SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_025274981.1 NCBI__GCF_000527155.1:WP_025274981.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

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

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

Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58) (see 2 papers)
28% identity, 95% coverage: 24:542/546 of query aligns to 9:500/517 of Q9JZG1

query
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Q9JZG1

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D16 (= D31) binding Mn(2+)
H204 (= H231) binding Mn(2+)
H206 (≠ Q233) binding Mn(2+)
N240 (= N267) 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)
29% identity, 67% coverage: 24:390/546 of query aligns to 24:370/399 of 6ktqA

query
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6ktqA

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binding 2-oxoglutaric acid: R30 (= R30), R154 (≠ F160), T156 (≠ D162), E158 (= E164), S184 (≠ V193), T188 (= T197), H216 (= H231), H218 (≠ Q233)
binding coenzyme a: V67 (≠ A67), R96 (≠ G99), A97 (≠ I100), F116 (≠ L119), H128 (≠ R131), E158 (= E164)
binding zinc ion: E31 (≠ D31), H216 (= H231), H218 (≠ Q233)

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
29% identity, 68% coverage: 24:395/546 of query aligns to 20:394/409 of 6e1jA

query
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I

Y

A

T

N

G

M

L

P

Y

P

V

N

Q

E

P

H

H

A

K

P

P

Y

I

V

V

G

G

H

A

A

N

A

C

F

F

A

V

H

H

K

E

A
x
S

G
|
G

L
x
I

H

H

A

Q

S
x
D

A

G

I

I

K

L

T
x
K

D

N

P

R

G

S

L

T

Y

Y

N

E

H

I

I

I

D

S

P

P

Q

E

V

D

V

V

G

G

-

V

-

K

-

S

N

Q

D

N

M

S

R

G

I

I

L

V

V

L

T

G

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K

M
x
L

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|
R

A
x
H

S

A

I

V

E

K

L

G

K

R

S

L

R

K

D

E

L

L

G

G

I

Y

E

E

L

I

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G

D

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E

K

K

D

-

V

-

L

L

D

N

R

E

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V

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F

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R

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F

K

R

D

D

L

L

E

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A

K

Q

Q

binding coenzyme a: Q30 (= Q34), F60 (≠ W64), S63 (≠ P69), I95 (= I100), R97 (≠ A102), F121 (≠ L121), K132 (≠ A133), L133 (= L134), S322 (≠ A325), G323 (= G326), I324 (≠ L327), D327 (≠ S330), K331 (≠ T334), L359 (≠ M358), R362 (= R361), H363 (≠ A362)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ C195), T194 (= T197), H225 (= H231), H227 (≠ Q233)
binding manganese (ii) ion: D27 (= D31), V82 (≠ M94), E84 (≠ R96), H225 (= H231), H227 (≠ Q233)

P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
29% identity, 70% coverage: 23:403/546 of query aligns to 86:469/503 of P0DO78

query
sites
P0DO78

H

R

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F

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D

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D

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A

-

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F

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F

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-

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A

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-

G

-

N

R

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A

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E

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I

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N

G

F

Y

K

I

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P

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-

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A

A

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Q

A

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I

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A

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E

-

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A

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T

S

S

D

D

I

I

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-

H

H

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H

Y

A

K

L

L

K

K

A

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T

P

K

A

E

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E

N

V

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I

E

E

M

M

I

A

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E

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-

E

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D

-

V

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Q

-

L

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C

C

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-

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-

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D

G

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F

G

R

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F

A

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S

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S

A

F

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K

A

A

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G

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A

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A

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N

L

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A

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A

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I

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V

G

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Y

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A

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T

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D

D

D

I

I

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|
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x
H

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N

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G

C

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A

A

V

T

A

A

N

N

T

T

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A

A

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V

E

C

S

A

G

G

V

A

M

R

H

Q

V

V

Q

E

G

V

T

T

A

V

N

N

G

G

Y

I

G

G

E

E

R

R

P

S

G

G

N

N

A

A

D

P

I

L

F

E

S

E

V

V

I

V

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M

G

A

L

L

Q

K

T

C

K

R

M

-

G

G

M

A

R

Y

V

V

L

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P

-

G

D

G

G

L

V

-

Y

-

T

-

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-

I

-

D

-

T

E

R

K

Q

M

I

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M

H

A

T

T

S

S

H

K

S

M

I

V

A

Q

A

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I

Y

A

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N

G

M

L

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P

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Q

E

P

H

H

A

K

P

P

Y

I

V

V

G

G

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A

A

N

A

C

F

F

A

V

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E

A

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H

A

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D

A

G

I

I

K

L

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K

D

N

P

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Y

Y

N

E

H

I

I

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D

S

P

P

Q

E

V

D

V

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G

G

-

V

-

K

-

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Q

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N

M

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G

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M

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A

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D

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D

R93 (= R30) mutation to A: Lost catalytic activity.
D94 (= D31) mutation to A: Lost catalytic activity.
H292 (= H231) mutation to A: Lost catalytic activity.
H294 (≠ Q233) mutation to A: Lost catalytic activity.
H392 (= H328) mutation to A: Lost catalytic activity.

Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 73% coverage: 24:421/546 of query aligns to 87:503/503 of Q9FN52

query
sites
Q9FN52

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A

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A

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A

A

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A

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|
G

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P

A

E

D

D

D

I

I

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F

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A

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I

H

H

A

C

Q

H

N

N

D

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C

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A

A

V

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A

A

N

N

T

T

L

I

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A

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G

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A

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A

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N

N

G

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I

G

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L

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-

G

-

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-

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M

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D

A

N

A

C

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F

A

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A

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N

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D

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A

E

D

A

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A

W

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A

G

A

A

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A

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E

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A

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V

G263 (= G199) 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)
27% identity, 72% coverage: 24:414/546 of query aligns to 87:480/506 of Q9FG67

query
sites
Q9FG67

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x
A

I

V

H

H

A

C

Q

H

N

N

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A

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N

N

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P

P

Q

E

V

D

V

I

G

G

-

I

-

V

-

K

-

S

N

Q

D

N

M

S

R

G

I

L

L

V

V

L

T

G

E

K

M

L

A

S

G

G

R

R

A

H

S

A

I

V

E

K

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K

R

S

L

R

K

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E

L

L

G

G

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Y

E

E

L

L

R

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G

D

Q

E

K

K

D

-

V

-

L

L

D

N

R

A

V

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T

F

K

S

R

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F

K

R

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D

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A

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F

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E

L

I

S102 (≠ R39) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ G229) 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)
26% identity, 93% coverage: 20:525/546 of query aligns to 6:491/516 of Q8F3Q1

query
sites
Q8F3Q1

T

T

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R

F

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E

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x
V

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-

K

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R16 (= R30) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 30:31) binding pyruvate
D17 (= D31) 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 (≠ V90) 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 (= F92) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ V122) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ D162) 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 (= E164) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T197) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H328) mutation H->A,N: Loss of activity.
D304 (≠ S330) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ P336) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ G337) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ L338) mutation to A: Loss of activity.
Y430 (≠ V466) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (≠ N467) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L489) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y492) 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 (= I496) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (= T503) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (≠ T507) 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.

