SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013134754.1 NCBI__GCF_000092245.1:WP_013134754.1 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)

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)
31% identity, 83% coverage: 9:276/322 of query aligns to 5:272/347 of Q53WI0

query
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Q53WI0

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Sites not aligning to the query:

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

4lrsA Crystal and solution structures of the bifunctional enzyme (aldolase/aldehyde dehydrogenase) from thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and coa accommodation whithin the shared cofactor-binding site
25% identity, 83% coverage: 15:282/322 of query aligns to 4:272/337 of 4lrsA

query
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4lrsA

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active site: D13 (= D24), H16 (≠ L27), H195 (= H209), H197 (= H211)
binding magnesium ion: D13 (= D24), H195 (= H209), H197 (= H211)
binding pyruvic acid: R12 (= R23), D13 (= D24), F134 (≠ N147), M136 (= M149), V164 (≠ A177), S166 (= S179), H195 (= H209), H197 (= H211)

Sites not aligning to the query:

active site: 286
binding pyruvic acid: 286

4jn6C Crystal structure of the aldolase-dehydrogenase complex from mycobacterium tuberculosis hrv37 (see paper)
24% identity, 77% coverage: 14:261/322 of query aligns to 3:247/339 of 4jn6C

query
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4jn6C

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active site: D13 (= D24), H16 (≠ L27), H195 (= H209), H197 (= H211)
binding manganese (ii) ion: D13 (= D24), H195 (= H209), H197 (= H211)
binding oxalate ion: R12 (= R23), M136 (= M149), V164 (≠ A177), S166 (= S179), H195 (= H209), H197 (= H211)

Sites not aligning to the query:

active site: 286
binding oxalate ion: 286

P9WMK5 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxopentanoate aldolase; 4-hydroxy-2-oxovalerate aldolase; HOA; EC 4.1.3.43; EC 4.1.3.39 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
24% identity, 77% coverage: 14:261/322 of query aligns to 6:250/346 of P9WMK5

query
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P9WMK5

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D16 (= D24) binding Mn(2+)
H198 (= H209) binding Mn(2+)
H200 (= H211) binding Mn(2+)

Sites not aligning to the query:

322 G→F: Abolishes substrate channeling to HsaG.

8ih7A Amng-amnh complex
25% identity, 85% coverage: 6:279/322 of query aligns to 1:275/340 of 8ih7A

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M
|
M

A

M

I

S

S

H

K

M

S

Q

F

T

D

P

D

V

E

G

L

L

N

A

E

Q

V

Q

L

A

E

K

Q

L

L

M

S

E

K

N

T

Y

N

G

V

A

D

Q

I

C

I

I

Y

Y

I

V

A

V

D

D

S
|
S

F

G

G

G

S

A

F

M

Y

N

P

M

E

W

Q

D

I

I

N

A

-

E

-

R

-

F

K

K

L

A

T

L

E

K

K

D

Y

V

L

L

S

D

Y

P

A

A

E

T

K

Q

T

T

G

G

K

-

I

-

G

-

I

M

H
|
H

A

A

H
|
H

N

H

N

N

L

L

Q

S

L

L

A

G

Y

V

A

A

N

N

T

S

I

L

E

V

A

A

M

L

M

E

Y

N

G

G

A

C

S

D

F

R

L

V

D

D

V

A

T

S

I

L

S

T

G

G

L

M

G

G

R

A

G

G

A

A

G

G

N

N

C

A

P

P

L

L

E

E

L

V

L

F

I

I

G

A

F

A

L

A

K

E

-

R

-

M

-

G

-

L

N

N

P

H

K

G

Y

C

K

D

L

V

M

K

P

K

V

L

L

I

K

N

F

A

I

A

E

E

E

D

Y

I

I

V

V

R

P

P

L

L

E

Q

K

E

E

R

binding oxalate ion: R18 (= R23), D19 (= D24), M142 (= M149), S172 (= S179), H201 (= H209), H203 (= H211)
binding zinc ion: D19 (= D24), H201 (= H209), H203 (= H211)

Sites not aligning to the query:

binding oxalate ion: 292

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
31% identity, 37% coverage: 133:252/322 of query aligns to 124:244/311 of 3bliA

query
sites
3bliA

L

V

I

I

E

E

E

Y

A

A

H

I

A

K

K

S

G

G

Y

L

E

K

T

I

T

N

V

V

N
x
Y

I

L

M
x
E

A

D

I

W

S

S

K

N

S

G

F

F

D

R

-

N

-

S

-

P

D

D

E

Y

L

V

N

K

E

S

V

L

L

V

E

E

Q

H

L

L

S

S

K

K

T

E

N

H

V

I

D

E

I

R

I

I

Y

F

I

L

A
x
P

D

D

S
x
T

F

L

G

G

S

V

F

L

Y

S

P

P

E

E

Q

E

-

T

-

F

-

Q

-

G

I

V

N

D

K

S

L

L

T

I

E

Q

K

K

Y

Y

L

P

S

D

Y

I

A

-

E

-

K

-

T

-

G

-

K

-

K

H

I

F

G

E

I

F

H
|
H

A

G

H
|
H

N

N

N

D

L

Y

Q

D

L

L

A

S

Y

V

A

A

N

N

T

S

I

L

E

Q

A

A

M

I

M

R

Y

A

G

G

A

V

S

K

F

G

L

L

D

H

V

A

T

S

I

I

S

N

G

G

L

L

G

G

R

E

G

R

A

A

G

G

N

N

C

T

P

P

L

L

E

E

L

A

L

L

I

V

binding acetyl coenzyme *a: E140 (≠ M149)
binding pyruvic acid: Y138 (≠ N147), P171 (≠ A177), T173 (≠ S179)
binding zinc ion: H201 (= H209), H203 (= H211)

Sites not aligning to the query:

