SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012992063.1 NCBI__GCF_000025605.1:WP_012992063.1 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)
54% identity, 96% coverage: 3:499/519 of query aligns to 6:501/517 of Q9JZG1

query
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Q9JZG1

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D16 (= D13) binding Mn(2+)
H204 (= H201) binding Mn(2+)
H206 (= H203) binding Mn(2+)
N240 (= N237) binding Mn(2+)

Sites not aligning to the query:

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

P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
50% identity, 72% coverage: 4:379/519 of query aligns to 85:474/503 of P0DO78

query
sites
P0DO78

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R93 (= R12) mutation to A: Lost catalytic activity.
D94 (= D13) mutation to A: Lost catalytic activity.
H292 (= H201) mutation to A: Lost catalytic activity.
H294 (= H203) mutation to A: Lost catalytic activity.
H392 (= H300) mutation to A: Lost catalytic activity.

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
49% identity, 72% coverage: 4:379/519 of query aligns to 18:407/409 of 6e1jA

query
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E

E

I

I

M

I

N

S

P

P

E

E

D

D

V

V

G

G

F

V

P

V

S

K

S

S

R

Q

-

N

-

S

-

G

I

I

I

V

L

L

G

G

K

K

H
x
L

S

S

G

G

R
|
R

H
|
H

A

A

L

V

K

K

K

G

K

R

L

L

Q

K

Q

E

M

L

G

G

I

Y

E

E

V

I

S

S

E

D

A

E

E

K

L

L

E

N

R

E

I

V

F

F

E

S

K

R

F

F

K

R

E

D

L

L

A

T

D

K

K

Q

K

K

E

R

I

V

Y

T

D

D

E

D

D

D

L

L

E

K

A

A

L

L

V

V

binding coenzyme a: Q30 (= Q16), F60 (= F46), S63 (≠ A49), I95 (≠ L72), R97 (= R74), F121 (= F98), K132 (= K109), L133 (= L110), S322 (= S297), G323 (= G298), I324 (= I299), D327 (≠ H302), K331 (≠ S306), L359 (≠ H331), R362 (= R334), H363 (= H335)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P168), T194 (= T170), H225 (= H201), H227 (= H203)
binding manganese (ii) ion: D27 (= D13), V82 (vs. gap), E84 (vs. gap), H225 (= H201), H227 (= H203)

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
61% identity, 61% coverage: 3:321/519 of query aligns to 3:307/308 of 3rmjB

