SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_034273566.1 NCBI__GCF_000504245.1:WP_034273566.1 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, 83% coverage: 17:467/544 of query aligns to 9:439/517 of Q9JZG1

query
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Q9JZG1

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D16 (= D24) binding Mn(2+)
H204 (= H218) binding Mn(2+)
H206 (≠ Q220) binding Mn(2+)
N240 (= N254) binding Mn(2+)

Sites not aligning to the query:

366:517 Required for the condensation reaction. Not required to bind substrate

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 66% coverage: 6:362/544 of query aligns to 76:443/506 of Q9FG67

query
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Q9FG67

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S102 (= S32) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ G216) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 68% coverage: 15:383/544 of query aligns to 4:359/376 of O87198

query
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O87198

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R12 (= R23) binding 2-oxoglutarate
E13 (≠ D24) binding Mg(2+)
H72 (≠ A85) 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 (≠ A104) binding L-lysine
R133 (≠ F154) binding 2-oxoglutarate
S135 (≠ D156) binding L-lysine
T166 (= T191) binding 2-oxoglutarate; binding L-lysine
H195 (= H218) binding Mg(2+)
H197 (≠ Q220) binding Mg(2+)

P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
26% identity, 74% coverage: 6:408/544 of query aligns to 76:485/503 of P0DO78

query
sites
P0DO78

P

P

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L

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P

L

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A

R93 (= R23) mutation to A: Lost catalytic activity.
D94 (= D24) mutation to A: Lost catalytic activity.
H292 (= H218) mutation to A: Lost catalytic activity.
H294 (≠ Q220) mutation to A: Lost catalytic activity.
H392 (= H315) mutation to A: Lost catalytic activity.

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
26% identity, 66% coverage: 6:365/544 of query aligns to 9:379/409 of 6e1jA

query
sites
6e1jA

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binding coenzyme a: Q30 (= Q27), F60 (≠ W57), S63 (≠ P62), I95 (≠ T89), R97 (≠ K91), F121 (≠ V116), K132 (≠ A127), L133 (= L128), S322 (≠ A312), G323 (= G313), I324 (≠ L314), D327 (≠ S317), K331 (≠ V321), L359 (≠ M345), R362 (= R348), H363 (≠ A349)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ C189), T194 (= T191), H225 (= H218), H227 (≠ Q220)
binding manganese (ii) ion: D27 (= D24), V82 (≠ L76), E84 (≠ L78), H225 (= H218), H227 (≠ Q220)

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
27% identity, 67% coverage: 17:378/544 of query aligns to 24:371/399 of 6ktqA

query
sites
6ktqA

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binding 2-oxoglutaric acid: R30 (= R23), R154 (≠ F154), T156 (≠ D156), E158 (= E158), S184 (≠ V187), T188 (= T191), H216 (= H218), H218 (≠ Q220)
binding coenzyme a: V67 (≠ A60), R96 (≠ T94), A97 (≠ T95), F116 (≠ L115), H128 (≠ L128), E158 (= E158)
binding zinc ion: E31 (≠ D24), H216 (= H218), H218 (≠ Q220)

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: 6:403/544 of query aligns to 76:492/503 of Q9FN52

query
sites
Q9FN52

P

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-

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-

A

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A

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A

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N

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N

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A

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P

P

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D

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G

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I

-

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N

M

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G

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V

L

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G

E

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M

L

A

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G

G

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R

A

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S

A

L

V

E

K

L

D

K

R

G

L

R

K

E

E

L

L

G

G

V

Y

-

E

-

I

-

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-

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-

E

-

K

-

F

-

N

D

D

L

I

A

F

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Y

T

R

A

E

L

L

T

T

N

K

V

D

V

K

E

K

K

R

V

I

K

T

A

D

L

A

E

D

A

L

K

K

G

A

W

L

S

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F

V

E

N

A

G

A

A

D

E

A

I

S

S

L

S

E

E

L

K

L

L

L

N

R

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K

A

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M

I

D

N

D

D

G263 (= G193) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic 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: 15:520/544 of query aligns to 8:492/516 of Q8F3Q1

query
sites
Q8F3Q1

F

L

H

E

V

I

Y

L

D

D

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D

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N

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G

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A

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A

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A

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Q

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I

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x
L

A

G

L
x
F

L

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D

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N

N

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-

T

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A

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L

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x
L

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x
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x
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x
D

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K

A

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|
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P

G

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|
T

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A

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-
x
V

-

E

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R

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L

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H

R16 (= R23) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 23:24) binding pyruvate
D17 (= D24) 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 (≠ R103) 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 (≠ L105) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ V116) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ D156) 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 (= E158) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T191) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H315) mutation H->A,N: Loss of activity.
D304 (≠ S317) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ P323) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (= L324) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ L325) mutation to A: Loss of activity.
Y430 (≠ V460) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (≠ H461) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L483) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y486) 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 (= I490) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (= T497) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (vs. gap) 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.

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
30% identity, 60% coverage: 15:342/544 of query aligns to 4:313/314 of 2zyfA

query
sites
2zyfA

F

W

H

K

V

I

Y

I

D

D

T

S

T

T

L

L

R
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R

D
x
E

G

G

A

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Q

R

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E

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D

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A

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P

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A

A

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P

P

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Q

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K

D

D

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A

E

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F

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A

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R

-

A

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L

L

A

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L

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A

A

K

A

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A
x
H

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A

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R

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A

A

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A

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A

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A

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V

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R

-

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L
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x
R

