SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011734424.1 NCBI__GCF_000015045.1:WP_011734424.1 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)
56% identity, 96% coverage: 16:513/518 of query aligns to 9:508/517 of Q9JZG1

query
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Q9JZG1

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D16 (= D23) binding Mn(2+)
H204 (= H212) binding Mn(2+)
H206 (= H214) binding Mn(2+)
N240 (= N248) binding Mn(2+)

Sites not aligning to the query:

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

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
48% identity, 73% coverage: 10:389/518 of query aligns to 14:407/409 of 6e1jA

query
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6e1jA

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binding coenzyme a: Q30 (= Q26), F60 (= F56), S63 (≠ A59), I95 (≠ L82), R97 (= R84), F121 (= F109), K132 (= K120), L133 (= L121), S322 (= S307), G323 (= G308), I324 (= I309), D327 (≠ H312), K331 (≠ M316), L359 (≠ H341), R362 (= R344), H363 (= H345)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P179), T194 (= T181), H225 (= H212), H227 (= H214)
binding manganese (ii) ion: D27 (= D23), V82 (vs. gap), E84 (vs. gap), H225 (= H212), H227 (= H214)

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
61% identity, 61% coverage: 16:332/518 of query aligns to 6:308/308 of 3rmjB

query
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3rmjB

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-

H

-

Q

-

H

-

G

-

M

-

D

-

S

-

T

T

Y

Y

E

E

I

I

M

M

T

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P

A

E

E

S

S

V

V

G

G

L

W

A

A

active site: Q16 (= Q26)
binding manganese (ii) ion: D13 (= D23), H201 (= H212), H203 (= H214), N237 (= N248)

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: 14:398/518 of query aligns to 85:485/506 of Q9FG67

query
sites
Q9FG67

I

V

R

R

I

V

F

F

D

D

T

T

L

L

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R

D

D

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G

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Q

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P

G

G

N

G

S
|
S

M

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E

Q

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K

L

L

R

E

V

I

A

A

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R

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Q

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E

A

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K

L

L

N

R

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V

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D

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F

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P

I

G

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L

E

E

A

T

V

I

K

K

R

T

I

I

A

A

Q

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T

L

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K

N

-

E

-

V

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D

-

E

-

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Y

-

V

P

P

Q

V

I

I

A

C

G

A

L

I

C

A

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C

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K

R

D

D

I

I

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R

A

A

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W

E

E

A

A

V

L

Q

K

Y

Y

A

A

G

-

E

K

R

R

A

P

R

R

I

I

H

L

T

V

F

F

I

T

A

S

T

T

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D

D

I

I

H

H

M

M

K

K

Y

Y

K

K

L

L

Q

K

M

K

E

T

P

Q

A

E

K

E

V

V

L

I

A

E

T

M

A

A

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S

A

S

V

I

K

R

Y

F

A

A

K

K

G

S

Y

L

T

G

S

F

N

N

-

D

V

I

E

Q

F

F

S

G

C

C

E

E

D

D

A

G

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G

R

R

T

S

R

D

L

K

P

D

F

F

L

L

A

C

E

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V

L

E

G

A

E

T

A

I

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K

A

A

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T

T

V

V

V

N

T

I

I

P

G

D

D

T

T

V

V

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G

Y

I

T

N

T

M

P

P

S

H

E

E

F

Y

Y

G

N

E

I

L

I

V

R

T

Y

Y

L

L

K

K

E

A

N

N

V

T

S

P

N

G

I

I

E

D

K

D

A

V

V

V

I

V

S
x
A

V

V

H

H

C

C

H

H

N

N

D

D

L

L

G

G

L

L

S

A

V

T

A

A

N

N

S

S

L

I

A

A

A

G

I

I

Q

R

A

A

G

G

A

A

G

R

Q

Q

V

V

E

E

C

V

T

T

I

I

N

N

G

G

I

I

G

G

E

E

R

R

A

S

G

G

N

N

C

A

S

S

L

L

E

E

L

V

V

V

M

M

V

A

L

L

R

K

T

C

R

R

-

G

-

A

H

Y

D

V

I

I

L

N

P

G

Y

V

Y

Y

T

T

N

K

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I

A

D

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T

E

R

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Q

L

I

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M

S

A

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S

S

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M

L

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S

Q

T

E

I

Y

T

T

G

G

I

L

M

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

H

D

G

G

M

I

M

L

M

K

D

N

S

R

S

S

T

T

Y

Y

E

E

I

I

M

L

T

S

P

P

E

E

S

D

V

I

G

G

L

I

A

V

A

K

-

S

-

Q

-

N

G

S

A

G

L

L

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

H

H

A

A

F

V

K

K

K

D

R

R

L

L

Q

K

E

E

L

L

G

G

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Y

E

E

L

L

D

D

E

E

M

K

L

L

N

N

R

A

A

V

F

F

V

S

R

L

F

F

K

R

A

D

L

L

A

T

D

K

L

N

K

K

E

R

V

I

F

T

D

D

E

A

D

D

L

L

D

K

A

A

I

L

V

V

-

T

-

S

A

S

D

D

E

E

S

I

R

S

E

L

E

E

E

K

M

L

S102 (= S31) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ S210) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

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, 74% coverage: 11:391/518 of query aligns to 82:476/503 of Q9FN52

query
sites
Q9FN52

R

K

R

N

L

Y

I

V

R

R

I

V

F

L

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

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S

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P

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G

N

A

S

A

M

L

N

T

M

P

E

P

E

Q

K

K

L

L

R

E

V

I

A

A

R

R

Q

Q

L

L

E

A

K

K

L

L

N

R

V

V

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D

I

I

I

M

E

E

A

V

G

G

F

F

P

P

I

V

A

S

S

S

V

E

G

E

D

E

F

F

E

E

A

A

V

I

K

K

R

T

I

I

A

A

Q

K

T

T

L

V

T

G

K

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

V

P

P

Q

V

I

I

A

C

G

G

L

I

C

A

R

R

S

C

S

K

D

K

K

R

D

D

I

I

D

E

R

A

A

T

W

W

E

E

A

A

V

L

Q

K

Y

Y

A

A

G

-

E

K

R

R

A

P

R

R

I

V

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M

T

L

F

F

I

T

A

S

T

T

S

S

D

E

I

I

H

H

M

M

K

K

Y

Y

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L

Q

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M

K

E

T

P

K

A

E

K

E

V

V

L

I

A

E

T

M

A

A

V

V

K

N

A

S

V

V

K

K

Y

Y

A

A

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K

-

S

-

L

G

G

Y

F

T

-

S

K

N

D

V

I

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F

F

S

G

C

C

E

E

D

D

A

G

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G

R

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D

F

F

L

I

A

C

E

K

V

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A

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S

I

I

D

K

A

A

G

G

A

A

T

T

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A

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D

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G
|
G

Y

I

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Y

G

N

E

I

L

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I

A

E

D

K

D

A

I

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V

I

F

S

A

V

I

H

H

C

C

H

H

N

N

D

D

L

L

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G

L

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S

A

V

T

A

A

N

N

S

T

L

I

A

S

A

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C

A

A

G

G

A

A

G

R

Q

Q

V

V

E

E

C

V

T

T

I

I

N

N

G

G

I

I

G

G

E

E

R

R

A

S

G

G

N

N

C

A

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P

L

L

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E

L

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M

V

A

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G

D

E

I

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L

L

-

M

-

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Y

Y

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K

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I

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R

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M

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A

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S

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T

E

I

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T

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G

G

I

M

M

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

H

D

G

G

M

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D

N

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R

S

S

T

T

Y

Y

E

E

I

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P

P

E

E

S

D

V

V

G

G

L

I

A

V

A

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-

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-

N

G

S

A

G

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I

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V

L

L

G

G

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A

A

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V

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E

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G

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Y

E

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N

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D

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A

A

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L

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V

A

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D

N

G263 (= G183) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
34% identity, 73% coverage: 16:393/518 of query aligns to 24:389/399 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

