SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013834785.1 NCBI__GCF_000214825.1:WP_013834785.1 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 MC58) (see 2 papers)
63% identity, 100% coverage: 3:516/516 of query aligns to 5:517/517 of Q9JZG1

query
sites
Q9JZG1

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I

D16 (= D14) binding Mn(2+)
H204 (= H202) binding Mn(2+)
H206 (= H204) binding Mn(2+)
N240 (= N238) binding Mn(2+)
366:517 (vs. 364:516, 50% identical) Required for the condensation reaction. Not required to bind substrate

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
64% identity, 62% coverage: 3:322/516 of query aligns to 2:308/308 of 3rmjB

query
sites
3rmjB

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active site: Q16 (= Q17)
binding manganese (ii) ion: D13 (= D14), H201 (= H202), H203 (= H204), N237 (= N238)

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
49% identity, 74% coverage: 2:381/516 of query aligns to 15:408/409 of 6e1jA

query
sites
6e1jA

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E

D

L

L

A

T

D

K

R

Q

K

K

H

K

E

R

I

V

Y

T

D

D

E

D

D

D

L

L

Q

K

A

A

L

L

V

V

T

T

binding coenzyme a: Q30 (= Q17), F60 (= F47), S63 (≠ A50), I95 (≠ L73), R97 (= R75), F121 (= F99), K132 (= K110), L133 (= L111), S322 (= S297), G323 (= G298), I324 (= I299), D327 (= D302), K331 (= K306), L359 (≠ H331), R362 (= R334), H363 (≠ N335)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P169), T194 (= T171), H225 (= H202), H227 (= H204)
binding manganese (ii) ion: D27 (= D14), V82 (vs. gap), E84 (vs. gap), H225 (= H202), H227 (= H204)

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)
47% identity, 73% coverage: 2:380/516 of query aligns to 82:474/503 of Q9FN52

query
sites
Q9FN52

K

K

D

N

H

Y

L

V

I

R

I

V

F

L

D

D

T

T

L

L

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D

D

G

G

E

E

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Q

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S

P

P

G

G

A

A

S

A

M

L

T

T

K

P

E

P

E

Q

K

K

V

L

R

E

I

I

A

A

K

R

Q

Q

L

L

E

A

K

K

M

L

R

R

V

V

D

D

V

I

I

M

E

E

A

V

G

G

F

F

P

P

A

V

A

S

S

S

D

E

G

E

D

E

F

F

E

E

S

A

V

I

Q

K

A

T

V

I

A

A

K

K

V

T

I

V

K

G

D

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

V

S

P

T

V

V

I

C

C

G

G

L

I

A

A

R

R

A

C

V

K

E

K

H

R

D

D

I

I

V

E

K

A

A

T

G

W

Q

E

A

A

I

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A

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P

Y

A

A

N

K

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R

G

P

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V

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M

T

L

F

F

I

T

A

S

T

T

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S

P

E

I

I

H

H

M

M

E

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M

Y

K

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L

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M

K

T

T

P

K

D

E

Q

E

V

V

V

I

E

E

R

M

A

A

V

V

W

N

A

S

V

V

K

K

R

Y

A

A

R

K

D

S

F

L

T

G

-

F

D

K

N

D

V

I

E

Q

F

F

S

G

P

C

E

E

D

D

A

G

G

G

R

R

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T

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E

L

K

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D

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C

R

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I

I

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A

E

A

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I

I

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K

A

A

G

G

A

A

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A

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|
G

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F

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G

Y

E

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L

F

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A

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Y

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L

I

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N

I

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P

N

G

A

A

D

D

K

D

A

I

I

V

F

F

S

A

A

I

H

H

C

C

H

H

N

N

D

D

L

L

G

G

L

V

A

A

V

T

A

A

N

N

S

T

I

I

A

S

A

G

V

I

T

C

N

A

G

G

A

A

R

R

Q

Q

V

V

E

E

C

V

T

T

I

I

N

N

G

G

L

I

G

G

E

E

R

R

A

S

G

G

N

N

T

A

A

P

L

L

E

E

L

V

V

V

M

M

A

A

V

L

R

K

T

C

R

R

Q

G

D

E

Y

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F

L

-

M

-

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Y

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Q

I

I

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M

T

A

A

T

S

S

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L

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E

I

H

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G

F

M

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Y

V

V

Q

Q

P

P

N

H

K

K

A

P

I

I

V

V

G

G

A

D

N

N

A

C

F

F

A

V

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H

E

E

S

S

G

G

I

I

H

H

Q

Q

D

D

G

G

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I

L

L

K

K

H

N

R

R

E

S

T

T

Y

Y

E

E

I

I

M

L

R

S

A

P

E

E

D

D

V

V

G

G

W

I

S

V

T

K

N

S

K

E

-

N

-

S

-

G

M

I

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

N

H

A

A

F

V

K

K

T

D

R

R

L

L

Q

K

E

E

L

L

G

G

V

Y

E

E

F

I

E

-

T

S

E

D

Q

E

Q

K

L

F

N

N

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D

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I

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L

L

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K

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D

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L

Q

K

A

A

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L

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V

G263 (= G173) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
47% identity, 74% coverage: 3:384/516 of query aligns to 83:478/506 of Q9FG67

query
sites
Q9FG67

D

N

H

Y

L

V

I

R

I

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F

F

D

D

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T

L

L

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|
S

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A

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N

-

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-

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G

-

Y

-

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T

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A

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E

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A

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I

K

R

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A

A

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F

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N

-

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A

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D

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I

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A

I

D

D

K

D

A

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x
A

A

V

H

H

C

C

H

H

N

N

D

D

L

L

G

G

L

L

A

A

V

T

A

A

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N

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S

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I

A

A

A

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N

A

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G

A

A

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I

I

N

N

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G

L

I

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M

A

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G

D

A

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Y

F

V

-

I

-

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A

A

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S

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K

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M

V

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Q

N

E

I

Y

T

T

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G

F

L

S

Y

V

V

Q

Q

P

A

N

H

K

K

A

P

I

I

V

V

G

G

A

A

N

N

A

C

F

F

A

V

H

H

E

E

S

S

G

G

I

I

H

H

Q

Q

D

D

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R

R

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T

T

Y

Y

E

E

I

I

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L

R

S

A

P

E

E

D

D

V

I

G

G

W

I

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-

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-

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-

G

M

L

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V

L

L

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L

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G

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R

N

H

A

A

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E

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F

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L

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N

D

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L

F

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L

L

A

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K

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E

A

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D

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L

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T

E

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A

S

N

D

S102 (= S22) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ S200) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
35% identity, 69% coverage: 7:362/516 of query aligns to 24:370/399 of 6ktqA

query
sites
6ktqA

I

I

F

L

D

D

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S

T

T

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R

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x
E

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G

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A

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F

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P

A

A

A
x
V

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S

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G

D

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I

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Y

E

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I

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R

A

R

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A

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I

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D

E

-

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R

A
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A

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K

-

A

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-

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A

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F

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x
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x
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x
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E