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A

A

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A

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A

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D

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H

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A

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R

A

N

G

G

N

I

A

T

D

P

L

L

F

G

A

G

V

F

I

L

G

A

N

R

L

M

V

Y

T

T

-

L

-

Q

-

P

-

E

-

Y

-

V

-

R

K

K

L

Y

D

K

M

L

D

E

V

M

L

L

P

P

T

-

G

-

A

-

E

E

L

L

T

D

R

R

V

M

S

-

H

-

A

-

L

V

A

A

E

R

I

M

A

V

N

G

I

V

A

E

P

I

D

P

T

F

H

N

Q

N

A

Y

Y

I

V

T

G

G

A

E

S

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

V

I

D

N

P

P

L

E

L

A

Y

Y

N

E

H

P

I

Y

D

P

P

P

P

E

V

V

V

F

G

G

N

V

D

K

M

R

R

K

V

L

L

I

V

I

active site: Q16 (= Q27)
binding 2-oxoglutaric acid: R12 (= R23), H72 (≠ A85), L94 (= L115), R127 (≠ F154), T160 (= T191), H189 (= H218)
binding magnesium ion: E13 (≠ D24), H189 (= H218), H191 (≠ Q220)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
30% identity, 60% coverage: 15:342/544 of query aligns to 4:311/312 of 2ztjA

query
sites
2ztjA

F

W

H

K

V

I

Y

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

R

F

E

E

G

K

I

A

S

N

Y

F

S

S

V

T

T

Q

D

D

K

K

L

V

A

E

V

I

A

A

R

K

L

A

L

L

D

D

E

E

L

F

G

G

V

I

G

E

F

Y

I

I

E

E

G

V

G

T

W

T

P

P

G

V

A

A

L

S

P

P

-

Q

-

S

-

R

K

K

D

D

T

A

E

E

F

V

F

L

A

A

R

-

A

-

S

-

G

-

E

S

L

L

A

G

L

L

K

K

H

A

A

K

A

V

L

V

V

T

A
x
H

F

I

G

Q

A

C

T

R

R

L

K

D

A

A

G

A

T

K

T

V

A

A

S

V

E

E

D

-

A

-

Q

-

V

-

R

-

A

-

L

-

D

-

S

T

N

G

A

V

P

Q

V

G

I

I

T

D

L

L

V
x
L

A

F

K

G

S

T

D

G

R

R

R

-

H

D

I

I

E

P

R

R

A

I

L

I

K

E

V

-

D

E

V

A

A

K

E

E

A

V

C

I

A

A

M

Y

V

I

R

R

D

E

T

A

V

A

S

P

F

H

L

V

V

-

S

-

E

-

G

-

R

-

R

E

V

V

F
x
R

L

F

D

S

A

A

E

E

H

-

F

-

D

D

G

T

Y

F

A

R

F

S

D

E

P

E

D

Q

T

D

A

L

L

L

R

A

V

V

L

Y

R

E

A

A

G

V

A

A

D

P

G

Y

G

-

A

V

D

D

V

R

A

V

V

G

L

L

C
x
A

D

D

T
|
T

N

V

G

G

G

V

Q

A

L

T

P

P

L

R

G

Q

I

V

A

Y

E

A

T

L

V

V

R

R

E

E

V

V

A

R

D

R

K

V

T

V

G

G

L

P

R

R

L

V

G

D

I

I

-

E

-

F

H
|
H

C

G

Q
x
H

D

N

D

D

T

T

S

G

C

C

A

A

V

I

A

A

N

N

S

A

V

Y

A

E

A

A

V

I

Q

E

A

A

G

G

A

A

T

T

H

H

V

V

Q

D

C

T

T

T

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

D

P

L

L

F

G

A

G

V

F

I

L

G

A

N

R

L

M

V

Y

T

T

-

L

-

Q

-

P

-

E

-

Y

-

V

-

R

K

K

L

Y

D

K

M

L

D

E

V

M

L

L

P

P

T

-

G

-

A

-

E

E

L

L

T

D

R

R

V

M

S

-

H

-

A

-

L

V

A

A

E

R

I

M

A

V

N

G

I

V

A

E

P

I

D

P

T

F

H

N

Q

N

A

Y

Y

I

V

T

G

G

A

E

S

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

V

I

D

N

P

P

L

E

L

A

Y

Y

N

E

H

P

I

Y

D

P

P

P

P

E

V

V

V

F

G

G

N

V

D

K

M

R

R

K

V

L

L

I

V

I

active site: Q16 (= Q27)
binding 2-oxoglutaric acid: R12 (= R23), H72 (≠ A85), L94 (≠ V116), R125 (≠ F154), A156 (≠ C189), T158 (= T191), H187 (= H218), H189 (≠ Q220)
binding copper (ii) ion: E13 (≠ D24), H187 (= H218), H189 (≠ Q220)

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
30% identity, 54% coverage: 17:311/544 of query aligns to 6:295/308 of 3rmjB