Sites not aligning to the query:

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)
31% identity, 55% coverage: 24:324/546 of query aligns to 6:295/308 of 3rmjB

query
sites
3rmjB

I

I

F

F

D

D

T

T

L

L

R

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D
|
D

G

G

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Q
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Q

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x
H

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E

active site: Q16 (= Q34)
binding manganese (ii) ion: D13 (= D31), H201 (= H231), H203 (≠ Q233), N237 (= N267)

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 69% coverage: 21:396/546 of query aligns to 3:359/376 of O87198

query
sites
O87198

D

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G

S

G

V

F

I

L

G

A

G

R

L

M

Q

Y

T

T

K

L

M

Q

G

P

M

E

R

Y

V

V

L

R

P

R

P

K

G

Y

G

K

L

L

E

E

K

M

M

L

T

P

H

E

T

L

S

D

H

R

S

M

I

V

A

A

A

R

I

M

-

V

-

G

A

V

N

E

M

I

P

P

P

F

N

N

E

N

H

Y

A

I

P

-

Y

-

V

T

G

G

H

E

A

T

A

A

F

F

A

S

H

H

K

K

A

A

G

G

L

M

H

H

A

L

S

K

A

A

I

I

K

Y

T

I

D

N

P

P

G

E

L

A

Y

Y

N

E

H

P

I

Y

D

P

P

P

Q

E

V

V

V

F

G

G

N

V

D

K

M

R

R

K

I

L

L

I

V

I

-

A

T

S

E

R

M

L

A

T

G

G

R

R

A

H

S

A

I

I

E

K

L

A

K

R

S

A

R

E

D

E

L

L

G

G

I

L

E

H

L

Y

R

-

G

G

Q

E

K

E

D

E

V

-

L

L

D

H

R

R

V

V

T

T

K

Q

R

H

V

I

K

K

D

A

L

L

E

A

A

D

Q

R

G

G

R12 (= R30) binding 2-oxoglutarate
E13 (≠ D31) binding Mg(2+)
H72 (≠ F92) 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 (= D113) binding L-lysine
R133 (≠ F160) binding 2-oxoglutarate
S135 (≠ D162) binding L-lysine
T166 (= T197) binding 2-oxoglutarate; binding L-lysine
H195 (= H231) binding Mg(2+)
H197 (≠ Q233) binding Mg(2+)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
27% identity, 65% coverage: 19:375/546 of query aligns to 1:347/380 of 4ov9A

query
sites
4ov9A

P

P

T

K

D

T

F

I

H

H

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

A

N

Q
|
Q

M

A

E

L

G

K

L

R

R

P

Y

W

S

T

V

I

A

D

D

E

K

K

M

I

S

E

V

V

A

F

R

D

L

L

I

L

D

V

E

E

L

L

G

N

V

V

D

D

Y

G

I

I

E

E

G

V

G

G

W

F

P

P

G

S

A

S

L

-

P

-

S

N

D

E

T

T

E

E

F

F

F

H

-

T

-

C

-

Q

-

V

-

L

-

S

E

K

R

R

A

A

S

P

E

-

I

-

N

-

F

-

K

K

H

G

A

K

K

P

L

I

V

A

A

A

F
x
L

G

S

M

R

T

A

R

N

R

Q

A

N

G

E

I

I

A

A

A

V

A

T

D

W

D

E

E

-

G

-

L

-

G

-

A

A

L

I

I

Q

D

K

S

A

R

D

A

C

P

P

T

R

L

M

C

H

L

I

V

V

A

Y

K

P

S

V

D

S

I

D

R

F

H

S

V

I

R

K

H

H

A

V

L

L

K

K

A

I

S

S

P

E

A

K

E

E

N

V

L

L

E

Q

M

K

I

I

R

R

D

N

S

S

I

I

S

S

Y

F

G

A

R

R

E

S

Y

I

-

V

-

G

-

P

D

G

R

I

E

E

V

I

F

Q

I

F

D

S

C

G

E

E

H

H

F

F

F

G

D

D

G

A

F

I

R

E

H

N

S

F

P

A

D

-

Y

F

A

T

T

K

T

E

V

A

V

F

K

L

S

T

S

A

F

I

D

E

A

A

G

G

A

A

D

N

V

I

V

N

L

L

C

P

D

N

T
|
T

N

V

G

E

G

R

S

Y

I

R

P

P

S

M

D

V

I

F

A

V

R

N

I

M

I

V

G

K

D

E

L

I

R

K

S

-

R

-

L

-

A

-

D

D

T

V

M

V

R

K

P

D

E

K

D

A

I

I

R

-

L

I

G

S

I

I

H
|
H

A

T

Q
x
H

N

N

D

D

T

L

G

G

C

M

A

A

V

T

A

A

N

T

T

S

L

V

T

E

A

S

V

V

E

Y

S

V

G

G

V

A

M

E

H

Q

V

I

Q

E

G

V

T

A

A

L

N

N

G

G

Y

L

G

G

E

E

R

R

P

A

G

G

N

N

A

T

D

N

I

L

F

Y

-

E

S

T

V

A

I

I

G

A

G

L

L

H

Q

Q

T

N

K

G

M

E

G

N

M

L

R

N

V

I

L

-

P

-

G

-

G

N

L

F

E

Q

K

R

M

I

T

Y

H

P

T

T

S

A

H

K

S

R

I

I

A

S

A

E

I

L

A

T

N

G

M

I

P

P

P

I

N

G

E

E

H

K

A

T

P

P

Y

I

V

I

G

G

H

E

A

D

A

I

F

F

A

S

H

H

K

R

A

S

G

G

L

I

H

H

A

Q

S

T

A

-

I

L

K

H

T

Q

D

S

P

K

G

G

L

A

Y

Y

N

R

H

T

I

F

D

S

P

P

Q

E

V

F

V

V

G

G

-

R

-

M

N

D

D

K

M

E

R

T

I

I

L

S

V

F

T

T

E

N

M

Q

A

S

G

G

R

H

A

K

S

A

I

I

E

E

L

F

K

L

S

L

R

H

D

Q

L

R

G

G

I

I

E

Q

L

V

active site: Q16 (= Q34)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R30), L73 (≠ F92), T176 (= T197), H205 (= H231), H207 (≠ Q233)
binding zinc ion: D13 (= D31), H205 (= H231), H207 (≠ Q233)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
27% identity, 65% coverage: 19:375/546 of query aligns to 1:345/379 of 4ov4A

