SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013010707.1 NCBI__GCF_000025725.1:WP_013010707.1 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)

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 69% coverage: 5:368/526 of query aligns to 85:458/506 of Q9FG67

query
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Q9FG67

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S102 (≠ N22) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ G205) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain MC58) (see 2 papers)
28% identity, 92% coverage: 2:483/526 of query aligns to 4:469/517 of Q9JZG1

query
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Q9JZG1

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D16 (= D14) binding Mn(2+)
H204 (= H207) binding Mn(2+)
H206 (= H209) binding Mn(2+)
N240 (= N243) binding Mn(2+)

Sites not aligning to the query:

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

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
30% identity, 70% coverage: 5:371/526 of query aligns to 18:394/409 of 6e1jA

query
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6e1jA

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K

L
|
L

S

S

G

G

K
x
R

S
x
H

N

A

L

V

I

K

Y

G

K

R

A

L

K

K

D

E

F

L

G

G

L

Y

D

E

V

I

D

-

S

-

S

S

D

D

P

E

K

K

I

L

N

N

A

E

V

V

V

F

E

S

R

R

L

F

K

R

E

D

L

L

E

T

N

K

K

Q

binding coenzyme a: Q30 (= Q17), F60 (≠ W47), S63 (= S50), I95 (≠ T77), R97 (= R79), F121 (= F104), K132 (≠ A115), L133 (= L116), S322 (≠ G301), G323 (= G302), I324 (≠ V303), D327 (≠ S306), K331 (= K310), L359 (= L334), R362 (≠ K337), H363 (≠ S338)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ C177), T194 (= T179), H225 (= H207), H227 (= H209)
binding manganese (ii) ion: D27 (= D14), V82 (= V66), E84 (≠ D68), H225 (= H207), H227 (= H209)

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
31% identity, 71% coverage: 1:373/526 of query aligns to 18:377/399 of 6ktqA

query
sites
6ktqA

M

L

S

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K

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K

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V

E

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|
R

D
x
E

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Q

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D

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N

V

F

F

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T

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D

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E

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A

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Y

M

I

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A

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G

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x
V

N

S

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P

-

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-

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-

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G

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H

E

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I

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-

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-

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R
|
R

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x
A

A

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K

R

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T

-

C

-

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-

N

-

D

-

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-

N

D

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A

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A

A

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x
H

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E

N

A

L

L

E

R

L

S

I

I

N

A

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T

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S

Y

Y

L

A

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H

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A

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x
R

Y

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x
T

A

A

E
|
E

H

-

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-

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D

G

A

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T

K

R

A

A

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D

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Y

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K

A

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M

R

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G

A

A

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x
S

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T

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M

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I

P

E

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|
H

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H
|
H

N

N

D

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S

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D

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M

A

A

V

V

A

A

N

N

S

V

V

L

I

A

A

A

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E

H

G

G

G

I

A

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I

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Q

H

G

T

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T

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L

N

N

G

G

Y

L

G

G

E

E

R

R

C

V

G

G

N

I

A

A

N

P

I

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Q

S

V

V

V

I

A

P

A

N

A

L

L

Q

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L

Y

K

H

Y

F

G

G

Y

I

E

E

C

V

V

V

P

-

V

-

D

-

K

D

L

L

K

K

N

K

L

L

R

S

T

E

V

V

S

A

R

S

Y

L

I

V

N

E

E

K

L

Y

G

S

N

G

L

I

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A

H

L

N

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I

P

H

N

Q

F

P

P

Y

I

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G

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Y

A

A

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F

A

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H

K

K

G

A

G

G

V

V

H

H

V

V

S

A

A

G

I

V

M

L

K

N

N

D

S

P

S

K

T

T

Y

Y

E

E

H

F

I

L

E

P

P

P

E

E

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T

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F

G

G

N

R

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Q

R

R

D

V

Y

L

V

L

I

S

D

D

K

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T

G

G

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K

S

H

N

A

L

V

I

-

Y

-

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K

A

D

K

R

D

F

F

D

G

R

L

L

D

G

V

V

D

K

S

L

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D

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S

K

E

I

I

N

D

A

Q

V

V

V

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E

A

R

K

L

I

K

K

E

S

L

N

E

P

N

N

K

V

G

R

F

F

binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ F142), T156 (≠ D144), E158 (= E146), S184 (≠ I175), T188 (= T179), H216 (= H207), H218 (= H209)
binding coenzyme a: V67 (≠ S50), R96 (= R78), A97 (≠ R79), F116 (= F104), H128 (≠ L116), E158 (= E146)
binding zinc ion: E31 (≠ D14), H216 (= H207), H218 (= H209)

Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 73% coverage: 5:388/526 of query aligns to 85:488/503 of Q9FN52

query
sites
Q9FN52

V

V

E

R

I

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Y

L

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R

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A

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-

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A

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G

T

I

R

A

R

R

A

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K

K

R

K

T

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C

-

D

D

N

I

D

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E

A

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W

Q

E

A

A

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E

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P

N

R

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A

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N

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S

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K

Y

Y

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A

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-

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-

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-

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A

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F

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H

F

F

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-

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A

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A

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A

A

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|
G

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E

I

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A

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E

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-

G

-

A

-

D

D

D

Y

I

P

V

L

F

G

A

I

I

H

H

C

C

H

H

N

N

D

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L

D

G

C

V

A

A

V

T

A

A

N

N

S

T

V

I

I

S

A

G

V

I

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C

H

A

G

G

I

A

V

R

H

Q

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E

G

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T

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I

N

N

G

G

Y

I

G

G

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C

S

G

G

N

N

A

A

N

P

I

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E

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V

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-

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-

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A

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Y

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Y

G

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-

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-

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-

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E

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G

G

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A

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N

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P

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-

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K

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N

A

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R

E

E

L

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D

-

A

-

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-

L

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A

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G

G

A

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F

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E

L

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L

L

M

N

R

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K

G263 (= G181) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
28% identity, 70% coverage: 6:372/526 of query aligns to 5:359/376 of O87198