query
sites
3rmjB

V

I

Y

F

D

D

T

T

L

L

R

R

D
|
D

G

G

A

E

Q
|
Q

R

S

E

P

G

G

I

A

S

A

Y

M

S

T

V

K

T

E

D

E

K

K

L

I

A

R

V

V

A

A

R

R

L

Q

L

L

D

E

E

K

L

L

G

G

V

V

G

D

F

I

I

I

E

E

G

A

G

G

W

F

P

A

G

A

A

A

L

S

P

P

K

G

D

D

T

F

E

E

F

-

A

-

R

-

A

-

S

-

G

-

E

-

L

-

A

-

L

-

K

-

H

-

A

-

A

A

L

V

V

N

A

A

F

I

G

A

A

K

T

T

R

I

K

T

A

K

G

S

T

T

T

V

A

C

S

S

E

L

-

S

-

R

-

A

-

I

D

E

A

R

Q

D

V

I

R

R

A

Q

L

A

L

G

D

E

S

A

N

V

A

A

P

P

-

A

-

P

-

K

-

R

V

I

I

H

T

T

L

F

V

I

A

A

K

T

S

S

D

P

R

I

R

-

H

H

I

M

E

E

R

Y

A

K

L

L

K

K

V

M

D

K

V

P

A

K

E

Q

A

V

C

I

A

E

M

A

V

A

R

V

D

K

T

A

V

V

S

K

F

I

L

-

V

-

S

-

E

-

G

-

R

-

V

-

F

-

L

-

D

-

A

A

E

R

H

E

F

Y

F

T

D

D

G

D

Y

V

A

E

F

F

D

S

P

C

D

E

T

D

A

A

L

L

R

R

-

S

-

E

-

I

-

D

-

F

-

L

-

A

-

E

V

I

L

C

R

G

A

A

G

V

A

I

D

E

G

A

G

G

A

A

D

T

V

T

A

I

V

N

L

I

C

P

D

D

T

T

N

V

G

G

G

Y

Q

S

L

I

P

P

L

Y

G

K

I

T

A

E

E

E

T

F

V

F

R

R

E

E

V

L

A

I

D

A

K

K

T

T

-

P

-

N

-

G

G

K

L

V

R

V

L

W

G

S

I

A

H
|
H

C

C

Q
x
H

D

N

D

D

T

L

S

G

C

L

A

A

V

V

A

A

N

N

S

S

V

L

A

A

V

L

Q

K

A

G

G

G

A

A

T

R

H

Q

V

V

Q

E

C

C

T

T

A

V

N

N

G

G

Y

L

G

G

E

E

R

R

A

A

G

G

N
|
N

A

A

D

S

L

V

F

E

A

E

V

I

I

V

G

M

N

A

L

L

V

K

T

V

K

R

L

H

D

D

M

L

D

F

V

G

L

L

P

E

T

T

G

G

-

I

G

D

A

T

E

Q

L

I

T

V

R

P

V

S

S

S

H

K

A

L

L

V

A

S

E

T

I

I

A

T

N

G

I

Y

A

P

P

V

D

Q

T

P

H

N

Q

K

A

A

Y

I

V

V

G

G

A

A

S

N

A

A

F

F

A

S

H

H

K

E

active site: Q16 (= Q27)
binding manganese (ii) ion: D13 (= D24), H201 (= H218), H203 (≠ Q220), N237 (= N254)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
31% identity, 59% coverage: 15:335/544 of query aligns to 3:305/347 of 3a9iA

query
sites
3a9iA

F

W

H

K

V

I

Y

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q

Q

R

F

E

E

G

K

I

A

S

N

Y

F

S

S

V

T

T

Q

D

D

K

K

L

V

A

E

V

I

A

A

R

K

L

A

L

L

D

D

E

E

L

F

G

G

V

I

G

E

F

Y

I

I

E

E

G

V

G

T

W

T

P

P

G

V

A

A

L

S

P

P

-

Q

-

S

-

R

K

K

D

D

T

A

E

E

F

V

F

L

A

A

R

-

A

-

S

-

G

-

E

S

L

L

A

G

L

L

K

K

H

A

A

K

A

V

L

V

V

T

A

H

F

I

G

Q

A

C

T

R

R

L

K

D

A

A

G

A

T

K

T

V

A

A

S

V

E

E

D

T

A

G

Q

V

V

-

R

-

A

-

L

-

D

-

S

-

N

-

A

Q

P

G

V

I

I
x
D

T

L

L

L

V

F

A

G

K

T

S

S

D

K

R

Y

R

L

H

D

I

I

E

P

R

R

A

I

L

I

K

E

V

-

D

E

V

A

A

K

E

E

A

V

C

I

A

A

M

Y

V

I

R

R

D

E

T

A

V

A

S

P

F

H

L

V

V

-

S

-

E

-

G

-

R

-

R

E

V

V

F

R

L

F

D
x
S

A

A

E

E

H

-

F

-

D

D

G

T

Y

F

A

R

F

S

D

E

P

E

D

Q

T

D

A

L

L

L

R

A

V

V

L

Y

R

E

A

A

G

V

A

A

D

P

G

Y

G

-

A

V

D

D

V

R

A

V

V

G

L

L

C

A

D

D

T
|
T

N

V

G

G

G

V

Q

A

L

T

P

P

L

R

G

Q

I

V

A

Y

E

A

T

L

V

V

R

R

E

E

V

V

A

R

D

R

K

V

T

V

G

G

L

P

R

R

L

V

G

D

I

I

-

E

-

F

H
|
H

C

G

Q
x
H

D

N

D

D

T

T

S

G

C

C

A

A

V

I

A

A

N

N

S

A

V

Y

A

E

A

A

V

I

Q

E

A

A

G

G

A

A

T

T

H

H

V

V

Q

D

C

T

T

T

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

D

P

L

L

F

G

A

G

V

F

I

L

G

A

N

R

L

M

V

Y

T

T

-

L

-

Q

-

P

-

E

-

Y

-

V

-

R

K

K

L

Y

D

K

M

L

D

E

V

M

L

L

P

P

T

-

G

-

A

-

E

E

L

L

T

D

R

R

V

M

S

-

H

-

A

-

L

V

A

A

E

R

I

M

A

V

N

G

I

V

A

E

P

I

D

P

T

F

H

N

Q

N

A

Y

Y

I

V

T

G

G

A

E

S

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

V

I

D

N

P

P

L

E

L

A

Y

Y

N

E

H

P

I

Y

D

P

P

P

P

E

V

V

V

F

G

G

binding cobalt (ii) ion: E12 (≠ D24), H188 (= H218), H190 (≠ Q220)
binding lysine: R11 (= R23), D91 (≠ I113), S128 (≠ D156), T159 (= T191), H188 (= H218), H190 (≠ Q220)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
26% identity, 70% coverage: 14:393/544 of query aligns to 3:374/379 of 4ov4A

