G

V

T

P

-

V

-

S

-

E

-

R

-

Q

-

I

-

S

-

A

-

K

-

L

-

G

G

K

R

D

D

A

I

A

P

W

R

V

I

R

I

D

E

K

E

V

A

E

K

K

E

L

V

V

I

R

A

A

Y

A

I

S

R

W

E

A

A

G

A

H

P

K

H

V

V

S

E

V

V

-
x
R

-

F

G

S

A

A

E

E

D

D

A

T

S

F

R

R

A

S

D

E

P

E

F

Q

F

D

L

L

A

L

E

A

I

V

A

Y

H

E

V

A

A

V

A

A

E

P

A

Y

G

-

A

V

I

D

R

R

F

V

R

G

I

L

S
x
A

D

D

T
|
T

L

V

G

G

V

V

L

A

D

T

P

P

F

R

A

Q

A

V

H

Y

E

A

L

L

V

V

G

-

R

R

V

E

V

V

T

R

R

R

C

V

P

V

L

G

P

P

-

R

-

V

-

D

V

I

E

E

F

F

H
|
H

G

G

H
|
H

N

N

D

D

L

T

G

G

M

C

A

A

T

I

A

A

N

N

S

A

L

Y

A

E

A

A

A

I

R

E

A

A

G

G

A

A

S

T

H

H

L

V

S

D

V

T

T

T

V

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

A

P

L

L

E

G

V

F

A

L

A

A

-

R

-

M

-

Y

A

T

L

L

E

Q

A

P

A

E

G

Y

R

V

A

R

T

R

G

K

V

Y

A

K

L

L

G

E

Q

M

L

L

C

P

A

E

L

L

S

D

E

R

L

M

V

V

A

A

R

R

A

M

S

V

G

G

R

V

P

E

L

I

S

P

P

F

Q

N

K

N

P

Y

I

I

V

T

G

G

E

E

G

T

V

A

F

F

T

S

H

H

E

K

C

A

G

G

I

M

H

H

V

L

D

K

G

A

L

I

M

Y

K

I

D

N

R

P

A

E

T

A

Y

Y

E

E

S

P

A

Y

D

P

L

-

R

-

P

P

E

E

R

V

F

F

G

G

R

V

S

K

H

R

R

K

I

L

A

I

I

I

active site: Q16 (= Q31)
binding 2-oxoglutaric acid: R12 (= R27), H72 (vs. gap), L94 (≠ H107), R125 (vs. gap), A156 (≠ S179), T158 (= T181), H187 (= H208), H189 (= H210)
binding copper (ii) ion: E13 (≠ D28), H187 (= H208), H189 (= H210)

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)
32% identity, 66% coverage: 18:275/391 of query aligns to 10:268/347 of Q53WI0

query
sites
Q53WI0

P

P

V

P

A

V

L

V

C

V

D

D

T

T

L

L

R

R

D

D

G

G

E

S

Q

H

T

A

A

H

G

R

V

H

A

Q

F

Y

T

T

R

V

A

E

E

E

K

A

R

R

A

A

I

I

A

A

E

Q

A

A

L

L

Q

D

A

E

A

A

G

G

V

V

A

Y

E

A

V

I

E

E

V

V

-

S

-

H

-

G

-

D

-

G

-

L

-

G

G

G

V

S

P

S

A

L

M

Q

G

Y

E

G

E

F

E

S

R

R

A

T

D

D

-

E

-

M

-

E

-

L

I

I

R

R

A

A

V

V

A

R

A

E

V

T

L

V

K

R

T

R

A

A

A

K

-

V

-

A

-

L

P

P

V

G

V

I

W

G

C

T

R

R

L

-

R

-

A

-

E

K

D

E

L

L

A

K

A

E

A

A

Q

V

R

E

T

A

G

G

V

I

V

Q

R

M

L

V

H

R

I

I

G

A

V

T

P

Q

V

C

S

T

E

E

R

A

Q

D

I

I

S

S

A

-

K

-

L

-

G

-

K

-

D

-

A

-

W

-

V

-

R

-

D

-

K

-

V

-

E

E

K

Q

L

H

V

F

R

G

A

M

A

A

S

K

W

E

A

M

G

G

H

L

K

E

V

A

S

V

V

G

G

F

A

L

E

M

D

M

A

S

S

H

R

M

A

R

D

P

P

P

F

E

F

F

L

L

A

A

E

E

I

Q

A

A

H

R

V

L

A

M

A

E

E

G

A

Y

G

G

A

A

I

D

R

V

F

V

R

Y

I

I

S

V

D

D

T

S

L

A

G

G

V

A

L

M

-

L

-

P

-

E

D

D

P

A

F

Y

A

A

A

R

H

V

E

K

L

A

V

L

G

K

R

E

V

A

V

L

T

S

R

R

C

A

P

-

L

-

P

K

V

V

E

G

F

F

H

H

G

A

H

H

N

N

D

N

L

L

G

G

M

L

A

A

T

I

A

G

N

N

S

T

L

L

A

A

A

L

R

A

A

A

G

G

A

A

S

D

H

W

L

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S

D

V

A

T

T

V

L

N

R

G

G

L

Y

G

G

E

A

R

G

A

A

G

G

N

N

A

A

A

P

L

L

E

E

E

V

V

L

A

A

A

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L

L

E

D

A

K

A

A

G

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A

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P

G

G

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K

L

L

C

L

A

D

L

A

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Y

V

V

Sites not aligning to the query:

324 A→G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.

4jn6C Crystal structure of the aldolase-dehydrogenase complex from mycobacterium tuberculosis hrv37 (see paper)
28% identity, 66% coverage: 19:277/391 of query aligns to 4:264/339 of 4jn6C

query
sites
4jn6C

V

V

A

R

L

I

C

T

D

D

T

T

T

S

L

L

R
|
R

D
|
D

G

G

E

S

Q
x
H

T

H

A

K

G

R

V

H

A

Q

F

F

T

T

R

K

A

D

E

E

K

V

R

G

A

A

I

I

A

V

E

A

A

A

L

L

Q

D

A

A

G

G

V

V

A

P

E

V

V

I

E

E

V

V

-

T

-

H

-

G

-

D

-

G

-

L

-

G

-

S

-

F

-

N

-

Y

G

G

V

F

P

S

A

K

M

T

G

P

E

E

E

Q

E

E

R

-

A

-

D

-

I

L

R

I

A

K

V

L

A

A

V

A

L

T

K

A

T

K

A

E

A

A

P

R

V

I

V

A

W

F

C

L

R

M

L

L

-

P

-

G

-

V

-

G

R

T

A

K

E

D

D

D

L

I

A

K

A

E

A

A

Q

R

R

D

T

N

G

G

V

G

V

S

R

I

L

C

H

R

I

I

G

A

V

T

P

H

V

C

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T

E

E

R

A

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D

I

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S

S

A

I

K

Q

-

H

L

F

G

G

K

L

D

A

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E

W

L

V

G

R

L

D

E

K

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V

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G

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L

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x
M

R

M

A

A

A

H

S

T

W

I

A

A

G

-

H

-

K

-

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-

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-

V

-

G

-

A

-

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-

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-

P

P

F

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F

K

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L

A

A

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A

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A

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I

A

M

A

A

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A

A

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G

A

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I

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x
V

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x
S

L

A

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G

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A

L

L

D

V

P

L

F

D

A

G

A

V

H

A

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D

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V

V

G

S

R

A

V

L

V

V

T

A

R

E

C

L

-

G

-

E

P

D

L

A

P

Q

V

V

E

G

F

F

H
|
H

G

G

H
|
H

N

E

D

N

L

L

G

G

M

L

A

G

T

V

A

A

N

N

S

S

L

V

A

A

A

V

R

R

A

A

G

G

A

A

S

K

H

Q

L

I

S

D

V

G

T

S

V

C

N

R

G

R

L

F

G

G

E

A

R

G

A

A

G

G

N

N

A

A

A

P

L

V

E

E

E

A

V

L

A

I

A

G

A

V

L

F

E

D

A

K

A

I

G

G

R

V

A

K

T

T

G

G

V

I

A

D

L

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G

F

Q

D

L

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A

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E

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D

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V

A

V

R

R

active site: D13 (= D28), H16 (≠ Q31), H195 (= H208), H197 (= H210)
binding manganese (ii) ion: D13 (= D28), H195 (= H208), H197 (= H210)
binding oxalate ion: R12 (= R27), M136 (≠ V136), V164 (≠ S179), S166 (≠ T181), H195 (= H208), H197 (= H210)

Sites not aligning to the query:

active site: 286
binding oxalate ion: 286

Query Sequence

>WP_011841500.1 NCBI__GCF_000015985.1:WP_011841500.1
MSRQQPRASFLPESPLAPVALCDTTLRDGEQTAGVAFTRAEKRAIAEALQAAGVAEVEVG
VPAMGEEERADIRAVAAVLKTAAPVVWCRLRAEDLAAAQRTGVVRLHIGVPVSERQISAK
LGKDAAWVRDKVEKLVRAASWAGHKVSVGAEDASRADPFFLAEIAHVAAEAGAIRFRISD
TLGVLDPFAAHELVGRVVTRCPLPVEFHGHNDLGMATANSLAAARAGASHLSVTVNGLGE
RAGNAALEEVAAALEAAGRATGVALGQLCALSELVARASGRPLSPQKPIVGEGVFTHECG
IHVDGLMKDRATYESADLRPERFGRSHRIAIGKHSSAAGLARALAEAGLPADAATLAALM
PALRDWAATAKRAAAPEDLAALLAAQTETAR

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