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, 37% coverage: 133:252/322 of query aligns to 130:250/516 of Q8F3Q1

query
sites
Q8F3Q1

L

V

I

I

E

E

E

Y

A

A

H

I

A

K

K

S

G

G

Y

L

E

K

T

I

T

N

V

V

N
x
Y

I

L

M
x
E

A

D

I

W

S

S

K

N

S

G

F

F

D

R

-

N

-

S

-

P

D

D

E

Y

L

V

N

K

E

S

V

L

L

V

E

E

Q

H

L

L

S

S

K

K

T

E

N

H

V

I

D

E

I

R

I

I

Y

F

I

L

A

P

D

D

S
x
T

F

L

G

G

S

V

F

L

Y

S

P

P

E

E

Q

E

-

T

-

F

-

Q

-

G

I

V

N

D

K

S

L

L

T

I

E

Q

K

K

Y

Y

L

P

S

D

Y

I

A

-

E

-

K

-

T

-

G

-

K

-

K

H

I

F

G

E

I

F

H

H

A

G

H

H

N

N

N

D

L

Y

Q

D

L

L

A

S

Y

V

A

A

N

N

T

S

I

L

E

Q

A

A

M

I

M

R

Y

A

G

G

A

V

S

K

F

G

L

L

D

H

V

A

T

S

I

I

S

N

G

G

L

L

G

G

R

E

G

R

A

A

G

G

N

N

C

T

P

P

L

L

E

E

L

A

L

L

I

V

Y144 (≠ N147) 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 (≠ M149) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (≠ S179) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.

Sites not aligning to the query:

16 mutation R->K,Q: Loss of activity.
16:17 binding pyruvate
17 D→A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat.; D→N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat.
81 L→A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat.; L→V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat.
83 F→A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
104 L→V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
302 mutation H->A,N: Loss of activity.
304 D→A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
310 N→A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
311 L→A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
312 Y→A: Loss of activity.
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.

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
26% identity, 77% coverage: 10:256/322 of query aligns to 17:263/399 of 6ktqA

query
sites
6ktqA

S

S

V

L

R

H

E

M

D

K

I

V

K

G

V

I

F

L

D

D

C

S

T

T

I

L

R
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R

D
x
E

G

G

G

E

L

Q

V

T

N

P

N

G

Y

V

H

V

F

F

T

T

D

T

E

D

F

Q

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R

K

V

A

E

H

I

Y

A

E

K

T

A

C

L

V

S

A

D

A

I

G

G

V

V

D

Q

Y

M

M

I

E

E

I

A

G

G

K

H

N

-

S

-

P

P

S

A

I
x
V

M

-

S

S

E

P

D

D

E

I

Y

Y

G

-

A

-

W

-

N

-

F

-

C

-

K

-

E

-

E

E

D

G

I

I

R

R

I

I

V

I

G

K

E

L

N

K

N

R

T

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G

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K

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I

K

A

S

V

E

M

I

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D

A

I

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R
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R

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x
A

V

V

P

K

S

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E

D

L

I

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E

P

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K

G

S

A

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E

S

I

V

E

V

A

D

D

M

R

I

I

R

A

I

I

-
x
F

-

Y

-

G

-

I

-

S

-

D

-

T

-

H

-

L

-

K

A

A

T

K

Y
x
H

I

H

H

T

Q

T

L

R

P

D

A

E

A

A

I

L

E

R

L

S

I

I

E

A

E

E

-

T

-

V

A

S

H

Y

A

A

K

K

G

S

Y

H

E

G

T

V

T

K

V

V

N
x
R

I

F

M
x
T

A

A

I
x
E

S

D

K

A

S

T

F

R

D

A

D

D

E

Y

-

Q

-

Y

L

L

N

L

E

E

V

V

L

I

E

K

Q

T

L

V

S

R

K

D

T

A

N

G

V

A

D

D

I

R

I

V

Y
x
S

I

I

A

A

D

D

S
x
T

F

V

G

G

S

V

F

L

Y

Y

P

P

E

S

Q

R

I

T

N

R

K

E

L

L

T

F

E

K

K

D

Y

L

L

T

S

S

Y

R

A

F

E

P

K

D

T

I

G

-

K

-

K

E

I

F

G

D

I

I

H
|
H

A

A

H
|
H

N

N

N

D

L

L

Q

G

L

M

A

A

Y

V

A

A

N

N

T

V

I

L

E

A

A

A

M

A

M

E

Y

G

G

G

A

A

S

T

F

I

L

I

D

H

V

T

T

T

I

L

S

N

G

G

L

L

G

G

R

E

G

R

A

V

G

G

N

I

C

A

P

P

L

L

E

Q

L

V

I

A

G

A

F

A

L

L

K

K

binding 2-oxoglutaric acid: R30 (= R23), R154 (≠ N147), T156 (≠ M149), E158 (≠ I151), S184 (≠ Y175), T188 (≠ S179), H216 (= H209), H218 (= H211)
binding coenzyme a: V67 (≠ I63), R96 (= R101), A97 (≠ T102), F116 (vs. gap), H128 (≠ Y123), E158 (≠ I151)
binding zinc ion: E31 (≠ D24), H216 (= H209), H218 (= H211)