N

V

S

V

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F

N

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M

T

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R

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V

R

E

V

I

A

A

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A

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D

L

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N

G

V

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D

Q

I

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I

I

E

E

A

A

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G

F

H

P

P

I

A

A
x
V

S

S

V

P

G

D

D

I

F

Y

E

E

A

G

V

I

K

R

R

R

I

I

A

I

Q

K

T

L

-

K

-

R

-

E

-

G

L

V

T

I

K

K

P

S

Q

E

I

I

A

V

G

A

L

H

C

S

R
|
R

S
x
A

S

V

D

K

K

R

D

D

I

I

D

E

R

V

A

G

W

A

E

E

A

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V

-

Q

-

Y

-

A

-

G

-

E

E

R

A

A

D

R

R

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I

H

A

T

I

F
|
F

I

Y

A

G

T

I

S

S

D

D

I

T

H

H

M

L

K

K

Y

A

K

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L
x
H

Q

H

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T

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R

A

D

K

E

V

A

L

L

A

R

T

S

A

I

V

A

K

E

A

T

V

V

K

S

Y

Y

A

A

K

K

G

S

Y

H

T

G

S

V

N

K

V

V

E
x
R

F

F

S
x
T

C

A

E
|
E

D

D

A

A

V

T

R

R

T

A

R

D

L

Y

P

Q

F

Y

L

L

A

L

E

E

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V

V

I

E

K

A

T

T

V

I

R

D

D

A

A

G

G

A

A

T

D

T

R

V

V

N
x
S

I

I

P

A

D

D

T
|
T

V

V

G

G

Y

V

T

L

T

Y

P

P

S

S

E

R

F

T

Y

R

N

E

I

L

I

F

R

K

Y

D

L

L

K

T

E

S

N

R

V

F

S

P

N

D

I

I

E

E

K

-

A

-

V

-

I

F

S

D

V

I

H
|
H

C

A

H
|
H

N

N

D

D

L

L

G

G

L

M

S

A

V

V

A

A

N

N

S

V

L

L

A

A

I

A

Q

E

A

G

G

G

A

A

G

T

Q

I

V

I

E

H

C

T

T

T

I

L

N

N

G

G

I

L

G

G

E

E

R

R

A

V

G

G

N

I

C

A

S

P

L

L

E

Q

E

V

L

V

V

A

M

A

V

A

L

L

R

K

T

Y

R

H

H

F

D

G

I

I

L

-

P

-

Y

-

T

E

N

V

V

V

A

D

T

L

E

K

Q

K

L

L

T

S

S

E

S

V

S

A

R

S

L

L

L

V

S

E

T

K

I

Y

T

S

G

G

I

I

M

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

H

A

G

G

M

V

M

L

M

N

D

D

S

P

S

K

T

T

Y

Y

E

E

I

F

M

L

T

P

P

P

E

E

S

T

V

F

G

G

L

R

A

S

A

R

G

D

A

-

L

Y

V

V

L

I

G

D

K

K

H

Y

S

T

G

G

R

K

H

H

A

A

F

V

K

K

K

D

R

R

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F

Q

D

E

R

L

L

G

G

H

V

E

K

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L

D

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D

D

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M

E

L

I

N

D

R

Q

A

V

F

L

V

A

R

K

F

I

K

K

A

S

L

N

A

P

D

N

L

V

K

R

K

-

E

-

V

-

F

F

D

Y

E

R

D

D

L

V

D

D

A

L

I

L

V

E

A

L

D

A

E

E

S

S

binding 2-oxoglutaric acid: R30 (= R22), R154 (≠ E147), T156 (≠ S149), E158 (= E151), S184 (≠ N177), T188 (= T181), H216 (= H212), H218 (= H214)
binding coenzyme a: V67 (≠ A59), R96 (= R84), A97 (≠ S85), F116 (= F109), H128 (≠ L121), E158 (= E151)
binding zinc ion: E31 (≠ D23), H216 (= H212), H218 (= H214)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
32% identity, 73% coverage: 12:388/518 of query aligns to 2:377/379 of 4ov4A

query
sites
4ov4A

R

K

L

T

I

I

R

H

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

N

R

S

P

M

W

N

T

M

I

E

D

E

E

K

K

L

I

R

E

V

V

A

F

R

D

Q

L

L

L

E

V

K

E

L

L

N

N

V

V

D

D

I

G

I

I

E

E

A

V

G

G

F

F

P

P

I

S

A

S

S

N

V

E

G

T

D

E

F

F

E

H

A

T

V

C

K

Q

R

V

I

L

A

S

Q

K

T

R

L

A

T

P

K

K

P

G

Q

K

-

P

I

I

A

A

G

A

L

L

C

S

R

R

S

A

S

N

D

Q

K

N

D

E

I

I

D

A

R

V

A

T

W

W

E

E

A

A

V

I

Q

Q

Y

K

A

A

G

-

E

D

R

C

A

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

D

D

I

F

H

S

M

I

K

K

Y

H

K

V

L

L

Q

K

M

I

E

S

P

E

A

K

K

E

V

V

L

L

A

Q

T

K

A

I

V

R

K

N

A

S

V

I

K

S

Y

F

A

A

K

R

-

S

-

I

-

V

G

G

Y

P

T

G

S

I

N

E

V

I

E

Q

F

F

S

S

C

G

E

E

-

H

-

F

-

G

D

D

A

A

V

I

R

E

T

N

R

-

L

F

P

A

F

F

L

T

A

K

E

E

V

A

V

F

E

L

A

T

T

A

I

I

D

E

A

A

G

G

A

A

T

N

T

I

V

I

N

N

I

L

P
|
P

D

N

T
|
T

V

V

G

E

Y

R

T

Y

T

R

P

P

S

M

E

V

F

F

Y

V

N

N

I

M

I

V

R

K

Y

E

L

I

K

K

E

D

N

V

V

V

S

K

N

-

I

-

E

D

K

K

A

A

V

I

I

I

S

S

V

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

L

M

S

A

V

T

A

A

N

T

S

S

L

V

A

E

A

S

I

V

Q

Y

A

V

G

G

A

A

G

E

Q

Q

V

I

E

E

C

V

T

A

I

L

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N

N

C

T

S

N

L

L

E

Y

E

E

L

T

V

A

M

I

V

A

L

L

R

H

T

Q

R

N

H

G

D

E

I

N

L

L

P

-

Y

-

T

-

N

N

V

I

A

N

T

F

E

Q

Q

R

L

I

T

Y

S

P

S

T

S

A

R

K

L

R

L

I

S

S

T

E

I

L

T

T

G

G

I

I

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V

I

Q

G

P

E

N

K

K

T

A

P

I

I

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I

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G

A

E

N

D

A

I

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F

A

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

H

H

G

-

M

-

M

Q

D

S

S

K

S

G

T

A

Y

Y

E

R

I

T

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F

T

S

P

P

E

E

S

F

V

V

G

G

-

R

L

M

A

D

A

K

G

E

A

T

L

I

V

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

H

K

A

A

F

I

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E

K

F

R

L

L

L

Q

H

E

Q

L

R

G

G

H

I

E

Q

L

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D

S

D

K

E

E

M

G

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N

H

R

H

A

L

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F

V

S

R

L

F

A

K

K

A

S

L

I

A

S

D

S

L

R

K

E

-

N

K

R

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I

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E

E

A

D

E

L

L

D

V

A

A

I

L

active site: Q16 (= Q26)
binding 3-methyl-2-oxobutanoic acid: R12 (= R22), P174 (= P179), T176 (= T181), H205 (= H212), H207 (= H214)
binding zinc ion: D13 (= D23), H205 (= H212), H207 (= H214)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
32% identity, 73% coverage: 12:388/518 of query aligns to 2:379/380 of 4ov9A

