SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011766887.1 NCBI__GCF_000061505.1:WP_011766887.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

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

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

Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58) (see 2 papers)
70% identity, 97% coverage: 5:500/511 of query aligns to 7:502/517 of Q9JZG1

query
sites
Q9JZG1

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D16 (= D14) binding Mn(2+)
H204 (= H202) binding Mn(2+)
H206 (= H204) binding Mn(2+)
N240 (= N238) binding Mn(2+)

Sites not aligning to the query:

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

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
70% identity, 62% coverage: 5:321/511 of query aligns to 4:307/308 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)
50% identity, 74% coverage: 2:381/511 of query aligns to 15:408/409 of 6e1jA

query
sites
6e1jA

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S

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 (= E67), H225 (= H202), H227 (= H204)

P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
49% identity, 74% coverage: 2:381/511 of query aligns to 82:475/503 of P0DO78

query
sites
P0DO78

K

K

D

N

A

Y

L

V

I

R

I

V

F

F

D

D

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

S

A

P

P

G

G

A

G

S

A

M

L

T

T

R

P

D

P

E

Q

K

K

L

L

R

E

I

I

A

A

R

R

Q

K

L

L

E

A

R

K

M

L

R

R

V

V

D

D

V

V

I

M

E

E

A

V

G

G

F

F

A

P

A

G

A

S

S

S

N

E

G

E

D

E

F

F

E

E

S

T

V

V

R

K

S

T

I

I

A

A

E

K

A

T

I

V

K

G

E

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

I

S

P

T

V

V

I

C

C

S

A

L

I

A

A

R

R

A

S

N

K

E

Q

N

R

D

D

I

I

R

E

R

A

A

A

G

W

E

E

A

A

I

V

R

K

P

Y

A

A

A

K

R

R

G

P

R

K

I

I

H

L

T

I

F

F

I

T

A

S

T

T

S

S

P

D

I

I

H

H

M

M

E

K

K

Y

K

K

L

L

R

K

M

K

T

T

P

K

D

E

Q

E

V

V

V

I

E

E

Q

M

A

A

V

T

K

S

A

S

I

I

G

R

W

F

A

A

R

K

E

S

Y

L

-

G

T

F

D

I

D

D

I

V

E

Q

F

L

S

G

A

C

E

E

D

D

A

G

G

G

R

R

S

S

E

E

I

K

D

E

F

F

L

L

C

C

R

K

I

I

F

L

D

G

A

E

V

A

I

I

K

K

A

A

G

G

A

A

K

T

T

A

I

V

N

N

V

V

P

A

D

D

T

T

V

V

G

G

Y

I

N

N

V

M

P

P

E

E

Q

E

Y

Y

A

G

A

E

T

L

L

V

R

R

T

Y

L

L

I

K

E

A

R

N

V

T

P

P

N

G

A

I

D

D

K

D

V

I

I

V

W

F

S

S

V

V

H
|
H

C

C

H
|
H

N

N

D

D

L

L

G

G

L

V

A

A

V

T

S

A

N

N

S

T

L

I

A

A

A

G

V

V

M

C

A

A

G

G

A

A

R

R

Q

Q

V

V

E

E

C

V

T

T

I

V

N

N

G

G

L

I

G

G

E

E

R

R

A

S

G

G

N

N

A

A

S

P

L

L

E

E

I

V

V

V

M

M

A

A

V

L

R

K

T

C

R

R

A

G

D

A

V

Y

F

V

P

M

-

D

-

G

V

V

S

Y

T

T

N

R

I

I

D

D

T

T

T

R

Q

Q

I

I

V

M

P

A

A

T

S

S

K

K

L

M

V

V

S

Q

Q

E

I

Y

T

T

G

G

Y

L

P

Y

V

V

Q

Q

P

P

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

V

H
|
H

Q

Q

D

D

G

G

V

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

V

G

V

A

K

N

S

K

Q

-

N

-

S

-

G

L

I

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

N

H

A

A

F

V

R

K

A

D

R

R

L

L

Q

K

E

E

L

L

G

G

I

Y

E

E

I

L

G

-

S

D

E

D

E

E

Q

K

L

F

N

N

H

D

A

I

F

F

A

S

R

R

F

F

K

R

E

D

L

L

A

T

D

K

K

Q

K

K

H

K

E

R

I

I

F

T

D

D

E

A

D

D

L

L

H

K

A

A

L

L

M

V

S

T

R93 (= R13) mutation to A: Lost catalytic activity.
D94 (= D14) mutation to A: Lost catalytic activity.
H292 (= H202) mutation to A: Lost catalytic activity.
H294 (= H204) mutation to A: Lost catalytic activity.
H392 (= H300) mutation to A: Lost catalytic activity.

Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 75% coverage: 2:384/511 of query aligns to 82:478/503 of Q9FN52