query
sites
O87198

E

K

I

I

Y

I

D

D

T

S

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T

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L

R
|
R

D
x
E

G

G

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A

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N

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A

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A

A

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A

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K

A

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-
x
H

-

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A

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A

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A

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A

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x
D

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Y

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T

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K

A

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x
R

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x
S

A

A

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E

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F

F

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-

Y

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-

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-

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A

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E

E

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Y

V

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H
|
H

C

G

H
|
H

N

N

D

D

S

T

D

G

C

C

A

A

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I

A

A

N

N

S

A

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A

A

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E

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A

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G

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A

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H

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L

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Y

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E

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C

N

G

G

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-

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A

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-

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A

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G

R12 (= R13) binding 2-oxoglutarate
E13 (≠ D14) binding Mg(2+)
H72 (vs. gap) binding 2-oxoglutarate; mutation to L: Significant decrease in sensitivity to lysine inhibition. Large decrease in affinity for 2-oxoglutarate. Almost no effect on affinity for acetyl-CoA and on turnover number.
D92 (vs. gap) binding L-lysine
R133 (≠ F142) binding 2-oxoglutarate
S135 (≠ D144) binding L-lysine
T166 (= T179) binding 2-oxoglutarate; binding L-lysine
H195 (= H207) binding Mg(2+)
H197 (= H209) binding Mg(2+)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
28% identity, 62% coverage: 6:332/526 of query aligns to 5:314/314 of 2zyfA

query
sites
2zyfA

E

K

I

I

Y

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

T

E

Q
|
Q

S

F

E

E

D

K

V

A

N

N

F

F

T

S

I

T

A

Q

D

D

K

K

V

V

K

E

I

I

A

A

E

K

A

A

L

L

Y

D

D

E

F

F

G

G

V

I

R

E

Y

Y

I

I

E

E

G

V

G

T

W

T

P

P

G

V

S

A

N

S

P

P

R

-

D

-

I

-

G

-

F

-

K

Q

A

S

V

R

K

K

G

D

S

A

S

E

V

V

P

-

D

-

H

-

I

L

A

A

A

S

F

L

G

G

S

L

T

-

R

-

R

K

A

A

K

K

R

V

T

V

C

T

D

-

N

-

D

-

E

-

N
x
H

I

I

Q

Q

A

C

L

R

L

L

E

D

V

A

E

A

V

K

P

V

N

A

L

V

T

E

I

T

F

G

G

V

K

Q

T

G

W

I

D

D

L

L

H
x
L

V

F

T

G

E

T

A

S

L

K

K

G

I

R

E

D

L

I

D

P

Q

R

N

I

L

I

E

E

L

E

I

A

N

K

D

E

S

V

L

I

S

A

Y

Y

L

I

K

R

T

E

K

A

V

A

D

P

-

H

-

V

R

E

A

V

F
x
R

Y

F

D

S

A

A

E

E

H

D

F

T

F

F

D

R

G

-

Y

-

K

-

A

-

N

S

K

E

E

E

Y

Q

A

D

L

L

R

L

T

A

L

V

K

Y

A

E

A

A

M

V

D

A

A

P

K

Y

A

V

D

D

C

R

I

V

I

G

L

L

C

A

D

D

T
|
T

N

V

G

G

G

V

T

A

M

T

P

P

A

R

E

Q

I

V

G

Y

S

A

I

L

I

V

D

R

E

E

V

V

R

R

K

R

V

V

T

V

G

G

D

P

-

R

Y

V

P

D

L

I

G

E

I

F

H
|
H

C

G

H
|
H

N

N

D

D

S

T

D

G

C

C

A

A

V

I

A

A

N

N

S

A

V

Y

I

E

A

A

V

I

K

E

H

A

G

G

I

A

V

T

H

H

V

V

Q

D

G

T

T

T

V

I

N

L

G

G

Y

I

G

G

E

E

R

R

C

N

G

G

N

I

A

T

N

P

I

L

-

G

-

F

M

L

S

A

V

R

I

M

P

Y

N

T

L

L

Q

Q

L

P

K

E

Y

Y

G

V

Y

R

E

R

C

K

V

Y

P

-

V

-

D

-

K

K

L

L

K

E

N

M

L

L

R

P

T

E

V

L

S

D

R

R

Y

M

I

V

N

A

E

R

L

M

G

V

N

G

L

V

K

E

H

I

N

P

I

F

H

N

Q

N

P

Y

Y

I

V

T

G

G

R

E

S

T

A

A

F

F

A

S

H

H

K

K

G

A

G

G

V

M

H

H

V

L

S

K

A

A

I

I

M

Y

K

I

N

N

S

P

S

E

T

A

Y

Y

E

E

H

P

I

Y

E

P

P

P

E

E

L

V

V

F

G

G

N

V

R

K

Q

R

R

K

V

L

L

I

S

A

active site: Q16 (= Q17)
binding 2-oxoglutaric acid: R12 (= R13), H72 (≠ N89), L94 (≠ H111), R127 (≠ F142), T160 (= T179), H189 (= H207)
binding magnesium ion: E13 (≠ D14), H189 (= H207), H191 (= H209)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
28% identity, 62% coverage: 6:332/526 of query aligns to 5:312/312 of 2ztjA