query
sites
4ov4A

T

T

F

I

H

H

V

I

Y

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

A

N

Q
|
Q

R

A

E

L

G

K

I

R

S

P

Y

W

S

T

V

I

T

D

D

E

K

K

L

I

A

E

V

V

A

F

R

D

L

L

D

V

E

E

L

L

G

N

V

V

G

D

F

G

I

I

E

E

G

V

G

G

W

F

P

P

G

S

A

S

L

-

P

-

K

N

D

E

T

T

E

E

F

F

F

H

A

T

R

C

A

Q

S

V

S

L

G

S

E

K

L

R

A

A

L

P

K

K

H

G

A

K

A

P

L

I

V

A

A

A

F

L

G

S

A

R

T

A

R

N

K

Q

A

N

G

E

T

I

T

A

A

V

S

T

E

W

D

E

A

A

Q

I

V

Q

R

K

A

A

L

-

D

-

S

-

N

D

A

C

P

P

V

R

I

M

T

H

L

I

V

V

A

Y

K

P

S

V

D

S

R

D

R

F

H

S

I

I

E

K

R

H

A

V

L

L

K

K

V

I

D

S

V

E

A

K

E

E

A

V

C

L

A

Q

M

K

V

I

R

R

D

N

T

S

V

I

S

S

F

F

-

A

-

R

-

S

L

I

V

V

S

G

E

P

G

G

R

I

R

E

V

I

F

Q

L

F

D

S

A

G

E

E

H

H

F

F

F

G

D

D

-

A

-

I

-

E

G

N

Y

F

A

A

F

F

D

T

P

K

D

E

T

A

A

F

L

L

R

T

V

A

L

I

R

E

A

A

G

G

A

A

D

N

G

-

A

-

D

-

V

I

A

I

V

N

L

L

C
x
P

D

N

T
|
T

N

V

G

E

G

R

Q

Y

L

R

P

P

L

M

G

V

I

F

A

V

E

N

T

M

V

V

R

K

E

E

V

I

A

K

D

D

-

V

K

K

T

D

G

K

L

A

R

I

L

I

G

S

I

I

H
|
H

C

T

Q
x
H

D

N

D

D

T

L

S

G

C

M

A

A

V

T

A

A

N

T

S

S

V

V

A

E

A

S

V

V

Q

Y

A

V

G

G

A

A

T

E

H

Q

V

I

Q

E

C

V

T

A

A

L

N

N

G

G

Y

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

D

N

L

L

F

Y

A

E

V

T

I

A

G

I

N

A

L

L

V

H

T

Q

-

N

-

G

-

E

K

N

L

L

D

N

M

I

D

N

-

F

-

Q

-

R

V

I

L

Y

P

P

T

T

G

A

G

-

A

-

E

-

L

-

T

K

R

R

V

I

S

S

H

-

A

-

L

-

A

-

E

E

I

L

A

T

N

G

I

I

A

P

P

I

D

G

T

E

H

K

Q

T

A

P

Y

I

V

I

G

G

A

E

S

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

V

G

D

-

P

-

L

-

L

A

Y

Y

N

R

H

T

I

F

D

S

P

P

P

E

V

F

V

V

G

G

-

R

-

M

N

D

D

K

M

E

R

T

V

I

L

S

V

F

T

T

E

N

M

Q

A

S

G

G

R

H

A

K

S

A

L

I

E

E

L

F

K

L

G

L

R

H

E

Q

L

R

G

G

V

I

D

Q

L

V

A

S

S

K

Q

E

P

-

T

-

A

G

L

I

T

H

N

H

V

L

V

F

E

S

K

L

V

A

K

K

A

S

L

I

E

S

A

S

K

R

G

E

W

N

S

N

F

R

E

E

A

I

A

T

D

E

A

A

S

E

L

L

active site: Q16 (= Q27)
binding 3-methyl-2-oxobutanoic acid: R12 (= R23), P174 (≠ C189), T176 (= T191), H205 (= H218), H207 (≠ Q220)
binding zinc ion: D13 (= D24), H205 (= H218), H207 (≠ Q220)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
25% identity, 70% coverage: 14:393/544 of query aligns to 3:376/380 of 4ov9A

query
sites
4ov9A

T

T

F

I

H

H

V

I

Y

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

A

N

Q
|
Q

R

A

E

L

G

K

I

R

S

P

Y

W

S

T

V

I

T

D

D

E

K

K

L

I

A

E

V

V

A

F

R

D

L

L

D

V

E

E

L

L

G

N

V

V

G

D

F

G

I

I

E

E

G

V

G

G

W

F

P

P

G

S

A

S

L

-

P

-

K

N

D

E

T

T

E

E

F

F

F

H

A

T

R

C

A

Q

S

V

S

L

G

S

E

K

L

R

A

A

L

P

K

K

H

G

A

K

A

P

L

I

V

A

A

A

F
x
L

G

S

A

R

T

A

R

N

K

Q

A

N

G

E

T

I

T

A

A

V

S

T

E

W

D

E

A

A

Q

I

V

Q

R

K

A

A

L

-

D

-

S

-

N

D

A

C

P

P

V

R

I

M

T

H

L

I

V

V

A

Y

K

P

S

V

D

S

R

D

R

F

H

S

I

I

E

K

R

H

A

V

L

L

K

K

V

I

D

S

V

E

A

K

E

E

A

V

C

L

A

Q

M

K

V

I

R

R

D

N

T

S

V

I

S

S

F

F

-

A

-

R

-

S

L

I

V

V

S

G

E

P

G

G

R

I

R

E

V

I

F

Q

L

F

D

S

A

G

E

E

H

H

F

F

F

G

D

D

-

A

-

I

-

E

G

N

Y

F

A

A

F

F

D

T

P

K

D

E

T

A

A

F

L

L

R

T

V

A

L

I

R

E

A

A

G

G

A

A

D

N

G

-

A

-

D

-

V

I

A

I

V

N

L

L

C

P

D

N

T
|
T

N

V

G

E

G

R

Q

Y

L

R

P

P

L

M

G

V

I

F

A

V

E

N

T

M

V

V

R

K

E

E

V

I

A

K

D

D

-

V

K

K

T

D

G

K

L

A

R

I

L

I

G

S

I

I

H
|
H

C

T

Q
x
H

D

N

D

D

T

L

S

G

C

M

A

A

V

T

A

A

N

T

S

S

V

V

A

E

A

S

V

V

Q

Y

A

V

G

G

A

A

T

E

H

Q

V

I

Q

E

C

V

T

A

A

L

N

N

G

G

Y

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

D

N

L

L

F

Y

A

E

V

T

I

A

G

I

N

A

L

L

V

H

T

Q

-

N

-

G

-

E

K

N

L

L

D

N

M

I

D

N

-

F

-

Q

-

R

V

I

L

Y

P

P

T

T

G

A

G

-

A

-

E

-

L

-

T

K

R

R

V

I

S

S

H

-

A

-

L

-

A

-

E

E

I

L

A

T

N

G

I

I

A

P

P

I

D

G

T

E

H

K

Q

T

A

P

Y

I

V

I

G

G

A

E

S

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

V

Q

D

S

P

K

L

G

L

A

Y

Y

N

R

H

T

I

F

D

S

P

P

P

E

V

F

V

V

G

G

-

R

-

M

N

D

D

K

M

E

R

T

V

I

L

S

V

F

T

T

E

N

M

Q

A

S

G

G

R

H

A

K

S

A

L

I

E

E

L

F

K

L

G

L

R

H

E

Q

L

R

G

G

V

I

D

Q

L

V

A

S

S

K

Q

E

P

-

T

-

A

G

L

I

T

H

N

H

V

L

V

F

E

S

K

L

V

A

K

K

A

S

L

I

E

S

A

S

K

R

G

E

W

N

S

N

F

R

E

E

A

I

A

T

D

E

A

A

S

E

L

L

active site: Q16 (= Q27)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R23), L73 (≠ F86), T176 (= T191), H205 (= H218), H207 (≠ Q220)
binding zinc ion: D13 (= D24), H205 (= H218), H207 (≠ Q220)