query
sites
4ov4A

P

P

T

K

D

T

F

I

H

H

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

A

N

Q
|
Q

M

A

E

L

G

K

L

R

R

P

Y

W

S

T

V

I

A

D

D

E

K

K

M

I

S

E

V

V

A

F

R

D

L

L

I

L

D

V

E

E

L

L

G

N

V

V

D

D

Y

G

I

I

E

E

G

V

G

G

W

F

P

P

G

S

A

S

L

-

P

-

S

N

D

E

T

T

E

E

F

F

F

H

-

T

-

C

-

Q

-

V

-

L

-

S

E

K

R

R

A

A

S

P

E

-

I

-

N

-

F

-

K

K

H

G

A

K

K

P

L

I

V

A

A

A

F

L

G

S

M

R

T

A

R

N

R

Q

A

N

G

E

I

I

A

A

A

V

A

T

D

W

D

E

E

-

G

-

L

-

G

-

A

A

L

I

I

Q

D

K

S

A

R

D

A

C

P

P

T

R

L

M

C

H

L

I

V

V

A

Y

K

P

S

V

D

S

I

D

R

F

H

S

V

I

R

K

H

H

A

V

L

L

K

K

A

I

S

S

P

E

A

K

E

E

N

V

L

L

E

Q

M

K

I

I

R

R

D

N

S

S

I

I

S

S

Y

F

G

A

R

R

E

S

Y

I

-

V

-

G

-

P

D

G

R

I

E

E

V

I

F

Q

I

F

D

S

C

G

E

E

H

H

F

F

F

G

D

D

G

A

F

I

R

E

H

N

S

F

P

A

D

-

Y

F

A

T

T

K

T

E

V

A

V

F

K

L

S

T

S

A

F

I

D

E

A

A

G

G

A

A

D

N

V

I

V

N

L

L

C
x
P

D

N

T
|
T

N

V

G

E

G

R

S

Y

I

R

P

P

S

M

D

V

I

F

A

V

R

N

I

M

I

V

G

K

D

E

L

I

R

K

S

-

R

-

L

-

A

-

D

D

T

V

M

V

R

K

P

D

E

K

D

A

I

I

R

-

L

I

G

S

I

I

H
|
H

A

T

Q
x
H

N

N

D

D

T

L

G

G

C

M

A

A

V

T

A

A

N

T

T

S

L

V

T

E

A

S

V

V

E

Y

S

V

G

G

V

A

M

E

H

Q

V

I

Q

E

G

V

T

A

A

L

N

N

G

G

Y

L

G

G

E

E

R

R

P

A

G

G

N

N

A

T

D

N

I

L

F

Y

-

E

S

T

V

A

I

I

G

A

G

L

L

H

Q

Q

T

N

K

G

M

E

G

N

M

L

R

N

V

I

L

-

P

-

G

-

G

N

L

F

E

Q

K

R

M

I

T

Y

H

P

T

T

S

A

H

K

S

R

I

I

A

S

A

E

I

L

A

T

N

G

M

I

P

P

P

I

N

G

E

E

H

K

A

T

P

P

Y

I

V

I

G

G

H

E

A

D

A

I

F

F

A

S

H

H

K

R

A

S

G

G

L

I

H

H

A

Q

S

H

A

Q

I

S

K

K

T

-

D

-

P

-

G

G

L

A

Y

Y

N

R

H

T

I

F

D

S

P

P

Q

E

V

F

V

V

G

G

-

R

-

M

N

D

D

K

M

E

R

T

I

I

L

S

V

F

T

T

E

N

M

Q

A

S

G

G

R

H

A

K

S

A

I

I

E

E

L

F

K

L

S

L

R

H

D

Q

L

R

G

G

I

I

E

Q

L

V

active site: Q16 (= Q34)
binding 3-methyl-2-oxobutanoic acid: R12 (= R30), P174 (≠ C195), T176 (= T197), H205 (= H231), H207 (≠ Q233)
binding zinc ion: D13 (= D31), H205 (= H231), H207 (≠ Q233)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
29% identity, 61% coverage: 21:355/546 of query aligns to 3:311/312 of 2ztjA