query
sites
2ztjA

E

K

I

I

Y

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

T

E

Q
|
Q

S

F

E

E

D

K

V

A

N

N

F

F

T

S

I

T

A

Q

D

D

K

K

V

V

K

E

I

I

A

A

E

K

A

A

L

L

Y

D

D

E

F

F

G

G

V

I

R

E

Y

Y

I

I

E

E

G

V

G

T

W

T

P

P

G

V

S

A

N

S

P

P

R

-

D

-

I

-

G

-

F

-

K

Q

A

S

V

R

K

K

G

D

S

A

S

E

V

V

P

-

D

-

H

-

I

L

A

A

A

S

F

L

G

G

S

L

T

K

R

A

R

K

A

V

K

V

R

T

-
x
H

-

I

T

Q

C

C

D

R

N

L

D

D

E

A

N

A

I

-

Q

K

A

V

L

A

L

V

E

E

V

T

E

G

V

V

P

Q

N

G

L

I

-

D

T

L

I
x
L

F

F

G

G

K

T

T

G

W

R

D

D

L

I

-

P

H

R

V

I

T

I

E

E

A

-

L

-

K

-

I

-

E

E

L

A

D

K

Q

E

N

V

L

I

E

A

L

Y

I

I

N

R

D

E

S

A

L

A

S

P

Y

H

L

V

K

E

T

V

K
x
R

V

-

D

-

R

-

A

-

F

-

Y

F

D

S

A

A

E

E

H

D

F

T

F

F

D

R

G

-

Y

-

K

-

A

-

N

S

K

E

E

E

Y

Q

A

D

L

L

R

L

T

A

L

V

K

Y

A

E

A

A

M

V

D

A

A

P

K

Y

A

V

D

D

C

R

I

V

I

G

L

L

C
x
A

D

D

T
|
T

N

V

G

G

G

V

T

A

M

T

P

P

A

R

E

Q

I

V

G

Y

S

A

I

L

I

V

D

R

E

E

V

V

R

R

K

R

V

V

T

V

G

G

D

P

-

R

Y

V

P

D

L

I

G

E

I

F

H
|
H

C

G

H
|
H

N

N

D

D

S

T

D

G

C

C

A

A

V

I

A

A

N

N

S

A

V

Y

I

E

A

A

V

I

K

E

H

A

G

G

I

A

V

T

H

H

V

V

Q

D

G

T

T

T

V

I

N

L

G

G

Y

I

G

G

E

E

R

R

C

N

G

G

N

I

A

T

N

P

I

L

-

G

-

F

M

L

S

A

V

R

I

M

P

Y

N

T

L

L

Q

Q

L

P

K

E

Y

Y

G

V

Y

R

E

R

C

K

V

Y

P

-

V

-

D

-

K

K

L

L

K

E

N

M

L

L

R

P

T

E

V

L

S

D

R

R

Y

M

I

V

N

A

E

R

L

M

G

V

N

G

L

V

K

E

H

I

N

P

I

F

H

N

Q

N

P

Y

Y

I

V

T

G

G

R

E

S

T

A

A

F

F

A

S

H

H

K

K

G

A

G

G

V

M

H

H

V

L

S

K

A

A

I

I

M

Y

K

I

N

N

S

P

S

E

T

A

Y

Y

E

E

H

P

I

Y

E

P

P

P

E

E

L

V

V

F

G

G

N

V

R

K

Q

R

R

K

V

L

L

I

S

A

active site: Q16 (= Q17)
binding 2-oxoglutaric acid: R12 (= R13), H72 (vs. gap), L94 (≠ I103), R125 (≠ K137), A156 (≠ C177), T158 (= T179), H187 (= H207), H189 (= H209)
binding copper (ii) ion: E13 (≠ D14), H187 (= H207), H189 (= H209)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
29% identity, 61% coverage: 6:324/526 of query aligns to 4:305/347 of 3a9iA