query
sites
4ov9A

R

K

L

T

I

I

R

H

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

N

R

S

P

M

W

N

T

M

I

E

D

E

E

K

K

L

I

R

E

V

V

A

F

R

D

Q

L

L

L

E

V

K

E

L

L

N

N

V

V

D

D

I

G

I

I

E

E

A

V

G

G

F

F

P

P

I

S

A

S

S

N

V

E

G

T

D

E

F

F

E

H

A

T

V

C

K

Q

R

V

I

L

A

S

Q

K

T

R

L

A

T

P

K

K

P

G

Q

K

-

P

I

I

A

A

G

A

L
|
L

C

S

R

R

S

A

S

N

D

Q

K

N

D

E

I

I

D

A

R

V

A

T

W

W

E

E

A

A

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Q

Y

K

A

A

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-

E

D

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C

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A

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D

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I

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K

Y

H

K

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L

L

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K

M

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E

S

P

E

A

K

K

E

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V

L

L

A

Q

T

K

A

I

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R

K

N

A

S

V

I

K

S

Y

F

A

A

K

R

-

S

-

I

-

V

G

G

Y

P

T

G

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I

N

E

V

I

E

Q

F

F

S

S

C

G

E

E

-

H

-

F

-

G

D

D

A

A

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I

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R

-

L

F

P

A

F

F

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A

K

E

E

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A

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F

E

L

A

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T

A

I

I

D

E

A

A

G

G

A

A

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N

T

I

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I

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N

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T

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V

G

E

Y

R

T

Y

T

R

P

P

S

M

E

V

F

F

Y

V

N

N

I

M

I

V

R

K

Y

E

L

I

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K

E

D

N

V

V

V

S

K

N

-

I

-

E

D

K

K

A

A

V

I

I

I

S

S

V

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

L

M

S

A

V

T

A

A

N

T

S

S

L

V

A

E

A

S

I

V

Q

Y

A

V

G

G

A

A

G

E

Q

Q

V

I

E

E

C

V

T

A

I

L

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N

N

C

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S

N

L

L

E

Y

E

E

L

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V

A

M

I

V

A

L

L

R

H

T

Q

R

N

H

G

D

E

I

N

L

L

P

-

Y

-

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-

N

N

V

I

A

N

T

F

E

Q

Q

R

L

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Y

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P

S

T

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A

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K

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R

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S

T

E

I

L

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T

G

G

I

I

M

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I

Q

G

P

E

N

K

K

T

A

P

I

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I

G

G

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E

N

D

A

I

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F

A

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H

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G

I

I

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Q

Q

H

-

G

T

M

L

M

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M

Q

D

S

S

K

S

G

T

A

Y

Y

E

R

I

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F

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P

P

E

E

S

F

V

V

G

G

-

R

L

M

A

D

A

K

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E

A

T

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S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

H

K

A

A

F

I

K

E

K

F

R

L

L

L

Q

H

E

Q

L

R

G

G

H

I

E

Q

L

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D

S

D

K

E

E

M

G

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N

H

R

H

A

L

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F

V

S

R

L

F

A

K

K

A

S

L

I

A

S

D

S

L

R

K

E

-

N

K

R

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I

F

T

D

E

E

A

D

E

L

L

D

V

A

A

I

L

active site: Q16 (= Q26)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R22), L73 (= L82), T176 (= T181), H205 (= H212), H207 (= H214)
binding zinc ion: D13 (= D23), H205 (= H212), H207 (= H214)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
31% identity, 89% coverage: 10:468/518 of query aligns to 5:466/516 of Q8F3Q1