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A

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Y

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A

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A

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A

A

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G

A

A

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x
S

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A

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|
T

V

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L

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F

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L

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E

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R

I

F

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D

A

I

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E

K

-

A

-

I

-

F

F

S

D

A

I

H
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H

C

A

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

V

A

A

N

N

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V

I

L

A

A

V

A

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E

N

G

G

G

A

A

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I

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C

T

T

T

I

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N

N

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G

L

L

G

G

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E

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G

G

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M

A

A

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T

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R

-

Q

-

D

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-

I

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P

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N

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F

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I

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G

G

A

D

N

Y

A

A

F

F

A

V

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A

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H

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A

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E

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M

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F

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K

binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ E137), T156 (≠ S139), E158 (= E141), S184 (≠ N167), T188 (= T171), H216 (= H202), H218 (= H204)
binding coenzyme a: V67 (≠ A50), R96 (= R75), A97 (= A76), F116 (= F99), H128 (≠ L111), E158 (= E141)
binding zinc ion: E31 (≠ D14), H216 (= H202), H218 (= H204)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
31% identity, 72% coverage: 7:379/516 of query aligns to 6:379/380 of 4ov9A

query
sites
4ov9A

I

I

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P

K

K

D

G

S

K

T

P

V

I

C

A

G

A

L
|
L

A

S

R

R

A

A

V

N

E

Q

H

N

D

E

I

I

V

A

K

V

A

T

G

W

Q

E

A

A

I

I

A

Q

P

K

A

A

N

D

S

C

G

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

P

D

I

F

H

S

M

I

E

K

M

H

K

V

L

L

R

K

M

I

T

S

P

E

D

K

Q

E

V

V

V

L

E

Q

R

K

A

I

V

R

W

N

A

S

V

I

K

S

R

F

A

A

R

R

D

S

F

I

T

V

D

G

-

P

-

G

-

I

N

E

V

I

E

Q

F

F

S

S

P

G

E

E

D

H

A

F

G

G

R

D

S

A

-

I

-

E

E

N

L

F

D

A

F

F

L

T

C

K

R

E

V

A

I

F

E

L

A

T

A

A

I

I

D

E

A

A

G

G

A

A

T

N

T

I

I

I

N

N

I

L

P

P

D

N

T
|
T

V

V

G

E

Y

R

N

Y

V

R

P

P

D

M

Q

V

F

F

G

V

Y

N

L

M

F

V

K

K

Q

E

L

I

L

K

E

D

R

V

I

V

P

-

N

-

A

K

D

D

K

K

A

A

I

I

F

I

S

S

A

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

T

A

A

N

T

S

S

I

V

A

E

A

S

V

V

T

Y

N

V

G

G

A

A

R

E

Q

Q

V

I

E

E

C

V

T

A

I

L

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

T

T

A

N

L

L

E

Y

E

E

L

T

V

A

M

I

A

A

V

L

R

H

T

Q

R

N

Q

G

D

E

Y

N

F

L

S

N

V

I

D

N

T

F

R

Q

I

-

H

-

T

-

P

-

E

R

I

I

L

Y

T

P

A

T

S

A

R

K

L

R

V

I

S

S

N

E

I

L

T

T

G

G

F

I

S

P

V

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

A

E

N

D

A

I

F

F

A

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

D

T

G

-

V

L

L

H

K

Q

H

S

R

K

E

G

T

A

Y

Y

E

R

I

T

M

F

R

S

A

P

E

E

D

F

V

V

G

G

W

R

S

M

T

D

N

K

K

E

M

T

V

I

-

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

N

K

A

A

F

I

K

E

T

F

R

L

L

L

Q

H

E

Q

L

R

G

G

V

I

E

Q

F

V

E

-

T

S

E

K

Q

E

Q

G

L

I

N

H

D

H

T

L

F

F

V

S

R

L

F

A

K

K

E

S

L

I

A

S

D

S

R

R

K

E

H

N

-

N

-

R

E

E

I

I

Y

T

D

E

E

A

D

E

L

L

Q

V

A

A

L

L

active site: Q16 (= Q17)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R13), L73 (= L73), T176 (= T171), H205 (= H202), H207 (= H204)
binding zinc ion: D13 (= D14), H205 (= H202), H207 (= H204)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
31% identity, 72% coverage: 7:379/516 of query aligns to 6:377/379 of 4ov4A