query
sites
2ztjA

D

E

F

W

H

K

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

M

F

E

E

G

K

L

A

R

N

Y

F

S

S

V

T

A

Q

D

D

K

K

M

V

S

E

V

I

A

A

R

K

L

A

I

L

D

D

E

E

L

F

G

G

V

I

D

E

Y

Y

I

I

E

E

G

V

G

T

W

T

P

P

G

V

A

A

L

S

P

P

S

Q

D

S

T

R

E

K

F

D

F

A

E

E

R

V

A

L

S

A

E

S

E

-

I

L

N

G

F

L

K

K

H

-

A

A

K

K

L

V

V

V

A

T

F
x
H

G

I

M

Q

T

C

R

R

R

L

A

D

G

A

I

A

A

K

A

V

A

A

D

V

D

E

E

T

G

G

L

V

G

Q

A

G

L

I

I

-

D

-

S

-

R

-

A

-

P

-

T

D

L

L

C
x
L

L

F

V

G

A

T

K

G

S

R

D

D

I

I

R

P

H

R

V

I

R

-

H

-

A

-

L

-

K

-

A

-

S

-

P

-

A

-

E

-

N

-

L

I

E

E

M

E

I

A

R

K

D

E

S

V

I

I

S

A

Y

Y

G

I

R

R

E

E

Y

A

-

A

-

P

D

H

R

V

E

E

V

V

F
x
R

I

F

D

S

C

A

E

E

H

-

F

-

D

D

G

T

F

F

R

R

H

-

S

S

P

E

D

E

Y

Q

A

D

T

L

V

A

V

V

K

Y

S

E

S

A

F

V

D

A

A

P

G

Y

A

V

D

D

V

R

V

V

V

G

L

L

C
x
A

D

D

T
|
T

N

V

G

G

G

V

S

A

I

T

P

P

S

R

D

Q

I

V

A

Y

R

A

I

L

I

V

G

R

D

E

L

V

R

R

S

R

R

V

L

V

A

G

D

P

T

R

M

V

R

-

P

-

E

-

D

D

I

I

R

E

L

F

G

-

I

-

H
|
H

A

G

Q
x
H

N

N

D

D

T

T

G

G

C

C

A

A

V

I

A

A

N

N

T

A

L

Y

T

E

A

A

V

I

E

E

S

A

G

G

V

A

M

T

H

H

V

V

Q

D

G

T

T

T

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

P

N

G

G

N

I

A

T

D

P

I

L

F

G

S

G

V

F

I

L

G

A

G

R

L

M

Q

Y

T

T

K

L

M

Q

G

P

M

E

R

Y

V

V

L

R

P

R

P

K

G

Y

G

K

L

L

E

E

K

M

M

L

T

P

H

E

T

L

S

D

H

R

S

M

I

V

A

A

A

R

I

M

-

V

-

G

A

V

N

E

M

I

P

P

P

F

N

N

E

N

H

Y

A

I

P

-

Y

-

V

T

G

G

H

E

A

T

A

A

F

F

A

S

H

H

K

K

A

A

G

G

L

M

H

H

A

L

S

K

A

A

I

I

K

Y

T

I

D

N

P

P

G

E

L

A

Y

Y

N

E

H

P

I

Y

D

P

P

P

Q

E

V

V

V

F

G

G

N

V

D

K

M

R

R

K

I

L

L

I

V

I

active site: Q16 (= Q34)
binding 2-oxoglutaric acid: R12 (= R30), H72 (≠ F92), L94 (≠ C120), R125 (≠ F160), A156 (≠ C195), T158 (= T197), H187 (= H231), H189 (≠ Q233)
binding copper (ii) ion: E13 (≠ D31), H187 (= H231), H189 (≠ Q233)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 61% coverage: 21:355/546 of query aligns to 3:313/314 of 2zyfA

query
sites
2zyfA

D

E

F

W

H

K

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

M

F

E

E

G

K

L

A

R

N

Y

F

S

S

V

T

A

Q

D

D

K

K

M

V

S

E

V

I

A

A

R

K

L

A

I

L

D

D

E

E

L

F

G

G

V

I

D

E

Y

Y

I

I

E

E

G

V

G

T

W

T

P

P

G

V

A

A

L

S

P

P

S

Q

D

S

T

R

E

K

F

D

F

A

E

E

R

V

A

L

S

A

E

S

E

-

I

L

N

G

F

L

K

K

H

-

A

A

K

K

L

V

V

V

A

T

F
x
H

G

I

M

Q

T

C

R

R

R

L

A

D

G

A

I

A

A

K

A

V

A

A

D

V

D

E

E

T

G

G

L

V

G

Q

A

G

L

-

I

I

D

D

S

-

R

-

A

-

P

-

T

-

L

-

C

L

L
|
L

V

F

A

G

K

T

S

S

D

K

I

G

R

R

H

D

V

I

R

P

H

R

A

I

L

I

K

E

A

E

S

A

P

-

A

-

E

-

N

-

L

-

E

-

M

-

I

-

R

K

D

E

S

V

I

I

S

A

Y

Y

G

I

R

R

E

E

Y

A

-

A

-

P

D

H

R

V

E

E

V

V

F
x
R

I

F

D

S

C

A

E

E

H

-

F

-

D

D

G

T

F

F

R

R

H

-

S

S

P

E

D

E

Y

Q

A

D

T

L

V

A

V

V

K

Y

S

E

S

A

F

V

D

A

A

P

G

Y

A

V

D

D

V

R

V

V

V

G

L

L

C

A

D

D

T
|
T

N

V

G

G

G

V

S

A

I

T

P

P

S

R

D

Q

I

V

A

Y

R

A

I

L

I

V

G

R

D

E

L

V

R

R

S

R

R

V

L

V

A

G

D

P

T

R

M

V

R

-

P

-

E

-

D

D

I

I

R

E

L

F

G

-

I

-

H
|
H

A

G

Q
x
H

N

N

D

D

T

T

G

G

C

C

A

A

V

I

A

A

N

N

T

A

L

Y

T

E

A

A

V

I

E

E

S

A

G

G

V

A

M

T

H

H

V

V

Q

D

G

T

T

T

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

P

N

G

G

N

I

A

T

D

P

I

L

F

G

S

G

V

F

I

L

G

A

G

R

L

M

Q

Y

T

T

K

L

M

Q

G

P

M

E

R

Y

V

V

L

R

P

R

P

K

G

Y

G

K

L

L

E

E

K

M

M

L

T

P

H

E

T

L

S

D

H

R

S

M

I

V

A

A

A

R

I

M

-

V

-

G

A

V

N

E

M

I

P

P

P

F

N

N

E

N

H

Y

A

I

P

-

Y

-

V

T

G

G

H

E

A

T

A

A

F

F

A

S

H

H

K

K

A

A

G

G

L

M

H

H

A

L

S

K

A

A

I

I

K

Y

T

I

D

N

P

P

G

E

L

A

Y

Y

N

E

H

P

I

Y

D

P

P

P

Q

E

V

V

V

F

G

G

N

V

D

K

M

R

R

K

I

L

L

I

V

I

active site: Q16 (= Q34)
binding 2-oxoglutaric acid: R12 (= R30), H72 (≠ F92), L94 (= L121), R127 (≠ F160), T160 (= T197), H189 (= H231)
binding magnesium ion: E13 (≠ D31), H189 (= H231), H191 (≠ Q233)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
30% identity, 60% coverage: 21:348/546 of query aligns to 2:305/347 of 3a9iA