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
24% identity, 67% coverage: 13:376/544 of query aligns to 28:379/400 of 3ivtB

query
sites
3ivtB

D

N

T

N

F

F

H

S

V

I

Y

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

R

F

E

A

G

N

I

A

S

F

Y

F

S

D

V

T

T

E

D

K

K

K

L

I

A

Q

V

I

A

A

R

K

L

A

L

L

D

D

E

N

L

F

G

G

V

V

G

D

F

Y

I

I

E

E

G

L

G

T

W

S

P

P

G

V

A

A

L

S

P

E

K

Q

-

S

-

R

-

Q

D

D

T

C

E

E

F

A

F

I

A

C

R

K

A

-

S

-

G

-

E

-

L

L

A

G

L

L

K

K

H

C

A

K

A

I

L

L

V

T

A
x
H

F

I

G

-

A

-

T

-

R

-

K

-

A

-

G

-

T

R

T

C

A

H

S

M

E

D

D

D

A

A

Q

-

V

-

R

R

A

V

L

A

L

V

D

E

S

T

N

G

A

V

P

D

V

G

I

V

T

D

L

V

V

V

A

I

K

G

S

T

D

S

R

Q

R

Y

H

L

I

R

E

K

R

Y

A

S

L

H

K

G

V

K

D

D

V

M

A

T

E

Y

A

I

C

I

A

D

M

S

V

A

R

T

D

E

T

V

V

I

S

N

F

F

L

V

V

K

S

S

E

K

G

G

R

I

R

E

V

V

F
x
R

L

F

D
x
S

A

S

E

E

H

-

F

-

D

D

G

S

Y

F

A

R

F

S

D

D

P

L

D

V

T

D

A

L

L

L

R

S

V

L

L

Y

R

K

A

A

G

V

A

D

D

K

G

I

G

G

A

V

D

N

V

R

A

V

V

G

L

I

C

A

D

D

T
|
T

N

V

G

G

G

C

Q

A

L

T

P

P

L

R

G

Q

I

V

A

Y

E

D

T

L

V

I

R

R

E

T

V

L

A

R

D

G

K

V

T

V

G

S

L

C

R

D

L

I

G

E

I

C

H
|
H

C

F

Q
x
H

D

N

D

D

T

T

S

G

C

M

A

A

V

I

A

A

N

N

S

A

V

Y

A

C

A

A

V

L

Q

E

A

A

G

G

A

A

T

T

H

H

V

I

Q

D

C

T

T

S

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

D

P

L

L

F

G

A

A

V

L

I

L

G

A

N

R

L

M

V

Y

T

V

K

T

L

D

D

R

M

E

D

Y

V

I

L

T

P

H

T

K

G

Y

G

K

A

L

A

N

E

Q

L

L

T

R

R

E

V

L

S

E

H

N

A

L

L

V

A

A

E

D

I

A

A

V

N

E

I

V

A

Q

P

I

D

P

T

F

H

N

Q

N

A

Y

Y

I

V

T

G

G

A

M

S

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

V

A

D

N

P

P

L

S

L

T

Y

Y

N

E

H

I

I

L

D

K

P

P

P

E

V

D

V

F

G

G

N

M

D

S

M

R

R

Y

V

V

L

H

V

V

-

G

T

S

E

R

M

L

A

T

G

G

R

W

A

N

S

A

L

I

E

K

L

S

K

R

G

A

R

E

E

Q

L

L

G

N

V

L

D

H

L

L

A

T

-

D

S

A

Q

Q

P

A

T

K

A

E

L

L

T

T

N

V

V

R

V

I

E

K

K

K

V

L

active site: Q42 (= Q27)
binding 2-oxoglutaric acid: R38 (= R23), H98 (≠ A85), R158 (≠ F154), S160 (≠ D156), T192 (= T191), H219 (= H218), H221 (≠ Q220)
binding zinc ion: E39 (≠ D24), H219 (= H218), H221 (≠ Q220)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
24% identity, 67% coverage: 13:376/544 of query aligns to 33:384/418 of Q9Y823