query
sites
4ov4A

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

S

A

P

L

G

K

A

R

S

P

M

W

T

T

K

I

E

D

E

E

K

K

V

I

R

E

I

V

A

F

K

D

Q

L

L

L

E

V

K

E

M

L

R

N

V

V

D

D

V

G

I

I

E

E

A

V

G

G

F

F

P

P

A

S

S

N

D

E

G

T

D

E

F

F

E

H

S

T

V

C

Q

Q

A

V

V

L

A

S

K

K

-

R

V

A

I

P

K

K

D

G

S

K

T

P

V

I

C

A

G

A

L

L

A

S

R

R

A

A

V

N

E

Q

H

N

D

E

I

I

V

A

K

V

A

T

G

W

Q

E

A

A

I

I

A

Q

P

K

A

A

N

D

S

C

G

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

P

D

I

F

H

S

M

I

E

K

M

H

K

V

L

L

R

K

M

I

T

S

P

E

D

K

Q

E

V

V

V

L

E

Q

R

K

A

I

V

R

W

N

A

S

V

I

K

S

R

F

A

A

R

R

D

S

F

I

T

V

D

G

-

P

-

G

-

I

N

E

V

I

E

Q

F

F

S

S

P

G

E

E

D

H

A

F

G

G

R

D

S

A

-

I

-

E

E

N

L

F

D

A

F

F

L

T

C

K

R

E

V

A

I

F

E

L

A

T

A

A

I

I

D

E

A

A

G

G

A

A

T

N

T

I

I

I

N

N

I

L

P
|
P

D

N

T
|
T

V

V

G

E

Y

R

N

Y

V

R

P

P

D

M

Q

V

F

F

G

V

Y

N

L

M

F

V

K

K

Q

E

L

I

L

K

E

D

R

V

I

V

P

-

N

-

A

K

D

D

K

K

A

A

I

I

F

I

S

S

A

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

T

A

A

N

T

S

S

I

V

A

E

A

S

V

V

T

Y

N

V

G

G

A

A

R

E

Q

Q

V

I

E

E

C

V

T

A

I

L

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

T

T

A

N

L

L

E

Y

E

E

L

T

V

A

M

I

A

A

V

L

R

H

T

Q

R

N

Q

G

D

E

Y

N

F

L

S

N

V

I

D

N

T

F

R

Q

I

-

H

-

T

-

P

-

E

R

I

I

L

Y

T

P

A

T

S

A

R

K

L

R

V

I

S

S

N

E

I

L

T

T

G

G

F

I

S

P

V

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

A

E

N

D

A

I

F

F

A

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

D

H

G

-

V

-

L

-

K

Q

H

S

R

K

E

G

T

A

Y

Y

E

R

I

T

M

F

R

S

A

P

E

E

D

F

V

V

G

G

W

R

S

M

T

D

N

K

K

E

M

T

V

I

-

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

N

K

A

A

F

I

K

E

T

F

R

L

L

L

Q

H

E

Q

L

R

G

G

V

I

E

Q

F

V

E

-

T

S

E

K

Q

E

Q

G

L

I

N

H

D

H

T

L

F

F

V

S

R

L

F

A

K

K

E

S

L

I

A

S

D

S

R

R

K

E

H

N

-

N

-

R

E

E

I

I

Y

T

D

E

E

A

D

E

L

L

Q

V

A

A

L

L

active site: Q16 (= Q17)
binding 3-methyl-2-oxobutanoic acid: R12 (= R13), P174 (= P169), T176 (= T171), H205 (= H202), H207 (= H204)
binding zinc ion: D13 (= D14), H205 (= H202), H207 (= H204)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
30% identity, 91% coverage: 5:472/516 of query aligns to 8:476/516 of Q8F3Q1

query
sites
Q8F3Q1

L

L

I

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

S

T

P

R

G

G

A

V

S

S

M

F

T

S

K

T

E

S

E

E

K

K

V

L

R

N

I

I

A

A

K

K

-

F

Q

L

L

L

E

Q

K

K

M

L

R

N

V

V

D

D

V

R

I

V

E

E

A

I

G

A

F

S

P

A

A

R

A

V

S

S

D

K

G

G

D

E

F

L

E

E

S

T

V

V

Q

Q

A

-

V

-

A

-

K

K

V

I

I

M

K

E

D

W

S

A

T

A

V

T

C

E

G

Q

L

L

A

T

R

E

A

R

V

I

E

E

H

I

-
x
L

-

G

-
x
F

-

V

D

D

I

G

V

N

K

K

A

T

G

V

Q

D

A

W

I

I

A

K

P

D

A

S

N

G

S

A

G

K

R

V

I

L

H

N

T

L

F
x
L

I

T

A

K

T

G

S

S

P

L

I

H

H

H

M

L

E

E

M

K

K

Q

L

L

R

G

M

K

T

T

P

P

D

K

Q

E

V

F

E

T

R

D

A

V

V

S

W

F

A

V

V

I

K

E

R

Y

A

A

R

I

D

K

F

S

T

G

D

L

N

K

V

I

E

N

F

V

S
x
Y

P

L

E
|
E

D

D

A

W

G

S

-

N

-

G

-

F

R

R

S

N

E

S

L

P

D

D

F

Y

L

V

C

K

R

S

V

L

I

V

E

E

A

H

A

L

I

S

D

K

A

E

G

H

A

I

T

E

T

R

I

I

N

F

I

L

P

P

D

D

T
|
T

V

L

G

G

Y

V

N

L

V

S

P

P

D

E

Q

E

F

T

G

F

Y

Q

L

G

F

V

K

D

Q

S

L

L

L

I

E

Q

R

K

I

Y

P

P

N

D

A

I

D

H

K

-

A

-

I

-

F

F

S

E

A

F

H

H

C

G

H

H

N

N

D

D

L

Y

G

D

L

L

A

S

V

V

A

A

N

N

S

S

I

L

A

Q

A

A

V

I

T

R

N

A

G

G

A

V

R

K

Q

G

V

L

E

H

C

A

T

S

I

I

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

T

T

A

P

L

L

E

E

E

A

L

L

V

V

M

T

A

T

V

I

R

-

T

-

R

-

Q

H

D

D

Y

K

F

S

S

N

V

S

D

K

T

T

R

N

I

I

H

N

T

E

P

I

E

A

I

I

L

T

T

E

A

A

S

S

R

R

L

L

V

V

S

E

N

V

I

F

T

S

G

G

F

K

S

R

V

I

Q

S

P

A

N

N

K

R

A

P

I

I

V

V

G

G

A

E

N

D

A

V

F

F

A

T

H

Q

E

T

S

A

G

G

I

V

H
|
H

Q

A

D
|
D

G

G

V

D

L

K

K

K

H

G

R
x
N

E
x
L

T
x
Y

Y

A

E

N

I

P

M

I

R

L

A

P

E

E

D

R

V

F

G

G

W

-

S

R

T

K

N

R

K

S

M

Y

V

A

L

L

G

G

K

K

H

L

S

A

G

G

R

K

N

A

A

S

F

I

K

S

T

E

R

N

L

V

Q

K

E

Q

L

L

G

G

V

M

E

V

F

L

E

-

T

S

E

E

Q

V

L

L

N

Q

D

K

T

V

F

L

V

E

R

R

F

V

K

I

E

E

L

L

A

G

D

D

R

Q

K

N

H

K

E

L

I

V

Y

T

D

P

E

E

D

D

L

L

Q

P

A

F

L

I

V

I

T

A

E

D

A

V

N

S

I

-

E

G

R

R

V

T

E

G

N

E

E

K

S

V

I

L

R

T

L

I

V

K

A

S

L

C

K

N

V

I

A

H

A

S

E

G

M

I

G

G

E

I

Q

R

P

P

S

H

A

A

T

Q

I

I

T

E

L

L

S

E

V

Y

D

Q

G

G

Q

K

E

I

F

H

T

K

A

E

S

I

A

S

M

E

G

G

G

D

G

G

V

G

V
x
Y

D
|
D

A

A

T

F

F

M

K

N

A

A

I

L

E

T

Q

K

I

I

L

T

N

N

-

R

-

L

-

G

-

I

S

S

K

I

T

P

T

K

L
|
L

E

I

L

D

Y
|
Y

S

E

V

V

S

R

N
x
I

V

P

T

P

N

G

G

G

-

K

T
|
T

D

D

S

A

L

L

G
x
V

E

E

T

T

S

R

V

I

R

T

L

W

E

N

K

K

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 (≠ F99) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ S139) 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 (= E141) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T171) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H300) mutation H->A,N: Loss of activity.
D304 (= D302) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ R308) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ E309) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ T310) mutation to A: Loss of activity.
Y430 (≠ V431) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (= D432) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L448) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y451) 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 (≠ N455) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (= T460) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (≠ G464) 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.