query
sites
Q9FN52

K

K

D

N

A

Y

L

V

I

R

I

V

F

L

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

S

S

P

P

G

G

A

A

S

A

M

L

T

T

R

P

D

P

E

Q

K

K

L

L

R

E

I

I

A

A

R

R

Q

Q

L

L

E

A

R

K

M

L

R

R

V

V

D

D

V

I

I

M

E

E

A

V

G

G

F

F

A

P

A

V

A

S

S

S

N

E

G

E

D

E

F

F

E

E

S

A

V

I

R

K

S

T

I

I

A

A

E

K

A

T

I

V

-

G

-

N

-

E

-

V

K

D

E

E

S

E

T

T

-

G

-

Y

-

V

-

P

-

V

V

I

C

C

S

G

L

I

A

A

R

R

A

C

N

K

E

K

N

R

D

D

I

I

R

E

R

A

A

T

G

W

E

E

A

A

I

L

R

K

P

Y

A

A

A

K

R

R

G

P

R

R

I

V

H

M

T

L

F

F

I

T

A

S

T

T

S

S

P

E

I

I

H

H

M

M

E

K

K

Y

K

K

L

L

R

K

M

K

T

T

P

K

D

E

Q

E

V

V

V

I

E

E

Q

M

A

A

V

V

K

N

A

S

I

V

G

K

W

Y

A

A

R

K

E

S

Y

L

-

G

T

F

D

K

D

D

I

I

E

Q

F

F

S

G

A

C

E

E

D

D

A

G

G

G

R

R

S

T

E

E

I

K

D

D

F

F

L

I

C

C

R

K

I

I

F

L

D

G

A

E

V

S

I

I

K

K

A

A

G

G

A

A

K

T

T

T

I

V

N

G

V

F

P

A

D

D

T

T

V

V

G
|
G

Y

I

N

N

V

M

P

P

E

Q

Q

E

Y

F

A

G

A

E

T

L

L

V

R

A

T

Y

L

V

I

I

E

E

R

N

V

T

P

P

N

G

A

A

D

D

K

D

V

I

I

V

W

F

S

A

V

I

H

H

C

C

H

H

N

N

D

D

L

L

G

G

L

V

A

A

V

T

S

A

N

N

S

T

L

I

A

S

A

G

V

I

M

C

A

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

A

A

S

P

L

L

E

E

I

V

V

V

M

M

A

A

V

L

R

K

T

C

R

R

A

G

D

E

V

S

F

L

P

M

-

D

-

G

V

V

S

Y

T

T

N

K

I

I

D

D

T

S

T

R

Q

Q

I

I

V

M

P

A

A

T

S

S

K

K

L

M

V

V

S

Q

Q

E

I

H

T

T

G

G

Y

M

P

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

H

H

E

E

S

S

G

G

I

I

H

H

Q

Q

D

D

G

G

V

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

G

V

A

K

N

S

K

E

-

N

-

S

-

G

L

I

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

N

H

A

A

F

V

R

K

A

D

R

R

L

L

Q

K

E

E

L

L

G

G

I

Y

E

E

I

I

G

-

S

S

E

D

E

E

Q

K

L

F

N

N

H

D

A

I

F

F

A

S

R

R

F

Y

K

R

E

E

L

L

A

T

D

K

K

D

K

K

H

K

E

R

I

I

F

T

D

D

E

A

D

D

L

L

H

K

A

A

L

L

M

V

S

V

D

N

E

G

A

A

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)
49% identity, 74% coverage: 7:383/511 of query aligns to 87:479/506 of Q9FG67

query
sites
Q9FG67

I

V

F

F

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

S

S

P

P

G

G

A

G

S
|
S

M

L

T

T

R

P

D

P

E

Q

K

K

L

L

R

E

I

I

A

A

R

R

Q

Q

L

L

E

A

R

K

M

L

R

R

V

V

D

D

V

I

I

M

E

E

A

V

G

G

F

F

A

P

A

G

A

S

S

S

N

E

G

E

D

E

F

L

E

E

S

T

V

I

R

K

S

T

I

I

A

A

E

K

A

T

I

V

K

G

E

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

V

S

P

T

V

V

I

C

C

S

A

L

I

A

A

R

R

A

C

N

K

E

H

N

R

D

D

I

I

R

E

R

A

A

T

G

W

E

E

A

A

I

L

R

K

P

Y

A

A

A

K

R

R

G

P

R

R

I

I

H

L

T

V

F

F

I

T

A

S

T

T

S

S

P

D

I

I

H

H

M

M

E

K

K

Y

K

K

L

L

R

K

M

K

T

T

P

Q

D

E

Q

E

V

V

V

I

E

E

Q

M

A

A

V

V

K

S

A

S

I

I

G

R

W

F

A

A

R

K

E

S

Y

L

-

G

T

F

D

N

D

D

I

I

E

Q

F

F

S

G

A

C

E

E

D

D

A

G

G

G

R

R

S

S

E

D

I

K

D

D

F

F

L

L

C

C

R

K

I

I

F

L

D

G

A

E

V

A

I

I

K

K

A

A

G

G

A

V

K

T

T

V

I

V

N

T

V

I

P

G

D

D

T

T

V

V

G

G

Y

I

N

N

V

M

P

P

E

H

Q

E

Y

Y

A

G

A

E

T

L

L

V

R

T

T

Y

L

L

I

K

E

A

R

N

V

T

P

P

N

G

A

I

D

D

K

D

V

V

I

V

W

V

S
x
A

V

V

H

H

C

C

H

H

N

N

D

D

L

L

G

G

L

L

A

A

V

T

S

A

N

N

S

S

L

I

A

A

A

G

V

I

M

R

A

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

A

A

S

S

L

L

E

E

I

V

V

V

M

M

A

A

V

L

R

K

T

C

R

R

A

G

D

A

-

Y

-

V

V

I

F

N

P

G

V

V

S

Y

T

T

N

K

I

I

D

D

T

T

T

R

Q

Q

I

I

V

M

P

A

A

T

S

S

K

K

L

M

V

V

S

Q

Q

E

I

Y

T

T

G

G

Y

L

P

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

G

G

V

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

I

G

G

W

I

G

V

A

K

N

S

K

Q

-

N

-

S

-

G

L

L

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

N

H

A

A

F

V

R

K

A

D

R

R

L

L

Q

K

E

E

L

L

G

G

I

Y

E

E

I

L

G

-

S

D

E

D

E

E

Q

K

L

L

N

N

H

A

A

V

F

F

A

S

R

L

F

F

K

R

E

D

L

L

A

T

D

K

K

N

K

K

H

K

E

R

I

I

F

T

D

D

E

A

D

D

L

L

H

K

A

A

L

L

M

V

-

T

-

S

S

S

D

D

E

E

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)
32% identity, 75% coverage: 7:391/511 of query aligns to 24:396/399 of 6ktqA