query
sites
3a9iA

E

K

I

I

Y

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

T

E

Q

Q

S

F

E

E

D

K

V

A

N

N

F

F

T

S

I

T

A

Q

D

D

K

K

V

V

K

E

I

I

A

A

E

K

A

A

L

L

Y

D

D

E

F

F

G

G

V

I

R

E

Y

Y

I

I

E

E

G

V

G

T

W

T

P

P

G

V

S

A

N

S

P

P

R

-

D

-

I

-

G

-

F

-

K

Q

A

S

V

R

K

K

G

D

S

A

S

E

V

V

P

-

D

-

H

-

I

L

A

A

A

S

F

L

G

G

S

L

T

-

R

-

R

K

A

A

K

K

R

V

T

V

C

T

D

-

N

-

D

-

E

-

N

H

I

I

Q

Q

A

C

L

R

L

L

E

D

V

A

E

A

V

K

P

V

N

A

L

V

T

E

I

T

F

G

G

V

K

Q

T

G

W

I

D
|
D

L

L

H

L

V

F

T

G

E

T

A

S

L

K

K

Y

I

L

E

D

L

I

D

P

Q

R

N

I

L

I

E

E

L

E

I

A

N

K

D

E

S

V

L

I

S

A

Y

Y

L

I

K

R

T

E

K

A

V

A

D

P

-

H

-

V

R

E

A

V

F

R

Y

F

D
x
S

A

A

E

E

H

D

F

T

F

F

D

R

G

-

Y

-

K

-

A

-

N

S

K

E

E

E

Y

Q

A

D

L

L

R

L

T

A

L

V

K

Y

A

E

A

A

M

V

D

A

A

P

K

Y

A

V

D

D

C

R

I

V

I

G

L

L

C

A

D

D

T
|
T

N

V

G

G

G

V

T

A

M

T

P

P

A

R

E

Q

I

V

G

Y

S

A

I

L

I

V

D

R

E

E

V

V

R

R

K

R

V

V

T

V

G

G

D

P

-

R

Y

V

P

D

L

I

G

E

I

F

H
|
H

C

G

H
|
H

N

N

D

D

S

T

D

G

C

C

A

A

V

I

A

A

N

N

S

A

V

Y

I

E

A

A

V

I

K

E

H

A

G

G

I

A

V

T

H

H

V

V

Q

D

G

T

T

T

V

I

N

L

G

G

Y

I

G

G

E

E

R

R

C

N

G

G

N

I

A

T

N

P

I

L

-

G

-

F

M

L

S

A

V

R

I

M

P

Y

N

T

L

L

Q

Q

L

P

K

E

Y

Y

G

V

Y

R

E

R

C

K

V

Y

P

-

V

-

D

-

K

K

L

L

K

E

N

M

L

L

R

P

T

E

V

L

S

D

R

R

Y

M

I

V

N

A

E

R

L

M

G

V

N

G

L

V

K

E

H

I

N

P

I

F

H

N

Q

N

P

Y

Y

I

V

T

G

G

R

E

S

T

A

A

F

F

A

S

H

H

K

K

G

A

G

G

V

M

H

H

V

L

S

K

A

A

I

I

M

Y

K

I

N

N

S

P

S

E

T

A

Y

Y

E

E

H

P

I

Y

E

P

P

P

E

E

L

V

V

F

G

G

binding cobalt (ii) ion: E12 (≠ D14), H188 (= H207), H190 (= H209)
binding lysine: R11 (= R13), D91 (= D109), S128 (≠ D144), T159 (= T179), H188 (= H207), H190 (= H209)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
25% identity, 67% coverage: 3:352/526 of query aligns to 2:348/380 of 4ov9A

query
sites
4ov9A

K

K

R

T

V

I

E

H

I

I

Y

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

T

N

Q
|
Q

S

A

E

L

D

K

V

R

N

P

F

W

T

T

I

I

A

D

D

E

K

K

V

I

K

E

I

V

A

F

E

D

A

L

L

L

Y

V

D

E

F

L

G

N

V

V

R

D

Y

G

I

I

E

E

G

V

G

G

W

F

P

P

G

S

S

S

N

N

P

E

R

T

D

E

I

F

G

H

F

T

F

C

K

Q

A

V

V

L

K

S

G

K

S

R

S

A

V

P

P

K

D

G

D

K

H

P

I

I

A

A

F
x
L

G

S

S

-

T

-

R

-

A

-

K

-

R

R

T

A

C

N

D

Q

N

N

D

E

E

I

N

A

I

V

-

T

-

W

Q

E

A

A

L

I

L

Q

E

K

V

A

E

D

V

C

P

P

N

R

L

M

T

H

I

I

F

V

G

Y

K

P

T

V

W

S

D

D

L

F

H

S

V

I

T

K

E

H

A

V

L

L

K

K

I

I

E

S

L

E

D

K

Q

E

N

V

L

L

E

Q

L

K

I

I

N

R

D

N

S

S

L

I

S

S

Y

F

L

A

K

R

T

S

K

I

V

V

D

G

R

P

A

G

F

I

-

E

-

I

-

Q

Y

F

D

S

A

G

E

E

H

H

F

F

F

G

D

D

G

A

Y

I

K

E

A

-

N

N

K

F

E

A

Y

F

A

T

L

K

R

E

T

A

L

F

K

L

A

T

A

A

M

I

D

E

A

A

K

G

A

A

D

N

C

I

I

I

I

N

L

L

C

P

D

N

T
|
T

N

V

G

E

G

R

T

Y

M

R

P

P

A

M

E

V

I

F

G

V

S

N

I

M

I

V

D

K

E

E

V

I

R

K

K

D

V

V

T

V

G

K

D

D

Y

K

P

A

L

I

-

I

G

S

I

I

H
|
H

C

T

H
|
H

N

N

D

D

S

L

D

G

C

M

A

A

V

T

A

A

N

T

S

S

V

V

I

E

A

S

V

V

K

Y

H

V

G

G

I

A

V

E

H

Q

V

I

Q

E

G

V

T

A

V

L

N

N

G

G

Y

L

G

G

E

E

R

R

C

A

G

G

N

N

A

T

N

N

I

L

M

Y

S

E

V

T

I

A

P

-

N

-

L

I

Q

A

L

L

K

H

Y

Q

G

N

Y

G

E

E

C

N

V

L

P

N

V

I

D

N

K

-

L

F

K

Q

N

R

L

I

R

Y

T

P

V

T

S

A

R

K

Y

R

I

I

N

S

E

E

L

L

G

T

N

G

L

I

K

P

H

I

N

G

I

E

H

K

Q

T

P

P

Y

I

V

I

G

G

R

E

S

D

A

I

F

F

A

S

H

H

K

R

G

S

G

G

V

I

H

H

V

-

S

Q

A

T

I

L

M

H

K

Q

N

S

S

K

S

G

T

A

Y

Y

E

R

H

T

I

F

E

S

P

P

E

E

L

F

V

V

G

G

-

R

-

M

N

D

R

K

Q

E

R

T

V

I

L

S

L

F

S

T

D

N

L

Q

S

S

G

G

K

H

S

K

N

A

L

I

I

E

Y

F

K

L

A

L

K

H

D

Q

F

R

G

G

L

I

D

Q

V

V

D

S

active site: Q16 (= Q17)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R13), L73 (≠ F74), T176 (= T179), H205 (= H207), H207 (= H209)
binding zinc ion: D13 (= D14), H205 (= H207), H207 (= H209)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
25% identity, 67% coverage: 3:352/526 of query aligns to 2:346/379 of 4ov4A