query
sites
Q8F3Q1

E

E

R

T

R

R

L

L

I

-

R

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

N

V

S

S

M

F

N

S

M

T

E

S

E

E

K

K

L

L

R

N

V

I

A

A

R

K

-

F

Q

L

L

L

E

Q

K

K

L

L

N

N

V

V

D

D

I

R

I

V

E

E

A

I

G

A

F

S

P

A

I

R

A

V

S

S

V

K

G

G

D

E

F

L

E

E

A

T

V

V

K

Q

R

K

I

I

A

M

-

E

-

W

-

A

-

T

-

E

Q

Q

T

L

L

T

T

E

K

R

P

I

Q

E

I

I

A
x
L

G

G

L
x
F

C

V

R

-

S

D

S

G

D

N

K

K

D

T

I

V

D

D

R

-

A

-

W

W

E

-

A

-

V

I

Q

K

Y

D

A

S

G

G

E

-

R

-

A

A

R

K

I

V

H

L

T

N

F

L

I
x
L

A

T

T

K

S

G

D

S

I

L

H

H

-

H

M

L

K

E

Y

K

K

Q

L

L

Q

G

M

K

E

T

P

P

A

K

K

E

V

F

L

F

A

T

T

D

A

V

V

S

K

F

A

V

V

I

K

E

Y

Y

A

A

-

I

-

K

K

S

G

G

Y

L

T

K

S

I

N

N

V

V

E
x
Y

F

L

-
x
E

S

D

C

W

E

S

D

N

A

G

V

F

R

R

T

N

R

S

L

P

P

D

F

Y

L

V

A

K

E

S

V

L

V

V

E

E

A

H

T

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I

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D

K

A

E

G

H

A

I

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E

T

R

V

I

N

F

I

L

P

P

D

D

T
|
T

V

L

G

G

Y

V

T

L

T

S

P

P

S

E

E

E

F

T

Y

F

N

Q

I

G

I

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R

D

Y

S

L

L

K

I

E

Q

N

K

V

Y

S

P

N

D

I

I

E

H

K

-

A

-

V

-

I

F

S

E

V

F

H

H

C

G

H

H

N

N

D

D

L

Y

G

D

L

L

S

S

V

V

A

A

N

N

S

S

L

L

A

Q

A

A

I

I

Q

R

A

A

G

G

A

V

G

K

Q

G

V

L

E

H

C

A

T

S

I

I

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N

N

C

T

S

P

L

L

E

E

E

A

L

L

V

V

M

T

V

-

L

-

R

-

T

T

R

I

H

H

D

D

I

K

L

S

P

N

Y

S

Y

K

T

T

N

N

V

I

A

N

T

E

E

I

Q

A

L

I

T

T

S

E

S

A

S

S

R

R

L

L

L

V

S

E

T

V

I

F

T

S

G

G

I

K

M

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

H
x
D

G

G

M

D

M

K

D

G

S
x
N

S
x
L

T
x
Y

Y

A

E

N

I

P

M

I

T

L

P

P

E

E

S

R

V

F

G

G

L

R

A

K

A

R

G

-

A

S

L

Y

V

A

L

L

G

G

K

K

H

L

S

A

G

G

R

K

H

A

A

S

F

I

K

S

K

E

R

N

L

V

Q

K

E

Q

L

L

G

G

H

M

E

V

L

L

D

S

D

E

E

V

M

V

L

L

N

Q

R

K

A

V

F

L

V

E

R

R

F

V

K

I

A

E

L

L

A

G

D

D

L

Q

K

N

K

K

E

L

V

V

F

T

D

P

E

E

D

D

L

L

D

P

A

F

I

I

V

I

A

A

D

D

E

V

S

S

R

G

E

R

-

T

-

G

E

E

E

K

M

V

Y

L

K

T

L

I

V

K

L

S

L

C

N

N

V

I

S

H

C

S

G

G

S

I

L

G

S

I

V

R

A

P

T

H

A

A

T

Q

V

I

K

E

M

L

E

E

I

Y

N

Q

G

G

Q

K

L

I

L

H

R

K

A

E

A

I

E

S

L

E

G

G

D

D

G

G

P

G

V
x
Y

D
|
D

A

A

T

F

L

M

K

N

A

A

I

L

R

T

K

K

L

I

T

T

K

N

-

R

-

L

-

G

-

I

S

S

K

I

A

P

K

K

L
|
L

E

I

Q

D

F
x
Y

N

E

V

V

G

R

S
x
I

I

P

T

P

G

G

-

K

T
|
T

D

D

A

A

R16 (= R22) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 22:23) binding pyruvate
D17 (= D23) 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 (≠ A80) 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 (≠ L82) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ I110) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ E147) 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 (vs. gap) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T181) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H310) mutation H->A,N: Loss of activity.
D304 (≠ H312) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ S318) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ S319) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ T320) mutation to A: Loss of activity.
Y430 (≠ V437) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (= D438) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L454) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (≠ F457) 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 (≠ S461) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (= T466) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.

Sites not aligning to the query:

468 V→A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
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.

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
32% identity, 72% coverage: 16:389/518 of query aligns to 37:399/418 of Q9Y823

query
sites
Q9Y823

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R43 (= R22) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D23) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q26) mutation to A: Abolishes the catalytic activity.
E74 (= E53) 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 (≠ L82) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ H107) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ E147) 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 (= S149) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E151) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T181) 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 (≠ S210) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H212) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H214) binding 2-oxoglutarate; binding Zn(2+)
R288 (≠ T277) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y321) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ E353) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
32% identity, 72% coverage: 16:389/518 of query aligns to 32:394/400 of 3ivtB

query
sites
3ivtB

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active site: Q42 (= Q26)
binding 2-oxoglutaric acid: R38 (= R22), H98 (≠ L82), R158 (≠ E147), S160 (= S149), T192 (= T181), H219 (= H212), H221 (= H214)
binding zinc ion: E39 (≠ D23), H219 (= H212), H221 (= H214)

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
32% identity, 72% coverage: 16:389/518 of query aligns to 14:365/370 of 3mi3A

query
sites
3mi3A

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active site: Q24 (= Q26)
binding lysine: R20 (= R22), D100 (≠ H107), T163 (= T181), H190 (= H212), H192 (= H214)
binding zinc ion: E21 (≠ D23), H190 (= H212), H192 (= H214)

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
30% identity, 73% coverage: 12:389/518 of query aligns to 2:370/376 of O87198

query
sites
O87198

R

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E

I

W

R

K

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

N

A

S

N

M

F

N

S

M

T

E

Q

E

D

K

K

L

V

R

E

V

I

A

A

R

K

Q

A

L

L

E

D

K

E

L

F

N

G

V

I

D

E

I

Y

I

I

E

E

A

V

G

T

F

T

P

P

I

V

A

A

S

S

V

P

G

Q

D

S

F

R

E

K

A

D

V

A

K

E

R

V

I

L

A

A

Q

S

T

L

L

G

T

L

K

K

P

A

Q

K

I

V

A

V

G

T

-
x
H

-

I

L

Q

C

C

R

R

S

-

D

-

K

-

D

-

I

L

D

D

R

A

A

A

W

K

E

V

A

A

V

V

Q

E

Y

T

A

G

G

V

E

Q

R

G

A

-

R

-

I

I

H
x
D

T

L

F

L

I

F

A

G

T

T

S

S

D

K

I

-

H

Y

M

L

K

R

Y

A

K

A

L

H

Q

G

M

R

E

D

P

I

A

P

K

R

V

I

L

I

A

E

T

E

A

A

V

K

K

E

A

V

V

I

K

A

Y

Y

A

I

K

R

G

E

Y

A

T

A

S

P

N

H

V

V

E

E

-

V

-
x
R

F

F

S
|
S

C

A

E

E

D

D

A

T

V

F

R

R

T

S

R

E

L

E

P

Q

F

D

L

L

A

L

E

A

V

V

V

Y

E

E

A

A

T

-

I

V

D

A

A

P

G

Y

A

V

T

D

T

R

V

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

T

A

T

T

P

P

S

R

E

Q

F

V

Y

Y

N

A

I

L

I

V

R

R

Y

E

L

V

K

R

E

R

N

V

V

V

S

G

N

P

I

-

E

-

K

R

A

V

V

D

I

I

S

E

V

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

S

A

V

I

A

A

N

N

S

A

L

Y

A

E

A

A

I

I

Q

E

A

A

G

G

A

A

G

T

Q

H

V

V

E

D

C

T

T

T

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

C

T

S

P

L

L

E

G

L

F

V

L

M

A

V

R

L

M

R

Y

T

T

R

-

H

-

D

-

I

L

L

Q

P

P

Y

E

Y

Y

T

V

-

R

N

K

V

Y

A

K

T

L

E

E

Q

M

L

L

T

P

S

E

S

L

S

D

R

R

L

M

L

V

S

A

T

R

I

M

T

V

G

G

I

V

M

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

H

K

G

A

M

I

M

Y

M

I

D

N

S

P

S

E

T

A

Y

Y

E

E

I

P

M

Y

T

P

P

P

E

E

S

V

V

F

G

G

L

V

A

K

A

R

G

K

A

L

L

I

V

I

L

A

G

S

K

R

H

L

S

T

G

G

R

R

H

H

A

A

F

I

K

K

K

A

R

R

L

A

Q

E

E

E

L

L

G

G

H

L

E

H

L

Y

D

G

D

E

E

E

M

E

L

L

N

H

R

R

A

V

F

T

V

Q

R

H

F

I

K

K

A

A

L

L

A

A

D

D

L

-

K

R

K

G

E

Q

V

L

F

T

D

L

E

E

D

E

L

L

D

D

A

R

I

I

V

L

R12 (= R22) binding 2-oxoglutarate
E13 (≠ D23) binding Mg(2+)
H72 (vs. gap) binding 2-oxoglutarate; mutation to L: Significant decrease in sensitivity to lysine inhibition. Large decrease in affinity for 2-oxoglutarate. Almost no effect on affinity for acetyl-CoA and on turnover number.
D92 (≠ H107) binding L-lysine
R133 (vs. gap) binding 2-oxoglutarate
S135 (= S149) binding L-lysine
T166 (= T181) binding 2-oxoglutarate; binding L-lysine
H195 (= H212) binding Mg(2+)
H197 (= H214) binding Mg(2+)

