SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_152428518.1 NCBI__GCF_000385335.1:WP_152428518.1 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)
54% identity, 96% coverage: 19:528/532 of query aligns to 1:512/517 of Q9JZG1

query
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Q

D16 (= D34) binding Mn(2+)
H204 (= H222) binding Mn(2+)
H206 (= H224) binding Mn(2+)
N240 (= N258) binding Mn(2+)

Sites not aligning to the query:

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

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, 72% coverage: 16:399/532 of query aligns to 76:474/503 of Q9FN52

query
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Q9FN52

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G263 (= G193) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
49% identity, 72% coverage: 16:399/532 of query aligns to 9:407/409 of 6e1jA

query
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I

I

V

V

G

G

R

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

M

I

L

L

K
|
K

N

N

A

R

Q

S

T

T

Y

Y

E

E

I

I

M

I

T

S

P

P

E

E

S

D

V

V

G

G

V

V

N

V

K

K

T

S

S

Q

-

N

-

S

-

G

L

I

V

V

M

L

G

G

K

K

H
x
L

S

S

G

G

R
|
R

H
|
H

A

A

F

V

K

K

E

G

K

R

L

L

K

K

E

E

L

L

G

G

Y

Y

D

E

L

I

G

S

D

D

N

E

A

K

L

L

E

N

E

E

A

V

F

F

A

S

R

R

F

F

K

R

D

D

L

L

A

T

D

K

R

Q

K

K

I

R

V

V

Y

T

D

D

E

D

D

D

L

L

I

K

A

A

L

L

V

V

binding coenzyme a: Q30 (= Q37), F60 (= F67), S63 (≠ T70), I95 (≠ L93), R97 (= R95), F121 (= F119), K132 (= K130), L133 (= L131), S322 (= S317), G323 (= G318), I324 (= I319), D327 (= D322), K331 (= K326), L359 (≠ H351), R362 (= R354), H363 (= H355)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P189), T194 (= T191), H225 (= H222), H227 (= H224)
binding manganese (ii) ion: D27 (= D34), V82 (vs. gap), E84 (vs. gap), H225 (= H222), H227 (= H224)

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 73% coverage: 16:403/532 of query aligns to 76:480/506 of Q9FG67