P51016 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39 from Pseudomonas sp. (strain CF600) (see 2 papers)
26% identity, 81% coverage: 17:277/322 of query aligns to 11:272/345 of P51016

query
sites
P51016

V

I

F

S

D

D

C

V

T

T

I

L

R

R

D
|
D

G

G

G

S

L

H

V

A

N

I

N

R

Y

H

H

Q

F

Y

T

T

D

L

E

D

F

D

V

V

K

R

A

A

H

I

Y

A

E

R

T

A

C

L

V

D

A

K

A

A

G

K

V

V

D

D

Y

S

M

I

E

E

I

V

G

A

K

H

N

G

N

D

S

G

P

L

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Q

I

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M

G

S

S

E

S

D

F

E

N

Y

Y

G

G

A

F

W

G

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R

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H

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T

K

D

E

L

E

E

D

Y

I

I

R

E

R

A

I

V

V

A

G

G

E

E

N

I

N

S

T

H

G

A

M

-

K

Q

I

I

A

A

V

T

M

L

S

L

D

L

I

P

G

G

R

I

T

G

V

S

P

V

S

H

E

D

L

L

L

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K

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S

A

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G

V

A

D

R

M

V

I

V

R

R

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V

A

A

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H

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L

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P

D

A

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A

S

I

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L

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I

E

E

E

Y

A

A

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A

N

K

L

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M

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D

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V

V

G

N

F

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M

A

M

I

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H

K

M

S

I

F

P

D

A

D

E

E

K

L

L

N

A

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E

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Q

L

G

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K

Q

L

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M

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E

K

S

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Y

N

G

V

A

D

T

I

C

I

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Y

Y

I

M

A

A

D

D

S

S

F

G

G

G

S

A

F

M

Y

-

P

-

E

-

Q

S

I

M

N

N

K

D

L

I

T

R

E

D

K

R

Y

M

L

R

S

A

Y

F

A

K

E

A

-

V

-

L

K

K

T

P

G

E

K

T

K

Q

I

V

G

G

I

M

H
|
H

A

A

H
|
H

N

H

N

N

L

L

Q

S

L

L

A

G

Y

V

A

A

N

N

T

S

I

I

E

V

A

A

M

V

M

E

Y

E

G

G

A

C

S

D

F

R

L

V

D

D

V

A

T

S

I

L

S

A

G

G

L

M

G

G

R

A

G

G

A

A

G

G

N

N

C

A

P

P

L

L

E

E

L

V

L

F

I

I

G

A

F

V

L

A

K

E

-

R

-

L

-

G

-

W

N

N

P

H

K

G

Y

T

K

D

L

L

M

Y

P

T

V

L

L

M

K

D

F

A

I

A

E

D

Y

I

I

V

V

R

P

P

L

L

E

Q

D18 (= D24) binding Mn(2+)
H200 (= H209) binding Mn(2+)
H202 (= H211) binding Mn(2+)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1nvmA Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate (see paper)
26% identity, 81% coverage: 17:277/322 of query aligns to 10:271/340 of 1nvmA

query
sites
1nvmA

V

I

F

S

D

D

C

V

T

T

I

L

R
|
R

D
|
D

G

G

G

S

L
x
H

V

A

N

I

N

R

Y

H

H

Q

F

Y

T

T

D

L

E

D

F

D

V

V

K

R

A

A

H

I

Y

A

E

R

T

A

C

L

V

D

A

K

A

A

G

K

V

V

D

D

Y

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M

I

E

E

I

V

G

A

K

H

N

G

N

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S

G

P

L

S

Q

I

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M

G

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S

E

S

D

F

E

N

Y

Y

G

G

A

F

W

G

N

R

F

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C

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K

D

E

L

E

E

D

Y

I

I

R

E

R

A

I

V

V

A

G

G

E

E

N

I

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Q

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A

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M

L

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L

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G

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H

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L

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A

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Q

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A

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V

A

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M

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I

V

R

R

I

V

A

A

T

T

Y

H

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A

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Y

A

A

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A

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K

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x
F

I

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M
|
M

A

M

I

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S

H

K

M

S

I

F

P

D

A

D

E

E

K

L

L

N

A

E

E

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Q

L

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K

Q

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Y

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Y

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A

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S

F

G

G

G

S

A

F

M

Y

-

P

-

E

-

Q

S

I

M

N

N

K

D

L

I

T

R

E

D

K

R

Y

M

L

R

S

A

Y

F

A

K

E

A

-

V

-

L

K

K

T

P

G

E

K

T

K

Q

I

V

G

G

I

M

H
|
H

A

A

H
|
H

N

H

N

N

L

L

Q

S

L

L

A

G

Y

V

A

A

N

N

T

S

I

I

E

V

A

A

M

V

M

E

Y

E

G

G

A

C

S

D

F

R

L

V

D

D

V

A

T

S

I

L

S

A

G

G

L

M

G

G

R

A

G

G

A

A

G

G

N

N

C

A

P

P

L

L

E

E

L

V

L

F

I

I

G

A

F

V

L

A

K

E

-

R

-

L

-

G

-

W

N

N

P

H

K

G

Y

T

K

D

L

L

M

Y

P

T

V

L

L

M

K

D

F

A

I

A

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D

Y

I

I

V

V

R

P

P

L

L

E

Q

active site: D17 (= D24), H20 (≠ L27), H199 (= H209), H201 (= H211)
binding manganese (ii) ion: D17 (= D24), H199 (= H209), H201 (= H211)
binding oxalate ion: R16 (= R23), F138 (≠ N147), M140 (= M149), S170 (= S179), H199 (= H209), H201 (= H211)