query
sites
4ov4A

K

K

R

T

V

I

E

H

I

I

Y

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

T

N

Q
|
Q

S

A

E

L

D

K

V

R

N

P

F

W

T

T

I

I

A

D

D

E

K

K

V

I

K

E

I

V

A

F

E

D

A

L

L

L

Y

V

D

E

F

L

G

N

V

V

R

D

Y

G

I

I

E

E

G

V

G

G

W

F

P

P

G

S

S

S

N

N

P

E

R

T

D

E

I

F

G

H

F

T

F

C

K

Q

A

V

V

L

K

S

G

K

S

R

S

A

V

P

P

K

D

G

D

K

H

P

I

I

A

A

F

L

G

S

S

-

T

-

R

-

A

-

K

-

R

R

T

A

C

N

D

Q

N

N

D

E

E

I

N

A

I

V

-

T

-

W

Q

E

A

A

L

I

L

Q

E

K

V

A

E

D

V

C

P

P

N

R

L

M

T

H

I

I

F

V

G

Y

K

P

T

V

W

S

D

D

L

F

H

S

V

I

T

K

E

H

A

V

L

L

K

K

I

I

E

S

L

E

D

K

Q

E

N

V

L

L

E

Q

L

K

I

I

N

R

D

N

S

S

L

I

S

S

Y

F

L

A

K

R

T

S

K

I

V

V

D

G

R

P

A

G

F

I

-

E

-

I

-

Q

Y

F

D

S

A

G

E

E

H

H

F

F

F

G

D

D

G

A

Y

I

K

E

A

-

N

N

K

F

E

A

Y

F

A

T

L

K

R

E

T

A

L

F

K

L

A

T

A

A

M

I

D

E

A

A

K

G

A

A

D

N

C

I

I

I

I

N

L

L

C
x
P

D

N

T
|
T

N

V

G

E

G

R

T

Y

M

R

P

P

A

M

E

V

I

F

G

V

S

N

I

M

I

V

D

K

E

E

V

I

R

K

K

D

V

V

T

V

G

K

D

D

Y

K

P

A

L

I

-

I

G

S

I

I

H
|
H

C

T

H
|
H

N

N

D

D

S

L

D

G

C

M

A

A

V

T

A

A

N

T

S

S

V

V

I

E

A

S

V

V

K

Y

H

V

G

G

I

A

V

E

H

Q

V

I

Q

E

G

V

T

A

V

L

N

N

G

G

Y

L

G

G

E

E

R

R

C

A

G

G

N

N

A

T

N

N

I

L

M

Y

S

E

V

T

I

A

P

-

N

-

L

I

Q

A

L

L

K

H

Y

Q

G

N

Y

G

E

E

C

N

V

L

P

N

V

I

D

N

K

-

L

F

K

Q

N

R

L

I

R

Y

T

P

V

T

S

A

R

K

Y

R

I

I

N

S

E

E

L

L

G

T

N

G

L

I

K

P

H

I

N

G

I

E

H

K

Q

T

P

P

Y

I

V

I

G

G

R

E

S

D

A

I

F

F

A

S

H

H

K

R

G

S

G

G

V

I

H

H

V

Q

S

H

A

-

I

-

M

-

K

Q

N

S

S

K

S

G

T

A

Y

Y

E

R

H

T

I

F

E

S

P

P

E

E

L

F

V

V

G

G

-

R

-

M

N

D

R

K

Q

E

R

T

V

I

L

S

L

F

S

T

D

N

L

Q

S

S

G

G

K

H

S

K

N

A

L

I

I

E

Y

F

K

L

A

L

K

H

D

Q

F

R

G

G

L

I

D

Q

V

V

D

S

active site: Q16 (= Q17)
binding 3-methyl-2-oxobutanoic acid: R12 (= R13), P174 (≠ C177), T176 (= T179), H205 (= H207), H207 (= H209)
binding zinc ion: D13 (= D14), H205 (= H207), H207 (= H209)

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
28% identity, 61% coverage: 2:324/526 of query aligns to 1:306/308 of 3rmjB