query
sites
Q9FG67

P

P

A

N

S

K

I

L

A

P

N

D

T

G

N

N

Q

Y

V

V

L

R

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

L

P

E

P

E

Q

K

K

L

L

E

E

V

I

A

A

E

R

L

Q

L

L

D

A

T

K

M

L

G

R

V

V

D

D

I

I

I

M

E

E

A

V

G

G

F

F

P

P

V

G

T

S

S

S

E

E

G

E

D

E

F

L

E

E

A

T

V

I

S

K

E

T

I

I

S

A

R

K

R

T

A

V

K

G

R

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

V

A

P

T

V

I

I

A

C

G

A

L

I

A

A

R

R

L

C

A

K

A

H

K

R

D

D

I

I

D

E

R

A

C

T

A

W

E

E

A

A

V

L

R

K

H

Y

A

A

R

K

H

R

P

P

R

R

I

I

H

L

V

V

F

F

V

T

S

S

T

T

S

S

P

D

L

I

H

H

M

M

K

K

Y

Y

K

K

L

L

N

K

K

K

E

T

P

Q

E

E

Q

E

V

V

L

I

E

E

M

M

I

A

K

V

V

S

N

S

V

I

A

R

R

F

A

A

R

K

N

S

L

L

-

G

V

F

G

N

D

D

I

I

E

Q

W

F

S

G

A

C

E

E

D

D

G

G

T

G

R

R

S

S

E

D

I

K

D

D

F

F

L

L

C

C

R

K

C

I

V

L

E

G

A

E

A

A

I

I

N

K

A

A

G

G

A

V

T

T

T

V

I

V

N

T

I

I

P

G

D

D

T

T

V

V

G

G

Y

I

A

N

V

M

P

P

D

H

E

E

Y

Y

R

G

R

E

I

L

F

V

E

T

T

Y

V

L

R

K

E

A

R

N

V

T

P

P

N

G

S

I

D

D

K

D

A

V

I

V

F

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

A

A

N

N

T

S

L

I

A

A

G

G

V

I

A

R

G

A

G

G

A

A

R

R

Q

Q

I

V

E

E

C

V

T

T

V

I

N

N

G

G

L

I

G

G

E

E

R

R

A

S

G

G

N

N

A

A

A

S

L

L

E

E

V

V

M

M

A

A

L

L

R

K

V

C

R

R

G

G

D

A

A

Y

M

V

-

I

-

N

P

G

Y

V

H

Y

S

T

G

K

I

I

D

D

S

T

S

R

M

Q

L

I

V

M

R

A

A

T

S

S

K

K

L

M

V

V

S

Q

A

E

V

Y

S

T

S

G

F

L

P

Y

V

V

Q

Q

Y

A

N

H

K

K

A

P

I

I

V

V

G

G

R

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

M

I

L

L

K

K

N

N

A

R

Q

S

T

T

Y

Y

E

E

I

I

M

L

T

S

P

P

E

E

S

D

V

I

G

G

V

I

N

V

K

K

T

S

S

Q

-

N

-

S

-

G

L

L

V

V

M

L

G

G

K

K

H

L

S

S

G

G

R

R

H

H

A

A

F

V

K

K

E

D

K

R

L

L

K

K

E

E

L

L

G

G

Y

Y

D

E

L

L

G

D

D

D

N

E

A

K

L

L

E

N

E

A

A

V

F

F

A

S

R

L

F

F

K

R

D

D

L

L

A

T

D

K

R

N

K

K

I

R

V

I

Y

T

D

D

E

A

D

D

L

L

I

K

A

A

L

L

V

V

-

T

-

S

D

S

D

D

E

E

I

I

S102 (= S42) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ S220) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
56% identity, 60% coverage: 22:340/532 of query aligns to 1:306/308 of 3rmjB