Sites not aligning to the query:

active site: 290
binding oxalate ion: 290

P51015 4-hydroxy-2-oxovalerate aldolase 4; HOA 4; 4-hydroxy-2-keto-pentanoic acid aldolase 4; 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-oxopentanoate aldolase 4; EC 4.1.3.39; EC 4.1.3.43 from Paraburkholderia xenovorans (strain LB400) (see 3 papers)
27% identity, 74% coverage: 15:252/322 of query aligns to 8:242/346 of P51015

query
sites
P51015

I

V

K

T

V

V

F

H

D

D

C

M

T

T

I

L

R
|
R

D

D

G

G

G

M

L
x
H

V

P

N

K

N

R

Y

H

H

Q

F

M

T

T

D

L

E

E

F

Q

V

M

K

K

A

S

H

I

Y

A

E

C

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G

C

L

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D

A

A

G

G

V

I

D

P

Y

L

M

I

E

E

I

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G

T

K

H

N

G

N

D

S

G

P

L

S

G

I

G

M

S

S

S

E

V

D

N

E

-

Y

-

G

-

A

-

W

Y

N

G

F

F

C

P

K

A

E

H

E

S

D

D

I

-

R

-

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-

G

-

E

E

N

E

N

Y

T

L

G

G

M

A

K

V

I

I

A

P

V

L

M

M

S

K

D

Q

I

-

G

-

R

A

T

K

V

V

P

S

S

A

E
x
L

L

L

L
|
L

P

P

K

G

S

I

E

G

S

T

V

V

-

E

-

H

-

L

-

K

-

M

-

A

-

K

-

D

-

L

-

G

V

V

D

N

M

T

I

I

R

R

I

V

A

A

T

T

Y

H

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A

P

D

A

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A

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I

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Q

L

H

I

I

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E

Q

A

S

H

R

A

K

K

L

G

G

Y

L

E

D

T

T

T

V

V

G

N

F

I

L

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M

A

M

I

A

S

H

K

M

S

A

F

S

D

P

D

E

E

K

L

L

N

V

E

S

V

Q

L

A

E

L

Q

L

L

M

S

Q

K

G

T

Y

N

G

V

A

D

N

I

C

I

I

Y

Y

I

V

A

T

D

D

S

S

F

A

G

G

S

Y

F

M

Y

L

P

P

E

D

Q

D

I

V

N

-

K

K

L

A

T

R

E

L

K

S

Y

A

L

V

S

R

Y

A

A

A

E

L

K

K

T

P

G

E

K

T

K

E

I

L

G

G

I

F

H

H

A

G

H

H

N

H

N

N

L

L

Q

A

L

M

A

G

Y

V

A

A

N

N

T

S

I

I

E

A

A

A

M

I

M

E

Y

A

G

G

A

A

S

T

F

R

L

I

D

D

V

A

T

A

I

A

S

A

G

G

L

L

G

G

R

A

G

G

A

A

G

G

N

N

C

T

P

P

L

M

E

E

L

V

L

F

I

I

R16 (= R23) mutation to A: Loss of aldol cleavage activity.; mutation to K: 4000-fold decrease in the catalytic efficiency of the aldol cleavage reaction.
H20 (≠ L27) mutation H->A,S: 100-fold decrease in the catalytic efficiency of the aldol cleavage reaction. Dramatic reduction in acetaldehyde and propanaldehyde channeling efficiency by more than 70%.
L87 (≠ E106) mutation to A: 32-fold reduction in the catalytic efficiency with acetaldehyde as substrate of the aldol addition reaction, but no change in the catalytic efficiency using propanaldehyde; thus, exhibits a 40-fold preference for propanaldehyde over acetaldehyde.; mutation L->N,W: Loss of aldolase activity (with either enantiomer of HOPA), but retains some decarboxylase activity for the smaller oxaloacetate substrate. In the retro-aldol cleavage reaction, is inactive toward 4(S)-HOPA but is active toward 4(R)-HOPA, albeit with a great reduction in catalytic efficiency, and in the aldol addition reaction, produces also exclusively the 4(R)-enantiomer; when associated with F-290.
L89 (= L108) mutation to A: As the wild-type enzyme, exhibits similar catalytic efficiency with acetaldehyde or propanaldehyde as substrate in the aldol addition reaction but displays higher catalytic efficiency with longer aldehydes (50-fold increase using pentaldehyde). Shows a reduction in aldehyde channeling efficiency by 30%.

Sites not aligning to the query:

290 Y→F: Loss of stereochemical control as the mutant is able to catalyze the aldol cleavage of substrates with both R and S configurations at C4 with similar kinetic parameters. 3.5-fold decrease in the catalytic efficiency of the aldol cleavage reaction. Reduction in aldehyde channeling efficiency by more than 30%. In the retro-aldol cleavage reaction, is inactive toward 4(S)-HOPA but is active toward 4(R)-HOPA, albeit with a great reduction in catalytic efficiency, and in the aldol addition reaction, produces also exclusively the 4(R)-enantiomer; when associated with N-87 or W-87.; Y→S: Loss of stereochemical control as the mutant is able to catalyze the aldol cleavage of substrates with both R and S configurations at C4 with similar kinetic parameters. 3.5-fold decrease in the catalytic efficiency of the aldol cleavage reaction.
322 G→A: Displays a reduction in aldehyde channeling efficiency of about 20%.; mutation G->F,L: Unable to channel either acetaldehyde or propanaldehyde.
323 G→A: Able to channel butyraldehyde (with less efficiency than wild-type) but not its isomer isobutyraldehyde.; G→F: Unable to channel either acetaldehyde or propanaldehyde.; G→L: Able to channel acetaldehyde but not the larger propanaldehyde.

P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
27% identity, 75% coverage: 15:256/322 of query aligns to 85:339/503 of P0DO78