query
sites
Q9Y823

D

N

T

N

F

F

H

S

V

I

Y

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

R

F

E

A

G

N

I

A

S

F

Y

F

S

D

V

T

T

E

D

K

K

K

L

I

A

Q

V

I

A

A

R

K

L

A

L

L

D

D

E

N

L

F

G

G

V

V

G

D

F

Y

I

I

E
|
E

G

L

G

T

W

S

P

P

G

V

A

A

L

S

P

E

K

Q

-

S

-

R

-

Q

D

D

T

C

E

E

F

A

F

I

A

C

R

K

A

-

S

-

G

-

E

-

L

L

A

G

L

L

K

K

H

C

A

K

A

I

L

L

V

T

A
x
H

F

I

G

-

A

-

T

-

R

-

K

-

A

-

G

-

T

R

T

C

A

H

S

M

E

D

D

D

A

A

Q

-

V

-

R

R

A

V

L

A

L

V

D

E

S

T

N

G

A

V

P

D

V

G

I

V

T
x
D

L

V

V

V

A

I

K

G

S

T

D

S

R

Q

R

Y

H

L

I

R

E

K

R

Y

A

S

L

H

K

G

V

K

D

D

V

M

A

T

E

Y

A

I

C

I

A

D

M

S

V

A

R

T

D

E

T

V

V

I

S

N

F

F

L

V

V

K

S

S

E

K

G

G

R

I

R

E

V

V

F
x
R

L

F

D
x
S

A

S

E
|
E

H

-

F

-

D

D

G

S

Y

F

A

R

F

S

D

D

P

L

D

V

T

D

A

L

L

L

R

S

V

L

L

Y

R

K

A

A

G

V

A

D

D

K

G

I

G

G

A

V

D

N

V

R

A

V

V

G

L

I

C

A

D

D

T
|
T

N

V

G

G

G

C

Q

A

L

T

P

P

L

R

G

Q

I

V

A

Y

E

D

T

L

V

I

R

R

E

T

V

L

A

R

D

G

K

V

T

V

G

S

L

C

R

D

L

I

G
x
E

I

C

H
|
H

C

F

Q
x
H

D

N

D

D

T

T

S

G

C

M

A

A

V

I

A

A

N

N

S

A

V

Y

A

C

A

A

V

L

Q

E

A

A

G

G

A

A

T

T

H

H

V

I

Q

D

C

T

T

S

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

D

P

L

L

F

G

A

A

V

L

I

L

G

A

N

R

L

M

V

Y

T

V

K

T

L

D

D

R

M

E

D

Y

V

I

L

T

P

H

T

K

G

Y

G

K

A

L

A

N

E

Q

L

L

T
x
R

R

E

V

L

S

E

H

N

A

L

L

V

A

A

E

D

I

A

A

V

N

E

I

V

A

Q

P

I

D

P

T

F

H

N

Q

N

A

Y

Y

I

V

T

G

G

A

M

S

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

V

A

D

N

P

P

L

S

L

T

Y
|
Y

N

E

H

I

I

L

D

K

P

P

P

E

V

D

V

F

G

G

N

M

D

S

M

R

R

Y

V

V

L

H

V

V

-

G

T

S

E

R

M

L

A

T

G

G

R

W

A

N

S

A

L

I

E

K

L

S

K

R

G

A

R

E

E
x
Q

L

L

G

N

V

L

D

H

L

L

A

T

-

D

S

A

Q

Q

P

A

T

K

A

E

L

L

T

T

N

V

V

R

V

I

E

K

K

K

V

L

R43 (= R23) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D24) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q27) mutation to A: Abolishes the catalytic activity.
E74 (= E54) 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 (≠ A85) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ T114) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ F154) 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 (≠ D156) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E158) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T191) 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 (≠ G216) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H218) binding 2-oxoglutarate; binding Zn(2+)
H226 (≠ Q220) binding 2-oxoglutarate; binding Zn(2+)
R288 (≠ T282) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y326) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ E357) 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, 67% coverage: 13:376/544 of query aligns to 10:350/370 of 3mi3A

query
sites
3mi3A

D

N

T

N

F

F

H

S

V

I

Y

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

A

E

Q
|
Q

R

F

E

A

G

N

I

A

S

F

Y

F

S

D

V

T

T

E

D

K

K

K

L

I

A

Q

V

I

A

A

R

K

L

A

L

L

D

D

E

N

L

F

G

G

V

V

G

D

F

Y

I

I

E

E

G

L

G

T

W

S

P

P

G

V

A

A

L

S

P

E

K

Q

-

S

-

R

-

Q

D

D

T

C

E

E

F

A

F

I

A

C

R

K

A

-

S

-

G

-

E

-

L

L

A

G

L

L

K

K

H

C

A

K

A

I

L

L

V

T

A

H

F

I

G

R

A

C

T

-

R

-

K

-

A

-

G

-

T

-

A

H

S

M

E

D

D

D

A

A

Q

-

V

-

R

R

A

V

L

A

L

V

D

E

S

T

N

G

A

V

P

D

V

G

I

V

T
x
D

L

V

V

V

A

I

K

G

S

T

D

S

R

M

R

T

H

Y

I

I

E

-

R

-

A

-

L

-

K

-

V

I

D

D

V

S

A

A

E

T

A

-

C

-

A

-

M

-

V

-

R

-

D

E

T

V

V

I

S

N

F

F

L

V

V

K

S

S

E

K

G

G

R

I

R

E

V

V

F

R

L

F

D

S

A

S

E

E

H

-

F

-

D

D

G

S

Y

F

A

R

F

S

D

D

P

L

D

V

T

D

A

L

L

L

R

S

V

L

L

Y

R

K

A

A

G

V

A

D

D

K

G

I

G

G

A

V

D

N

V

R

A

V

V

G

L

I

C

A

D

D

T
|
T

N

V

G

G

G

C

Q

A

L

T

P

P

L

R

G

Q

I

V

A

Y

E

D

T

L

V

I

R

R

E

T

V

L

A

R

D

G

K

V

T

V

G

S

L

C

R

D

L

I

G

E

I

C

H
|
H

C

F

Q
x
H

D

N

D

D

T

T

S

G

C

M

A

A

V

I

A

A

N

N

S

A

V

Y

A

C

A

A

V

L

Q

E

A

A

G

G

A

A

T

T

H

H

V

I

Q

D

C

T

T

S

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

D

P

L

L

F

G

A

A

V

L

I

L

G

A

N

R

L

M

V

Y

T

V

K

T

L

D

D

R

M

E

D

Y

V

I

L

T

P

H

T

K

G

Y

G

K

A

L

A

N

E

Q

L

L

T

R

R

E

V

L

S

E

H

N

A

L

L

V

A

A

E

D

I

A

A

V

N

E

I

V

A

Q

P

I

D

P

T

F

H

N

Q

N

A

Y

Y

I

V

T

G

G

A

M

S

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

V

A

D

N

P

P

L

S

L

T

Y

Y

N

E

H

I

I

L

D

K

P

P

P

E

V

D

V

F

G

G

N

M

D

S

M

R

R

Y

V

V

L

H

V

V

-

G

T

S

E

R

M

L

A

T

G

G

R

W

A

N

S

A

L

I

E

K

L

S

K

R

G

A

R

E

E

Q

L

L

G

N

V

L

D

H

L

L

A

T

-

D

S

A

Q

Q

P

A

T

K

A

E

L

L

T

T

N

V

V

R

V

I

E

K

K

K

V

L

active site: Q24 (= Q27)
binding lysine: R20 (= R23), D100 (≠ T114), T163 (= T191), H190 (= H218), H192 (≠ Q220)
binding zinc ion: E21 (≠ D24), H190 (= H218), H192 (≠ Q220)