query
sites
3rmjB

T

T

N

N

Q

R

V

V

L

I

I

I

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

A

S

A

M

M

T

T

L

K

E

E

K

K

L

I

E

R

V

V

A

A

E

R

L

Q

L

L

D

E

T

K

M

L

G

G

V

V

D

D

I

I

E

E

A

A

G

G

F

F

P

A

V

A

T

A

S

S

E

P

G

G

D

D

F

F

E

E

A

A

V

V

S

N

E

A

I

I

S

A

R

K

R

T

A

I

K

T

R

K

A

S

T

T

I

V

A

C

G

S

L

L

A

S

R

R

L

A

A

I

A

E

K

R

D

D

I

I

D

R

R

Q

C

A

A

G

E

E

A

A

V

V

R

A

H

P

A

A

R

P

H

K

P

K

R

R

I

I

H

H

V

T

F

F

V

I

S

A

T

T

S

S

P

P

L

I

H

H

M

M

K

E

Y

Y

K

K

L

L

N

K

K

M

E

K

P

P

E

K

Q

Q

V

V

L

I

E

E

M

A

I

A

K

V

V

K

N

A

V

V

A

K

R

I

A

A

R

R

N

E

L

Y

V

T

G

D

D

D

I

V

E

E

W

F

S

S

A

C

E

E

D

D

G

A

T

L

R

R

S

S

E

E

I

I

D

D

F

F

L

L

C

A

R

E

C

I

V

C

E

G

A

A

A

V

I

I

N

E

A

A

G

G

A

A

T

T

I

I

N

N

I

I

P

P

D

D

T

T

V

V

G

G

Y

Y

A

S

V

I

P

P

D

Y

E

K

Y

T

R

E

I

F

F

F

E

R

T

E

V

L

R

I

E

A

R

K

V

T

P

P

N

N

S

G

D

G

K

K

A

V

I

V

F

W

S

S

V

A

H
|
H

C

C

H
|
H

N

N

D

D

L

L

G

G

L

L

A

A

V

V

A

A

N

N

T

S

L

L

A

A

G

A

V

L

A

K

G

G

A

A

R

R

Q

Q

I

V

E

E

C

C

T

T

V

V

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N
|
N

A

A

A

S

L

V

E

E

V

I

V

V

M

M

A

A

L

L

R

K

V

V

R

R

G

H

D

D

A

L

M

F

P

G

Y

L

H

E

S

T

G

G

I

I

D

D

S

T

M

Q

L

I

V

V

R

P

A

S

S

S

K

K

L

L

V

V

S

S

A

T

V

I

S

T

S

G

F

Y

P

P

V

V

Q

Q

Y

P

N

N

K

K

A

A

I

I

V

V

G

G

R

A

N

N

A

A

F

F

A

S

H

H

E

E

S

-

G

-

I

-

H

-

Q

-

D

-

G

-

M

-

L

-

K

-

N

-

A

-

Q

-

T

T

Y

Y

E

E

I

I

M

M

T

S

P

A

E

E

S

S

V

V

G

G

active site: Q16 (= Q37)
binding manganese (ii) ion: D13 (= D34), H201 (= H222), H203 (= H224), N237 (= N258)

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: 24:409/532 of query aligns to 21:398/399 of 6ktqA