query
sites
3rmjB

S

T

K

N

R

R

V

V

E

I

I

I

Y

F

D

D

T

T

L

L

R

R

D
|
D

G

G

T

E

Q
|
Q

S

S

E

P

D

G

V

A

N

A

F

M

T

T

I

K

A

E

D

E

K

K

V

I

K

R

I

V

A

A

E

R

A

Q

L

L

Y

E

D

K

F

L

G

G

V

V

R

D

Y

I

I

I

E

E

G

A

G

G

W

F

P

A

G

A

S

A

N

S

P

P

R

G

D

D

I

-

G

-

F

-

F

F

K

E

A

A

V

V

K

N

G

A

S

I

S

A

V

K

P

T

D

I

D

T

H

K

I

S

A

T

A

V

F

C

G

S

S

L

T

S

R

R

R

A

A

I

K

E

R

R

T

-

C

-

D

D

N

I

D

R

E

Q

N

A

I

G

Q

E

A

A

L

V

L

A

E

P

V

A

E

P

V

K

P

K

N

R

L

I

T

H

I

T

F

F

G

I

K

A

T

T

W

S

D

P

L

I

H

H

V

M

T

E

E

Y

A

K

L

L

K

K

I

M

E

K

L

P

D

K

Q

Q

N

V

L

I

E

E

L

A

I

A

N

V

D

K

S

A

L

V

S

K

Y

I

L

A

K

R

T

E

K

Y

V

T

D

D

R

D

A

V

F

E

Y

F

D

S

A

C

E

E

H

-

F

-

D

D

G

A

Y

L

K

R

A

S

N

E

K

I

E

D

Y

F

A

L

L

A

R

E

T

I

L

C

K

G

A

A

A

V

M

I

D

E

A

A

K

G

A

A

D

T

C

T

I

I

I

N

L

I

C

P

D

D

T

T

N

V

G

G

G

Y

T

S

M

I

P

P

A

Y

E

K

I

T

G

E

S

E

I

F

D

R

E

E

V

L

R

I

K

A

V

K

T

T

-

P

-

N

-

G

G

G

D

K

Y

V

P

V

L

W

G

S

I

A

H
|
H

C

C

H
|
H

N

N

D

D

S

L

D

G

C

L

A

A

V

V

A

A

N

N

S

S

V

L

I

A

A

A

V

L

K

K

H

G

G

G

I

A

V

R

H

Q

V

V

Q

E

G

C

T

T

V

V

N

N

G

G

Y

L

G

G

E

E

R

R

C

A

G

G

N
|
N

A

A

N

S

I

V

M

E

S

E

V

I

I

V

P

M

N

A

L

L

Q

K

L

V

K

R

-

H

-

D

-

L

Y

F

G

G

Y

L

E

E

C

-

V

T

P

G

V

I

D

D

K

T

L

T

K

Q

N

I

L

V

R

P

T

S

V

-

S

S

R

K

Y

L

I

V

N

S

E

T

L

I

G

T

N

G

L

Y

K

P

H

V

N

Q

I

P

H

N

Q

K

P

A

Y

I

V

V

G

G

R

A

S

N

A

A

F

F

A

S

H

H

K

E

G

-

V

-

H

-

V

-

S

-

A

-

I

-

M

-

K

-

N

-

S

-

T

T

Y

Y

E

E

H

I

I

M

E

S

P

A

E

E

L

S

V

V

G

G

active site: Q16 (= Q17)
binding manganese (ii) ion: D13 (= D14), H201 (= H207), H203 (= H209), N237 (= N243)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
23% identity, 96% coverage: 4:510/526 of query aligns to 7:502/516 of Q8F3Q1