3ivsA Homocitrate synthase lys4 (see paper)
23% identity, 70% coverage: 13:393/544 of query aligns to 10:359/364 of 3ivsA

query
sites
3ivsA

D

N

T

N

F

F

H

S

V

I

Y

I

D

E

T

S

T

T

L

L

R

R

D
x
E

G

G

A

E

Q
|
Q

R

F

E

A

G

N

I

A

S

F

Y

F

S

D

V

T

T

E

D

K

K

K

L

I

A

Q

V

I

A

A

R

K

L

A

L

L

D

D

E

N

L

F

G

G

V

V

G

D

F

Y

I

I

E

E

G

L

G

T

W

S

P

P

G

V

A

A

L

S

P

E

K

Q

D

S

T

R

E

Q

F

-

A

-

R

-

A

-

S

-

G

-

E

-

L

-

A

-

L

-

K

D

H

C

A

E

A

A

L

I

V

C

A

K

F

L

G

G

A

L

T

K

R

C

K

K

A

I

G

L

T

T

T

-

A

-

S

-

E

-

D

-

A

-

Q

H

V

I

R

R

A

C

L

H

L

M

D

D

S

D

N

A

A

-

P

-

V

-

I

-

T

-

L

-

V

-

A

-

K

-

S

-

D

-

R

R

R

V

H

A

I

V

E

E

R

T

A

G

L

V

K

D

-

G

V

V

D

D

V

V

A

V

E

I

A

G

C

T

A

T

M

Y

V

I

R

I

D

D

T

S

-

A

-

T

-

E

-

V

V

I

S

N

F

F

L

V

V

K

S

S

E

K

G

G

R

I

R

E

V

V

F

R

L

F

D

S

A

S

E

E

H

-

F

-

D

D

G

S

Y

F

A

R

F

S

D

D

P

L

D

V

T

D

A

L

L

L

R

S

V

L

L

Y

R

K

A

A

G

V

A

D

D

K

G

I

G

G

A

V

D

N

V

R

A

V

V

G

L

I

C

A

D

D

T

T

N

V

G

G

G

C

Q

A

L

T

P

P

L

R

G

Q

I

V

A

Y

E

D

T

L

V

I

R

R

E

T

V

L

A

R

D

G

K

V

T

V

G

S

L

C

R

D

L

I

G

E

I

C

H
|
H

C

F

Q
x
H

D

N

D

D

T

T

S

G

C

M

A

A

V

I

A

A

N

N

S

A

V

Y

A

C

A

A

V

L

Q

E

A

A

G

G

A

A

T

T

H

H

V

I

Q

D

C

T

T

S

A

I

N

L

G

G

Y

I

G

G

E

E

R

R

A

N

G

G

N

I

A

T

D

P

L

L

F

G

A

A

V

L

I

L

G

A

N

R

L

M

V

Y

T

V

K

T

L

D

D

R

M

E

D

Y

V

I

L

T

P

H

T

K

G

Y

G

K

A

L

A

N

E

Q

L

L

T

R

R

E

V

L

S

E

H

N

A

L

L

V

A

A

E

D

I

A

A

V

N

E

I

V

A

Q

P

I

D

P

T

F

H

N

Q

N

A

Y

Y

I

V

T

G

G

A

M

S

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

V

A

D

N

P

P

L

S

L

T

Y

Y

N

E

H

I

I

L

D

K

P

P

P

E

V

D

V

F

G

G

N

M

D

S

M

R

R

Y

V

V

L

H

V

V

-

G

T

S

E

R

M

L

A

T

G

G

R

W

A

N

S

A

L

I

E

K

L

S

K

R

G

A

R

E

E

Q

L

L

G

N

V

L

D

H

L

L

A

Q

S

A

Q

K

P

E

T

L

A

T

L

V

T

-

N

-

V

-

E

-

K

R

V

I

K

K

A

K

L

L

E

A

A

V

K

R

G

T

W

L

S

A

F

M

E

D

A

D

A

V

D

D

A

R

S

V

L

L

active site: Q24 (= Q27)
binding cobalt (ii) ion: E21 (≠ D24), H188 (= H218), H190 (≠ Q220)

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
25% identity, 56% coverage: 17:323/544 of query aligns to 4:304/311 of 3bliA