query
sites
P0DO78

I

V

K

R

V

V

F

F

D

D

C

T

T

T

I

L

R
|
R

D
|
D

G

G

G

E

L

Q

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A

N

P

N

G

Y

G

H

A

F

L

T

T

D

P

E

P

F

Q

V

K

K

L

A

E

H

I

Y

A

E

R

T

K

C

L

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A

A

K

A

L

G

R

V

V

D

D

Y

V

M

M

E

E

I

V

G

G

K

F

N

P

N

G

S

S

P

-

S

-

I

-

M

-

S

S

E

E

D

E

E

E

Y

-

G

-

A

-

W

-

N

-

F

F

C

E

K

T

E

V

E

K

D

T

I

I

R

A

R

K

I

T

V

V

G

G

-

N

-

E

-

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E

D

N

E

T

T

G

G

M

Y

K

-

I

I

A

P

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V

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C

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A

I

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A

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R

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S

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S

R

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L

I

L

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P

A

K

A

S

W

E

E

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A

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V

V

K

D

Y

M

A

I

K

R

R

I

P

A

K

T

I

Y

L

I

I

H

F

Q

T

L

S

P

T

A

S

A

D

I

I

-

H

-

M

-

K

-

Y

-

K

-

L

-

K

-

T

-

K

-

E

E

E

L

V

I

I

E

E

E

M

A

A

H

T

A

S

K

S

-

I

G

R

Y

F

E

A

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S

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N

G

I

F

M

I

A

D

I

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Q

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S

G

F

C

D

E

D

D

E

G

-

G

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R

-

S

-

E

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K

-

E

-

F

L

L

N

C

E

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I

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Q

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A

S

I

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A

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A

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T

I

A

I

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Y

N

I

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A

A

D

D

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F

V

G

G

S

I

F

N

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M

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P

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E

Q

E

I

Y

N

G

K

E

L

L

T

V

E

-

K

R

Y

Y

L

L

S

K

Y

A

A

N

E

T

K

P

T

G

G

I

K

D

I

I

-

V

-

F

G

S

I

V

H
|
H

A

C

H
|
H

N

N

N

D

L

L

Q

G

L

V

A

A

Y

T

A

A

N

N

T

T

I

I

E

A

A

G

M

V

M

C

Y

A

G

G

A

A

S

R

F

Q

L

V

D

E

V

V

T

T

I

V

S

N

G

G

L

I

G

G

R

E

G

R

A

S

G

G

N

N

C

A

P

P

L

L

E

E

L

E

L

V

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V

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M

F

A

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L

K

K

R93 (= R23) mutation to A: Lost catalytic activity.
D94 (= D24) mutation to A: Lost catalytic activity.
H292 (= H209) mutation to A: Lost catalytic activity.
H294 (= H211) mutation to A: Lost catalytic activity.

Sites not aligning to the query:

392 H→A: Lost catalytic activity.

Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 33% coverage: 157:263/322 of query aligns to 239:346/503 of Q9FN52

query
sites
Q9FN52

D

D

E

F

L

I

N

C

E

K

V

I

L

L

E

G

Q

E

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S

S

I

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K

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A

N

G

V

A

D

T

I

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I

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Y

G

I

F

A

A

D

D

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F

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G

S

I

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Y

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Q

E

I

F

N

G

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E

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L

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A

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A

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T

A

G

D

K

D

K

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G

A

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I

H

H

A

C

H

H

N

N

N

D

L

L

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G

L

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A

A

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T

A

A

N

N

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A

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M

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M

C

Y

A

G

G

A

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V

T

T

I

I

S

N

G

G

L

I

G

G

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G

R

A

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G

G

N

N

C

A

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P

L

L

E

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L

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L

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I

V

G

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A

L

L

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K

N

C

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R

K

G

Y

E

K

S

L

L

M

M

G263 (= G181) 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)
32% identity, 37% coverage: 153:272/322 of query aligns to 235:368/506 of Q9FG67

query
sites
Q9FG67

K

R

S

S

F

D

D

K

D

D

E

F

L

L

N

C

E

K

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I

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L

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A

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I

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L

L

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V

E

-

K

T

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Y

L

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Y

-

A

A

E

N

K

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G

G

K

I

K

D

-

D

-

V

I

V

G
x
A

I

V

H

H

A

C

H

H

N

N

N

D

L

L

Q

G

L

L

A

A

Y

T

A

A

N

N

T

S

I

I

E

A

A

G

M

I

M

R

Y

A

G

G

A

A

S

R

F

Q

L

V

D

E

V

V

T

T

I

I

S

N

G

G

L

I

G

G

R

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G

R

A

S

G

G

N

N

C

A

P

S

L

L

E

E

L

E

L

V

I

V

G

M

F

A

L

L

K

K

-

C

-

R

-

G

-

A

-

Y

-

V

-

I

N

N

P

G

K

V

Y

Y

-

T

-

K

-

I

-

D

-

T

-

R

K

Q

L

I

M

M

P

A

V

T

L

S

K

K

F

M

I

V

E

Q

E

E

Y

Y

A290 (≠ G207) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

Sites not aligning to the query:

102 S→F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
25% identity, 75% coverage: 17:256/322 of query aligns to 6:248/308 of 3rmjB

query
sites
3rmjB

V

I

F

F

D

D

C

T

T

T

I

L

R

R

D
|
D

G

G

G

E

L
x
Q

V

S

N

P

N

G

Y

A

H

A

F

M

T

T

D

K

E

E

F

E

V

K

K

I

A

R

H

V

Y

A

E

R

T

Q

C

L

V

E

A

K

A

L

G

G

V

V

D

D

Y

I

M

I

E

E

I

A

G

G

K

F

N

-

S

-

P

-

S

A

I

A

M

A

S

S

E

P

D

G

E

D

Y

F

G

E

A

A

W

V

N

N

F

A

C

I

K

A

E

-

D

-

I

-

R

K

R

T

I

I

V

T

G

K

E

S

N

T

N

V

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G

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K

S

I

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A

A

V

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M

E

S

R

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D

I

I

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Q

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S

E

E

A

L

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L

A

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K

A

S

P

E

K

S

K

V

-

D

-

M

-

I

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R

R

I

I

A

H

T

T

Y

F

I

I

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A

Q

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P

P

A

I

A

H

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E

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E

L

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K

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I

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T

A

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A

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I

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A

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F

Y

D

T

D

D

E

D

L

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N

E

E

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C

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E

Q

D

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A

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S

N

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I

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D

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F

-

L

-

A

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E

-

I

-

C

-

G

-

A

-

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-

I

-

E

-

A

-

G

-

A

-

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I

I

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N

I

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G

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Y

F

S

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Y

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N

E

K

E

L

F

T

F

E

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K

E

Y

L

L

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A

Y

K

A

T

E

P

K

N

T

G

G

G

K

K

K

V

I

V

-

W

G

S

I

A

H
|
H

A

C

H
|
H

N

N

N

D

L

L

Q

G

L

L

A

A

Y

V

A

A

N

N

T

S

I

L

E

A

A

A

M

L

M

K

Y

G

G

G

A

A

S

R

F

Q

L

V

D

E

V

C

T

T

I

V

S

N

G

G

L

L

G

G

R

E

G

R

A

A

G

G

N
|
N

C

A

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S

L

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E

E

L

E

L

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F

A

L

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K

K

active site: Q16 (≠ L27)
binding manganese (ii) ion: D13 (= D24), H201 (= H209), H203 (= H211), N237 (= N245)