query
sites
6ktqA

I

I

F

L

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

S

T

P

P

G

G

A

V

S

V

M

F

T

T

R

T

D

D

E

Q

K

R

L

V

R

E

I

I

A

A

R

K

Q

A

L

L

E

S

R

D

M

I

R

G

V

V

D

Q

V

M

I

I

E

E

A

A

G

G

F

H

A

P

A

A

A
x
V

S

S

N

P

G

D

D

I

F

Y

E

E

S

G

V

I

R

R

S

R

I

I

A

I

E

K

A

L

I

K

K

R

E

E

S

G

T

V

V

I

C

K

S

S

L

E

A

I

R

V

A

A

N

H

E

S

N
x
R

D
x
A

I

V

R

K

R

R

A

D

G

I

E

E

A

V

I

G

R

A

P

E

A

I

A

E

R

A

G

D

R

R

I

I

H

A

T

I

F
|
F

I

Y

A

G

T

I

S

S

P

D

I

T

H

H

M

L

E

K

K

A

K

K

L
x
H

R

H

M

T

T

T

P

R

D

D

Q

E

V

A

V

L

E

R

Q

S

A

I

V

A

K

E

A

T

I

V

G

S

W

Y

A

A

R

K

E

S

Y

H

T

G

D

V

D

K

I

V

E
x
R

F

F

S
x
T

A

A

E
|
E

D

D

A

A

G

T

R

R

S

A

E

D

I

Y

D

Q

F

Y

L

L

C

L

R

E

I

V

F

I

D

K

A

T

V

V

I

R

K

D

A

A

G

G

A

A

K

D

T

R

I

V

N
x
S

V

I

P

A

D

D

T
|
T

V

V

G

G

Y

V

N

L

V

Y

P

P

E

S

Q

R

Y

T

A

R

A

E

T

L

L

F

R

K

T

D

L

L

I

T

E

S

R

R

V

F

P

P

N

D

A

I

D

E

K

-

V

-

I

-

W

F

S

D

V

I

H
|
H

C

A

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

V

S

A

N

N

S

V

L

L

A

A

V

A

M

E

A

G

G

G

A

A

R

T

Q

I

V

I

E

H

C

T

T

T

I

L

N

N

G

G

L

L

G

G

E

E

R

R

A

V

G

G

N

I

A

A

S

P

L

L

E

Q

E

V

I

V

V

A

M

A

A

A

V

L

R

K

T

Y

R

H

A

-

D

-

V

-

F

F

P

G

V

I

S

E

T

V

N

-

I

V

D

D

T

L

T

K

Q

K

I

L

V

S

P

E

A

V

S

A

K

S

L

L

V

V

S

E

Q

K

I

Y

T

S

G

G

Y

I

P

A

V

L

Q

P

P

P

N

N

K

F

A

P

I

I

V

T

G

G

A

D

N

Y

A

A

F

F

A

V

H

H

E

K

S

A

G

G

I

V

H

H

Q

V

D

A

G

G

V

V

L

L

K

N

H

D

R

P

E

K

T

T

Y

Y

E

E

I

F

M

L

R

P

A

P

E

E

D

T

V

F

G

G

W

R

G

-

A

S

N

R

K

D

L

Y

V

V

L

I

G

D

K

K

H

Y

S

T

G

G

R

K

N

H

A

A

F

V

R

K

A

D

R

R

L

F

Q

D

E

R

L

L

G

G

I

V

E

K

I

L

G

-

S

T

E

D

E

S

Q

E

L

I

N

D

H

Q

A

V

F

L

A

A

R

K

F

I

K

K

E

S

L

N

A

P

D

N

K

V

K

R

H

-

E

-

I

-

F

F

D

Y

E

R

D

D

L

V

H

D

A

L

L

L

M

E

S

L

D

A

E

E

A

S

V

V

T

T

P

G

E

R

Q

L

E

E

H

H

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 (≠ N79), A97 (≠ D80), 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)
33% identity, 73% coverage: 7:379/511 of query aligns to 6:379/380 of 4ov9A

query
sites
4ov9A

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

R

I

D

D

E

E

K

K

L

I

R

E

I

V

A

F

R

D

Q

L

L

L

E

V

R

E

M

L

R

N

V

V

D

D

V

G

I

I

E

E

A

V

G

G

F

F

A

P

A

S

S

N

N

E

G

T

D

E

F

F

E

H

S

T

V

C

R

Q

S

V

I

L

A

S

E

K

-

R

A

A

I

P

K

K

E

G

S

K

T

P

V

I

C

A

S

A

L
|
L

A

S

R

R

A

A

N

N

E

Q

N

N

D

E

I

I

R

A

R

V

A

T

G

W

E

E

A

A

I

I

R

Q

P

K

A

A

A

D

R

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

K

H

K

V

L

L

R

K

M

I

T

S

P

E

D

K

Q

E

V

V

V

L

E

Q

Q

K

A

I

V

R

K

N

A

S

I

I

G

S

W

F

A

A

R

R

E

S

Y

I

T

V

D

G

-

P

-

G

-

I

D

E

I

I

E

Q

F

F

S

S

A

G

E

E

D

H

A

F

G

G

R

D

S

A

-

I

-

E

E

N

I

F

D

A

F

F

L

T

C

K

R

E

I

A

F

F

D

L

A

T

V

A

I

I

K

E

A

A

G

G

A

A

K

N

T

I

I

I

N

N

V

L

P

P

D

N

T
|
T

V

V

G

E

Y

R

N

Y

V

R

P

P

E

M

Q

V

Y

F

A

V

A

N

T

M

L

V

R

K

T

E

L

I

I

K

E

D

R

V

V

V

P

-

N

-

A

K

D

D

K

K

V

A

I

I

W

I

S

S

V

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

T

S

A

N

T

S

S

L

V

A

E

A

S

V

V

M

Y

A

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

A

T

S

N

L

L

E

Y

E

E

I

T

V

A

M

I

A

A

V

L

R

H

T

Q

R

N

A

G

D

E

V

-

F

-

P

-

V

-

S

N

T

L

N

N

I

I

D

N

T

F

T

Q

Q

R

I

I

V

Y

P

P

A

T

S

A

K

K

L

R

V

I

S

S

Q

E

I

L

T

T

G

G

Y

I

P

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

-

R

W

M

G

D

A

K

N

E

K

T

L

I

V

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

N

K

A

A

F

I

R

E

A

F

R

L

L

L

Q

H

E

Q

L

R

G

G

I

I

E

Q

I

V

G

-

S

S

E

K

E

E

Q

G

L

I

N

H

H

H

A

L

F

F

A

S

R

L

F

A

K

K

E

S

L

I

A

S

D

S

K

R

K

E

H

N

-

N

-

R

E

E

I

I

F

T

D

E

E

A

D

E

L

L

H

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)
33% identity, 73% coverage: 7:379/511 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

R

I

D

D

E

E

K

K

L

I

R

E

I

V

A

F

R

D

Q

L

L

L

E

V

R

E

M

L

R

N

V

V

D

D

V

G

I

I

E

E

A

V

G

G

F

F

A

P

A

S

S

N

N

E

G

T

D

E

F

F

E

H

S

T

V

C

R

Q

S

V

I

L

A

S

E

K

-

R

A

A

I

P

K

K

E

G

S

K

T

P

V

I

C

A

S

A

L

L

A

S

R

R

A

A

N

N

E

Q

N

N

D

E

I

I

R

A

R

V

A

T

G

W

E

E

A

A

I

I

R

Q

P

K

A

A

A

D

R

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

K

H

K

V

L

L

R

K

M

I

T

S

P

E

D

K

Q

E

V

V

V

L

E

Q

Q

K

A

I

V

R

K

N

A

S

I

I

G

S

W

F

A

A

R

R

E

S

Y

I

T

V

D

G

-

P

-

G

-

I

D

E

I

I

E

Q

F

F

S

S

A

G

E

E

D

H

A

F

G

G

R

D

S

A

-

I

-

E

E

N

I

F

D

A

F

F

L

T

C

K

R

E

I

A

F

F

D

L

A

T

V

A

I

I

K

E

A

A

G

G

A

A

K

N

T

I

I

I

N

N

V

L

P
|
P

D

N

T
|
T

V

V

G

E

Y

R

N

Y

V

R

P

P

E

M

Q

V

Y

F

A

V

A

N

T

M

L

V

R

K

T

E

L

I

I

K

E

D

R

V

V

V

P

-

N

-

A

K

D

D

K

K

V

A

I

I

W

I

S

S

V

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

T

S

A

N

T

S

S

L

V

A

E

A

S

V

V

M

Y

A

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

A

T

S

N

L

L

E

Y

E

E

I

T

V

A

M

I

A

A

V

L

R

H

T

Q

R

N

A

G

D

E

V

-

F

-

P

-

V

-

S

N

T

L

N

N

I

I

D

N

T

F

T

Q

Q

R

I

I

V

Y

P

P

A

T

S

A

K

K

L

R

V

I

S

S

Q

E

I

L

T

T

G

G

Y

I

P

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

-

R

W

M

G

D

A

K

N

E

K

T

L

I

V

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

N

K

A

A

F

I

R

E

A

F

R

L

L

L

Q

H

E

Q

L

R

G

G

I

I

E

Q

I

V

G

-

S

S

E

K

E

E

Q

G

L

I

N

H

H

H

A

L

F

F

A

S

R

L

F

A

K

K

E

S

L

I

A

S

D

S

K

R

K

E

H

N

-

N

-

R

E

E

I

I

F

T

D

E

E

A

D

E

L

L

H

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)
29% identity, 97% coverage: 5:501/511 of query aligns to 8:511/516 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