query
sites
6ktqA

Q

K

V

V

L

G

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

L

T

E

D

E

Q

K

R

L

V

E

E

V

I

A

A

E

K

L

A

L

L

D

S

T

D

M

I

G

G

V

V

D

Q

I

M

I

I

E

E

A

A

G

G

F

H

P

P

V

A

T
x
V

S

S

E

P

G

D

D

I

F

Y

E

E

A

G

V

I

S

R

E

R

I

I

S

I

R

K

R

L

A

K

K

R

-

E

-

G

-

V

-

I

R

K

A

S

T

E

I

I

A

V

G

A

L

H

A

S

R
|
R

L
x
A

A

V

A

K

K

R

D

D

I

I

D

E

R

V

C

G

A

A

E

E

A

-

V

-

R

-

H

-

A

I

R

E

H

A

P

D

R

R

I

I

H

A

V

I

F
|
F

V

Y

S

G

T

I

S

S

P

D

L

T

H

H

M

L

K

K

Y

A

K

K

L
x
H

N

H

K

T

E

T

P

R

E

D

Q

E

V

A

L

L

E

R

M

S

I

I

K

A

V

E

N

T

V

V

A

S

R

Y

A

A

R

K

N

S

L

H

V

G

G

V

D

K

I

V

E
x
R

W

F

S
x
T

A

A

E
|
E

D

D

G

A

T

T

R

R

S

A

E

D

I

Y

D

Q

F

Y

L

L

C

L

R

E

C

V

V

I

E

K

A

T

A

V

I

R

N

D

A

A

G

G

A

A

T

D

T

R

I

V

N
x
S

I

I

P

A

D

D

T
|
T

V

V

G

G

Y

V

A

L

V

Y

P

P

D

S

E

R

Y

T

R

R

R

E

I

L

F

F

E

K

T

D

V

L

R

T

E

S

R

R

V

F

P

P

N

D

S

I

D

E

K

-

A

-

I

-

F

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

A

A

N

N

T

V

L

L

A

A

G

A

V

A

A

E

G

G

A

A

R

T

Q

I

I

I

E

H

C

T

T

T

V

L

N

N

G

G

L

L

G

G

E

E

R

R

A

V

G

G

N

I

A

A

A

P

L

L

E

Q

E

V

V

V

V

A

M

A

A

A

L

L

R

K

V

-

R

-

G

-

D

-

A

-

M

-

P

-

Y

Y

H

H

S

F

G

G

I

I

-

E

-

V

D

D

S

L

S

K

M

K

L

L

V

S

R

E

A

V

S

A

K

S

L

L

V

V

S

E

A

K

V

Y

S

S

S

G

F

I

P

A

V

L

Q

P

Y

P

N

N

K

F

A

P

I

I

V

T

G

G

R

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

M

V

L

L

K

N

N

D

A

P

Q

K

T

T

Y

Y

E

E

I

F

M

L

T

P

P

P

E

E

S

T

V

F

G

G

V

R

N

S

K

R

T

-

S

D

L

Y

V

V

M

I

G

D

K

K

H

Y

S

T

G

G

R

K

H

H

A

A

F

V

K

K

E

D

K

R

L

F

K

D

E

R

L

L

G

G

Y

V

D

K

L

L

G

T

D

D

N

S

A

E

L

I

E

D

E

Q

A

V

F

L

A

A

R

K

F

I

K

K

D

S

L

N

A

P

D

N

R

-

K

V

K

R

I

F

V

Y

Y

R

D

D

E

V

D

D

L

L

I

L

A

E

L

L

V

A

D

E

D

S

E

V

I

T

G

G

H

R

-

L

Q

E

H

H

E

H

H

H

binding 2-oxoglutaric acid: R30 (= R33), R154 (≠ E157), T156 (≠ S159), E158 (= E161), S184 (≠ N187), T188 (= T191), H216 (= H222), H218 (= H224)
binding coenzyme a: V67 (≠ T70), R96 (= R95), A97 (≠ L96), F116 (= F119), H128 (≠ L131), E158 (= E161)
binding zinc ion: E31 (≠ D34), H216 (= H222), H218 (= H224)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
34% identity, 70% coverage: 27:398/532 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

L

I

E

D

E

E

K

K

L

I

E

E

V

V

A

F

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D

L

L

D

V

T

E

M

L

G

N

V

V

D

D

I

G

I

I

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E

A

V

G

G

F

F

P

P

V

S

T

S

S

N

E

E

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D

E

F

F

E

H

A

T

V

C

S

Q

E

V

I

L

S

S

R

K

R

R

A

A

K

P

R

K

A

G

T

K

-

P

I

I

A

A

G

A

L
|
L

A

S

R

R

L

A

A

N

A

Q

K

N

D

E

I

I

D

A

R

V

C

T

A

W

E

E

A

A

V

I

R

Q

H

K

A

A

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D

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C

P

P

R

R

I

M

H

H

V

I

F

V

V

Y

S

P

T

V

S

S

P

D

L

F

H

S

M

I

K

K

Y

H

K

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L

L

N

K

K

I

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S

P

E

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K

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V

L

L

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I

I

K

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N

S

V

I

A

S

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F

A

A

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N

S

L

I

V

V

G

G

-

P

-

G

-

I

D

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I

I

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Q

W

F

S

S

A

G

E

E

-

H

-

F

-

G

D

D

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|
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D

K

K

A

A

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H
|
H

C

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H
|
H

N

N

D

D

L

L

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G

L

M

A

A

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T

A

A

N

T

T

S

L

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A

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V

A

Y

G

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G

G

A

A

R

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Q

Q

I

I

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C

V

T

A

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L

N

N

G

G

L

L

G

G

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E

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R

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A

G

G

N

N

A

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A

N

L

L

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Y

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H

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G

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I

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Q

D

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M

L

L

H

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Q

N

S

A

K

Q

G

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A

Y

Y

E

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I

T

M

F

T

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P

P

E

E

S

F

V

V

G

G

-

R

V

M

N

D

K

K

T

E

S

T

L

I

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S

M

F

G

T

K

N

H

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S

S

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G

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H

H

K

A

A

F

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K

E

E

F

K

L

L

L

K

H

E

Q

L

R

G

G

Y

I

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Q

L

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G

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D

K

N

E

A

G

L

I

E

H

A

L

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F

A

S

R

L

F

A

K

K

D

S

L

I

A

S

D

S

R

R

K

E

-

N

K

R

I

E

V

I

Y

T

D

E

E

A

D

E

L

L

I

V

A

A

L

L

active site: Q16 (= Q37)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R33), L73 (= L93), T176 (= T191), H205 (= H222), H207 (= H224)
binding zinc ion: D13 (= D34), H205 (= H222), H207 (= H224)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
33% identity, 70% coverage: 25:398/532 of query aligns to 4:377/379 of 4ov4A