3ivsA Homocitrate synthase lys4 (see paper)
25% identity, 76% coverage: 9:253/322 of query aligns to 6:232/364 of 3ivsA

query
sites
3ivsA

L

L

S

S

V

R

R

V

E

N

D

N

I

F

K

S

V

I

F

I

D

E

C

S

T

T

I

L

R

R

D
x
E

G

G

G

E

L
x
Q

V

F

N

A

N

N

Y

A

H

F

F

F

T

D

D

T

E

E

F

K

V

K

K

I

A

Q

H

I

Y

A

E

K

T

A

C

L

V

D

A

N

A

F

G

G

V

V

D

D

Y

Y

M

I

E

E

I

L

G

-

K

-

N

-

N

T

S

S

P

P

S

V

I

A

M

S

S

E

E

Q

D

S

E

R

Y

Q

G

D

A

C

W

E

N

A

F

I

C

C

K

K

E

-

D

-

I

-

R

-

I

-

V

-

G

-

E

-

N

-

T

L

G

G

M

L

K

K

I

C

A

K

V

I

M

L

S

T

D

H

I

I

G

R

R

C

T

H

V

M

P

D

S

D

E

A

L

R

L

V

P

A

K

V

S

E

E

T

S

G

V

V

-

D

-

G

V

V

D

D

M

V

I

V

R

I

I

G

A

T

T

T

Y

Y

I

I

H

-

Q

-

L

I

P

D

A

S

A

A

I

T

E

E

L

V

I

I

E

N

E

F

A

V

H

K

A

S

K

K

G

G

Y

I

E

E

T

V

T

R

V

-

N

-

I

-

M

F

A

S

I

S

S

E

K

D

S

S

F

F

D

R

D

S

E

D

L

L

N

V

E

D

V

L

L

L

-

S

-

L

-

Y

E

K

Q

A

L

V

S

D

K

K

T

I

N

G

V

V

D

N

I

R

I

V

Y

G

I

I

A

A

D

D

S

T

F

V

G

G

S

C

F

A

Y

T

P

P

E

R

Q

Q

I

V

N

Y

K

D

L

L

T

I

E

R

K

T

Y

L

L

R

S

G

Y

V

A

-

E

-

K

-

T

V

G

S

K

C

K

D

I

I

G

E

I

C

H
|
H

A

F

H
|
H

N

N

N

D

L

T

Q

G

L

M

A

A

Y

I

A

A

N

N

T

A

I

Y

E

C

A

A

M

L

M

E

Y

A

G

G

A

A

S

T

F

H

L

I

D

D

V

T

T

S

I

I

S

L

G

G

L

I

G

G

R

E

G

R

A

N

G

G

N

I

C

T

P

P

L

L

E

G

L

A

L

L

I

L

G

A

active site: Q24 (≠ L27)
binding cobalt (ii) ion: E21 (≠ D24), H188 (= H209), H190 (= H211)

Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58) (see 2 papers)
25% identity, 75% coverage: 17:256/322 of query aligns to 9:251/517 of Q9JZG1