3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 69% coverage: 16:374/518 of query aligns to 14:346/364 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

N

A

S

F

M

F

N

D

M

T

E

E

E

K

K

K

L

I

R

Q

V

I

A

A

R

K

Q

A

L

L

E

D

K

N

L

F

N

G

V

V

D

D

I

Y

I

I

E

E

A

L

G

T

F

S

P

P

I

V

A

A

S

S

V

E

G

Q

D

S

F

R

E

Q

A

D

V

C

K

E

R

A

I

I

A

C

Q

K

T

L

L

G

T

L

K

K

P

C

Q

K

I

I

A

L

G

T

L

H

C

I

R

R

S

C

S

H

D

M

K

D

D

D

I

-

D

-

R

-

A

-

W

-

E

-

A

-

V

-

Q

-

Y

-

A

-

G

-

E

A

R

R

A

V

R

A

I

V

H

E

T

T

F

G

I

V

A

D

T

G

S

V

D

D

I

V

H

-

M

-

K

-

Y

-

K

-

L

-

Q

V

M

I

E

G

P

T

A

T

K

Y

V

I

L

I

A

D

T

S

A

A

V

T

K

E

A

V

V

I

K

N

Y

F

A

V

K

K

G

S

Y

K

T

G

S

I

N

E

V

V

E

R

F

F

S

S

C

S

E

E

D

D

A

S

V

F

R

R

T

S

R

D

L

L

P

V

F

D

L

L

A

L

E

S

V

L

V

Y

E

K

A

A

T

V

I

D

D

K

A

I

G

G

A

V

T

N

T

R

V

V

N

G

I

I

P

A

D

D

T

T

V

V

G

G

Y

C

T

A

T

T

P

P

S

R

E

Q

F

V

Y

Y

N

D

I

L

I

I

R

R

Y

T

L

L

K

R

E

G

N

V

V

V

S

S

N

-

I

-

E

-

K

-

A

C

V

D

I

I

S

E

V

C

H
|
H

C

F

H
|
H

N

N

D

D

L

T

G

G

L

M

S

A

V

I

A

A

N

N

S

A

L

Y

A

C

A

A

I

L

Q

E

A

A

G

G

A

A

G

T

Q

H

V

I

E

D

C

T

T

S

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

C

T

S

P

L

L

E

G

E

A

L

L

V

L

-

A

-

R

M

M

V

Y

L

V

R

T

T

D

R

R

H

E

D

Y

I

I

L

T

P

H

Y

K

Y

Y

T

K

N

-

V

-

A

-

T

L

E

N

Q

Q

L

L

T

R

S

E

S

L

S

E

R

N

L

L

L

V

S

A

T

D

I

A

T

V

G

E

I

V

M

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

H

K

G

A

M

I

M

L

M

A

D

N

S

P

S

S

T

T

Y

Y

E

E

I

I

M

L

T

K

P

P

E

E

S

D

V

F

G

G

L

M

A

S

A

R

G

Y

A

V

L

H

V

V

L

G

G

S

K

R

H

L

S

T

G

G

R

W

H

N

A

A

F

I

K

K

K

S

R

R

L

A

Q

E

E

Q

L

L

G

N

H

L

E

H

L

L

D

Q

D

A

E

K

M

E

L

L

N

T

R

-

A

-

F

-

V

V

R

R

F

I

K

K

A

K

L

L

A

A

active site: Q24 (= Q26)
binding cobalt (ii) ion: E21 (≠ D23), H188 (= H212), H190 (= H214)

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
32% identity, 57% coverage: 14:310/518 of query aligns to 2:296/311 of 3bliA

query
sites
3bliA

I

L

R

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

N

V

S

S

M

F

N

S

M

T

E

S

E

E

K

K

L

L

R

N

V

I

A

A

R

K

-

F

Q

L

L

L

E

Q

K

K

L

L

N

N

V

V

D

D

I

R

I

V

E

E

A

I

G

A

F

S

P

A

I
x
R

A
x
V

S

S

V

K

G

G

D

E

F

L

E

E

A

T

V

V

K

Q

R

K

I

I

A

M

-

E

-

W

-

A

-

T

-

E

Q

Q

T

L

L

T

T

E

K

R

P

I

Q

E

I

I

A

L

G

G

L

F

C

V

R

-

S

D

S

G

D

N

K

K

D

T

I

V

D

D

R

-

A

-

W

W

E

-

A

-

V

I

Q

K

Y

D

A

S

G

G

E

-

R

-

A

A

R

K

I

V

H

L

T

N

F

L

I

L

A

T

T

K

S

G

D

S

I

L

H

H

-

H

M

L

K

E

Y

K

K

Q

L

L

Q

G

M

K

E

T

P

P

A

K

K

E

V

F

L

F

A

T

T

D

A

V

V

S

K

F

A

V

V

I

K

E

Y

Y

A

A

-

I

-

K

K

S

G

G

Y

L

T

K

S

I

N

N

V

V

E
x
Y

F

L

-
x
E

S

D

C

W

E

S

D

N

A

G

V

F

R

R

T

N

R

S

L

P

P

D

F

Y

L

V

A

K

E

S

V

L

V

V

E

E

A

H

T

L

I

S

D

K

A

E

G

H

A

I

T

E

T

R

V

I

N

F

I

L

P
|
P

D

D

T
|
T

V

L

G

G

Y

V

T

L

T

S

P

P

S

E

E

E

F

T

Y

F

N

Q

I

G

I

V

R

D

Y

S

L

L

K

I

E

Q

N

K

V

Y

S

P

N

D

I

I

E

H

K

-

A

-

V

-

I

F

S

E

V

F

H
|
H

C

G

H
|
H

N

N

D

D

L

Y

G

D

L

L

S

S

V

V

A

A

N

N

S

S

L

L

A

Q

A

A

I

I

Q

R

A

A

G

G

A

V

G

K

Q

G

V

L

E

H

C

A

T

S

I

I

N

N

G

G

I

L

G

G

E

E

R

R

A

A

G

G

N

N

C

T

S

P

L

L

E

E

E

A

L

L

V

V

M

T

V

-

L

-

R

-

T

T

R

I

H

H

D

D

I

K

L

S

P

N

Y

S

Y

K

T

T

N

N

V

I

A

N

T

E

E

I

Q

A

L

I

T

T

S

E

S

A

S

S

R

R

L

L

L

V

S

E

T

V

I

F

T

S

G

G

I

K

M

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 (= Q26)
binding acetyl coenzyme *a: Q14 (= Q26), R47 (≠ I58), V48 (≠ A59), E140 (vs. gap)
binding pyruvic acid: R10 (= R22), Y138 (≠ E147), P171 (= P179), T173 (= T181)
binding zinc ion: D11 (= D23), H201 (= H212), H203 (= H214)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
28% identity, 73% coverage: 12:389/518 of query aligns to 1:341/347 of 3a9iA