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
30% identity, 70% coverage: 7:366/516 of query aligns to 32:381/400 of 3ivtB

query
sites
3ivtB

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D

active site: Q42 (= Q17)
binding 2-oxoglutaric acid: R38 (= R13), H98 (≠ A76), R158 (≠ E137), S160 (= S139), T192 (= T171), H219 (= H202), H221 (= H204)
binding zinc ion: E39 (≠ D14), H219 (= H202), H221 (= H204)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
30% identity, 70% coverage: 7:366/516 of query aligns to 37:386/418 of Q9Y823

query
sites
Q9Y823

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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 (≠ A76) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ H97) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ E137) 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 (= S139) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E141) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T171) 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 (≠ S200) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H202) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H204) binding 2-oxoglutarate; binding Zn(2+)
R288 (≠ L267) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y311) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ E343) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
30% identity, 70% coverage: 7:366/516 of query aligns to 14:352/370 of 3mi3A

query
sites
3mi3A

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active site: Q24 (= Q17)
binding lysine: R20 (= R13), D100 (≠ H97), T163 (= T171), H190 (= H202), H192 (= H204)
binding zinc ion: E21 (≠ D14), H190 (= H202), H192 (= H204)

3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 72% coverage: 7:375/516 of query aligns to 14:356/364 of 3ivsA

query
sites
3ivsA

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E

A

A

V

I

A

C

K

K

V

L

I

-

K

-

D

-

S

G

T

L

V

K

C

C

G

K

L

I

A

L

R

T

A

H

V

I

E

R

H

C

D

H

I

M

V

D

K

D

A

A

G

R

Q

V

A

A

I

V

A

E

P

T

A

G

N

V

S

D

G

G

R

-

I

V

H

D

T

V

F

V

I

I

A

G

T

T

S

T

P

Y

I

I

H

-

M

-

E

-

M

-

K

-

L

-

R

-

M

-

T

-

P

-

D

-

Q

-

V

-

V

I

E

D

R

S

A

A

V

T

W

E

A

V

V

I

K

N

R

F

A

V

R

K

D

S

F

K

T

G

D

I

N

E

V

V

E

R

F

F

S

S

P

S

E

E

D

D

A

S

G

F

R

R

S

S

E

D

L

L

D

V

F

D

L

L

C

L

R

S

V

L

I

Y

E

K

A

A

A

V

I

D

D

K

A

I

G

G

A

V

T

N

T

R

I

V

N

G

I

I

P

A

D

D

T

T

V

V

G

G

Y

C

N

A

V

T

P

P

D

R

Q

Q

F

V

G

-

Y

Y

L

D

F

L

K

I

Q

R

L

T

L

L

E

R

R

G

I

V

P

V

N

S

A

C

D

D

K

-

A

-

I

-

F

I

S

E

A

C

H
|
H

C

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

A

A

N

N

S

A

I

Y

A

C

A

A

V

L

T

E

N

A

G

G

A

A

R

T

Q

H

V

I

E

D

C

T

T

S

I

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

T

T

A

P

L

L

E

G

E

A

L

L

V

L

M

A

A

R

V

M

R

Y

-

V

T

T

R

D

Q

R

D

E

Y

Y

F

I

S

T

V

H

D

K

T

Y

R

K

I

L

H

N

T

-

P

-

E

Q

I

L

L

R

T

E

A

L

S

E

R

N

L

L

V

V

S

A

N

D

I

A

T

V

G

E

F

V

S

Q

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

M

N

C

A

A

F

F

A

T

H

H

E

K

S

A

G

G

I

I

H

H

Q

A

D

K

G

A

V

I

L

L

K

A

H

N

R

P

E

S

T

T

Y

Y

E

E

I

I

M

L

R

K

A

P

E

E

D

D

V

F

G

G

W

M

S

S

T

R

N

Y

K

V

M

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

K

K

T

S

R

R

L

A

Q

E

E

Q

L

L

G

N

V

L

E

H

F

L

E

-

T

-

E

-

Q

-

Q

Q

L

A

N

K

D

E

T

L

F

T

V

V

R

R

F

I

K

K

E

K

L

L

A

A

D

V

R

R

K

T

H

L

E

A

I

M

Y

D

D

D

E

V

D

D

active site: Q24 (= Q17)
binding cobalt (ii) ion: E21 (≠ D14), H188 (= H202), H190 (= H204)

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
31% identity, 70% coverage: 7:367/516 of query aligns to 6:358/376 of O87198