query
sites
Q8F3Q1

R

R

V

L

E

E

I

I

Y

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

T

E

Q

Q

S

T

E

R

D

G

V

V

N

S

F

F

T

S

I

T

A

S

D

E

K

K

V

L

K

N

I

I

A

A

E

K

A

F

L

L

Y

L

D

Q

-

K

F

L

G

N

V

V

R

D

Y

R

I

V

E

E

G

-

W

-

P

-

G

-

S

-

N

-

P

-

R

-

D

-

I

I

G

A

F

S

F

A

K

R

A

V

V

S

K

K

G

G

S

E

S

L

V

E

P

T

D

V

D

Q

H

K

I

I

A

M

A

E

F

W

G

A

S

A

T

T

R

E

R

Q

A

L

K

T

R

E

T

R

-

I

-

E

-

I

-
x
L

-

G

-
x
F

C

V

D

D

N

G

D

N

E

K

N

T

I

V

Q

D

A

W

L

I

L

K

E

D

V

S

E

G

V

A

P

K

N

V

L

L

T

N

I

L

F
x
L

G

T

K

K

T

G

W

S

D

L

L

H

H

H

V

L

T

E

E

K

A

Q

L

L

K

G

I

K

E

T

L

P

D

K

Q

E

N

F

L

F

E

T

L

D

I

V

N

S

D

F

S

V

L

I

S

E

Y

Y

-

A

L

I

K

K

T

S

K

G

V

L

D

K

R

I

A

N

F

V

Y
|
Y

D

-

A

L

E
|
E

H

D

F

W

F

S

D

N

G

G

Y

F

K

R

A

N

N

S

K

P

E

D

Y

Y

A

V

L

K

R

S

T

L

L

V

K

E

A

H

A

L

M

S

D

K

A

E

K

H

A

I

D

E

C

R

I

I

I

F

L

L

C

P

D

D

T
|
T

N

L

G

G

G

V

T

L

M

S

P

P

A

E

E

E

I

T

G

F

S

Q

I

G

I

V

D

D

E

S

V

L

R

I

K

Q

V

K

T

Y

G

P

D

D

Y

I

P

H

L

F

G

E

I

F

H

H

C

G

H

H

N

N

D

D

S

Y

D

D

C

L

A

S

V

V

A

A

N

N

S

S

V

L

I

Q

A

A

V

I

K

R

H

A

G

G

I

V

V

K

H

G

V

L

Q

H

G

A

T

S

V

I

N

N

G

G

Y

L

G

G

E

E

R

R

C

A

G

G

N

N

A

T

N

P

I

L

M

E

S

A

V

L

I

V

P

T

N

T

L

I

Q

H

L

D

K

K

Y

S

G

N

Y

S

E

K

C

T

V

-

P

N

V

I

D

N

K

E

L

I

K

A

N

-

L

I

R

T

T

E

V

A

S

S

R

R

Y

L

I

V

N

E

E

V

L

F

G

S

N

G

L

K

K

R

H

I

N

S

I

A

H

N

Q

R

P

P

Y

I

V

V

G

G

R

E

S

D

A

V

F

F

A

T

H

Q

K

T

G

A

G

G

V

V

H
|
H

V

A

S
x
D

A

G

I

D

M

K

K

K

N

G

S
x
N

S
x
L

T
x
Y

Y

A

E

N

H

P

I

I

E

L

P

P

E

E

L

R

V

F

G

G

N

R

R

K

Q

R

R

S

V

Y

L

A

L

L

S

G

D

K

L

L

S

A

G

G

K

K

S

A

N

S

L

I

I

S

Y

E

K

N

A

V

K

K

D

Q

F

L

G

G

L

M

D

V

V

L

D

-

S

-

S

S

D

E

P

V

K

V

I

L

N

Q

A

K

V

V

V

L

E

E

R

R

L

V

K

I

E

E

L

L

E

G

N

D

K

Q

G

N

F

K

Q

L

F

V

E

T

G

P

A

E

E

D

A

L

S

P

F

F

E

-

L

-

L

I

M

I

R

A

K

D

T

V

M

S

G

G

T

-

F

-

T

-

P

-

F

-

D

-

S

R

I

T

S

G

Y

E

R

K

V

V

I

L

D

T

E

I

M

K

N

S

T

C

N

N

M

I

G

H

S

S

P

G

L

I

A

G

-

I

-

R

-

P

E

H

A

A

T

Q

V

I

M

E

I

L

K

E

V

Y

D

Q

G

G

E

K

Q

I

E

H

H

K

T

E

A

I

A

S

A

E

G

G

N

D

G

G

P

G

V
x
Y

N
x
D

A

A

I

F

D

M

N

N

A

A

I

L

R

T

K

K

A

I

L

T

L

N

N

R

F

L

Y

G

P

I

N

S

L

I

K

P

D

-

M

-

E

K

L
|
L

V

I

D

D

Y
|
Y

K

E

V

V

R

R

I
|
I

L

P

T

P

T

G

G

G

T

K

G

-

T

-

E

-

A

-

V

-

T
|
T

R

D

V

A

L

L

V
|
V

E

E

S

T

K

R

D

I

T

T

-

W

-

N

-

K

-

S

-

L

-

D

-

L

-

E

D

D

G

Q

T

T

W

F

G

K

T

T

V

M

G

G

V

V

A

H

T
x
P

N

D

I
x
Q

V

T

D

V

A

A

S

A

Y

V

Q

H

A

A

R16 (= R13) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 13:14) binding pyruvate
D17 (= D14) 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 (vs. gap) 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 (vs. gap) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ F104) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (= Y143) 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 (= E146) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T179) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H304) mutation H->A,N: Loss of activity.
D304 (≠ S306) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ S312) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ S313) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ T314) mutation to A: Loss of activity.
Y430 (≠ V440) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (≠ N441) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L463) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y466) 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 (= I470) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (= T481) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (= V485) mutation to A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
P493 (≠ T501) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
Q495 (≠ I503) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
25% identity, 69% coverage: 7:368/526 of query aligns to 14:350/370 of 3mi3A

query
sites
3mi3A

I

I

Y

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

T

E

Q
|
Q

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F

E

A

D

N

V

A

N

F

F

F

T

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I

T

A

E

D

K

K

K

V

I

K

Q

I

I

A

A

E

K

A

A

L

L

Y

D

D

N

F

F

G

G

V

V

R

D

Y

Y

I

I

E

E

G

L

G

T

W

S

P

P

G

V

S

A

N

S

P

E

R

Q

D

-

I

-

G

-

F

-

K

-

A

-

V

-

K

-

G

-

S

S

S

R

V

Q

P

D

D

C

D

E

H

A

I

I

A

C

A

K

F

L

G

G

S

L

T

K

R

C

R

K

-

I

-

L

A

T

K

H

R

I

T

R

C

C

D

H

N

M

D

D

E

D

N

A

I

-

Q

R

A

V

L

A

L

V

E

E

V

T

E

G

V

V

P

D

N

G

L

V

T

-

I

-

F

-

G

-

K

-

T

-

W

-

D
|
D

L

V

H

V

V

I

T

G

E

T

A

S

L

M

K

T

I

Y

E

I

L

I

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D

Q

S

N

A

L

T

E

E

L

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I

I

N

N

D

-

S

-

L

-

S

-

Y

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K

K

V

G

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I

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R

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F

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A

S

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E

H

-

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-

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F

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A

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E

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Y

D

A

L

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L

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L

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Y

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K

A

A

A

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M

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K

G

A

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D

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I

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T
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T

N

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T

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P

A

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E

Q

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L

I

I

D

R

E

T

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L

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R

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G

V

V

T

V

G

S

D

-

Y

C

P

D

L

I

G

E

I

C

H
|
H

C

F

H
|
H

N

N

D

D

S

T

D

G

C

M

A

A

V

I

A

A

N

N

S

A

V

Y

I

C

A

A

V

L

K

E

H

A

G

G

I

A

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H

H

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I

Q

D

G

T

T

S

V

I

N

L

G

G

Y

I

G

G

E

E

R

R

C

N

G

G

N

I

A

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N

P

I

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A

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I

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A

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R

L

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L

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T

Y

D

G

R

Y

E

E

Y

C

I

V

T

P

H

V

K

D

Y

K

K

L

L

K

N

N

Q

L

L

R

R

T

E

V

L

S

E

R

N

Y

L

I

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N

A

E

D

L

A

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N

E

L

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Q

H

I

N

P

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H

N

Q

N

P

Y

Y

I

V

T

G

G

R

M

S

C

A

A

F

F

A

T

H

H

K

K

G

A

G

G

V

I

H

H

V

A

S

K

A

A

I

I

M

L

K

A

N

N

S

P

S

S

T

T

Y

Y

E

E

H

I

I

L

E

K

P

P

E

E

L

D

V

F

G

G

N

M

R

S

Q

R

R

Y

V

V

L

H

L

V

-

G

S

S

D

R

L

L

S

T

G

G

K

W

S

N

N

A

L

I

I

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Y

S

K

R

A

A

K

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D

Q

F

L

G

N

L

L

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H

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L

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-

S

-

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A

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R

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K

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L

active site: Q24 (= Q17)
binding lysine: R20 (= R13), D100 (= D109), T163 (= T179), H190 (= H207), H192 (= H209)
binding zinc ion: E21 (≠ D14), H190 (= H207), H192 (= H209)

3ivsA Homocitrate synthase lys4 (see paper)
25% identity, 69% coverage: 7:368/526 of query aligns to 14:345/364 of 3ivsA

query
sites
3ivsA

I

I

Y

I

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T

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L

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x
E

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-

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M

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A

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A

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A

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N

G

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-

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-

E

-

A

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-

E

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-

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-

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A

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A

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D

-

Y

C

P

D

L

I

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E

I

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H
|
H

C

F

H
|
H

N

N

D

D

S

T

D

G

C

M

A

A

V

I

A

A

N

N

S

A

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Y

I

C

A

A

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E

H

A

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G

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A

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H

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D

G

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T

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I

N

L

G

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Y

I

G

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E

R

R

C

N

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G

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A

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G

R

Y

E

E

Y

C

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P

H

V

K

D

Y

K

K

L

L

K

N

N

Q

L

L

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R

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E

V

L

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E

R

N

Y

L

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N

A

E

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L

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L

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N

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Y

I

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T

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G

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C

A

A

F

F

A

T

H

H

K

K

G

A

G

G

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H

H

V

A

S

K

A

A

I

I

M

L

K

A

N

N

S

P

S

S

T

T

Y

Y

E

E

H

I

I

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K

P

P

E

E

L

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G

G

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R

R

Y

V

V

L

H

L

V

-

G

S

S

D

R

L

L

S

T

G

G

K

W

S

N

N

A

L

I

I

K

Y

S

K

R

A

A

K

E

D

Q

F

L

G

N

L

L

D

H

V

L

D

Q

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A

S

K

D

E

P

L

K

T

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N

-

A

-

V

-

E

-

R

R

L

I

K

K

E

K

L

L

active site: Q24 (= Q17)
binding cobalt (ii) ion: E21 (≠ D14), H188 (= H207), H190 (= H209)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
26% identity, 69% coverage: 7:368/526 of query aligns to 37:384/418 of Q9Y823