query
sites
3rmjB

K

R

V

V

Y

I

I

I

F

F

D

D

T

T

L

L

R

R

D
|
D

G

G

E

E

Q
|
Q

A

S

P

P

G

G

F

A

S

A

M

M

T

T

S

K

E

E

K

K

L

I

Q

R

M

V

A

A

L

R

Q

Q

L

L

A

E

R

K

L

L

G

G

V

V

D

D

V

I

L

I

E

E

A

A

G

G

F

F

A

A

S

S

K

P

G

G

D

D

Y

F

E

E

A

A

V

V

K

N

L

A

I

I

A

A

Q

K

E

T

V

I

K

T

G

K

P

S

V

T

I

V

C

C

S

S

L

L

A

S

R

R

A

A

L

I

E

E

K

R

D

D

I

I

D

R

L

Q

A

A

A

G

E

E

A

A

L

V

A

A

P

P

A

A

E

P

R

K

K

K

R

R

I

I

H

H

T

T

F

F

I

I

A

A

T

T

S

S

E

P

I

I

H

H

M

M

R

E

Y

Y

K

K

L

L

R

K

M

M

S

K

P

P

Q

K

D

Q

V

V

L

I

E

E

R

A

A

A

K

V

R

K

A

A

V

V

S

K

Y

I

A

A

R

R

R

E

Y

Y

T

T

D

D

V

V

E

E

F

F

S

S

C

C

E

E

D

D

A

A

T

L

R

R

S

S

Q

E

R

I

E

D

F

F

L

L

Y

A

R

E

V

I

I

C

E

G

E

A

A

V

I

I

K

E

A

A

G

G

A

A

T

T

V

T

I

I

N

N

I

I

P

P

D

D

T

T

V

V

G

G

Y

Y

S

S

V

I

P

P

E

Y

E

K

F

T

A

E

Q

E

L

F

I

F

E

R

D

E

I

L

R

I

N

A

N

K

V

T

P

P

N

N

I

G

D

G

K

K

V

V

I

V

I

W

S

S

V

A

H
|
H

C

C

H
|
H

D

N

D

D

L

L

G

G

L

L

A

A

V

V

A

A

N

N

S

S

L

L

M

A

A

A

V

L

K

K

H

G

G

G

A

A

R

R

Q

Q

V

V

E

E

C

C

T

T

I

V

N

N

G

G

I

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

K

K

V

V

R

R

K

H

D

D

F

L

F

F

G

G

D

-

L

L

Y

E

T

T

S

G

I

I

N

D

T

T

K

T

E

Q

I

I

Y

V

K

P

T

S

S

S

R

K

L

L

L

V

C

S

R

T

I

I

T

T

G

G

S

Y

F

P

V

V

Q

Q

P

P

N

N

K

K

A

A

I

I

V

V

G

G

D

A

N

N

A

A

F

F

S

S

H

H

E

E

S

-

G

-

I

-

H

-

Q

-

H

-

G

-

V

-

L

-

S

-

N

-

P

-

L

-

T

T

Y

Y

E

E

I

I

M

M

N

S

P

A

E

E

D

S

V

V

G

G

F

W

active site: Q16 (= Q16)
binding manganese (ii) ion: D13 (= D13), H201 (= H201), H203 (= H203), N237 (= N237)

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
49% identity, 72% coverage: 4:379/519 of query aligns to 85:474/506 of Q9FG67