query
sites
3a9iA

D

E

F

W

H

K

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q

Q

M

F

E

E

G

K

L

A

R

N

Y

F

S

S

V

T

A

Q

D

D

K

K

M

V

S

E

V

I

A

A

R

K

L

A

I

L

D

D

E

E

L

F

G

G

V

I

D

E

Y

Y

I

I

E

E

G

V

G

T

W

T

P

P

G

V

A

A

L

S

P

P

S

Q

D

S

T

R

E

K

F

D

F

A

E

E

R

V

A

L

S

A

E

S

E

-

I

L

N

G

F

L

K

K

H

-

A

A

K

K

L

V

V

V

A

T

F

H

G

I

M

Q

T

C

R

R

R

L

A

D

G

A

I

A

A

K

A

V

A

A

D

V

D

E

E

T

G

G

L

V

G

Q

A

G

L

-

I

I

D
|
D

S

L

R

L

A

F

P

G

T

T

L

S

C

K

L

Y

V

L

A

-

K

-

S

-

D

D

I

I

R

P

H

R

V

I

R

-

H

-

A

-

L

-

K

-

A

-

S

-

P

-

A

-

E

-

N

-

L

I

E

E

M

E

I

A

R

K

D

E

S

V

I

I

S

A

Y

Y

G

I

R

R

E

E

Y

A

-

A

-

P

D

H

R

V

E

E

V

V

F

R

I

F

D
x
S

C

A

E

E

H

-

F

-

D

D

G

T

F

F

R

R

H

-

S

S

P

E

D

E

Y

Q

A

D

T

L

V

A

V

V

K

Y

S

E

S

A

F

V

D

A

A

P

G

Y

A

V

D

D

V

R

V

V

V

G

L

L

C

A

D

D

T
|
T

N

V

G

G

G

V

S

A

I

T

P

P

S

R

D

Q

I

V

A

Y

R

A

I

L

I

V

G

R

D

E

L

V

R

R

S

R

R

V

L

V

A

G

D

P

T

R

M

V

R

-

P

-

E

-

D

D

I

I

R

E

L

F

G

-

I

-

H
|
H

A

G

Q
x
H

N

N

D

D

T

T

G

G

C

C

A

A

V

I

A

A

N

N

T

A

L

Y

T

E

A

A

V

I

E

E

S

A

G

G

V

A

M

T

H

H

V

V

Q

D

G

T

T

T

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

P

N

G

G

N

I

A

T

D

P

I

L

F

G

S

G

V

F

I

L

G

A

G

R

L

M

Q

Y

T

T

K

L

M

Q

G

P

M

E

R

Y

V

V

L

R

P

R

P

K

G

Y

G

K

L

L

E

E

K

M

M

L

T

P

H

E

T

L

S

D

H

R

S

M

I

V

A

A

A

R

I

M

-

V

-

G

A

V

N

E

M

I

P

P

P

F

N

N

E

N

H

Y

A

I

P

-

Y

-

V

T

G

G

H

E

A

T

A

A

F

F

A

S

H

H

K

K

A

A

G

G

L

M

H

H

A

L

S

K

A

A

I

I

K

Y

T

I

D

N

P

P

G

E

L

A

Y

Y

N

E

H

P

I

Y

D

P

P

P

Q

E

V

V

V

F

G

G

binding cobalt (ii) ion: E12 (≠ D31), H188 (= H231), H190 (≠ Q233)
binding lysine: R11 (= R30), D91 (= D113), S128 (≠ D162), T159 (= T197), H188 (= H231), H190 (≠ Q233)

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
25% identity, 57% coverage: 22:331/546 of query aligns to 2:299/311 of 3bliA

query
sites
3bliA

F

L

H

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

A

E

Q
|
Q

M

T

E

R

G

G

L

V

R

S

Y

F

S

S

V

T

A

S

D

E

K

K

M

L

S

N

V

I

A

A

R

K

-

F

L

L

I

L

D

Q

E

K

L

L

G

N

V

V

D

D

Y

R

I

V

E

E

G

I

G

A

W

S

-

A

-
x
R

-
x
V

-

S

P

K

G

G

A

E

L

L

P

E

S

T

D

V

T

Q

E

K

F

I

F

M

E

E

R

W

A

A

S

A

E

T

E

E

I

Q

N

L

F

T

K

E

H

R

A

I

K

E

L

I

V

L

A

G

F

F

G

-

M

-

T

-

R

-

A

-

G

-

I

-

A

-

A

V

A

D

D

G

D

N

E

K

G

T

L

V

G

D

A

W

L

I

I

K

D

D

S

S

R

G

A

A

P

K

T

V

L

L

C

N

L

L

V

L

A

T

K

K

S

G

D

S

I

L

R

H

H

H

V

L

R

E

H

K

A

Q

L

L

K

G

A

K

S

T

P

P

A

K

E

E

N

F

L

F

E

T

M

D

I

V

R

S

D

F

S

V

I

I

S

E

Y

Y

G

A

R

I

E

K

Y

S

D

G

R

L

E

K

V

I

F

N

I

V

D
x
Y

C

L

E
|
E

H

D

F

W

F

S

D

N

G

G

F

F

R

R

H

N

S

S

P

P

D

D

Y

Y

A

V

T

K

T

S

V

L

V

V

K

E

S

H

S

L

F

S

D

K

A

E

G

H

A

I

D

E

V

R

V

I

V

F

L

L

C
x
P

D

D

T
|
T

N

L

G

G

G

V

S

L

I

S

P

P

S

E

D

E

I

T

A

F

R

Q

I

G

I

V

G

D

D

S

L

L

R

-

S

-

R

-

L

-

A

-

D

-

T

I

M

Q

R

K

P

Y

E

P

D

D

I

I

R

H

L

F

G

E

I

F

H
|
H

A

G

Q
x
H

N

N

D

D

T

Y

G

D

C

L

A

S

V

V

A

A

N

N

T

S

L

L

T

Q

A

A

V

I

E

R

S

A

G

G

V

V

M

K

H

G

V

L

Q

H

G

A

T

S

A

I

N

N

G

G

Y

L

G

G

E

E

R

R

P

A

G

G

N

N

A

T

D

P

I

L

F

E

S

A

V

L

I

V

G

T

L

I

Q

H

T

D

K

K

M

S

G

N

M

S

R

K

V

T

L

-

P

-

G

-

G

N

L

I

E

N

K

E

-

I

-

A

M

I

T

T

H

E

T

A

S

S

H

R

S

L

I

V

A

E

A

V

I

F

A

S

N

G

M

K

P

R

P

I

N

S

E

A

H

N

A

R

P

P

Y

I

V

V

G

G

H

E

A

D

A

V

F

F

A

T

H

Q

K

T

A

A

G

G

L

V

H

N

A

L

S

Y

A

A

active site: Q14 (= Q34)
binding acetyl coenzyme *a: Q14 (= Q34), R47 (vs. gap), V48 (vs. gap), E140 (= E164)
binding pyruvic acid: R10 (= R30), Y138 (≠ D162), P171 (≠ C195), T173 (= T197)
binding zinc ion: D11 (= D31), H201 (= H231), H203 (≠ Q233)