R

T

D

S

E

E

K

K

L

L

R

N

I

I

A

A

R

K

-

F

Q

L

L

L

E

Q

R

K

M

L

R

N

V

V

D

D

V

R

I

V

E

E

A

I

G

A

F

S

A

A

A

R

A

V

S

S

N

K

G

G

D

E

F

L

E

E

S

T

V

V

R

Q

S

K

I

I

A

M

E

E

-

W

A

A

I

A

K

T

E

E

S

Q

T

L

V

T

C

E

S

R

L

I

A

E

R

I

A
x
L

N

G

E
x
F

N

V

D

D

I

G

R

N

R

K

A

T

G

V

E

D

A

W

I

I

R

K

P

D

A

S

A

G

R

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

K

K

K

Q

L

L

R

G

M

K

T

T

P

P

D

K

Q

E

-

F

-

T

-

D

-

V

-

S

-

F

V

V

V

I

E

E

Q

Y

A

A

V

I

K

K

A

S

I

G

G

L

W

K

A

I

R

N

E

V

Y
|
Y

T

L

D
x
E

D

D

I

-

E

-

F

-

S

-

A

W

E

S

D

N

A

G

G

F

R

R

S

N

E

S

I

P

D

D

F

Y

L

V

C

K

R

S

I

L

F

V

D

E

A

H

V

L

I

S

K

K

A

E

G

H

A

I

K

E

T

R

I

I

N

F

V

L

P

P

D

D

T
|
T

V

L

G

G

Y

V

N

L

V

S

P

P

E

E

Q

E

Y

T

A

F

A

Q

T

G

L

V

R

D

T

S

L

L

I

I

E

Q

R

K

V

Y

P

P

N

D

A

-

D

-

K

-

V

I

I

H

W

F

S

E

V

F

H

H

C

G

H

H

N

N

D

D

L

Y

G

D

L

L

A

S

V

V

S

A

N

N

S

S

L

L

A

Q

A

A

V

I

M

R

A

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

A

T

S

P

L

L

E

E

E

A

I

L

V

V

M

T

A

T

V

I

R

H

T

D

R

K

A

S

D

N

V

-

F

-

P

-

V

S

S

K

T

T

N

N

I

I

D

N

T

E

T

I

Q

A

I

I

V

T

P

E

A

A

S

S

K

R

L

L

V

V

S

E

Q

V

I

F

T

S

G

G

Y

K

P

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

-

G

R

A

K

N

R

K

S

L

Y

V

A

L

L

G

G

K

K

H

L

S

A

G

G

R

K

N

A

A

S

F

I

R

S

A

E

R

N

L

V

Q

K

E

Q

L

L

G

G

I

M

E

-

I

V

G

L

S

S

E

E

E

V

Q

V

L

L

N

Q

H

K

A

V

F

L

A

E

R

R

F

V

K

I

E

E

L

L

A

G

D

D

K

Q

K

N

H

K

E

L

I

V

F

T

D

P

E

E

D

D

L

L

H

P

A

F

L

I

M

I

S

A

D

D

E

V

A

S

V

G

T

R

P

T

E

G

Q

E

E

K

H

V

F

L

R

T

L

I

V

K

A

S

T

C

R

N

F

I

H

H

S

S

E

G

T

I

G

G

E

I

T

R

P

P

R

H

A

A

E

Q

V

I

T

E

L

L

A

E

I

Y

G

Q

G

G

Q

K

E

I

T

H

R

K

S

E

Q

I

A

S

E

E

G

G

S

D

G

G

P

G

V
x
Y

D
|
D

A

A

A

F

F

M

K

N

A

A

I

L

E

T

S

K

V

I

A

T

G

N

-

R

-

L

-

G

-

I

S

S

G

I

S

P

E

K

L
|
L

L

I

L

D

Y
|
Y

S

E

V

V

N

R

A
x
I

I

P

T

P

T

G

G

G

-

K

T
|
T

D

D

A

A

Q

L

G
x
V

E

E

V

T

T

R

V

I

R

T

L

W

A

N

K

K

-

S

-

L

-

D

-

L

-

E

D

E

G

D

R

Q

V

T

V

F

N

K

G

T

Q

M

G

G

A

V

D

H

T
x
P

D

D

I
x
Q

I

T

V

V

A

A

S

A

A

V

K

H

A

A

Y

T

L

E

N

K

A

M

L

L

N

N

K

Q

L

I

C

L

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 (≠ A76) 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 (≠ E78) 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 (= Y132) 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 (≠ D134) 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 (≠ V430) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (= D431) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L447) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y450) 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 (≠ A454) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (= T459) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (≠ G463) 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 (≠ T483) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
Q495 (≠ I485) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
32% identity, 58% coverage: 5:300/511 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

R

T

D

S

E

E

K

K

L

L

R

N

I

I

A

A

R

K

-

F

Q

L

L

L

E

Q

R

K

M

L

R

N

V

V

D

D

V

R

I

V

E

E

A

I

G

A

F

S

A

A

A
x
R

A
x
V

S

S

N

K

G

G

D

E

F

L

E

E

S

T

V

V

R

Q

S

K

I

I

A

M

E

E

-

W

A

A

I

A

K

T

E

E

S

Q

T

L

V

T

C

E

S

R

L

I

A

E

R

I

A

L

N

G

E

F

N

V

D

D

I

G

R

N

R

K

A

T

G

V

E

D

A

W

I

I

R

K

P

D

A

S

A

G

R

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

K

K

K

Q

L

L

R

G

M

K

T

T

P

P

D

K

Q

E

-

F

-

T

-

D

-

V

-

S

-

F

V

V

V

I

E

E

Q

Y

A

A

V

I

K

K

A

S

I

G

G

L

W

K

A

I

R

N

E

V

Y
|
Y

T

L

D
x
E

D

D

I

-

E

-

F

-

S

-

A

W

E

S

D

N

A

G

G

F

R

R

S

N

E

S

I

P

D

D

F

Y

L

V

C

K

R

S

I

L

F

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E

A

H

V

L

I

S

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K

A

E

G

H

A

I

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E

T

R

I

I

N

F

V

L

P
|
P

D

D

T
|
T

V

L

G

G

Y

V

N

L

V

S

P

P

E

E

Q

E

Y

T

A

F

A

Q

T

G

L

V

R

D

T

S

L

L

I

I

E

Q

R

K

V

Y

P

P

N

D

A

-

D

-

K

-

V

I

I

H

W

F

S

E

V

F

H
|
H

C

G

H
|
H

N

N

D

D

L

Y

G

D

L

L

A

S

V

V

S

A

N

N

S

S

L

L

A

Q

A

A

V

I

M

R

A

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

A

T

S

P

L

L

E

E

E

A

I

L

V

V

M

T

A

T

V

I

R

H

T

D

R

K

A

S

D

N

V

-

F

-

P

-

V

S

S

K

T

T

N

N

I

I

D

N

T

E

T

I

Q

A

I

I

V

T

P

E

A

A

S

S

K

R

L

L

V

V

S

E

Q

V

I

F

T

S

G

G

Y

K

P

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 (≠ D134)
binding pyruvic acid: R10 (= R13), Y138 (= Y132), P171 (= P169), T173 (= T171)
binding zinc ion: D11 (= D14), H201 (= H202), H203 (= H204)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
28% identity, 74% coverage: 7:382/511 of query aligns to 37:408/418 of Q9Y823