query
sites
4ov4A

V

I

L

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

A

R

S

P

M

W

T

T

L

I

E

D

E

E

K

K

L

I

E

E

V

V

A

F

E

D

L

L

D

V

T

E

M

L

G

N

V

V

D

D

I

G

I

I

E

E

A

V

G

G

F

F

P

P

V

S

T

S

S

N

E

E

G

T

D

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F

F

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H

A

T

V

C

S

Q

E

V

I

L

S

S

R

K

R

R

A

A

K

P

R

K

A

G

T

K

-

P

I

I

A

A

G

A

L

L

A

S

R

R

L

A

A

N

A

Q

K

N

D

E

I

I

D

A

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C

T

A

W

E

E

A

A

V

I

R

Q

H

K

A

A

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C

P

P

R

R

I

M

H

H

V

I

F

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Y

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P

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V

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S

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D

L

F

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M

I

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Y

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L

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P

E

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Q

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V

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L

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Q

M

K

I

I

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N

S

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I

A

S

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F

A

A

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R

N

S

L

I

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V

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G

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P

-

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-

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A

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H

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F

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G

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L

A

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A

A

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E

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G

A

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T

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A

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P

D

M

E

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Y

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R

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-

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D

D

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K

A

A

I

I

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I

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I

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|
H

C

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H
|
H

N

N

D

D

L

L

G

G

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M

A

A

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A

A

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A

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A

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G

G

A

A

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I

I

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T

A

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L

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G

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L

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E

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R

A

A

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G

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A

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A

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L

L

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Y

E

E

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V

A

M

I

A

A

L

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A

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-

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-

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N

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M

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A

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A

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K

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V

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A

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V

L

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G

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V

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A

P

I

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D

A

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H

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G

G

I

I

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Q

Q

D

H

G

-

M

-

L

-

K

Q

N

S

A

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Q

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A

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Y

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P

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L

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A

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L

L

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H

E

Q

L

R

G

G

Y

I

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Q

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D

K

N

E

A

G

L

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A

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A

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L

F

A

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K

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S

L

I

A

S

D

S

R

R

K

E

-

N

K

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D

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L

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A

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active site: Q16 (= Q37)
binding 3-methyl-2-oxobutanoic acid: R12 (= R33), P174 (= P189), T176 (= T191), H205 (= H222), H207 (= H224)
binding zinc ion: D13 (= D34), H205 (= H222), H207 (= H224)

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, 93% coverage: 27:519/532 of query aligns to 10:511/516 of Q8F3Q1

query
sites
Q8F3Q1

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

L

T

E

S

E

E

K

K

L

L

E

N

V

I

A

A

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K

-

F

L

L

D

Q

T

K

M

L

G

N

V

V

D

D

I

R

I

V

E

E

A

I

G

A

F

S

P

A

V

R

T

V

S

S

E

K

G

G

D

E

F

L

E

E

A

T

V

V

S

Q

E

K

I

I

S

M

R

E

R

W

A

A

-

A

-

T

-

E

-

Q

-

L

-

T

K

E

R

R

A

I

T

E

I

I

A
x
L

G

G

L
x
F

A

V

R

-

L

-

A

-

K

-

D

D

I

G

D

N

R

K

C

T

A

V

E

D

A

W

V

I

R

K

H

D

A

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R

G

H

A

P

K

R

V

I

L

H

N

V

L

F
x
L

V

T

S

K

T

G

S

S

P

L

L

H

H

H

M

L

K

E

Y

K

K

Q

L

L

N

G

K

K

E

T

P

P

E

K

Q

E

-

F

-

T

-

D

-

V

-

S

-

F

V

V

L

I

E

E

M

Y

-

A

-

I

-

K

-

S

-

G

I

L

K

K

V

I

N

N

V

V

A
x
Y

R

L

A
x
E

R

-

N

-

L

-

V

-

G

-

D

-

I

-

E

D

W

W

S

S

A

-

E

-

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N

G

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N

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Y

L

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C

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A

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|
T

V

L

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A

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P

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E

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T

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R

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R

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Y

P

P

N

D

S

I

D

H

K

-

A

-

I

-

F

F

S

E

V

F

H

H

C

G

H

H

N

N

D

D

L

Y

G

D

L

L

A

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V

V

A

A

N

N

T

S

L

L

A

Q

G

A

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I

A

R

G

A

G

G

A

V

R

K

Q

G

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H

C

A

T

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V

I

N

N

G

G

L

L

G

G

E

E

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R

A

A

G

G

N

N

A

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A

P

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L

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E

A

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M

T

A

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A

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A

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A

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A

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H
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H