query
sites
3a9iA

R

R

L

E

I

W

R

K

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

N

A

S

N

M

F

N

S

M

T

E

Q

E

D

K

K

L

V

R

E

V

I

A

A

R

K

Q

A

L

L

E

D

K

E

L

F

N

G

V

I

D

E

I

Y

I

I

E

E

A

V

G

T

F

T

P

P

I

V

A

A

S

S

V

P

G

Q

D

S

F

R

E

K

A

D

V

A

K

E

R

V

I

L

A

A

Q

S

T

L

L

G

T

L

K

K

P

A

Q

K

I

V

A

V

G

T

-

H

-

I

L

Q

C

C

R

R

S

-

D

-

K

-

D

-

I

L

D

D

R

A

A

A

W

K

E

V

A

A

V

V

Q

E

Y

-

A

-

G

-

E

-

R

-

A

-

R

-

I

-

H

-

T

T

F

G

I

V

A

Q

T

G

S

I

D
|
D

I

L

H

L

M

F

K

G

Y

T

K

S

L

K

Q

Y

M

L

E

D

P

I

A

P

K

R

V

I

L

I

A

E

T

E

A

A

V

K

K

E

A

V

V

I

K

A

Y

Y

A

I

K

R

G

E

Y

A

T

A

S

P

N

H

V

V

E

E

-

V

-

R

F

F

S
|
S

C

A

E

E

D

D

A

T

V

F

R

R

T

S

R

E

L

E

P

Q

F

D

L

L

A

L

E

A

V

V

V

Y

E

E

A

A

T

-

I

V

D

A

A

P

G

Y

A

V

T

D

T

R

V

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

T

A

T

T

P

P

S

R

E

Q

F

V

Y

Y

N

A

I

L

I

V

R

R

Y

E

L

V

K

R

E

R

N

V

V

V

S

G

N

P

I

-

E

-

K

R

A

V

V

D

I

I

S

E

V

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

S

A

V

I

A

A

N

N

S

A

L

Y

A

E

A

A

I

I

Q

E

A

A

G

G

A

A

G

T

Q

H

V

V

E

D

C

T

T

T

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

C

T

S

P

L

L

E

G

L

F

V

L

M

A

V

R

L

M

R

Y

T

T

R

-

H

-

D

-

I

L

L

Q

P

P

Y

E

Y

Y

T

V

-

R

N

K

V

Y

A

K

T

L

E

E

Q

M

L

L

T

P

S

E

S

L

S

D

R

R

L

M

L

V

S

A

T

R

I

M

T

V

G

G

I

V

M

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

H

K

G

A

M

I

M

Y

M

I

D

N

S

P

S

E

T

A

Y

Y

E

E

I

P

M

Y

T

P

P

P

E

E

S

V

V

F

G

G

L

-

A

-

G

-

A

-

L

-

V

V

L

K

G

G

K

L

H

H

S

Y

G

G

R

-

H

-

A

-

F

-

K

-

R

-

L

-

Q

-

E

-

L

-

G

-

H

-

E

-

L

-

D

-

D

E

E

E

M

E

L

L

N

H

R

R

A

V

F

T

V

Q

R

H

F

I

K

K

A

A

L

L

A

A

D

D

L

-

K

R

K

G

E

Q

V

L

F

T

D

L

E

E

D

E

L

L

D

D

A

R

I

I

V

L

binding cobalt (ii) ion: E12 (≠ D23), H188 (= H212), H190 (= H214)
binding lysine: R11 (= R22), D91 (= D114), S128 (= S149), T159 (= T181), H188 (= H212), H190 (= H214)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
28% identity, 62% coverage: 12:331/518 of query aligns to 2:305/312 of 2ztjA

query
sites
2ztjA

R

R

L

E

I

W

R

K

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

N

A

S

N

M

F

N

S

M

T

E

Q

E

D

K

K

L

V

R

E

V

I

A

A

R

K

Q

A

L

L

E

D

K

E

L

F

N

G

V

I

D

E

I

Y

I

I

E

E

A

V

G

T

F

T

P

P

I

V

A

A

S

S

V

P

G

Q

D

S

F

R

E

K

A

D

V

A

K

E

R

V

I

L

A

A

Q

S

T

L

L

G

T

L

K

K

P

A

Q

K

I

V

A

V

G

T

-
x
H

-

I

L

Q

C

C

R

R

S

-

D

-

K

-

D

-

I

L

D

D

R

A

A

A

W

K

E

V

A

A

V

V

Q

E

Y

-

A

-

G

-

E

-

R

-

A

-

R

-

I

-

H

-

T

-

F

-

I

T

A

G

T

V

S

Q

D

G

I

I

H

D

M

L

K
x
L

Y

F

K

G

L

T

Q

G

M

R

E

D

P

I

A

P

K

R

V

I

L

I

A

E

T

E

A

A

V

K

K

E

A

V

V

I

K

A

Y

Y

A

I

K

R

G

E

Y

A

T

A

S

P

N

H

V

V

E

E

-

V

-
x
R

F

F

S

S

C

A

E

E

D

D

A

T

V

F

R

R

T

S

R

E

L

E

P

Q

F

D

L

L

A

L

E

A

V

V

V

Y

E

E

A

A

T

-

I

V

D

A

A

P

G

Y

A

V

T

D

T

R

V

V

N

G

I

L

P
x
A

D

D

T
|
T

V

V

G

G

Y

V

T

A

T

T

P

P

S

R

E

Q

F

V

Y

Y

N

A

I

L

I

V

R

R

Y

E

L

V

K

R

E

R

N

V

V

V

S

G

N

P

I

-

E

-

K

R

A

V

V

D

I

I

S

E

V

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

S

A

V

I

A

A

N

N

S

A

L

Y

A

E

A

A

I

I

Q

E

A

A

G

G

A

A

G

T

Q

H

V

V

E

D

C

T

T

T

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

C

T

S

P

L

L

E

G

L

F

V

L

M

A

V

R

L

M

R

Y

T

T

R

-

H

-

D

-

I

L

L

Q

P

P

Y

E

Y

Y

T

V

-

R

N

K

V

Y

A

K

T

L

E

E

Q

M

L

L

T

P

S

E

S

L

S

D

R

R

L

M

L

V

S

A

T

R

I

M

T

V

G

G

I

V

M

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

H

K

G

A

M

I

M

Y

M

I

D

N

S

P

S

E

T

A

Y

Y

E

E

I

P

M

Y

T

P

P

P

E

E

S

V

V

F

G

G

L

V

active site: Q16 (= Q26)
binding 2-oxoglutaric acid: R12 (= R22), H72 (vs. gap), L94 (≠ K118), R125 (vs. gap), A156 (≠ P179), T158 (= T181), H187 (= H212), H189 (= H214)
binding copper (ii) ion: E13 (≠ D23), H187 (= H212), H189 (= H214)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
29% identity, 62% coverage: 12:331/518 of query aligns to 2:307/314 of 2zyfA