query
sites
Q9FG67

V

V

Y

R

I

V

F

F

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

A

S

P

P

G

G

F

G

S
|
S

M

L

T

T

S

P

E

P

E

Q

K

K

L

L

Q

E

M

I

A

A

L

R

Q

Q

L

L

A

A

R

K

L

L

G

R

V

V

D

D

V

I

L

M

E

E

A

V

G

G

F

F

A

P

A

G

A

S

S

S

K

E

G

E

D

E

Y

L

E

E

A

T

V

I

K

K

L

T

I

I

A

A

Q

K

E

T

V

V

K

G

G

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

V

P

P

V

V

I

I

C

C

S

A

L

I

A

A

R

R

A

C

L

K

E

H

K

R

D

D

I

I

D

E

L

A

A

T

A

W

E

E

A

A

L

L

A

K

P

Y

A

A

E

K

R

R

K

P

R

R

I

I

H

L

T

V

F

F

I

T

A

S

T

T

S

S

E

D

I

I

H

H

M

M

R

K

Y

Y

K

K

L

L

R

K

M

K

S

T

P

Q

Q

E

D

E

V

V

L

I

E

E

R

M

A

A

K

V

R

S

A

S

V

I

S

R

Y

F

A

A

R

K

R

S

Y

L

T

G

-

F

D

N

D

D

V

I

E

Q

F

F

S

G

C

C

E

E

D

D

A

G

T

G

R

R

S

S

Q

D

R

K

E

D

F

F

L

L

Y

C

R

K

V

I

I

L

E

G

E

E

A

A

I

I

K

K

A

A

G

G

A

V

T

T

V

V

I

V

N

T

I

I

P

G

D

D

T

T

V

V

G

G

Y

I

S

N

V

M

P

P

E

H

E

E

F

Y

A

G

Q

E

L

L

I

V

E

T

D

Y

I

L

R

K

N

A

N

N

V

T

P

P

N

G

I

I

D

D

K

D

V

V

I

V

S
x
A

V

V

H

H

C

C

H

H

D

N

D

D

L

L

G

G

L

L

A

A

V

T

A

A

N

N

S

S

L

I

M

A

A

G

V

I

K

R

H

A

G

G

A

A

R

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

A

A

A

S

L

L

E

E

V

V

M

M

A

A

L

L

K

K

V

C

R

R

K

G

D

A

F

Y

-

V

F

I

G

N

D

G

L

V

Y

Y

T

T

S

K

I

I

N

D

T

T

K

R

E

Q

I

I

Y

M

K

A

T

T

S

S

R

K

L

M

L

V

C

Q

R

E

I

Y

T

T

G

G

S

L

F

Y

V

V

Q

Q

P

A

N

H

K

K

A

P

I

I

V

V

G

G

D

A

N

N

A

C

F

F

S

V

H

H

E

E

S

S

G

G

I

I

H

H

Q

Q

H

D

G

G

V

I

L

L

S

K

N

N

P

R

L

S

T

T

Y

Y

E

E

I

I

M

L

N

S

P

P

E

E

D

D

V

I

G

G

F

I

P

V

S

K

S

S

R

Q

-

N

-

S

-

G

I

L

I

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

H

H

A

A

L

V

K

K

K

D

K

R

L

L

Q

K

Q

E

M

L

G

G

I

Y

E

E

V

L

S

D

E

D

A

E

E

K

L

L

E

N

R

A

I

V

F

F

E

S

K

L

F

F

K

R

E

D

L

L

A

T

D

K

K

N

K

K

E

R

I

I

Y

T

D

D

E

A

D

D

L

L

E

K

A

A

L

L

V

V

S102 (= S21) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ S199) 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)
48% identity, 72% coverage: 4:379/519 of query aligns to 85:474/503 of Q9FN52