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A

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|
D

G

G

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D

L

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K

N

G

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x
N

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x
L

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x
Y

Y

A

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N

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M

I

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-

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H

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I

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L

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I

-

K

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L

C

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N

V

I

M

H

A

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G

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T

I

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G

G

I

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R

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P

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H

A

A

A

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E

L

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Q

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Q

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G

G

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D

G

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G

I
x
Y

D
|
D

A

A

I

F

F

M

N

N

A

A

I

L

M

T

A

K

L

I

V

T

P

N

H

R

G

L

A

G

V

I

-

S

-

I

-

P

-

K

L
|
L

E

I

L

D

Y
|
Y

Q

E

V

V

H

R

A
x
I

V

P

T

P

Q

G

G

G

-

K

T
|
T

D

D

A

A

Q

L

A
x
V

E

E

V

T

-

R

-

I

-

T

-

W

-

N

-

K

S

S

V

L

R

D

L

L

A

E

E

E

D

D

G

-

K

Q

S

T

V

F

T

K

A

T

K

M

G

G

A

V

D

H

P
|
P

D

D

T
x
Q

L

T

V

V

A

A

S

A

A

V

R

H

A

A

Y

T

I

E

A

K

A

M

L

L

N

N

K

Q

L

I

M

L

R16 (= R33) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 33:34) binding pyruvate
D17 (= D34) 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 (≠ A91) 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 (≠ L93) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ F119) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ A147) 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 (≠ A149) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T191) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H320) mutation H->A,N: Loss of activity.
D304 (= D322) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ A328) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ Q329) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ T330) mutation to A: Loss of activity.
Y430 (≠ I448) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (= D449) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L465) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y468) 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 (≠ A472) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (= T477) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (≠ A481) 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 (= P501) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
Q495 (≠ T503) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
28% identity, 74% coverage: 2:393/532 of query aligns to 7:389/400 of 3ivtB

query
sites
3ivtB

T

T

Q

E

D

T

T

I

S

K

A

P

P

P

G

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Q

P

A

Y

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P

P

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N

A

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P

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A

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A

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N

N

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T

T

L

L

R
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R

D
x
E

G

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Q

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F

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A

G

N

A

A

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F

T

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L

T

E

E

E

K

K

K

L

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E

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I

A

A

E

K

L

A

L

L

D

D

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N

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D

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A

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A

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E

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Q

A

D

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C

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E

E

A

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I

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R

L

A

G

K

L

R

K

A

C

T

K

I

I

A

L

G

T

L
x
H

A

I

R

R

L

C

A

H

A

M

K

D

D

D

I

-

D

-

R

-

C

-

A

A

E

R

A

V

V

A

R

V

H

E

A

T

R

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H

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D

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Y

V

I

L

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-

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-

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N

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L

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G

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x
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S

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L

L

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A

A

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T

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A

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Y

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R

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V

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D

-

K

-

A

-

I

-

F

I

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H
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H

C

F

H
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H

N

N

D

D

L

T

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G

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M

A

A

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I

A

A

N

N

T

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Y

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G

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A

A

D

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A

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Q

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F

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A

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A

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Q

A

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A

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A

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A

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D

active site: Q42 (= Q37)
binding 2-oxoglutaric acid: R38 (= R33), H98 (≠ L93), R158 (≠ E157), S160 (= S159), T192 (= T191), H219 (= H222), H221 (= H224)
binding zinc ion: E39 (≠ D34), H219 (= H222), H221 (= H224)

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: 2:393/532 of query aligns to 9:394/418 of Q9Y823

query
sites
Q9Y823

T

T

Q

E

D

T

T

I

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K

A

P

P

P

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Q

N

A

G

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A

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-

S

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R

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E

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Q

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A

A

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E

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A

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K

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A

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L

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D

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E

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A

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H

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-

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D

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-

E

-

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x
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S

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E

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T

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K

-

A

-

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x
E

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H

C

F

H
|
H

N

N

D

D

L

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G

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A

A

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A

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A