query
sites
2zyfA

R

R

L

E

I

W

R

K

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

N

A

S

N

M

F

N

S

M

T

E

Q

E

D

K

K

L

V

R

E

V

I

A

A

R

K

Q

A

L

L

E

D

K

E

L

F

N

G

V

I

D

E

I

Y

I

I

E

E

A

V

G

T

F

T

P

P

I

V

A

A

S

S

V

P

G

Q

D

S

F

R

E

K

A

D

V

A

K

E

R

V

I

L

A

A

Q

S

T

L

L

G

T

L

K

K

P

A

Q

K

I

V

A

V

G

T

-
x
H

-

I

L

Q

C

C

R

R

S

-

D

-

K

-

D

-

I

L

D

D

R

A

A

A

W

K

E

V

A

A

V

V

Q

E

Y

-

A

-

G

-

E

-

R

-

A

-

R

-

I

-

H

-

T

T

F

G

I

V

A

Q

T

G

S

I

D

D

I

L

H
x
L

M

F

K

G

Y

T

K

S

L

K

Q

G

M

R

E

D

P

I

A

P

K

R

V

I

L

I

A

E

T

E

A

A

V

K

K

E

A

V

V

I

K

A

Y

Y

A

I

K

R

G

E

Y

A

T

A

S

P

N

H

V

V

E

E

-

V

-
x
R

F

F

S

S

C

A

E

E

D

D

A

T

V

F

R

R

T

S

R

E

L

E

P

Q

F

D

L

L

A

L

E

A

V

V

V

Y

E

E

A

A

T

-

I

V

D

A

A

P

G

Y

A

V

T

D

T

R

V

V

N

G

I

L

P

A

D

D

T
|
T

V

V

G

G

Y

V

T

A

T

T

P

P

S

R

E

Q

F

V

Y

Y

N

A

I

L

I

V

R

R

Y

E

L

V

K

R

E

R

N

V

V

V

S

G

N

P

I

-

E

-

K

R

A

V

V

D

I

I

S

E

V

F

H
|
H

C

G

H
|
H

N

N

D

D

L

T

G

G

L

C

S

A

V

I

A

A

N

N

S

A

L

Y

A

E

A

A

I

I

Q

E

A

A

G

G

A

A

G

T

Q

H

V

V

E

D

C

T

T

T

I

I

N

L

G

G

I

I

G

G

E

E

R

R

A

N

G

G

N

I

C

T

S

P

L

L

E

G

L

F

V

L

M

A

V

R

L

M

R

Y

T

T

R

-

H

-

D

-

I

L

L

Q

P

P

Y

E

Y

Y

T

V

-

R

N

K

V

Y

A

K

T

L

E

E

Q

M

L

L

T

P

S

E

S

L

S

D

R

R

L

M

L

V

S

A

T

R

I

M

T

V

G

G

I

V

M

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

H

K

G

A

M

I

M

Y

M

I

D

N

S

P

S

E

T

A

Y

Y

E

E

I

P

M

Y

T

P

P

P

E

E

S

V

V

F

G

G

L

V

active site: Q16 (= Q26)
binding 2-oxoglutaric acid: R12 (= R22), H72 (vs. gap), L94 (≠ H116), R127 (vs. gap), T160 (= T181), H189 (= H212)
binding magnesium ion: E13 (≠ D23), H189 (= H212), H191 (= H214)

3figB Crystal structure of leucine-bound leua from mycobacterium tuberculosis (see paper)
26% identity, 94% coverage: 21:506/518 of query aligns to 62:574/577 of 3figB

query
sites
3figB

L

L

R

R

D
|
D

G

G

E

N

Q

Q

S

A

P

L

G

I

N

D

S

P

M

M

N

S

M

P

E

A

E

R

K

K

L

R

R

R

V

M

A

F

R

D

Q

L

L

L

E

V

K

R

L

M

N

G

V

Y

D

K

I

E

I

I

E

E

A

V

G

G

F

F

P

P

I

S

A

A

S

S

V

Q

G

T

D

D

F

F

E

D

A

F

V

V

K

R

R

E

I

I

A

I

Q

E

T

Q

L

G

T

A

K

I

P

P

-

D

-

V

-

T

-

I

Q

Q

I

V

A

L

G

T

L

Q

C

C

R

R

S

P

S

-

D

-

K

E

D

L

I

I

D

E

R

R

A

T

W

F

E

Q

A

A

V

C

Q

S

Y

G

A

A

G

-

E

P

R

R

A

A

R

I

I

V

H

H

T

F

F

Y

I

N

A

S

T

T

S

S

D

I

I

L

H

Q

M

R

K

R

Y

V

K

V

L

F

Q

R

M

A

E

N

P

R

A

A

K

E

V

V

L

Q

A

A

T

I

A

A

V

T

-

D

-

G

-

A

-

R

-

K

-

C

-

V

-

E

K

Q

A

A

V

A

K

K

Y

Y

A

-

K

P

G

G

Y

T

T

Q

S

W

N

R

V

F

E

E

F

Y

S

S

C

P

E

E

D

S

A

Y

V

T

R

G

T

T

R

E

L

L

P

E

F

Y

L

A

A

K

E

Q

V

V

V

C

E

D

A

A

T

V

I

G

D

E

A

V

G

I

A

A

T

P

T

T

-

P

-

E

-

R

-

P

-

I

V

F

N

N

I

L

P

P

D

A

T

T

V

V

G

E

Y

M

T

T

P

P

S

N

E

V

F

Y

Y

A

N

D

I

S

I

I

R

E

Y

W

L

M

K

S

E

R

N

N

V

L

S

A

N

N

I

R

E

E

K

S

A

V

V

I

I

L

S

S

V

L

H
|
H

C

P

H
|
H

N

N

D

D

L

R

G

G

L

T

S

A

V

V

A

A

N

A

S

A

L

E

A

L

A

G

I

F

Q

A

A

A

G

G

A

A

G

D

Q

R

V

I

E

E

C

G

T

C

I

L

N

F

G

G

I

N

G

G

E

E

R

R

A

T

G

G

N

N

C

V

S

C

L

L

E

V

E

T

L

L

V

G

M

L

V

N

L

L

R

F

T

S

R

R

H

-

D

G

I

V

L

D

P

P

Y

-

T

-

N

Q

V

I

A

D

T

F

E

S

Q

N

L

I

T

D

S

E

S

I

S

R

R

R

L

T

L

V

S

E

T

Y

I

C

T

N

G

Q

I

L

M

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

H

D

G

A

M

I

-

N

-

K

-

G

-

L

-

D

-

A

-

M

-

K

-

L

-

D

-

A

-

D

-

A

-

D

-

C

-

D

-

V

-

D

M

M

M

L

D

W

S

Q

S

V

T

P

Y

Y

E

L

I

P

M

I

T

D

P

P

E

R

S

D

V

V

G

G

L

R

A

T

A

Y

G

E

A

A

L

V

V

I

L

R

G

V

K

N

H

K

S

G

G

G

R

-

H

-

A

-

F

-

K

V

K

A

R

Y

L

I

Q

M

E

K

L

T

G

D

H

H

E

G

L

L

D

-

E

S

M

L

L

P

N

R

R

R

A

L

F

Q

V

I

R

E

F

F

K

S

A

Q

L

V

A

I

D

Q

-

K

-

V

L

S

K

P

K

K

E

E

V

M

F

W

D

D

E

A

D

F

L

A

D

E

A

E

I

Y

V

L

A

A

D

P

E

V

S

R

R

P

E

L

E

E

E

R

M

I

Y

R

K

Q

L

H

V

V

L

D

L

A

N

A

V

D

S

D

C

D

G

G

S

G

L

T

S

T

V

S

A

I

T

T

A

A

T

T

V

V

K

K

M

-

E

-

I

I

N

N

G

G

Q

V

L

E

L

T

R

E

A

I

A

S

E

G

L

S

G

G

D

N

G
|
G

P
|
P

V
x
L

D
x
A

A

A

T

F

L

V

K

H

A

A

I

L

R

A

K

D

L

V

T

G

K

F

S

D

K

V

A

A

K

V

L

L

E

D

Q

Y

F

Y

N

E

V

-

G

H

S

A

I

M

T

S

G

A

G

G

T
x
D

D

D

A
|
A

Q

Q

G

A

E

A

V

A

T

Y

M

V

R

E

V

A

S

S

-

V

-

T

-

I

D

A

G

T

N

S

H

K

L

T

V

V

V

W

G

G

K

V

G

G

S

I

S

A

T
x
P

D

S

I
|
I

I

T

E

T

A

A

S

S

A

L

K

R

A

A

F

V

V

V

H

S

A

A

L

V

N

N

R

R

binding leucine: G501 (= G435), P502 (= P436), L503 (≠ V437), A504 (≠ D438), D531 (≠ T466), A533 (= A468), P558 (≠ T490), I560 (= I492)
binding zinc ion: D64 (= D23), H268 (= H212), H270 (= H214)