query
sites
3bliA

V

I

Y

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

A

E

Q
|
Q

R

T

E

R

G

G

I

V

S

S

Y

F

S

S

V

T

T

S

D

E

K

K

L

L

A

N

V

I

A

A

R

K

-

F

L

L

D

Q

E

K

L

L

G

N

V

V

G

D

F

R

I

V

E

E

G

I

G

A

W

-

P

-

G

-

A

-

L

-

P

-

K

-

D

-

T

-

E

-

F

-

F

S

A

A

R
|
R

A
x
V

S

S

S

K

G

G

E

E

L

L

A

E

L

T

K

V

H

Q

A

K

A

-

L

I

V

M

A

E

F

W

G

A

A

A

T

T

R

E

K

Q

A

L

G

-

T

-

A

-

S

T

E

E

D

R

A

I

Q

E

V

I

R

L

A

G

L

F

L

V

D

D

S

G

N

N

-

K

-

T

-

V

-

D

-

W

-

I

-

K

-

D

-

S

-

G

A

A

P

K

V

V

I

L

T

N

L

L

V

L

A

T

K

K

S

G

D

S

R

L

R

H

H

H

I

L

E

E

R

K

A

Q

L

L

K

G

V

K

D

T

V

P

A

K

E

E

A

F

C

F

A

T

M

D

V

V

R

S

D

F

T

V

V

I

S

E

F

Y

L

A

V

I

S

K

E

S

G

G

R

L

R

K

V

I

F

N

L

V

D
x
Y

A

L

E
|
E

H

D

F

W

F

S

D

N

G

G

Y

F

A

R

F

N

D

S

P

P

D

D

T

Y

A

V

L

K

R

S

V

L

L

V

R

E

A

H

G

L

A

S

D

K

G

E

G

H

A

I

D

E

V

R

A

I

V

F

L

L

C
x
P

D

D

T
|
T

N

L

G

G

G

V

Q

L

L

S

P

P

-

E

-

T

-

F

L

Q

G

G

I

V

A

D

E

S

T

L

V

I

R

Q

E

K

V

Y

A

P

D

D

K

-

T

-

G

-

L

I

R

H

L

F

G

E

I

F

H
|
H

C

G

Q
x
H

D

N

D

D

T

Y

S

D

C

L

A

S

V

V

A

A

N

N

S

S

V

L

A

Q

A

A

V

I

Q

R

A

A

G

G

A

V

T

K

H

G

V

L

Q

H

C

A

T

S

A

I

N

N

G

G

Y

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

D

P

L

L

F

E

A

A

V

L

I

V

G

T

N

T

L

I

-

H

-

D

-

K

-

S

V

N

T

S

K

K

L

T

D

N

M

I

D

N

V

E

L

I

P

A

T

I

G

T

G

E

A

A

A

S

E

R

L

L

T

V

R

E

V

V

S

F

H

S

A

G

L

K

A

R

E

I

I

S

A

A

N

N

I

-

A

-

P

-

D

-

T

-

H

-

Q

R

A

P

Y

I

V

V

G

G

A

E

S

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

I

N

K

P

V

I

D

L

P

P

active site: Q14 (= Q27)
binding acetyl coenzyme *a: Q14 (= Q27), R47 (= R70), V48 (≠ A71), E140 (= E158)
binding pyruvic acid: R10 (= R23), Y138 (≠ D156), P171 (≠ C189), T173 (= T191)
binding zinc ion: D11 (= D24), H201 (= H218), H203 (≠ Q220)

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)
26% identity, 63% coverage: 17:359/544 of query aligns to 13:343/347 of Q53WI0

query
sites
Q53WI0

V

V

Y

V

D

D

T

T

L

L

R

R

D

D

G

G

A

S

Q

H

R

A

E

H

G

R

I

H

S

Q

Y

Y

S

T

V

V

T

E

D

E

K

A

L

R

A

A

V

I

A

A

R

Q

L

A

L

L

D

D

E

E

L

A

G

G

V

V

G

Y

F

A

I

I

E

E

G

V

G

S

W

H

P

G

G

D

A

G

L

L

P

G

K

G

D

S

T

S

E

L

F

Q

F

Y

A

G

R

F

A

S

S

R

S

T

G

D

E

E

L

M

A

E

L

L

K

I

H

R

A

A

A

V

L

R

V

E

A

T

F

V

G

R

A

R

T

A

R

K

K

V

A

A

G

A

T

L

A

L

S

P

E

G

D

I

A

G

Q

T

V

R

R

K

A

E

L

L

L

K

D

E

S

A

N

V

A

E

P

A

V

G

I

I

T

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M

V

V

A

-

K

-

S

-

D

-

R

-

R

R

H

I

I

A

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T

R

Q

A

C

L

T

K

E

V

A

D

D

V

I

A

S

E

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-

Q

-

H

-

F

-

G

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M

A

A

C

K

A

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M

M

V

G

R

L

D

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V

S

G

F

F

L

L

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M

S

M

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M

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-

P

-

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L

A

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-

G

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G

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V

V

A

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G

G

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L

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G

G

I

F

H

H

C

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N

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A

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G

A

A

T

D

H

W

V

V

Q

D

C

A

T

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A

L

N

R

G

G

Y

Y

G

G

E

A

R

G

A

A

G

G

N

N

A

A

D

P

-

L

-

E

-

V

L

L

F

A

A

A

V

V

I

L

G

D

N

K

L

A

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G

T

L

K

N

L

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D

G

M

L

D

D

V

V

L

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G

L

G

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A

A

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-

T

-

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-

H

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A

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A

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-

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T

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G

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A

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A

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T

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F

G

L

L

L

H

H

A

A

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K

A

R

I

I

-

G

-

K

-

E

-

L

K

G

V

V

D

D

P

P

-

L

-

A

-

I

L

L

Y

E

N

L

H

G

I

R

D

R

P

Q

P

A

V

V

V
x
A

G

G

N

Q

D

E

M

D

R

W

V

I

L

L

V

-

T

-

E

-

M

-

A

-

G

-

R

R

A

V

S

A

L

L

E

E

L

L

K

K

G

E

R

K

E

E

L

A

G

G

A324 (≠ V334) mutation to G: Increases the channeling efficiency of propanaldehyde from 57% to 94%.

Query Sequence

>WP_034273566.1 NCBI__GCF_000504245.1:WP_034273566.1
MNRTEPADTPLGDTFHVYDTTLRDGAQREGISYSVTDKLAVARLLDELGVGFIEGGWPGA
LPKDTEFFARASSGELALKHAALVAFGATRKAGTTASEDAQVRALLDSNAPVITLVAKSD
RRHIERALKVDVAEACAMVRDTVSFLVSEGRRVFLDAEHFFDGYAFDPDTALRVLRAGAD
GGADVAVLCDTNGGQLPLGIAETVREVADKTGLRLGIHCQDDTSCAVANSVAAVQAGATH
VQCTANGYGERAGNADLFAVIGNLVTKLDMDVLPTGGAAELTRVSHALAEIANIAPDTHQ
AYVGASAFAHKAGLHASAIKVDPLLYNHIDPPVVGNDMRVLVTEMAGRASLELKGRELGV
DLASQPTALTNVVEKVKALEAKGWSFEAADASLELLLRRAMDDDGDGSGDTLAPEAPFEL
ESYRVVLDHRSNDEVISEATVKVHVAGERVIATAEGNGPVHALDAALRKALTPRLAWLDS
VDLTDYKVRILPGTHGTEAVTRVLIESSDREREWTTVGVHENIVEASWLALCDALVHKSM
RVRP

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