query
sites
O87198

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

S

F

P

E

G

K

A

A

S

N

M

F

T

S

K

T

E

Q

E

D

K

K

V

V

R

E

I

I

A

A

K

K

Q

A

L

L

E

D

K

E

M

F

R

G

V

I

D

E

V

Y

I

I

E

E

A

V

G

T

F

T

P

P

A

V

A

A

S

S

D

P

G

Q

D

S

F

R

E

K

S

D

V

A

Q

E

A

V

V

L

A

A

K

S

V

L

I

-

K

-

D

-

S

-

T

-

V

-

C

-

G

G

L

L

-

K

A

A

R

K

A

V

V

V

E

T

H
|
H

D

I

I

Q

V

C

K

R

A

L

G

D

Q

A

A

A

I

K

A

V

P

A

A

V

N

E

S

T

G

G

-

V

-

Q

R

G

I

I

H
x
D

T

L

F

L

I

F

A

G

T

T

S

S

P

K

I

Y

H

L

M

R

E

A

M

A

K

H

L

G

R

R

M

D

T

I

P

P

D

-

Q

R

V

I

E

E

R

E

A

A

V

K

W

E

A

V

V

I

K

A

R

Y

A

I

R

R

D

E

F

A

T

A

D

P

N

H

V

V

E

E

-

V

-
x
R

F

F

S
|
S

P

A

E

E

D

D

A

T

G

F

R

R

S

S

E

E

L

E

D

Q

F

D

L

L

C

L

R

A

V

V

I

Y

E

E

A

A

A

-

I

V

D

A

A

P

G

Y

A

V

T

D

T

R

I

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

N

A

V

T

P

P

D

R

Q

Q

F

V

G

Y

Y

A

L

L

F

V

K

R

Q

E

L

V

L

R

E

R

R

V

I

V

-

G

P

P

N

R

A

V

D

D

K

-

A

-

I

-

F

I

S

E

A

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

A

A

N

N

S

A

I

Y

A

E

A

A

V

I

T

E

N

A

G

G

A

A

R

T

Q

H

V

V

E

D

C

T

T

T

I

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

T

T

A

P

L

L

E

G

L

F

V

L

M

A

A

R

V

M

R

Y

T

T

R

L

Q

Q

-

P

D

E

Y

Y

F

V

S

R

V

R

D

K

T

Y

R

K

I

L

H

E

T

M

-

L

P

P

E

E

I

L

L

-

T

-

A

-

S

D

R

R

L

M

V

V

S

A

N

R

I

M

T

V

G

G

F

V

S

E

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

E

N

T

A

A

F

F

A

S

H

H

E

K

S

A

G

G

I

M

H

H

Q

L

D

K

G

A

V

I

L

Y

K

I

H

N

R

P

E

E

T

A

Y

Y

E

E

I

P

M

Y

R

P

A

P

E

E

D

V

V

F

G

G

W

V

S

K

T

R

N

K

K

L

M

I

V

I

L

A

G

S

K

R

H

L

S

T

G

G

R

R

N

H

A

A

F

I

K

K

T

A

R

R

L

A

Q

E

E

E

L

L

G

G

V

L

E

H

F

Y

E

-

T

G

E

E

Q

E

L

L

N

H

D

R

T

V

F

T

V

Q

R

H

F

I

K

K

E

A

L

L

A

A

D

D

R

R

R12 (= R13) binding 2-oxoglutarate
E13 (≠ D14) binding Mg(2+)
H72 (= H79) 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 (≠ H97) binding L-lysine
R133 (vs. gap) binding 2-oxoglutarate
S135 (= S139) binding L-lysine
T166 (= T171) binding 2-oxoglutarate; binding L-lysine
H195 (= H202) binding Mg(2+)
H197 (= H204) binding Mg(2+)

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
32% identity, 57% coverage: 5:300/516 of query aligns to 2:296/311 of 3bliA

query
sites
3bliA

L

L

I

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q
|
Q

S

T

P

R

G

G

A

V

S

S

M

F

T

S

K

T

E

S

E

E

K

K

V

L

R

N

I

I

A

A

K

K

-

F

Q

L

L

L

E

Q

K

K

M

L

R

N

V

V

D

D

V

R

I

V

E

E

A

I

G

A

F

S

P

A

A
x
R

A
x
V

S

S

D

K

G

G

D

E

F

L

E

E

S

T

V

V

Q

Q

A

-

V

-

A

-

K

K

V

I

I

M

K

E

D

W

S

A

T

A

V

T

C

E

G

Q

L

L

A

T

R

E

A

R

V

I

E

E

H

I

-

L

-

G

-

F

-

V

D

D

I

G

V

N

K

K

A

T

G

V

Q

D

A

W

I

I

A

K

P

D

A

S

N

G

S

A

G

K

R

V

I

L

H

N

T

L

F

L

I

T

A

K

T

G

S

S

P

L

I

H

H

H

M

L

E

E

M

K

K

Q

L

L

R

G

M

K

T

T

P

P

D

K

Q

E

V

F

E

T

R

D

A

V

V

S

W

F

A

V

V

I

K

E

R

Y

A

A

R

I

D

K

F

S

T

G

D

L

N

K

V

I

E

N

F

V

S
x
Y

P

L

E
|
E

D

D

A

W

G

S

-

N

-

G

-

F

R

R

S

N

E

S

L

P

D

D

F

Y

L

V

C

K

R

S

V

L

I

V

E

E

A

H

A

L

I

S

D

K

A

E

G

H

A

I

T

E

T

R

I

I

N

F

I

L

P
|
P

D

D

T
|
T

V

L

G

G

Y

V

N

L

V

S

P

P

D

E

Q

E

F

T

G

F

Y

Q

L

G

F

V

K

D

Q

S

L

L

L

I

E

Q

R

K

I

Y

P

P

N

D

A

I

D

H

K

-

A

-

I

-

F

F

S

E

A

F

H
|
H

C

G

H
|
H

N

N

D

D

L

Y

G

D

L

L

A

S

V

V

A

A

N

N

S

S

I

L

A

Q

A

A

V

I

T

R

N

A

G

G

A

V

R

K

Q

G

V

L

E

H

C

A

T

S

I

I

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

T

T

A

P

L

L

E

E

E

A

L

L

V

V

M

T

A

T

V

I

R

-

T

-

R

-

Q

H

D

D

Y

K

F

S

S

N

V

S

D

K

T

T

R

N

I

I

H

N

T

E

P

I

E

A

I

I

L

T

T

E

A

A

S

S

R

R

L

L

V

V

S

E

N

V

I

F

T

S

G

G

F

K

S

R

V

I

Q

S

P

A

N

N

K

R

A

P

I

I

V

V

G

G

A

E

N

D

A

V

F

F

A

T

H

Q

E

T

S

A

G

G

I

V

H

N

active site: Q14 (= Q17)
binding acetyl coenzyme *a: Q14 (= Q17), R47 (≠ A49), V48 (≠ A50), E140 (= E141)
binding pyruvic acid: R10 (= R13), Y138 (≠ S139), P171 (= P169), T173 (= T171)
binding zinc ion: D11 (= D14), H201 (= H202), H203 (= H204)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
30% identity, 70% coverage: 7:367/516 of query aligns to 5:329/347 of 3a9iA