query
sites
Q9Y823

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

P

A

G

N

A

A

S

F

M

F

T

D

R

T

D

E

E

K

K

K

L

I

R

Q

I

I

A

A

R

K

Q

A

L

L

E

D

R

N

M

F

R

G

V

V

D

D

V

Y

I

I

E
|
E

A

L

G

T

F

S

A

P

A

V

A

A

S

S

N

E

G

Q

D

S

F

R

E

Q

S

D

V

C

R

E

S

A

I

I

A

C

E

K

A

L

I

G

K

L

E

K

S

C

T

K

V

I

C

L

S

T

L
x
H

A

I

R

R

A

C

N

H

E

M

N

D

D

D

I

A

R

R

R

V

A

A

G

V

E

E

A

T

I

-

R

-

P

-

A

-

A

G

R

V

G

D

R

G

I

V

H
x
D

T

V

F

V

I

I

A

G

T

T

S

S

P

Q

I

Y

H

L

M

R

E

K

K

Y

K

S

L

H

R

G

M

K

T

D

P

M

D

T

Q

Y

V

I

E

D

Q

S

A

A

V

T

K

E

A

V

I

I

G

N

W

F

A

V

R

K

E

S

Y

K

T

G

D

I

D

E

I

V

E
x
R

F

F

S
|
S

A

S

E
|
E

D

D

A

S

G

F

R

R

S

S

E

D

I

L

D

V

F

D

L

L

C

L

R

S

I

L

F

Y

D

K

A

A

V

V

I

D

K

K

A

I

G

G

A

V

K

N

T

R

I

V

N

G

V

I

P

A

D

D

T
|
T

V

V

G

G

Y

C

N

A

V

T

P

P

E

R

Q

Q

Y

V

A

Y

A

D

T

L

L

I

R

R

T

T

L

L

I

-

E

R

R

G

V

V

P

V

N

S

A

C

D

D

K

-

V

-

I

-

W

I

S
x
E

V

C

H
|
H

C

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

S

A

N

N

S

A

L

Y

A

C

A

A

V

L

M

E

A

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

A

T

S

P

L

L

E

G

E

A

I

L

V

L

-

A

-

R

M

M

A

Y

V

V

R

T

T

D

R

R

A

E

D

-

V

-

F

-

P

Y

V

I

S

T

T

H

N

K

I

Y

D

K

T

L

T

N

Q

Q

I

L

V
x
R

P

E

A

L

S

E

K

N

L

L

V

V

S

A

Q

D

I

A

T

V

G

E

Y

V

P

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

G

S

A

R

N

Y

K

V

L

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

R

K

A

S

R

R

L

A

Q

E

E
x
Q

L

L

G

N

I

L

E

H

I

L

G

-

S

T

E

D

E

A

Q

Q

L

A

N

K

H

E

A

L

F

T

A

V

R

R

F

I

K

K

E

K

L

L

A

A

D

D

K

V

K

R

H

T

E

L

I

A

F

M

D

D

E

D

-

V

-

D

-

R

-

V

-

L

-

R

D

E

L

Y

H

H

A

A

L

D

M

L

S

S

D

D

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 (≠ L73) 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 (≠ V267) 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.

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
28% identity, 72% coverage: 7:374/511 of query aligns to 32:389/400 of 3ivtB

query
sites
3ivtB

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

P

A

G

N

A

A

S

F

M

F

T

D

R

T

D

E

E

K

K

K

L

I

R

Q

I

I

A

A

R

K

Q

A

L

L

E

D

R

N

M

F

R

G

V

V

D

D

V

Y

I

I

E

E

A

L

G

T

F

S

A

P

A

V

A

A

S

S

N

E

G

Q

D

S

F

R

E

Q

S

D

V

C

R

E

S

A

I

I

A

C

E

K

A

L

I

G

K

L

E

K

S

C

T

K

V

I

C

L

S

T

L
x
H

A

I

R

R

A

C

N

H

E

M

N

D

D

D

I

A

R

R

R

V

A

A

G

V

E

E

A

T

I

-

R

-

P

-

A

-

A

G

R

V

G

D

R

G

I

V

H

D

T

V

F

V

I

I

A

G

T

T

S

S

P

Q

I

Y

H

L

M

R

E

K

K

Y

K

S

L

H

R

G

M

K

T

D

P

M

D

T

Q

Y

V

I

E

D

Q

S

A

A

V

T

K

E

A

V

I

I

G

N

W

F

A

V

R

K

E

S

Y

K

T

G

D

I

D

E

I

V

E
x
R

F

F

S
|
S

A

S

E

E

D

D

A

S

G

F

R

R

S

S

E

D

I

L

D

V

F

D

L

L

C

L

R

S

I

L

F

Y

D

K

A

A

V

V

I

D

K

K

A

I

G

G

A

V

K

N

T

R

I

V

N

G

V

I

P

A

D

D

T
|
T

V

V

G

G

Y

C

N

A

V

T

P

P

E

R

Q

Q

Y

V

A

Y

A

D

T

L

L

I

R

R

T

T

L

L

I

-

E

R

R

G

V

V

P

V

N

S

A

C

D

D

K

-

V

-

I

-

W

I

S

E

V

C

H
|
H

C

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

S

A

N

N

S

A

L

Y

A

C

A

A

V

L

M

E

A

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

A

T

S

P

L

L

E

G

E

A

I

L

V

L

-

A

-

R

M

M

A

Y

V

V

R

T

T

D

R

R

A

E

D

-

V

-

F

-

P

Y

V

I

S

T

T

H

N

K

I

Y

D

K

T

L

T

N

Q

Q

I

L

V

R

P

E

A

L

S

E

K

N

L

L

V

V

S

A

Q

D

I

A

T

V

G

E

Y

V

P

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

G

S

A

R

N

Y

K

V

L

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

R

K

A

S

R

R

L

A

Q

E

E

Q

L

L

G

N

I

L

E

H

I

L

G

-

S

T

E

D

E

A

Q

Q

L

A

N

K

H

E

A

L

F

T

A

V

R

R

F

I

K

K

E

K

L

L

A

A

D

D

K

V

K

R

H

T

E

L

I

A

F

M

D

D

E

D

active site: Q42 (= Q17)
binding 2-oxoglutaric acid: R38 (= R13), H98 (≠ L73), R158 (≠ E137), S160 (= S139), T192 (= T171), H219 (= H202), H221 (= H204)
binding zinc ion: E39 (≠ D14), H219 (= H202), H221 (= H204)