3hpzB Crystal structure of mycobacterium tuberculosis leua complexed with bromopyruvate
26% identity, 94% coverage: 21:506/518 of query aligns to 62:574/576 of 3hpzB

query
sites
3hpzB

L

L

R

R

D
|
D

G

G

E

N

Q

Q

S

A

P

L

G

I

N

D

S

P

M

M

N

S

M

P

E

A

E

R

K

K

L

R

R

R

V

M

A

F

R

D

Q

L

L

L

E

V

K

R

L

M

N

G

V

Y

D

K

I

E

I

I

E

E

A

V

G

G

F

F

P

P

I

S

A

A

S

S

V

Q

G

T

D

D

F

F

E

D

A

F

V

V

K

R

R

E

I

I

A

I

Q

E

T

Q

L

G

T

A

K

I

P

P

-

D

-

V

-

T

-

I

Q

Q

I

V

A

L

G

T

L

Q

C

C

R

R

S

P

S

-

D

-

K

E

D

L

I

I

D

E

R

R

A

T

W

F

E

Q

A

A

V

C

Q

S

Y

G

A

A

G

-

E

P

R

R

A

A

R

I

I

V

H

H

T

F

F

Y

I

N

A

S

T

T

S

S

D

I

I

L

H

Q

M

R

K

R

Y

V

K

V

L

F

Q

R

M

A

E

N

P

R

A

A

K

E

V

V

L

Q

A

A

T

I

A

A

V

T

-

D

-

G

-

A

-

R

-

K

-

C

-

V

-

E

K

Q

A

A

V

A

K

K

Y

Y

A

-

K

P

G

G

Y

T

T

Q

S

W

N

R

V

F

E

E

F

Y

S

S

C

P

E
|
E

D

S

A

Y

V

T

R

G

T

T

R

E

L

L

P

E

F

Y

L

A

A

K

E

Q

V

V

V

C

E

D

A

A

T

V

I

G

D

E

A

V

G

I

A

A

T

P

T

T

-

P

-

E

-

R

-

P

-

I

V

F

N

N

I

L

P
|
P

D

A

T
|
T

V

V

G

E

Y

M

T

T

P

P

S

N

E

V

F

Y

Y

A

N

D

I

S

I

I

R

E

Y

W

L

M

K

S

E

R

N

N

V

L

S

A

N

N

I

R

E

E

K

S

A

V

V

I

I

L

S

S

V

L

H
|
H

C

P

H
|
H

N

N

D

D

L

R

G

G

L

T

S

A

V

V

A

A

N

A

S

A

L

E

A

L

A

G

I

F

Q

A

A

A

G

G

A

A

G

D

Q

R

V

I

E

E

C

G

T

C

I

L

N

F

G

G

I

N

G

G

E

E

R

R

A

T

G

G

N

N

C

V

S

C

L

L

E

V

E

T

L

L

V

G

M

L

V

N

L

L

R

F

T

S

R

R

H

-

D

G

I

V

L

D

P

P

Y

-

T

-

N

Q

V

I

A

D

T

F

E

S

Q

N

L

I

T

D

S

E

S

I

S

R

R

R

L

T

L

V

S

E

T

Y

I

C

T

N

G

Q

I

L

M

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

H

D

G

A

M

I

-

N

-

K

-

G

-

L

-

D

-

A

-

M

-

K

-

L

-

D

-

A

-

D

-

A

-

D

-

C

-

D

-

V

-

D

M

M

M

L

D

W

S

Q

S

V

T

P

Y

Y

E

L

I

P

M

I

T

D

P

P

E

R

S

D

V

V

G

G

L

R

A

T

A

Y

G

E

A

A

L

V

V

I

L

R

G

V

K

N

H

K

S

G

G

G

R

-

H

-

A

-

F

-

K

V

K

A

R

Y

L

I

Q

M

E

K

L

T

G

D

H

H

E

G

L

L

D

-

E

S

M

L

L

P

N

R

R

R

A

L

F

Q

V

I

R

E

F

F

K

S

A

Q

L

V

A

I

D

Q

-

K

-

V

L

S

K

P

K

K

E

E

V

M

F

W

D

D

E

A

D

F

L

A

D

E

A

E

I

Y

V

L

A

A

D

P

E

V

S

R

R

P

E

L

E

E

E

R

M

I

Y

R

K

Q

L

H

V

V

L

D

L

A

N

A

V

D

S

D

C

D

G

G

S

G

L

T

S

T

V

S

A

I

T

T

A

A

T

T

V

V

K

K

M

-

E

-

I

I

N

N

G

G

Q

V

L

E

L

T

R

E

A

I

A

S

E

G

L

S

G

G

D

N

G

G

P

P

V

L

D

A

A

A

T

F

L

V

K

H

A

A

I

L

R

A

K

D

L

V

T

G

K

F

S

D

K

V

A

A

K

V

L

L

E

D

Q

Y

F

Y

N

E

V

-

G

H

S

A

I

M

T

S

G

A

G

G

T

D

D

D

A

A

Q

Q

G

A

E

A

V

A

T

Y

M

V

R

E

V

A

S

S

-

V

-

T

-

I

D

A

G

T

N

S

H

K

L

T

V

V

V

W

G

G

K

V

G

G

S

I

S

A

T

P

D

S

I

I

I

T

E

T

A

A

S

S

A

L

K

R

A

A

F

V

V

V

H

S

A

A

L

V

N

N

R

R

binding Bromopyruvate: E201 (= E151), P235 (= P179), T237 (= T181), H268 (= H212), H270 (= H214)
binding zinc ion: D64 (= D23), H268 (= H212), H270 (= H214)

Query Sequence

>WP_011734424.1 NCBI__GCF_000015045.1:WP_011734424.1
MAQETKNGAERRLIRIFDTTLRDGEQSPGNSMNMEEKLRVARQLEKLNVDIIEAGFPIAS
VGDFEAVKRIAQTLTKPQIAGLCRSSDKDIDRAWEAVQYAGERARIHTFIATSDIHMKYK
LQMEPAKVLATAVKAVKYAKGYTSNVEFSCEDAVRTRLPFLAEVVEATIDAGATTVNIPD
TVGYTTPSEFYNIIRYLKENVSNIEKAVISVHCHNDLGLSVANSLAAIQAGAGQVECTIN
GIGERAGNCSLEELVMVLRTRHDILPYYTNVATEQLTSSSRLLSTITGIMVQPNKAIVGA
NAFAHESGIHQHGMMMDSSTYEIMTPESVGLAAGALVLGKHSGRHAFKKRLQELGHELDD
EMLNRAFVRFKALADLKKEVFDEDLDAIVADESREEEMYKLVLLNVSCGSLSVATATVKM
EINGQLLRAAELGDGPVDATLKAIRKLTKSKAKLEQFNVGSITGGTDAQGEVTMRVSDGN
HLVVGKGSSTDIIEASAKAFVHALNRLHYRQKKMNGGV

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