query
sites
3a9iA

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

S

F

P

E

G

K

A

A

S

N

M

F

T

S

K

T

E

Q

E

D

K

K

V

V

R

E

I

I

A

A

K

K

Q

A

L

L

E

D

K

E

M

F

R

G

V

I

D

E

V

Y

I

I

E

E

A

V

G

T

F

T

P

P

A

V

A

A

S

S

D

P

G

Q

D

S

F

R

E

K

S

D

V

A

Q

E

A

V

V

L

A

A

K

S

V

L

I

-

K

-

D

-

S

-

T

-

V

-

C

-

G

G

L

L

-

K

A

A

R

K

A

V

V

V

E

T

H

H

D

I

I

Q

V

C

K

R

A

L

G

D

Q

A

A

A

I

K

A

V

P

A

A

V

N

E

S

T

G

G

-

V

-

Q

R

G

I

I

H
x
D

T

L

F

L

I

F

A

G

T

T

S

S

P

-

I

-

H

-

M

-

E

-

M

-

K

K

L

Y

R

L

M

D

T

I

P

P

D

-

Q

R

V

I

E

E

R

E

A

A

V

K

W

E

A

V

V

I

K

A

R

Y

A

I

R

R

D

E

F

A

T

A

D

P

N

H

V

V

E

E

-

V

-

R

F

F

S
|
S

P

A

E

E

D

D

A

T

G

F

R

R

S

S

E

E

L

E

D

Q

F

D

L

L

C

L

R

A

V

V

I

Y

E

E

A

A

A

-

I

V

D

A

A

P

G

Y

A

V

T

D

T

R

I

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

N

A

V

T

P

P

D

R

Q

Q

F

V

G

Y

Y

A

L

L

F

V

K

R

Q

E

L

V

L

R

E

R

R

V

I

V

-

G

P

P

N

R

A

V

D

D

K

-

A

-

I

-

F

I

S

E

A

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

A

A

N

N

S

A

I

Y

A

E

A

A

V

I

T

E

N

A

G

G

A

A

R

T

Q

H

V

V

E

D

C

T

T

T

I

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

T

T

A

P

L

L

E

G

L

F

V

L

M

A

A

R

V

M

R

Y

T

T

R

L

Q

Q

-

P

D

E

Y

Y

F

V

S

R

V

R

D

K

T

Y

R

K

I

L

H

E

T

M

-

L

P

P

E

E

I

L

L

-

T

-

A

-

S

D

R

R

L

M

V

V

S

A

N

R

I

M

T

V

G

G

F

V

S

E

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

E

N

T

A

A

F

F

A

S

H

H

E

K

S

A

G

G

I

M

H

H

Q

L

D

K

G

A

V

I

L

Y

K

I

H

N

R

P

E

E

T

A

Y

Y

E

E

I

P

M

Y

R

P

A

P

E

E

D

V

V

F

G

G

W

-

S

-

T

-

N

-

K

-

M

-

V

V

L

K

G

G

K

L

H

H

S

Y

G

G

R

-

N

-

A

-

F

-

K

-

T

-

R

-

L

-

Q

-

E

-

L

-

G

-

V

-

E

-

F

-

E

-

T

-

E

E

Q

E

L

L

N

H

D

R

T

V

F

T

V

Q

R

H

F

I

K

K

E

A

L

L

A

A

D

D

R

R

binding cobalt (ii) ion: E12 (≠ D14), H188 (= H202), H190 (= H204)
binding lysine: R11 (= R13), D91 (≠ H97), S128 (= S139), T159 (= T171), H188 (= H202), H190 (= H204)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
31% identity, 61% coverage: 7:320/516 of query aligns to 6:306/314 of 2zyfA

query
sites
2zyfA

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

P

E

G

K

A

A

S

N

M

F

T

S

K

T

E

Q

E

D

K

K

V

V

R

E

I

I

A

A

K

K

Q

A

L

L

E

D

K

E

M

F

R

G

V

I

D

E

V

Y

I

I

E

E

A

V

G

T

F

T

P

P

A

V

A

A

S

S

D

P

G

Q

D

S

F

R

E

K

S

D

V

A

Q

E

A

V

V

L

A

A

K

S

V

L

I

-

K

-

D

-

S

-

T

-

V

-

C

-

G

G

L

L

-

K

A

A

R

K

A

V

V

V

E

T

H
|
H

D

I

I

Q

V

C

K

R

A

L

G

D

Q

A

A

A

I

K

A

V

P

A

A

V

N

E

S

T

G

G

-

V

-

Q

R

G

I

I

H

D

T

L

F
x
L

I

F

A

G

T

T

S

S

P

-

I

-

H

-

M

-

E

-

M

-

K

K

L

G

R

R

M

D

T

I

P

P

D

-

Q

R

V

I

E

E

R

E

A

A

V

K

W

E

A

V

V

I

K

A

R

Y

A

I

R

R

D

E

F

A

T

A

D

P

N

H

V

V

E

E

-

V

-
x
R

F

F

S

S

P

A

E

E

D

D

A

T

G

F

R

R

S

S

E

E

L

E

D

Q

F

D

L

L

C

L

R

A

V

V

I

Y

E

E

A

A

A

-

I

V

D

A

A

P

G

Y

A

V

T

D

T

R

I

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

N

A

V

T

P

P

D

R

Q

Q

F

V

G

Y

Y

A

L

L

F

V

K

R

Q

E

L

V

L

R

E

R

R

V

I

V

-

G

P

P

N

R

A

V

D

D

K

-

A

-

I

-

F

I

S

E

A

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

A

A

N

N

S

A

I

Y

A

E

A

A

V

I

T

E

N

A

G

G

A

A

R

T

Q

H

V

V

E

D

C

T

T

T

I

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

T

T

A

P

L

L

E

G

L

F

V

L

M

A

A

R

V

M

R

Y

T

T

R

L

Q

Q

-

P

D

E

Y

Y

F

V

S

R

V

R

D

K

T

Y

R

K

I

L

H

E

T

M

-

L

P

P

E

E

I

L

L

-

T

-

A

-

S

D

R

R

L

M

V

V

S

A

N

R

I

M

T

V

G

G

F

V

S

E

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

E

N

T

A

A

F

F

A

S

H

H

E

K

S

A

G

G

I

M

H

H

Q

L

D

K

G

A

V

I

L

Y

K

I

H

N

R

P

E

E

T

A

Y

Y

E

E

I

P

M

Y

R

P

A

P

E

E

D

V

V

F

G

G

active site: Q16 (= Q17)
binding 2-oxoglutaric acid: R12 (= R13), H72 (= H79), L94 (≠ F99), R127 (vs. gap), T160 (= T171), H189 (= H202)
binding magnesium ion: E13 (≠ D14), H189 (= H202), H191 (= H204)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
31% identity, 61% coverage: 7:320/516 of query aligns to 6:304/312 of 2ztjA