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
28% identity, 72% coverage: 7:374/511 of query aligns to 14:360/370 of 3mi3A

query
sites
3mi3A

I

I

F

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

P

A

G

N

A

A

S

F

M

F

T

D

R

T

D

E

E

K

K

K

L

I

R

Q

I

I

A

A

R

K

Q

A

L

L

E

D

R

N

M

F

R

G

V

V

D

D

V

Y

I

I

E

E

A

L

G

T

F

S

A

P

A

V

A

A

S

S

N

E

G

Q

D

S

F

R

E

Q

S

D

V

C

R

E

S

A

I

I

A

C

E

K

A

L

I

G

K

L

E

K

S

C

T

K

V

I

C

L

S

T

L

H

A

I

R

R

A

C

N

H

E

M

N

D

D

D

I

A

R

R

R

V

A

A

G

V

E

E

A

T

I

-

R

-

P

-

A

-

A

G

R

V

G

D

R

G

I

V

H
x
D

T

V

F

V

I

I

A

G

T

T

S

S

P

M

I

T

H

Y

M

-

E

-

K

-

L

-

R

-

M

-

T

-

P

-

D

-

Q

-

V

I

E

D

Q

S

A

A

V

T

K

E

A

V

I

I

G

N

W

F

A

V

R

K

E

S

Y

K

T

G

D

I

D

E

I

V

E

R

F

F

S

S

A

S

E

E

D

D

A

S

G

F

R

R

S

S

E

D

I

L

D

V

F

D

L

L

C

L

R

S

I

L

F

Y

D

K

A

A

V

V

I

D

K

K

A

I

G

G

A

V

K

N

T

R

I

V

N

G

V

I

P

A

D

D

T
|
T

V

V

G

G

Y

C

N

A

V

T

P

P

E

R

Q

Q

Y

V

A

Y

A

D

T

L

L

I

R

R

T

T

L

L

I

-

E

R

R

G

V

V

P

V

N

S

A

C

D

D

K

-

V

-

I

-

W

I

S

E

V

C

H
|
H

C

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

S

A

N

N

S

A

L

Y

A

C

A

A

V

L

M

E

A

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

A

T

S

P

L

L

E

G

E

A

I

L

V

L

-

A

-

R

M

M

A

Y

V

V

R

T

T

D

R

R

A

E

D

-

V

-

F

-

P

Y

V

I

S

T

T

H

N

K

I

Y

D

K

T

L

T

N

Q

Q

I

L

V

R

P

E

A

L

S

E

K

N

L

L

V

V

S

A

Q

D

I

A

T

V

G

E

Y

V

P

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

G

S

A

R

N

Y

K

V

L

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

R

K

A

S

R

R

L

A

Q

E

E

Q

L

L

G

N

I

L

E

H

I

L

G

-

S

T

E

D

E

A

Q

Q

L

A

N

K

H

E

A

L

F

T

A

V

R

R

F

I

K

K

E

K

L

L

A

A

D

D

K

V

K

R

H

T

E

L

I

A

F

M

D

D

E

D

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)
28% identity, 72% coverage: 7:375/511 of query aligns to 14:356/364 of 3ivsA

query
sites
3ivsA

I

I

F

I

D

E

T

S

T

T

L

L

R

R

D
x
E

G

G

E

E

Q
|
Q

S

F

P

A

G

N

A

A

S

F

M

F

T

D

R

T

D

E

E

K

K

K

L

I

R

Q

I

I

A

A

R

K

Q

A

L

L

E

D

R

N

M

F

R

G

V

V

D

D

V

Y

I

I

E

E

A

L

G

T

F

S

A

P

A

V

A

A

S

S

N

E

G

Q

D

S

F

R

E

Q

S

D

V

C

R

E

S

A

I

I

A

C

E

K

A

L

I

G

K

L

E

K

S

C

T

K

V

I

C

L

S

T

L

H

A

I

R

R

A

C

N

H

E

M

N

D

D

D

I

A

R

R

R

V

A

A

G

V

E

E

A

T

I

-

R

-

P

-

A

-

A

G

R

V

G

D

R

G

I

V

H

D

T

V

F

V

I

I

A

G

T

T

S

T

P

Y

I

I

H

-

M

-

E

-

K

-

L

-

R

-

M

-

T

-

P

-

D

-

Q

-

V

-

V

I

E

D

Q

S

A

A

V

T

K

E

A

V

I

I

G

N

W

F

A

V

R

K

E

S

Y

K

T

G

D

I

D

E

I

V

E

R

F

F

S

S

A

S

E

E

D

D

A

S

G

F

R

R

S

S

E

D

I

L

D

V

F

D

L

L

C

L

R

S

I

L

F

Y

D

K

A

A

V

V

I

D

K

K

A

I

G

G

A

V

K

N

T

R

I

V

N

G

V

I

P

A

D

D

T

T

V

V

G

G

Y

C

N

A

V

T

P

P

E

R

Q

Q

Y

V

A

Y

A

D

T

L

L

I

R

R

T

T

L

L

I

-

E

R

R

G

V

V

P

V

N

S

A

C

D

D

K

-

V

-

I

-

W

I

S

E

V

C

H
|
H

C

F

H
|
H

N

N

D

D

L

T

G

G

L

M

A

A

V

I

S

A

N

N

S

A

L

Y

A

C

A

A

V

L

M

E

A

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

A

T

S

P

L

L

E

G

E

A

I

L

V

L

-

A

-

R

M

M

A

Y

V

V

R

T

T

D

R

R

A

E

D

-

V

-

F

-

P

Y

V

I

S

T

T

H

N

K

I

Y

D

K

T

L

T

N

Q

Q

I

L

V

R

P

E

A

L

S

E

K

N

L

L

V

V

S

A

Q

D

I

A

T

V

G

E

Y

V

P

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

G

S

A

R

N

Y

K

V

L

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

N

N

A

A

F

I

R

K

A

S

R

R

L

A

Q

E

E

Q

L

L

G

N

I

L

E

H

I

L

G

Q

S

A

E

K

E

E

Q

L

L

T

N

-

H

-

A

-

F

-

A

V

R

R

F

I

K

K

E

K

L

L

A

A

D

V

K

R

K

T

H

L

E

A

I

M

F

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)
30% identity, 72% coverage: 7:374/511 of query aligns to 6:365/376 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