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
24% identity, 70% coverage: 11:392/546 of query aligns to 19:379/400 of 3ivtB

query
sites
3ivtB

D

N

P

P

T

S

E

D

S

F

P

L

S

S

T

R

P

V

T

N

D

N

F

F

H

S

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

M

F

E

A

G

N

L

A

R

F

Y

F

S

D

V

T

A

E

D

K

K

K

M

I

S

Q

V

I

A

A

R

K

L

A

I

L

D

D

E

N

L

F

G

G

V

V

D

D

Y

Y

I

I

E

E

G

L

G

T

W

S

P

P

G

V

A

A

L

-

P

-

S

-

D

-

T

S

E

E

F

Q

F

S

E

R

R

Q

A

D

S

C

E

E

E

A

I

I

N

C

F

K

K

L

H

G

A

L

K

K

L

C

V

K

A

I

F

L

G

T

M
x
H

T

I

R

R

-

C

-

H

-

M

-

D

-

A

R

R

A

V

G

A

I

V

A

E

A

T

A

G

D

V

D

D

E

-

G

G

L

V

G

D

A

V

L

V

I

I

D

G

S

T

R

S

A

-

P

-

T

-

L

-

C

-

L

-

V

-

A

-

K

-

S

-

D

-

I

-

R

-

H

-

V

-

R

Q

H

Y

A

L

L

R

K

K

A

Y

S

S

P

H

A

G

E

K

N

D

L

M

E

T

M

Y

I

I

R

I

D

D

S

S

-

A

-

T

-

E

-

V

I

I

S

N

Y

F

G

V

R

K

E

S

Y

K

D

G

R

I

E

E

V

V

F
x
R

I

F

D
x
S

C

S

E

E

H

-

F

-

D

D

G

S

F

F

R

R

H

S

S

D

P

L

D

V

Y

D

A

L

T

L

T

S

V

L

V

Y

K

K

S

A

S

V

F

D

D

K

A

I

G

G

A

V

D

N

V

R

V

V

V

G

L

I

C

A

D

D

T
|
T

N

V

G

G

G

C

S

A

I

T

P

P

S

R

D

Q

I

V

A

Y

R

D

I

L

I

I

G

R

D

T

L

L

R

R

S

G

R

V

L

V

A

S

D

-

T

-

M

-

R

-

P

-

E

-

D

-

I

C

R

D

L

I

G

E

I

C

H
|
H

A

F

Q
x
H

N

N

D

D

T

T

G

G

C

M

A

A

V

I

A

A

N

N

T

A

L

Y

T

C

A

A

V

L

E

E

S

A

G

G

V

A

M

T

H

H

V

I

Q

D

G

T

T

S

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

P

N

G

G

N

I

A

T

D

P

I

L

F

G

S

A

V

L

I

L

G

A

G

R

L

M

Q

Y

T

V

K

T

M

D

G

R

M

E

R

Y

V

I

L

T

P

H

P

K

G

Y

G

K

L

L

E

N

K

Q

M

L

T

R

H

E

T

L

S

E

H

N

S

L

I

V

-

A

-

D

A

A

A

V

I

E

A

V

N

Q

M

I

P

P

P

F

N

N

E

N

H

Y

A

I

P

-

Y

-

V

T

G

G

H

M

A

C

A

A

F

F

A

T

H

H

K

K

A

A

G

G

L

I

H

H

A

A

S

K

A

A

I

I

K

L

T

A

D

N

P

P

G

S

L

T

Y

Y

N

E

H

I

I

L

D

K

P

P

Q

E

V

D

V

F

G

G

N

M

D

S

M

R

R

Y

I

V

L

H

V

V

-

G

T

S

E

R

M

L

A

T

G

G

R

W

A

N

S

A

I

I

E

K

L

S

K

R

S

A

R

E

D

Q

L

L

G

N

I

L

E

H

L

L

R

T

G

D

Q

A

K

Q

D

-

V

-

L

A

D

K

R

E

V

L

T

T

K

V

R

R

V

I

K

K

D

K

L

L

active site: Q42 (= Q34)
binding 2-oxoglutaric acid: R38 (= R30), H98 (≠ M94), R158 (≠ F160), S160 (≠ D162), T192 (= T197), H219 (= H231), H221 (≠ Q233)
binding zinc ion: E39 (≠ D31), H219 (= H231), H221 (≠ Q233)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
24% identity, 70% coverage: 11:392/546 of query aligns to 24:384/418 of Q9Y823