query
sites
Q9FN52

V

V

Y

R

I

V

F

L

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

A

S

P

P

G

G

F

A

S

A

M

L

T

T

S

P

E

P

E

Q

K

K

L

L

Q

E

M

I

A

A

L

R

Q

Q

L

L

A

A

R

K

L

L

G

R

V

V

D

D

V

I

L

M

E

E

A

V

G

G

F

F

A

P

A

V

A

S

S

S

K

E

G

E

D

E

Y

F

E

E

A

A

V

I

K

K

L

T

I

I

A

A

Q

K

E

T

V

V

K

G

G

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

V

P

P

V

V

I

I

C

C

S

G

L

I

A

A

R

R

A

C

L

K

E

K

K

R

D

D

I

I

D

E

L

A

A

T

A

W

E

E

A

A

L

L

A

K

P

Y

A

A

E

K

R

R

K

P

R

R

I

V

H

M

T

L

F

F

I

T

A

S

T

T

S

S

E

E

I

I

H

H

M

M

R

K

Y

Y

K

K

L

L

R

K

M

K

S

T

P

K

Q

E

D

E

V

V

L

I

E

E

R

M

A

A

K

V

R

N

A

S

V

V

S

K

Y

Y

A

A

R

K

R

S

Y

L

T

G

-

F

D

K

D

D

V

I

E

Q

F

F

S

G

C

C

E

E

D

D

A

G

T

G

R

R

S

T

Q

E

R

K

E

D

F

F

L

I

Y

C

R

K

V

I

I

L

E

G

E

E

A

S

I

I

K

K

A

A

G

G

A

A

T

T

V

T

I

V

N

G

I

F

P

A

D

D

T

T

V

V

G
|
G

Y

I

S

N

V

M

P

P

E

Q

E

E

F

F

A

G

Q

E

L

L

I

V

E

A

D

Y

I

V

R

I

N

E

N

N

V

T

P

P

N

G

I

A

D

D

K

D

V

I

I

V

I

F

S

A

V

I

H

H

C

C

H

H

D

N

D

D

L

L

G

G

L

V

A

A

V

T

A

A

N

N

S

T

L

I

M

S

A

G

V

I

K

C

H

A

G

G

A

A

R

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

A

A

A

P

L

L

E

E

V

V

M

M

A

A

L

L

K

K

V

C

R

R

K

G

D

E

F

S

F

L

G

M

D

D

-

G

L

V

Y

Y

T

T

S

K

I

I

N

D

T

S

K

R

E

Q

I

I

Y

M

K

A

T

T

S

S

R

K

L

M

L

V

C

Q

R

E

I

H

T

T

G

G

S

M

F

Y

V

V

Q

Q

P

P

N

H

K

K

A

P

I

I

V

V

G

G

D

D

N

N

A

C

F

F

S

V

H

H

E

E

S

S

G

G

I

I

H

H

Q

Q

H

D

G

G

V

I

L

L

S

K

N

N

P

R

L

S

T

T

Y

Y

E

E

I

I

M

L

N

S

P

P

E

E

D

D

V

V

G

G

F

I

-

V

-

K

-

S

P

E

S

N

S

S

R

G

I

I

I

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

H

H

A

A

L

V

K

K

K

D

K

R

L

L

Q

K

Q

E

M

L

G

G

I

Y

E

E

V

I

S

S

E

D

A

E

E

K

L

F

E

N

R

D

I

I

F

F

E

S

K

R

F

Y

K

R

E

E

L

L

A

T

D

K

K

D

K

K

E

R

I

I

Y

T

D

D

E

A

D

D

L

L

E

K

A

A

L

L

V

V

G263 (= G172) 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)
36% identity, 69% coverage: 3:361/519 of query aligns to 21:370/399 of 6ktqA