R

T

D

Q

E

D

K

K

L

V

R

E

I

I

A

A

R

K

Q

A

L

L

E

D

R

E

M

F

R

G

V

I

D

E

V

Y

I

I

E

E

A

V

G

T

F

T

A

P

A

V

A

A

S

S

N

P

G

Q

D

S

F

R

E

K

S

D

V

A

R

E

S

V

I

L

A

A

E

S

-

L

A

G

I

L

K

K

E

A

S

K

T

V

V

V

C

T

S
x
H

L

I

A

-

R

-

A

-

N

-

E

Q

N

C

D

R

I

L

R

D

R

A

A

A

G

K

E

V

A

A

I

V

R

E

P

T

A

G

A

V

R

Q

G

G

R

-

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

K

A

K

H

L

G

R

R

M

D

T

I

P

P

D

-

Q

R

V

I

E

E

Q

E

A

A

V

K

K

E

A

V

I

I

G

A

W

Y

A

I

R

R

E

E

Y

A

T

A

D

P

D

H

I

V

E

E

-

V

-
x
R

F

F

S
|
S

A

A

E

E

D

D

A

T

G

F

R

R

S

S

E

E

I

E

D

Q

F

D

L

L

C

L

R

A

I

V

F

Y

D

E

A

A

V

V

I

A

K

P

A

Y

G

-

A

V

K

D

T

R

I

V

N

G

V

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

N

A

V

T

P

P

E

R

Q

Q

Y

V

A

Y

A

A

T

L

L

V

R

R

T

E

L

-

I

V

E

R

R

R

V

V

-

V

-

G

P

P

N

R

A

V

D

D

K

-

V

-

I

-

W

I

S

E

V

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

A

A

V

I

S

A

N

N

S

A

L

Y

A

E

A

A

V

I

M

E

A

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

A

T

S

P

L

L

E

G

I

F

V

L

M

A

A

R

V

M

R

Y

T

T

R

L

A

Q

D

P

V

E

F

Y

P

-

V

V

S

R

T

R

N

K

I

Y

D

K

T

L

T

E

Q

M

I

L

V

P

P

E

A

L

S

D

K

R

L

M

V

V

S

A

Q

R

I

M

T

V

G

G

Y

V

P

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

G

K

A

R

N

K

K

L

L

I

V

I

L

A

G

S

K

R

H

L

S

T

G

G

R

R

N

H

A

A

F

I

R

K

A

A

R

R

L

A

Q

E

E

E

L

L

G

G

I

L

E

H

I

Y

G

G

S

-

E

E

Q

E

L

L

N

H

H

R

A

V

F

T

A

Q

R

H

F

I

K

K

E

A

L

L

A

A

D

D

K

R

K

G

H

Q

E

L

I

T

F

L

D

E

E

E

R12 (= R13) binding 2-oxoglutarate
E13 (≠ D14) binding Mg(2+)
H72 (≠ S72) 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+)

3hq1A Crystal structure of mycobacterium tuberculosis leua complexed with citrate and mn2+
27% identity, 95% coverage: 12:499/511 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

R

P

D

A

E

R

K

K

L

R

R

R

I

M

A

F

R

D

Q

L

L

L

E

V

R

R

M

M

R

G

V

Y

D

K

V

E

I

I

E

E

A

V

G

G

F

F

A

P

A

S

A

A

S

S

N

Q

G

T

D

D

F

F

E

D

S

F

V

V

R

R

S

E

I

I

A

I

E

E

-

Q

-

G

A

A

I

I

K

P

E

D

S

D

-

V

T

T

V

I

C

Q

S

V

L

L

A

T

R

Q

A

C

N

R

E

P

N

E

D

L

I

I

R

E

R

R

A

T

G

F

E

Q

A

A

I

C

R

S

P

G

A

A

A

P

R

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

K

V

L

F

R

R

M

A

T

N

P

R

D

A

Q

E

V

V

-

Q

-

A

-

I

-

A

-

T

-

D

-

G

-

A

-

R

-

K

-

C

V

V

E

E

Q

Q

A

A

V

A

K

K

A

Y

I

P

G

G

W

T

A

Q

R

W

E

R

Y

F

T

-

D

-

I

-

E

E

F

Y

S

S

A

P

E

E

D

S

A

Y

G

T

R

G

S

T

E

E

I

L

D

E

F

Y

L

A

C

K

R

Q

I

V

F

C

D

D

A

A

V

V

I

G

K

E

A

V

G

I

A

A

K

P

T

T

-

P

-

E

-

R

-

P

-

I

I

F

N

N

V

L

P

P

D

A

T

T

V

V

G

E

Y

M

N

T

V

T

P

P

E

N

Q

V

Y

Y

A

A

A

D

T

S

L

I

R

E

T

W

L

M

I

S

E

R

R

N

V

L

P

A

N

N

A

R

D

E

K

S

V

V

I

I

W

L

S

S

V

L

H
|
H

C

P

H
|
H

N

N

D

D

L

R

G

G

L

T

A

A

V

V

S

A

N

A

S

A

L

E

A

L

A

G

V

F

M

A

A

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

A

V

S

C

L

L

E

V

E

T

I

L

V

G

M

L

A

N

V

L

R

F

T

S

R

R

A

G

D

-

V

-

F

-

P

-

V

V

S

D

T

P

N

Q

I

I

D

D

T

F

T

S

Q

N

I

I

V

D

P

E

A

I

S

R

K

R

L

T

V

V

S

E

Q

Y

I

C

T

N

G

Q

Y

L

P

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

H

G

R

L

E

D

T

A

Y

M

E

K

I

L

M

D

R

A

A

D

E

A

D

A

V

D

G

C

-

D

-

V

-

D

-

M

-

L

W

W

G

Q

A

V

N

P

K

Y

L

L

V

P

L

I

G

D

K

P

H

R

S

D

G

V

R

G

N

R

A

T

F

Y

R

E

A

A

R

V

L

I

Q

K

-

G

-

V

-

A

-

Y

-

I

-

M

-

K

-

T

E

D

L

H

G

G

I

L

E

S

I

L

G

P

S

R

E

R

E

L

Q

Q

L

I

N

E

H

-

A

-

F

-

A

-

R

-

F

F

K

S

E

Q

L

V

A

I

D

-

K

Q

K

K

H

I

E

E

I

V

F

S

D

P

E

K

D

E

L

M

H

W

A

D

L

A

M

F

S

A

D

E

E

E

A

Y

V

L

T

A

P

P

E

V

Q

R

E

P

H

L

F

E

R

R

L

I

V

-

A

-

T

-

R

R

F

Q

H

H

-

V

-

D

-

A

S

D

E

D

T

D

G

G

E

G

T

T

P

T

R

S

A

I

E

T

V

A

T

T

L

V

A

K

I

I

G

N

G

G

Q

V

E

E

T

T

R

E

S

I

Q

S

A

G

E

S

G

G

S

N

G

G

P

P

V

L

D

A

A

A

A

F

F

V

K

H

A

A

I

L

E

A

S

D

V

V

A

-

G

G

S

F

G

D

S

V

E

A

L

V

L

L

L

D

Y

Y

S

Y

V

E

N

H

A

A

I

M

T

S

T

A

G

G

T

D

D

D

A

A

Q

Q

G

A

-

A

-

Y

-

V

E

E

V

A

T

S

V

V

R

T

L

I

A

S

K

K

D

-

G

-

R

-

V

T

V

V

N

W

G

G

Q

V

G

G

A

I

D

A

T

P

D

S

I

I

I

T

V

T

A

A

S

S

A

L

K

R

A

A

Y

V

L

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)
27% identity, 95% coverage: 12:499/511 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