query
sites
Q9Y823

D

N

P

P

T

S

E

D

S

F

P

L

S

S

T

R

P

V

T

N

D

N

F

F

H

S

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

M

F

E

A

G

N

L

A

R

F

Y

F

S

D

V

T

A

E

D

K

K

K

M

I

S

Q

V

I

A

A

R

K

L

A

I

L

D

D

E

N

L

F

G

G

V

V

D

D

Y

Y

I

I

E
|
E

G

L

G

T

W

S

P

P

G

V

A

A

L

-

P

-

S

-

D

-

T

S

E

E

F

Q

F

S

E

R

R

Q

A

D

S

C

E

E

E

A

I

I

N

C

F

K

K

L

H

G

A

L

K

K

L

C

V

K

A

I

F

L

G

T

M
x
H

T

I

R

R

-

C

-

H

-

M

-

D

-

A

R

R

A

V

G

A

I

V

A

E

A

T

A

G

D

V

D

D

E

-

G

G

L

V

G
x
D

A

V

L

V

I

I

D

G

S

T

R

S

A

-

P

-

T

-

L

-

C

-

L

-

V

-

A

-

K

-

S

-

D

-

I

-

R

-

H

-

V

-

R

Q

H

Y

A

L

L

R

K

K

A

Y

S

S

P

H

A

G

E

K

N

D

L

M

E

T

M

Y

I

I

R

I

D

D

S

S

-

A

-

T

-

E

-

V

I

I

S

N

Y

F

G

V

R

K

E

S

Y

K

D

G

R

I

E

E

V

V

F
x
R

I

F

D
x
S

C

S

E
|
E

H

-

F

-

D

D

G

S

F

F

R

R

H

S

S

D

P

L

D

V

Y

D

A

L

T

L

T

S

V

L

V

Y

K

K

S

A

S

V

F

D

D

K

A

I

G

G

A

V

D

N

V

R

V

V

V

G

L

I

C

A

D

D

T
|
T

N

V

G

G

G

C

S

A

I

T

P

P

S

R

D

Q

I

V

A

Y

R

D

I

L

I

I

G

R

D

T

L

L

R

R

S

G

R

V

L

V

A

S

D

-

T

-

M

-

R

-

P

-

E

-

D

-

I

C

R

D

L

I

G
x
E

I

C

H
|
H

A

F

Q
x
H

N

N

D

D

T

T

G

G

C

M

A

A

V

I

A

A

N

N

T

A

L

Y

T

C

A

A

V

L

E

E

S

A

G

G

V

A

M

T

H

H

V

I

Q

D

G

T

T

S

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

P

N

G

G

N

I

A

T

D

P

I

L

F

G

S

A

V

L

I

L

G

A

G

R

L

M

Q

Y

T

V

K

T

M

D

G

R

M

E

R

Y

V

I

L

T

P

H

P

K

G

Y

G

K

L

L

E

N

K

Q

M

L

T
x
R

H

E

T

L

S

E

H

N

S

L

I

V

-

A

-

D

A

A

A

V

I

E

A

V

N

Q

M

I

P

P

P

F

N

N

E

N

H

Y

A

I

P

-

Y

-

V

T

G

G

H

M

A

C

A

A

F

F

A

T

H

H

K

K

A

A

G

G

L

I

H

H

A

A

S

K

A

A

I

I

K

L

T

A

D

N

P

P

G

S

L

T

Y
|
Y

N

E

H

I

I

L

D

K

P

P

Q

E

V

D

V

F

G

G

N

M

D

S

M

R

R

Y

I

V

L

H

V

V

-

G

T

S

E

R

M

L

A

T

G

G

R

W

A

N

S

A

I

I

E

K

L

S

K

R

S

A

R

E

D
x
Q

L

L

G

N

I

L

E

H

L

L

R

T

G

D

Q

A

K

Q

D

-

V

-

L

A

D

K

R

E

V

L

T

T

K

V

R

R

V

I

K

K

D

K

L

L

R43 (= R30) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D31) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q34) mutation to A: Abolishes the catalytic activity.
E74 (= E61) 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 (≠ M94) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ G109) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ F160) 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 (≠ D162) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E164) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T197) 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 (≠ G229) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H231) binding 2-oxoglutarate; binding Zn(2+)
H226 (≠ Q233) binding 2-oxoglutarate; binding Zn(2+)
R288 (≠ T295) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y339) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ D370) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
24% identity, 70% coverage: 11:392/546 of query aligns to 1:350/370 of 3mi3A

query
sites
3mi3A

D

N

P

P

T

S

E

D

S

F

P

L

S

S

T

R

P

V

T

N

D

N

F

F

H

S

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

M

F

E

A

G

N

L

A

R

F

Y

F

S

D

V

T

A

E

D

K

K

K

M

I

S

Q

V

I

A

A

R

K

L

A

I

L

D

D

E

N

L

F

G

G

V

V

D

D

Y

Y

I

I

E

E

G

L

G

T

W

S

P

P

G

-

A

-

L

-

P

-

S

-

D

-

T

-

E

-

F

-

E

-

R

V

A

A

S

S

E

E

E

Q

I

S

N

R

F

Q

K

D

H

C

A

E

K

A

L

I

V

C

A

K

F

L

G

G

M

L

T

K

R

C

R

K

-

I

-

L

A

T

G

H

I

I

A

R

A

C

A

H

D

M

D

D

E

-

G

-

L

-

G

-

A

-

L

-

I

-

D

D

S

A

R

R

A

V

P

A

T

V

L

E

C

T

L

G

V

V

A

D

K

G

S

V

D
|
D

I

V

R

-

H

-

V

-

R

-

H

-

A

V

L

I

K

G

A

T

S

S

P

M

A

T

E

Y

N

I

L

I

E

D

M

S

I

A

R

T

D

E

S

V

I

I

S

N

Y

F

G

V

R

K

E

S

Y

K

D

G

R

I

E

E

V

V

F

R

I

F

D

S

C

S

E

E

H

-

F

-

D

D

G

S

F

F

R

R

H

S

S

D

P

L

D

V

Y

D

A

L

T

L

T

S

V

L

V

Y

K

K

S

A

S

V

F

D

D

K

A

I

G

G

A

V

D

N

V

R

V

V

V

G

L

I

C

A

D

D

T
|
T

N

V

G

G

G

C

S

A

I

T

P

P

S

R

D

Q

I

V

A

Y

R

D

I

L

I

I

G

R

D

T

L

L

R

R

S

G

R

V

L

V

A

S

D

-

T

-

M

-

R

-

P

-

E

-

D

-

I

C

R

D

L

I

G

E

I

C

H
|
H

A

F

Q
x
H

N

N

D

D

T

T

G

G

C

M

A

A

V

I

A

A

N

N

T

A

L

Y

T

C

A

A

V

L

E

E

S

A

G

G

V

A

M

T

H

H

V

I

Q

D

G

T

T

S

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

P

N

G

G

N

I

A

T

D

P

I

L

F

G

S

A

V

L

I

L

G

A

G

R

L

M

Q

Y

T

V

K

T

M

D

G

R

M

E

R

Y

V

I

L

T

P

H

P

K

G

Y

G

K

L

L

E

N

K

Q

M

L

T

R

H

E

T

L

S

E

H

N

S

L

I

V

-

A

-

D

A

A

A

V

I

E

A

V

N

Q

M

I

P

P

P

F

N

N

E

N

H

Y

A

I

P

T

Y

-

V

-

G

G

H

M

A

C

A

A

F

F

A

T

H

H

K

K

A

A

G

G

L

I

H

H

A

A

S

K

A

A

I

I

K

L

T

A

D

N

P

P

G

S

L

T

Y

Y

N

E

H

I

I

L

D

K

P

P

Q

E

V

D

V

F

G

G

N

M

D

S

M

R

R

Y

I

V

L

H

V

V

-

G

T

S

E

R

M

L

A

T

G

G

R

W

A

N

S

A

I

I

E

K

L

S

K

R

S

A

R

E

D

Q

L

L

G

N

I

L

E

H

L

L

R

T

G

D

Q

A

K

Q

D

-

V

-

L

A

D

K

R

E

V

L

T

T

K

V

R

R

V

I

K

K

D

K

L

L

active site: Q24 (= Q34)
binding lysine: R20 (= R30), D100 (= D126), T163 (= T197), H190 (= H231), H192 (≠ Q233)
binding zinc ion: E21 (≠ D31), H190 (= H231), H192 (≠ Q233)