query
sites
2ztjA

I

I

F

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

P

E

G

K

A

A

S

N

M

F

T

S

K

T

E

Q

E

D

K

K

V

V

R

E

I

I

A

A

K

K

Q

A

L

L

E

D

K

E

M

F

R

G

V

I

D

E

V

Y

I

I

E

E

A

V

G

T

F

T

P

P

A

V

A

A

S

S

D

P

G

Q

D

S

F

R

E

K

S

D

V

A

Q

E

A

V

V

L

A

A

K

S

V

L

I

-

K

-

D

-

S

-

T

-

V

-

C

-

G

G

L

L

-

K

A

A

R

K

A

V

V

V

E

T

H
|
H

D

I

I

Q

V

C

K

R

A

L

G

D

Q

A

A

A

I

K

A

V

P

A

A

V

N

E

S

T

G

G

-

V

-

Q

R

G

I

I

H

D

T

L

F
x
L

I

F

A

G

T

T

S

G

P

-

I

-

H

-

M

-

E

-

M

-

K

-

L

-

R

R

M

D

T

I

P

P

D

-

Q

R

V

I

E

E

R

E

A

A

V

K

W

E

A

V

V

I

K

A

R

Y

A

I

R

R

D

E

F

A

T

A

D

P

N

H

V

V

E

E

-

V

-
x
R

F

F

S

S

P

A

E

E

D

D

A

T

G

F

R

R

S

S

E

E

L

E

D

Q

F

D

L

L

C

L

R

A

V

V

I

Y

E

E

A

A

A

-

I

V

D

A

A

P

G

Y

A

V

T

D

T

R

I

V

N

G

I

L

P
x
A

D

D

T
|
T

V

V

G

G

Y

V

N

A

V

T

P

P

D

R

Q

Q

F

V

G

Y

Y

A

L

L

F

V

K

R

Q

E

L

V

L

R

E

R

R

V

I

V

-

G

P

P

N

R

A

V

D

D

K

-

A

-

I

-

F

I

S

E

A

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

A

A

N

N

S

A

I

Y

A

E

A

A

V

I

T

E

N

A

G

G

A

A

R

T

Q

H

V

V

E

D

C

T

T

T

I

I

N

L

G

G

L

I

G

G

E

E

R

R

A

N

G

G

N

I

T

T

A

P

L

L

E

G

L

F

V

L

M

A

A

R

V

M

R

Y

T

T

R

L

Q

Q

-

P

D

E

Y

Y

F

V

S

R

V

R

D

K

T

Y

R

K

I

L

H

E

T

M

-

L

P

P

E

E

I

L

L

-

T

-

A

-

S

D

R

R

L

M

V

V

S

A

N

R

I

M

T

V

G

G

F

V

S

E

V

I

Q

P

P

F

N

N

K

N

A

Y

I

I

V

T

G

G

A

E

N

T

A

A

F

F

A

S

H

H

E

K

S

A

G

G

I

M

H

H

Q

L

D

K

G

A

V

I

L

Y

K

I

H

N

R

P

E

E

T

A

Y

Y

E

E

I

P

M

Y

R

P

A

P

E

E

D

V

V

F

G

G

active site: Q16 (= Q17)
binding 2-oxoglutaric acid: R12 (= R13), H72 (= H79), L94 (≠ F99), R125 (vs. gap), A156 (≠ P169), T158 (= T171), H187 (= H202), H189 (= H204)
binding copper (ii) ion: E13 (≠ D14), H187 (= H202), H189 (= H204)

3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
26% identity, 95% coverage: 12:500/516 of query aligns to 62:571/573 of 3hq1A