G

I

A

D

S

P

M

M

T

S

R

P

D

A

E

R

K

K

L

R

R

R

I

M

A

F

R

D

Q

L

L

L

E

V

R

R

M

M

R

G

V

Y

D

K

V

E

I

I

E

E

A

V

G

G

F

F

A

P

A

S

A

A

S

S

N

Q

G

T

D

D

F

F

E

D

S

F

V

V

R

R

S

E

I

I

A

I

E

E

-

Q

-

G

A

A

I

I

K

P

E

D

S

D

-

V

T

T

V

I

C

Q

S

V

L

L

A

T

R

Q

A

C

N

R

E

P

N

E

D

L

I

I

R

E

R

R

A

T

G

F

E

Q

A

A

I

C

R

S

P

G

A

A

A

P

R

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

K

V

L

F

R

R

M

A

T

N

P

R

D

A

Q

E

V

V

-

Q

-

A

-

I

-

A

-

T

-

D

-

G

-

A

-

R

-

K

-

C

V

V

E

E

Q

Q

A

A

V

A

K

K

A

Y

I

P

G

G

W

T

A

Q

R

W

E

R

Y

F

T

-

D

-

I

-

E

E

F

Y

S

S

A

P

E

E

D

S

A

Y

G

T

R

G

S

T

E

E

I

L

D

E

F

Y

L

A

C

K

R

Q

I

V

F

C

D

D

A

A

V

V

I

G

K

E

A

V

G

I

A

A

K

P

T

T

-

P

-

E

-

R

-

P

-

I

I

F

N

N

V

L

P
|
P

D

A

T
|
T

V

V

G

E

Y

M

N

T

V

T

P

P

E

N

Q

V

Y

Y

A

A

A

D

T

S

L

I

R

E

T

W

L

M

I

S

E

R

R

N

V

L

P

A

N

N

A

R

D

E

K

S

V

V

I

I

W

L

S

S

V

L

H
|
H

C

P

H
|
H

N

N

D

D

L

R

G

G

L

T

A

A

V

V

S

A

N

A

S

A

L

E

A

L

A

G

V

F

M

A

A

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

A

V

S

C

L

L

E

V

E

T

I

L

V

G

M

L

A

N

V

L

R

F

T

S

R

R

A

G

D

-

V

-

F

-

P

-

V

V

S

D

T

P

N

Q

I

I

D

D

T

F

T

S

Q

N

I

I

V

D

P

E

A

I

S

R

K

R

L

T

V

V

S

E

Q

Y

I

C

T

N

G

Q

Y

L

P

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

H

G

R

L

E

D

T

A

Y

M

E

K

I

L

M

D

R

A

A

D

E

A

D

A

V

D

G

C

-

D

-

V

-

D

-

M

-

L

W

W

G

Q

A

V

N

P

K

Y

L

L

V

P

L

I

G

D

K

P

H

R

S

D

G

V

R

G

N

R

A

T

F

Y

R

E

A

A

R

V

L

I

Q

K

-

G

-

V

-

A

-

Y

-

I

-

M

-

K

-

T

E

D

L

H

G

G

I

L

E

S

I

L

G

P

S

R

E

R

E

L

Q

Q

L

I

N

E

H

-

A

-

F

-

A

-

R

-

F

F

K

S

E

Q

L

V

A

I

D

-

K

Q

K

K

H

I

E

E

I

V

F

S

D

P

E

K

D

E

L

M

H

W

A

D

L

A

M

F

S

A

D

E

E

E

A

Y

V

L

T

A

P

P

E

V

Q

R

E

P

H

L

F

E

R

R

L

I

V

-

A

-

T

-

R

R

F

Q

H

H

-

V

-

D

-

A

S

D

E

D

T

D

G

G

E

G

T

T

P

T

R

S

A

I

E

T

V

A

T

T

L

V

A

K

I

I

G

N

G

G

Q

V

E

E

T

T

R

E

S

I

Q

S

A

G

E

S

G

G

S

N

G

G

P

P

V

L

D

A

A

A

A

F

F

V

K

H

A

A

I

L

E

A

S

D

V

V

A

-

G

G

S

F

G

D

S

V

E

A

L

V

L

L

L

D

Y

Y

S

Y

V

E

N

H

A

A

I

M

T

S

T

A

G

G

T

D

D

D

A

A

Q

Q

G

A

-

A

-

Y

-

V

E

E

V

A

T

S

V

V

R

T

L

I

A

S

K

K

D

-

G

-

R

-

V

T

V

V

N

W

G

G

Q

V

G

G

A

I

D

A

T

P

D

S

I

I

I

T

V

T

A

A

S

S

A

L

K

R

A

A

Y

V

L

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)

3hpsA Crystal structure of mycobacterium tuberculosis leua complexed with ketoisocaproate (kic)
27% identity, 95% coverage: 12:499/511 of query aligns to 62:573/575 of 3hpsA

query
sites
3hpsA

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

R

P

D

A

E

R

K

K

L

R

R

R

I

M

A

F

R

D

Q

L

L

L

E

V

R

R

M

M

R

G

V

Y

D

K

V

E

I

I

E

E

A

V

G

G

F

F

A

P

A

S

A

A

S

S

N

Q

G

T

D

D

F

F

E

D

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binding 2-oxo-4-methylpentanoic acid: R63 (= R13), H150 (= H97), Y152 (≠ F99), P235 (= P169), T237 (= T171), H268 (= H202), H270 (= H204)
binding leucine: G500 (= G428), P501 (= P429), L502 (≠ V430), A503 (≠ D431), D530 (≠ T459), A532 (= A461), Q533 (= Q462), P557 (≠ T483), I559 (= I485)
binding zinc ion: D64 (= D14), H268 (= H202), H270 (= H204)

3figB Crystal structure of leucine-bound leua from mycobacterium tuberculosis (see paper)
26% identity, 95% coverage: 12:499/511 of query aligns to 62:574/577 of 3figB

query
sites
3figB

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binding leucine: G501 (= G428), P502 (= P429), L503 (≠ V430), A504 (≠ D431), D531 (≠ T459), A533 (= A461), P558 (≠ T483), I560 (= I485)
binding zinc ion: D64 (= D14), H268 (= H202), H270 (= H204)

Query Sequence

>WP_011766887.1 NCBI__GCF_000061505.1:WP_011766887.1
MKDALIIFDTTLRDGEQSPGASMTRDEKLRIARQLERMRVDVIEAGFAAASNGDFESVRS
IAEAIKESTVCSLARANENDIRRAGEAIRPAARGRIHTFIATSPIHMEKKLRMTPDQVVE
QAVKAIGWAREYTDDIEFSAEDAGRSEIDFLCRIFDAVIKAGAKTINVPDTVGYNVPEQY
AATLRTLIERVPNADKVIWSVHCHNDLGLAVSNSLAAVMAGARQVECTINGLGERAGNAS
LEEIVMAVRTRADVFPVSTNIDTTQIVPASKLVSQITGYPVQPNKAIVGANAFAHESGIH
QDGVLKHRETYEIMRAEDVGWGANKLVLGKHSGRNAFRARLQELGIEIGSEEQLNHAFAR
FKELADKKHEIFDEDLHALMSDEAVTPEQEHFRLVATRFHSETGETPRAEVTLAIGGQET
RSQAEGSGPVDAAFKAIESVAGSGSELLLYSVNAITTGTDAQGEVTVRLAKDGRVVNGQG
ADTDIIVASAKAYLNALNKLCGGSEKLNPQV

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