query
sites
6ktqA

K

K

V

V

Y

G

I

I

F

L

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

A

T

P

P

G

G

F

V

S

V

M

F

T

T

S

T

E

D

E

Q

K

R

L

V

Q

E

M

I

A

A

L

K

Q

A

L

L

A

S

R

D

L

I

G

G

V

V

D

Q

V

M

L

I

E

E

A

A

G

G

F

H

A

P

A

A

A
x
V

S

S

K

P

G

D

D

I

Y

Y

E

E

A

G

V

I

K

R

L

R

I

I

A

I

Q

K

E

L

V

K

K

R

G

E

P

G

V

V

I

I

C

K

S

S

-

E

-

I

-

V

-

A

L

H

A

S

R
|
R

A
|
A

L

V

E

K

K

R

D

D

I

I

D

E

L

V

A

G

A

A

E

E

A

-

L

-

A

-

P

-

A

I

E

E

R

A

K

D

R

R

I

I

H

A

T

I

F
|
F

I

Y

A

G

T

I

S

S

E

D

I

T

H

H

M

L

R

K

Y

A

K

K

L
x
H

R

H

M

T

S

T

P

R

Q

D

D

E

V

A

L

L

E

R

R

S

A

I

K

A

R

E

A

T

V

V

S

S

Y

Y

A

A

R

K

R

S

Y

H

T

G

D

V

D

K

V

V

E
x
R

F

F

S
x
T

C

A

E
|
E

D

D

A

A

T

T

R

R

S

A

Q

D

R

Y

E

Q

F

Y

L

L

Y

L

R

E

V

V

I

I

E

K

E

T

A

V

I

R

K

D

A

A

G

G

A

A

T

D

V

R

I

V

N
x
S

I

I

P

A

D

D

T
|
T

V

V

G

G

Y

V

S

L

V

Y

P

P

E

S

E

R

F

T

A

R

Q

E

L

L

I

F

E

K

D

D

I

L

R

T

N

S

N

R

V

F

P

P

N

D

I

I

D

E

K

-

V

-

I

-

I

F

S

D

V

I

H
|
H

C

A

H
|
H

D

N

D

D

L

L

G

G

L

M

A

A

V

V

A

A

N

N

S

V

L

L

M

A

A

A

V

A

K

E

H

G

G

G

A

A

R

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

A

A

A

P

L

L

E

Q

E

V

V

V

V

A

M

A

A

A

L

L

K

K

V

Y

R

H

K

-

D

-

F

-

F

F

G

G

D

-

L

-

Y

I

T

E

S

V

I

V

N

D

T

L

K

K

E

K

I

L

Y

S

K

E

T

V

S

A

R

S

L

L

L

V

C

E

R

K

I

Y

T

S

G

G

S

I

F

A

V

L

Q

P

P

P

N

N

K

F

A

P

I

I

V

T

G

G

D

D

N

Y

A

A

F

F

S

V

H

H

E

K

S

A

G

G

I

V

H

H

Q

V

H

A

G

G

V

V

L

L

S

N

N

D

P

P

L

K

T

T

Y

Y

E

E

I

F

M

L

N

P

P

P

E

E

D

T

V

F

G

G

F

-

P

R

S

S

S

R

R

D

I

Y

I

V

L

I

G

D

K

K

H

Y

S

T

G

G

R

K

H

H

A

A

L

V

K

K

K

D

K

R

L

F

Q

D

Q

R

M

L

G

G

I

V

E

K

V

L

S

T

E

D

A

S

E

E

L

I

E

D

R

Q

I

V

F

L

E

A

K

K

F

I

K

K

binding 2-oxoglutaric acid: R30 (= R12), R154 (≠ E136), T156 (≠ S138), E158 (= E140), S184 (≠ N166), T188 (= T170), H216 (= H201), H218 (= H203)
binding coenzyme a: V67 (≠ A49), R96 (= R74), A97 (= A75), F116 (= F98), H128 (≠ L110), E158 (= E140)
binding zinc ion: E31 (≠ D13), H216 (= H201), H218 (= H203)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
33% identity, 72% coverage: 4:378/519 of query aligns to 4:377/379 of 4ov4A

query
sites
4ov4A

V

I

Y

H

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

A

A

P

L

G

K

F

R

S

P

M

W

T

T

S

I

E

D

E

E

K

K

L

I

Q

E

M

V

A

F

L

D

Q

L

L

L

A

V

R

E

L

L

G

N

V

V

D

D

V

G

L

I

E

E

A

V

G

G

F

F

A

P

A

S

S

N

K

E

G

T

D

E

Y

F

E

H

A

T

V

C

K

Q

L

V

I

L

A

S

Q

K

E

R

V

A

-

P

K

K

G

G

P

K

V

P

I

I

C

A

S

A

L

L

A

S

R

R

A

A

L

N

E

Q

K

N

D

E

I

I

D

A

L

V

A

T

A

W

E

E

A

A

L

I

A

Q

P

K

A

A

E

D

R

C

K

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

E

D

I

F

H

S

M

I

R

K

Y

H

K

V

L

L

R

K

M

I

S

S

P

E

Q

K

D

E

V

V

L

L

E

Q

R

K

A

I

K

R

R

N

A

S

V

I

S

S

Y

F

A

A

R

R

R

S

Y

I

T

V

D

G

-

P

-

G

-

I

D

E

V

I

E

Q

F

F

S

S

C

G

E

E

D

H

A

F

T

G

R

D

S

A

Q

I

R

E

E

N

F

F

L

A

Y

F

-

T

-

K

R

E

V

A

I

F

E

L

E

T

A

A

I

I

K

E

A

A

G

G

A

A

T

N

V

I

I

I

N

N

I

L

P
|
P

D

N

T
|
T

V

V

G

E

Y

R

S

Y

V

R

P

P

E

M

E

V

F

F

A

V

Q

N

L

M

I

V

E

K

D

E

I

I

R

K

N

D

N

V

V

V

P

K

N

-

I

-

D

D

K

K

V

A

I

I

S

S

V

I

H
|
H

C

T

H
|
H

D

N

D

D

L

L

G

G

L

M

A

A

V

T

A

A

N

T

S

S

L

V

M

E

A

S

V

V

K

Y

H

V

G

G

A

A

R

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

A

T

A

N

L

L

E

Y

E

E

V

T

V

A

M

I

A

A

L

L

K

H

V

Q

R

N

K

G

D

E

F

N

F

L

G

-

D

-

L

-

Y

-

T

-

S

N

I

I

N

N

T

F

K

Q

E

R

I

I

Y

Y

K

P

T

T

S

A

R

K

L

R

L

I

C

S

R

E

I

L

T

T

G

G

S

I

F

P

V

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

D

E

N

D

A

I

F

F

S

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

H

H

G

-

V

-

L

-

S

Q

N

S

P

K

L

G

T

A

Y

Y

E

R

I

T

M

F

N

S

P

P

E

E

D

F

V

V

G

G

-

R

F

M

P

D

S

K

S

E

R

T

I

I

I

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

H

K

A

A

L

I

K

E

K

F

K

L

L

L

Q

H

Q

Q

M

R

G

G

I

I

E

Q

V

V

S

S

E

K

A

E

E

G

L

I

E

H

R

H

I

L

F

F

E

S

K

L

F

A

K

K

E

S

L

I

A

S

D

S

K

R

K

E

-

N

K

R

E

E

I

I

Y

T

D

E

E

A

D

E

L

L

E

V

A

A

L

L

active site: Q16 (= Q16)
binding 3-methyl-2-oxobutanoic acid: R12 (= R12), P174 (= P168), T176 (= T170), H205 (= H201), H207 (= H203)
binding zinc ion: D13 (= D13), H205 (= H201), H207 (= H203)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
33% identity, 72% coverage: 4:378/519 of query aligns to 4:379/380 of 4ov9A