query
sites
Q9Y823

I

I

Y

I

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R

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x
E

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E

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I

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L

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x
H

R

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H

N

M

D

D

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D

N

-

I

A

Q

R

A

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A

L

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E

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E

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P

D

N

G

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x
D

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L

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x
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x
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E
|
E

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T

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C

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D

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x
E

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|
H

C

F

H
|
H

N

N

D

D

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T

D

G

C

M

A

A

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I

A

A

N

N

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A

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C

A

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A

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G

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A

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N

L

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Y

I

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E

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N

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A

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Y

D

G

R

Y

E

E

Y

C

I

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H

V

K

D

Y

K

K

L

L

K

N

N

Q

L

L

R
|
R

T

E

V

L

S

E

R

N

Y

L

I

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N

A

E

D

L

A

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N

E

L

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I

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H

N

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Y

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A

A

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F

A

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H

H

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K

G

A

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H

H

V

A

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K

A

A

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I

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K

A

N

N

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Y
|
Y

E

E

H

I

I

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P

E

E

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F

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G

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H

L

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-

G

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L

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G

G

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W

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N

N

A

L

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A

A

K

E

D
x
Q

F

L

G

N

L

L

D

H

V

L

D

-

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-

S

T

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D

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A

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A

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K

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K

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L

R43 (= R13) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D14) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q17) mutation to A: Abolishes the catalytic activity.
E74 (= E44) 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 (≠ K81) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (vs. gap) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ F142) 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 (≠ D144) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E146) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T179) 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 (≠ G205) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H207) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H209) binding 2-oxoglutarate; binding Zn(2+)
R288 (= R271) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y315) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ D346) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
26% identity, 69% coverage: 7:368/526 of query aligns to 32:379/400 of 3ivtB

query
sites
3ivtB

I

I

Y

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

T

E

Q
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Q

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F

E

A

D

N

V

A

N

F

F

F

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I

T

A

E

D

K

K

K

V

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I

A

A

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A

A

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L

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D

D

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F

F

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G

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Y

Y

I

I

E

E

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L

G

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P

G

-

S

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N

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A

A

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A

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L

active site: Q42 (= Q17)
binding 2-oxoglutaric acid: R38 (= R13), H98 (≠ K81), R158 (≠ F142), S160 (≠ D144), T192 (= T179), H219 (= H207), H221 (= H209)
binding zinc ion: E39 (≠ D14), H219 (= H207), H221 (= H209)

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
23% identity, 58% coverage: 4:307/526 of query aligns to 1:299/311 of 3bliA

query
sites
3bliA

R

R

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|
H

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A

A

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A

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G

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N

N

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A

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G

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A

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L

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A

A

active site: Q14 (= Q17)
binding acetyl coenzyme *a: Q14 (= Q17), R47 (≠ K59), V48 (≠ A60), E140 (= E146)
binding pyruvic acid: R10 (= R13), Y138 (= Y143), P171 (≠ C177), T173 (= T179)
binding zinc ion: D11 (= D14), H201 (= H207), H203 (= H209)

3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
22% identity, 96% coverage: 12:515/526 of query aligns to 62:572/576 of 3hpzB

query
sites
3hpzB

L

L

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H

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binding Bromopyruvate: E201 (≠ D150), P235 (≠ C177), T237 (= T179), H268 (= H207), H270 (= H209)
binding zinc ion: D64 (= D14), H268 (= H207), H270 (= H209)

3figB Crystal structure of leucine-bound leua from mycobacterium tuberculosis (see paper)
22% identity, 96% coverage: 12:515/526 of query aligns to 62:572/577 of 3figB

query
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3figB

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binding leucine: G501 (= G438), P502 (= P439), L503 (≠ V440), A504 (≠ N441), D531 (≠ T475), A533 (≠ T477), P558 (≠ T501), I560 (= I503)
binding zinc ion: D64 (= D14), H268 (= H207), H270 (= H209)

Query Sequence

>WP_013010707.1 NCBI__GCF_000025725.1:WP_013010707.1
MSKRVEIYDTTLRDGTQSEDVNFTIADKVKIAEALYDFGVRYIEGGWPGSNPRDIGFFKA
VKGSSVPDDHIAAFGSTRRAKRTCDNDENIQALLEVEVPNLTIFGKTWDLHVTEALKIEL
DQNLELINDSLSYLKTKVDRAFYDAEHFFDGYKANKEYALRTLKAAMDAKADCIILCDTN
GGTMPAEIGSIIDEVRKVTGDYPLGIHCHNDSDCAVANSVIAVKHGIVHVQGTVNGYGER
CGNANIMSVIPNLQLKYGYECVPVDKLKNLRTVSRYINELGNLKHNIHQPYVGRSAFAHK
GGVHVSAIMKNSSTYEHIEPELVGNRQRVLLSDLSGKSNLIYKAKDFGLDVDSSDPKINA
VVERLKELENKGFQFEGAEASFELLMRKTMGTFTPFFDSISYRVIDEMNTNMGSPLAEAT
VMIKVDGEQEHTAAAGNGPVNAIDNAIRKALLNFYPNLKDMELVDYKVRILTTGTGTEAV
TRVLVESKDTDGTWGTVGVATNIVDASYQALMDSIEYKLLKDKEKE

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