3ivsA Homocitrate synthase lys4 (see paper)
25% identity, 43% coverage: 168:403/546 of query aligns to 132:356/364 of 3ivsA

query
sites
3ivsA

D

D

G

S

F

F

R

R

H

S

S

D

P

L

D

V

Y

D

A

L

T

L

T

S

V

L

V

Y

K

K

S

A

S

V

F

D

D

K

A

I

G

G

A

V

D

N

V

R

V

V

V

G

L

I

C

A

D

D

T

T

N

V

G

G

G

C

S

A

I

T

P

P

S

R

D

Q

I

V

A

Y

R

D

I

L

I

I

G

R

D

T

L

L

R

R

S

G

R

V

L

V

A

S

D

-

T

-

M

-

R

-

P

-

E

-

D

-

I

C

R

D

L

I

G

E

I

C

H
|
H

A

F

Q
x
H

N

N

D

D

T

T

G

G

C

M

A

A

V

I

A

A

N

N

T

A

L

Y

T

C

A

A

V

L

E

E

S

A

G

G

V

A

M

T

H

H

V

I

Q

D

G

T

T

S

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

P

N

G

G

N

I

A

T

D

P

I

L

F

G

S

A

V

L

I

L

G

A

G

R

L

M

Q

Y

T

V

K

T

M

D

G

R

M

E

R

Y

V

I

L

T

P

H

P

K

G

Y

G

K

L

L

E

N

K

Q

M

L

T

R

H

E

T

L

S

E

H

N

S

L

I

V

-

A

-

D

A

A

A

V

I

E

A

V

N

Q

M

I

P

P

P

F

N

N

E

N

H

Y

A

I

P

T

Y

-

V

-

G

G

H

M

A

C

A

A

F

F

A

T

H

H

K

K

A

A

G

G

L

I

H

H

A

A

S

K

A

A

I

I

K

L

T

A

D

N

P

P

G

S

L

T

Y

Y

N

E

H

I

I

L

D

K

P

P

Q

E

V

D

V

F

G

G

N

M

D

S

M

R

R

Y

I

V

L

H

V

V

-

G

T

S

E

R

M

L

A

T

G

G

R

W

A

N

S

A

I

I

E

K

L

S

K

R

S

A

R

E

D

Q

L

L

G

N

I

L

E

H

L

L

R

Q

G

A

Q

K

K

E

D

-

V

-

L

-

D

-

R

-

V

L

T

T

K

V

R

R

V

I

K

K

D

K

L

L

E

A

A

V

Q

R

G

T

W

L

S

A

F

M

E

D

A

D

A

V

D

D

binding cobalt (ii) ion: H188 (= H231), H190 (≠ Q233)

Sites not aligning to the query:

active site: 24
binding cobalt (ii) ion: 21

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)
25% identity, 68% coverage: 24:394/546 of query aligns to 13:342/347 of Q53WI0

query
sites
Q53WI0

I

V

F

V

D

D

T

T

L

L

R

R

D

D

G

G

A

S

Q

H

M

A

E

H

G

R

L

H

R

Q

Y

Y

S

T

V

V

A

E

D

E

K

A

M

R

S

A

V

I

A

A

R

Q

L

A

I

L

D

D

E

E

L

A

G

G

V

V

D

Y

Y

A

I

I

E

E

G

V

G

S

W

H

P

G

G

D

A

G

L

L

P

G

-

G

S

S

D

S

T

L

E

Q

F

Y

F

G

E

F

R

S

A

R

S

T

E

D

E

E

I

M

N

E

F

L

K

I

H

R

A

A

K

-

L

-

V

-

A

V

F

R

G

E

M

T

T

V

R

R

A

A

G

K

I

V

A

A

A

L

D

L

E

P

G

G

L

I

G

G

A

T

L

R

I

K

D

E

S

L

R

K

A

E

P

A

T

V

L

-

C

-

L

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V

-

A

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K

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S

A

D

G

I

I

R

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H

M

V

V

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R

H

I

A

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L

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Q

A

C

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A

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D

N

I

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-

I

-

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F

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G

Y

M

G

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K

E

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L

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V

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-

V

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G

F

F

I

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C

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G

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G

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A

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G

L

L

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H

H

A

A

S

K

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I

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K

G

T

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D

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L

G

G

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-

Y

-

N

-

H

-

I

V

D

D

P

P

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A

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G

-

N

-

D

-

M

-

R

-

I

-

L

-

V

L

T

L

E

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M

L

A

G

G

R

R

R

A

Q

S

A

I

V

E
x
A

L

-

K

-

S

-

R

-

D

-

L

-

G

-

I

-

E

-

L

-

R

-

G

G

Q

Q

K

E

D

D

V

W

L

I

D

L

R

R

V

V

T

A

K

L

R

E

V

L

K

K

D

E

L

K

E

E

A

A

A324 (≠ E365) mutation to G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.

Query Sequence

>WP_025274981.1 NCBI__GCF_000527155.1:WP_025274981.1
MRYSHDTNDTDPTESPSTPTDFHIFDTTLRDGAQMEGLRYSVADKMSVARLIDELGVDYI
EGGWPGALPSDTEFFERASEEINFKHAKLVAFGMTRRAGIAAADDEGLGALIDSRAPTLC
LVAKSDIRHVRHALKASPAENLEMIRDSISYGREYDREVFIDCEHFFDGFRHSPDYATTV
VKSSFDAGADVVVLCDTNGGSIPSDIARIIGDLRSRLADTMRPEDIRLGIHAQNDTGCAV
ANTLTAVESGVMHVQGTANGYGERPGNADIFSVIGGLQTKMGMRVLPPGGLEKMTHTSHS
IAAIANMPPNEHAPYVGHAAFAHKAGLHASAIKTDPGLYNHIDPQVVGNDMRILVTEMAG
RASIELKSRDLGIELRGQKDVLDRVTKRVKDLEAQGWSFEAADASFELLLDDELPQANRV
VRPFTVASYRVIIDHTRDGSVVCEATVRLEVDGEQTITTAQARGPVNALDAALRQALAER
FPGLSEINLSDYKVRILAGTSGTEAITRVLTTLSDGDDEWTTVGVDDNIVEASWRALIDA
LTYRLR

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