query
sites
3hq1A

L

L

R

R

D
|
D

G

G

E

N

Q

Q

S

A

P

L

G

I

A

D

S

P

M

M

T

S

K

P

E

A

E

R

K

K

V

R

R

R

I

M

A

F

K

D

Q

L

L

L

E

V

K

R

M

M

R

G

V

Y

D

K

V

E

I

I

E

E

A

V

G

G

F

F

P

P

A

S

A

A

S

S

D

Q

G

T

D

D

F

F

E

D

S

F

V

V

Q

R

A

E

V

I

-

I

-

E

-

Q

A

G

K

A

V

I

I

P

K

D

D

D

S

V

T

T

V

I

C

Q

G

V

L

L

A

T

R

Q

A

C

V

R

E

P

H

E

D

L

I

I

V

E

K

R

A

T

G

F

Q

Q

A

A

I

C

A

S

P

G

A

A

N

P

S

R

G

A

R

I

I

V

H

H

T

F

F

Y

I

N

A

S

T

T

S

S

P

I

I

L

H

Q

M

R

E

R

M

V

K

V

L

F

R

R

M

A

T

N

P

R

D

A

Q

E

V

V

-

Q

-

A

-

I

-

A

V

T

E

D

R

G

A

A

V

R

W

K

A

C

V

V

K

E

R

Q

A

A

R

A

D

K

F

Y

T

P

D

G

N

T

-

Q

-

W

-

R

V

F

E

E

F

Y

S

S

P

P

E

E

D

S

A

Y

G

T

R

G

S

T

E

E

L

L

D

E

F

Y

L

A

C

K

R

Q

V

V

I

C

E

D

A

A

A

V

I

G

D

E

A

V

G

I

A

A

T

P

T

T

-

P

-

E

-

R

-

P

-

I

I

F

N

N

I

L

P

P

D

A

T

T

V

V

G

E

Y

M

N

T

V

T

P

P

D

N

Q

V

F

Y

G

A

Y

D

L

S

F

I

K

E

Q

W

L

M

L

S

E

R

R

N

I

L

P

A

N

N

A

R

D

E

K

S

A

V

I

I

F

L

S

S

A

L

H
|
H

C

P

H
|
H

N

N

D

D

L

R

G

G

L

T

A

A

V

V

A

A

N

A

S

A

I

E

A

L

A

G

V

F

T

A

N

A

G

G

A

A

R

D

Q

R

V

I

E

E

C

G

T

C

I

L

N

F

G

G

L

N

G

G

E

E

R

R

A

T

G

G

N
|
N

T

V

A

C

L

L

E

V

E

T

L

L

V

G

M

L

A

N

V

L

R

F

T

S

R

R

Q

-

D

-

Y

-

F

-

S

G

V

V

D

D

T

P

R

Q

I

I

H

D

T

F

P

S

E

N

I

I

L

D

T

E

A

I

S

R

R

R

L

T

V

V

S

E

N

Y

I

C

T

N

G

Q

F

L

S

P

V

V

Q

H

P

E

N

R

K

H

A

P

I

Y

V

G

G

G

A

D

N

L

A

V

F

Y

A

T

H

A

E

F

S

S

G

G

I

S

H

H

Q

Q

D

D

G

A

V

I

L

N

K

K

-

G

-

L

-

D

-

A

-

M

-

K

-

L

-

D

-

A

-

D

-

A

-

D

-

C

-

D

-

V

-

D

-

M

-

L

H

W

R

Q

E

V

T

P

Y

Y

E

L

I

P

M

I

R

D

A

P

E

R

D

D

V

V

G

G

W

R

S

T

T

Y

N

E

K

A

M

V

V

I

L

K

G

G

-

G

-

V

-

A

-

Y

-

I

-

M

K

K

H

T

S

D

G

H

R

G

N

L

A

S

F

L

K

P

T

R

R

R

L

L

Q

Q

E

-

L

-

G

-

V

I

E

E

F

F

E

-

T

-

E

S

Q

Q

Q

V

L

I

N

Q

D

K

T

I

F

E

V

V

R

S

F

P

K

K

E

E

L

M

A

W

D

D

R

A

K

F

H

A

E

E

I

E

Y

Y

D

L

E

A

D

P

L

V

Q

R

A

P

L

L

V

-

T

-

E

-

A

-

N

-

I

-

E

E

R

R

V

I

E

R

N

Q

E

H

S

-

I

-

R

-

L

-

V

-

A

-

L

V

K

D

V

A

A

A

A

D

E

D

M

D

G

G

E

G

Q

T

P

T

S

S

A

I

T

T

I

A

T

T

L

V

S

K

V

I

D

N

G

G

Q

V

E

E

F

T

T

E

A

I

S

S

A

G

M

S

G

G

G

N

G

G

V

P

V

L

D

A

A

A

T

F

F

V

K

H

A

A

I

L

E

A

Q

D

I

V

L

G

N

F

S

D

K

V

T

A

T

V

L

L

E

D

L

Y

Y

Y

S

E

V

H

S

A

N

-

V

M

T

S

N

A

G

G

T

D

D

D

S

A

L

Q

G

A

-

A

-

Y

-

V

E

E

T

A

S

S

V

V

R

T

L

I

E

S

K

K

G

-

R

-

I

T

V

V

N

W

G

G

Q

V

G

G

S

I

D

A

T

P

D

S

I

I

V

T

T

T

A

A

S

S

A

L

K

R

A

A

Y

V

I

V

N

S

A

A

L

V

N

N

K

R

binding manganese (ii) ion: D64 (= D14), H268 (= H202), H270 (= H204), N304 (= N238)

1sr9A Crystal structure of leua from mycobacterium tuberculosis (see paper)
26% identity, 95% coverage: 12:500/516 of query aligns to 62:571/573 of 1sr9A

query
sites
1sr9A

L

L

R
|
R

D
|
D

G

G

E

N

Q

Q

S

A

P

L

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I

A

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M

M

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A

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K

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L

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M

M

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Y

D

K

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I

I

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A

V

G

G

F

F

P

P

A

S

A

A

S

S

D

Q

G

T

D

D

F

F

E

D

S

F

V

V

Q

R

A

E

V

I

-

I

-

E

-

Q

A

G

K

A

V

I

I

P

K

D

D

D

S

V

T

T

V

I

C

Q

G

V

L

L

A

T

R

Q

A

C

V

R

E

P

H

E

D

L

I

I

V

E

K

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A

T

G

F

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Q

A

A

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C

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G

A

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N

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H

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A

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I

L

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V

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A

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-

Q

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A

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A

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L

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A

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N

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|
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|
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N

A

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K

S

A

V

I

I

F

L

S

S

A

L

H
|
H

C

P

H
|
H

N

N

D

D

L

R

G

G

L

T

A

A

V

V

A

A

N

A

S

A

I

E

A

L

A

G

V

F

T

A

N

A

G

G

A

A

R

D

Q

R

V

I

E

E

C

G

T

C

I

L

N

F

G

G

L

N

G

G

E

E

R

R

A

T

G

G

N

N

T

V

A

C

L

L

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V

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L

L

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M

L

A

N

V

L

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F

T

S

R

R

Q

-

D

-

Y

-

F

-

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G

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V

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I

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Y

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N

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L

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F

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G

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K

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A

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Y

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D

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L

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L

L

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-

T

-

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-

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-

N

-

I

-

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-

I

-

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-

L

-

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A

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L

V

K

D

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A

A

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D

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G

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A

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L

V

S

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N

G

G

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F

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M

S

G

G

G

N

G

G

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P

V

L

D

A

A

A

T

F

F

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K

H

A

A

I

L

E

A

Q

D

I

V

L

G

N

F

S

D

K

V

T

A

T

V

L

L

E

D

L

Y

Y

Y

S

E

V

H

S

A

N

-

V

M

T

S

N

A

G

G

T

D

D

D

S

A

L

Q

G

A

-

A

-

Y

-

V

E

E

T

A

S

S

V

V

R

T

L

I

E

S

K

K

G

-

R

-

I

T

V

V

N

W

G

G

Q

V

G

G

S

I

D

A

T

P

D

S

I

I

V

T

T

T

A

A

S

S

A

L

K

R

A

A

Y

V

I

V

N

S

A

A

L

V

N

N

K

R

binding 3-methyl-2-oxobutanoic acid: R63 (= R13), P235 (= P169), T237 (= T171), H268 (= H202), H270 (= H204)
binding zinc ion: D64 (= D14), H268 (= H202), H270 (= H204)

Query Sequence

>WP_013834785.1 NCBI__GCF_000214825.1:WP_013834785.1
MKDHLIIFDTTLRDGEQSPGASMTKEEKVRIAKQLEKMRVDVIEAGFPAASDGDFESVQA
VAKVIKDSTVCGLARAVEHDIVKAGQAIAPANSGRIHTFIATSPIHMEMKLRMTPDQVVE
RAVWAVKRARDFTDNVEFSPEDAGRSELDFLCRVIEAAIDAGATTINIPDTVGYNVPDQF
GYLFKQLLERIPNADKAIFSAHCHNDLGLAVANSIAAVTNGARQVECTINGLGERAGNTA
LEELVMAVRTRQDYFSVDTRIHTPEILTASRLVSNITGFSVQPNKAIVGANAFAHESGIH
QDGVLKHRETYEIMRAEDVGWSTNKMVLGKHSGRNAFKTRLQELGVEFETEQQLNDTFVR
FKELADRKHEIYDEDLQALVTEANIERVENESIRLVALKVAAEMGEQPSATITLSVDGQE
FTASAMGGGVVDATFKAIEQILNSKTTLELYSVSNVTNGTDSLGETSVRLEKGGRIVNGQ
GSDTDIVTASAKAYINALNKFSDAAIKAHPQRQETV

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