query
sites
Q9JZG1

V

I

F

F

D

D

C

T

T

T

I

L

R

R

D
|
D

G

G

G

E

L

Q

V

S

N

P

N

G

Y

A

H

A

F

M

T

T

D

K

E

E

F

E

V

K

K

I

A

R

H

V

Y

A

E

R

T

Q

C

L

V

E

A

K

A

L

G

G

V

V

D

D

Y

I

M

I

E

E

I

A

G

G

K

F

N

-

S

-

P

-

S

A

I

A

M

A

S

S

E

P

D

G

E

D

Y

F

G

E

A

A

W

V

N

N

F

A

C

I

K

A

E

K

E

T

D

I

I

T

R

K

R

S

I

T

V

V

G

-

E

-

N

-

T

C

G

S

M

L

K

S

I

R

A

A

V

I

M

E

S

R

D

D

I

I

G

-

R

R

T

Q

V

A

P

G

S

E

E

A

L

V

L

A

P

P

K

A

S

P

E

K

S

K

V

-

D

-

M

-

I

-

R

R

I

I

A

H

T

T

Y

F

I

I

H

A

Q

T

L

S

P

P

A

I

A

H

I

M

E

E

L

Y

I

K

E

L

E

K

A

M

H

K

A

P

K

K

G

Q

Y

V

-

I

E

E

T

A

V

V

N

K

I

A

M

V

A

K

I

I

S

A

K

R

S

E

F

Y

D

T

D

D

E

D

L

V

N

E

E

F

V

S

L

C

E

E

Q

D

L

A

S

L

K

R

T

S

N

E

V

I

D

D

I

F

-

L

-

A

-

E

-

I

-

C

-

G

-

A

-

V

-

I

-

E

-

A

-

G

-

A

-

T

I

I

Y

N

I

I

A

P

D

D

S

T

F

V

G

G

S

Y

F

S

Y

I

P

P

E

Y

Q

K

I

T

N

E

K

E

L

F

T

F

E

R

K

E

Y

L

L

I

S

A

Y

K

A

T

E

P

K

N

T

G

G

G

K

K

K

V

I

V

-

W

G

S

I

A

H
|
H

A

C

H
|
H

N

N

N

D

L

L

Q

G

L

L

A

A

Y

V

A

A

N

N

T

S

I

L

E

A

A

A

M

L

M

K

Y

G

G

G

A

A

S

R

F

Q

L

V

D

E

V

C

T

T

I

V

S

N

G

G

L

L

G

G

R

E

G

R

A

A

G

G

N
|
N

C

A

P

S

L

V

E

E

L

E

L

I

I

V

G

M

F

A

L

L

K

K

D16 (= D24) binding Mn(2+)
H204 (= H209) binding Mn(2+)
H206 (= H211) binding Mn(2+)
N240 (= N245) 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)
27% identity, 75% coverage: 15:256/322 of query aligns to 18:272/409 of 6e1jA

query
sites
6e1jA

I

V

K

R

V

V

F

F

D

D

C

T

T

T

I

L

R

R

D
|
D

G

G

G

E

L
x
Q

V

S

N

P

N

G

Y

A

H

A

F

L

T

T

D

P

E

P

F

Q

V

K

K

I

A

E

H

I

Y

A

E

R

T

Q

C

L

V

A

A

K

A

L

G

R

V

V

D

D

Y

I

M

M

E

E

I

V

G

G

K
x
F

N

-

S

-

P

-

S

P

I

V

M
x
S

S

S

E

E

D

E

E

E

Y

F

G

E

A

T

W

I

N

-

F

-

C

-

K

-

E

-

E

Q

D

T

I

I

R

A

R

K

I

T

V

V

G

G

-

N

-

E

-
x
V

E

D

N
x
E

N

E

T

T

G

G

M

Y

K

-

I

I

A

P

V

V

M

I

S

C

D

V

I
|
I

G

A

R
|
R

T

S

V

K

P

E

S

R

E

D

L

I

L

K

P

A

K

A

S

W

E

E

S

S

V

V

V

K

D

Y

M

A

I

K

R

R

I

P

A

R

T

I

Y

V

I

I

H
x
F

Q

T

L

S

P

T

A

S

A

D

I

I

E

H

L

L

-

K

-

Y

-
x
K

-
x
L

-

K

-

M

-

T

-

R

-

E

-

V

-

D

-

M

-

V

-

A

-

S

I

I

E

R

E

F

A

A

H

K

A

S

K

L

G

G

Y

F

E

E

T

D

T

I

-

E

V

F

N

G

I

C

M

E

A

D

I

G

S

G

K

R

S

S

F

D

D

K

D

D

E

Y

L

I

N

C

E

T

V

V

L

F

E

E

Q

E

L

A

S

I

K

K

T

A

N

G

V

A

D

T

I

T

I

L

Y

A

I

C

A
x
P

D

D

S
x
T

F

V

G

G

S

I

F

N

Y

M

P

P

E

H

Q

E

I

Y

N

G

K

K

L

L

T

V

E

-

K

R

Y

Y

L

I

S

K

Y

-

A

A

E

N

K

T

T

P

G

G

K

I

K

D

-

D

-

V

-

I

I

F

G

S

I

A

H
|
H

A

C

H
|
H

N

N

N

D

L

L

Q

G

L

V

A

A

Y

T

A

A

N

N

T

T

I

I

E

A

A

G

M

I

M

C

Y

A

G

G

A

A

S

R

F

Q

L

V

D

E

V

V

T

T

I

I

S

N

G

G

L

I

G

G

R

E

G

R

A

S

G

G

N

N

C

A

P

P

L

L

E

E

L

E

L

V

I

V

G

M

F

A

L

L

K

K

binding coenzyme a: Q30 (≠ L27), F60 (≠ K57), S63 (≠ M64), I95 (= I99), R97 (= R101), F121 (≠ H125), K132 (vs. gap), L133 (vs. gap)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ A177), T194 (≠ S179), H225 (= H209), H227 (= H211)
binding manganese (ii) ion: D27 (= D24), V82 (vs. gap), E84 (≠ N87), H225 (= H209), H227 (= H211)

Sites not aligning to the query:

binding coenzyme a: 322, 323, 324, 327, 331, 359, 362, 363

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
25% identity, 76% coverage: 9:253/322 of query aligns to 6:234/370 of 3mi3A

query
sites
3mi3A

L

L

S

S

V

R

R

V

E

N

D

N

I

F

K

S

V

I

F

I

D

E

C

S

T

T

I

L

R
|
R

D
x
E

G

G

G

E

L
x
Q

V

F

N

A

N

N

Y

A

H

F

F

F

T

D

D

T

E

E

F

K

V

K

K

I

A

Q

H

I

Y

A

E

K

T

A

C

L

V

D

A

N

A

F

G

G

V

V

D

D

Y

Y

M

I

E

E

I

L

G

-

K

-

N

-

N

T

S

S

P

P

S

V

I

A

M

S

S

E

E

Q

D

S

E

R

Y

Q

G

D

A

C

W

E

N

A

F

I

C

C

K

K

E

-

D

-

I

-

R

-

I

-

V

-

G

-

E

-

N

-

T

L

G

G

M

L

K

K

I

C

A

K

V

I

M

L

S

T

D

H

I

I

G

-

R

R

T

C

V

H

P

M

S

D

E

D

L

A

L

R

P

V

K

A

S

V

E

E

S

T

V

G

V

V

D

D

M

G

I

V

R
x
D

I

V

A

V

-

I

-

G

-

T

-

S

-

M

T

T

Y

Y

I

I

H

-

Q

-

L

I

P

D

A

S

A

A

I

T

E

E

L

V

I

I

E

N

E

F

A

V

H

K

A

S

K

K

G

G

Y

I

E

E

T

V

T

R

V

-

N

-

I

-

M

F

A

S

I

S

S

E

K

D

S

S

F

F

D

R

D

S

E

D

L

L

N

V

E

D

V

L

L

L

-

S

-

L

-

Y

E

K

Q

A

L

V

S

D

K

K

T

I

N

G

V

V

D

N

I

R

I

V

Y

G

I

I

A

A

D

D

S
x
T

F

V

G

G

S

C

F

A

Y

T

P

P

E

R

Q

Q

I

V

N

Y

K

D

L

L

T

I

E

R

K

T

Y

L

L

R

S

G

Y

V

A

-

E

-

K

-

T

V

G

S

K

C

K

D

I

I

G

E

I

C

H
|
H

A

F

H
|
H

N

N

N

D

L

T

Q

G

L

M

A

A

Y

I

A

A

N

N

T

A

I

Y

E

C

A

A

M

L

M

E

Y

A

G

G

A

A

S

T

F

H

L

I

D

D

V

T

T

S

I

I

S

L

G

G

L

I

G

G

R

E

G

R

A

N

G

G

N

I

C

T

P

P

L

L

E

G

L

A

L

L

I

L

G

A

active site: Q24 (≠ L27)
binding lysine: R20 (= R23), D100 (≠ R119), T163 (≠ S179), H190 (= H209), H192 (= H211)
binding zinc ion: E21 (≠ D24), H190 (= H209), H192 (= H211)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
27% identity, 89% coverage: 16:302/322 of query aligns to 4:284/347 of 3a9iA

query
sites
3a9iA

K

K

V

I

F

I

D

D

C

S

T

T

I

L

R
|
R

D
x
E

G

G

G

E

L

Q

V

F

N

E

N

K

Y

A

H

N

F

F

T

S

D

T

-

Q

-

D

-

K

-

V

E

E

F

I

V

A

K

K

A

A

H

L

Y

D

E

E

T

F

C

-

V

-

A

-

G

G

V

I

D

E

Y

Y

M

I

E

E

I

V

G

T

K

T

N

P

-

V

N

A

S

S

P

P

S

Q

I

S

M

R

S

K

E

D

D

A

E

E

Y

V

G

L

A

A

W

S

N

L

F

G

C

L

K

K

E

A

E

K

D

V

I

V

R

T

R

H

I

I

V

Q

G

C

E

R

N

L

N

D

T

A

G

A

M

-

K

K

I

V

A

A

V

V

M

E

S

T

D

G

I

V

G

Q

R

G

T

I

V

-

P

-

S

-

E
x
D

L

L

P

F

K

G

S

T

E

S

S

K

V

Y

V

L

D

D

M

I

I

P

R

R

I

I

A

-

T

-

Y

-

I

I

H

E

Q

E

L

A

P

K

A

E

A

V

I

I

E

A

L

Y

I

I

E

R

E

E

A

A

H

-

A

A

K

P

G

H

Y

V

E

E

T

V

T

R

V

F

N
x
S

I

A

M

E

A

D

I

T

S

F

K

R

S

S

F

E

D

E

D

Q

E

D

L

L

N

L

E

A

V

V

L

Y

E

E

Q

A

L

V

S

A

K

P

T

-

N

Y

V

V

D

D

I

R

I

V

Y

G

I

L

A

A

D

D

S
x
T

F

V

G

G

S

V

F

A

Y

T

P

P

E

R

Q

Q

I

V

N

Y

K

A

L

L

T

V

E

R

K

E

Y

V

L

R

S

R

Y

V

A

-

E

-

K

-

T

V

G

G

K

P

K

R

I

V

G

D

I

I

-

E

-

F

H
|
H

A

G

H
|
H

N

N

N

D

L

T

Q

G

L

C

A

A

Y

I

A

A

N

N

T

A

I

Y

E

E

A

A

M

I

M

E

Y

A

G

G

A

A

S

T

F

H

L

V

D

D

V

T

T

T

I

I

S

L

G

G

L

I

G

G

R

E

G

R

A

N

G

G

N

I

C

T

P

P

L

L

E

G

L

-

I

-

G

G

F

F

L

L

K

A

N

R

P

-

K

M

Y

Y

K

T

L

L

M

Q

P

P

V

-

L

-

K

E

F

Y

I

V

-

R

E

R

E

K

Y

Y

I

K

V

L

P

E

L

M

E

L

K

P

E

E

L

L

D

D

W

R

-

M

-

V

-

A

-

R

-

M

-

V

G

G

Y

V

S

E

I

I

P

P

Y

F

-

N

M

Y

L

I

T

T

G

G

Q

E

L

T

N

A

E

F

H

S

P

H

R

K

A

A

A

G

M

M

binding cobalt (ii) ion: E12 (≠ D24), H188 (= H209), H190 (= H211)
binding lysine: R11 (= R23), D91 (≠ E106), S128 (≠ N147), T159 (≠ S179), H188 (= H209), H190 (= H211)

Query Sequence

>WP_013134754.1 NCBI__GCF_000092245.1:WP_013134754.1
MIEKKGSILSVREDIKVFDCTIRDGGLVNNYHFTDEFVKAHYETCVAAGVDYMEIGKNNS
PSIMSEDEYGAWNFCKEEDIRRIVGENNTGMKIAVMSDIGRTVPSELLPKSESVVDMIRI
ATYIHQLPAAIELIEEAHAKGYETTVNIMAISKSFDDELNEVLEQLSKTNVDIIYIADSF
GSFYPEQINKLTEKYLSYAEKTGKKIGIHAHNNLQLAYANTIEAMMYGASFLDVTISGLG
RGAGNCPLELLIGFLKNPKYKLMPVLKFIEEYIVPLEKELDWGYSIPYMLTGQLNEHPRA
AMKARDEGDTKYREFYRNLLAE

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