query
sites
4ov9A

V

I

Y

H

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

A

A

P

L

G

K

F

R

S

P

M

W

T

T

S

I

E

D

E

E

K

K

L

I

Q

E

M

V

A

F

L

D

Q

L

L

L

A

V

R

E

L

L

G

N

V

V

D

D

V

G

L

I

E

E

A

V

G

G

F

F

A

P

A

S

S

N

K

E

G

T

D

E

Y

F

E

H

A

T

V

C

K

Q

L

V

I

L

A

S

Q

K

E

R

V

A

-

P

K

K

G

G

P

K

V

P

I

I

C

A

S

A

L
|
L

A

S

R

R

A

A

L

N

E

Q

K

N

D

E

I

I

D

A

L

V

A

T

A

W

E

E

A

A

L

I

A

Q

P

K

A

A

E

D

R

C

K

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

E

D

I

F

H

S

M

I

R

K

Y

H

K

V

L

L

R

K

M

I

S

S

P

E

Q

K

D

E

V

V

L

L

E

Q

R

K

A

I

K

R

R

N

A

S

V

I

S

S

Y

F

A

A

R

R

R

S

Y

I

T

V

D

G

-

P

-

G

-

I

D

E

V

I

E

Q

F

F

S

S

C

G

E

E

D

H

A

F

T

G

R

D

S

A

Q

I

R

E

E

N

F

F

L

A

Y

F

-

T

-

K

R

E

V

A

I

F

E

L

E

T

A

A

I

I

K

E

A

A

G

G

A

A

T

N

V

I

I

I

N

N

I

L

P

P

D

N

T
|
T

V

V

G

E

Y

R

S

Y

V

R

P

P

E

M

E

V

F

F

A

V

Q

N

L

M

I

V

E

K

D

E

I

I

R

K

N

D

N

V

V

V

P

K

N

-

I

-

D

D

K

K

V

A

I

I

S

S

V

I

H
|
H

C

T

H
|
H

D

N

D

D

L

L

G

G

L

M

A

A

V

T

A

A

N

T

S

S

L

V

M

E

A

S

V

V

K

Y

H

V

G

G

A

A

R

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

A

T

A

N

L

L

E

Y

E

E

V

T

V

A

M

I

A

A

L

L

K

H

V

Q

R

N

K

G

D

E

F

N

F

L

G

-

D

-

L

-

Y

-

T

-

S

N

I

I

N

N

T

F

K

Q

E

R

I

I

Y

Y

K

P

T

T

S

A

R

K

L

R

L

I

C

S

R

E

I

L

T

T

G

G

S

I

F

P

V

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

D

E

N

D

A

I

F

F

S

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

H

-

G

T

V

L

L

H

S

Q

N

S

P

K

L

G

T

A

Y

Y

E

R

I

T

M

F

N

S

P

P

E

E

D

F

V

V

G

G

-

R

F

M

P

D

S

K

S

E

R

T

I

I

I

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

H

K

A

A

L

I

K

E

K

F

K

L

L

L

Q

H

Q

Q

M

R

G

G

I

I

E

Q

V

V

S

S

E

K

A

E

E

G

L

I

E

H

R

H

I

L

F

F

E

S

K

L

F

A

K

K

E

S

L

I

A

S

D

S

K

R

K

E

-

N

K

R

E

E

I

I

Y

T

D

E

E

A

D

E

L

L

E

V

A

A

L

L

active site: Q16 (= Q16)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R12), L73 (= L72), T176 (= T170), H205 (= H201), H207 (= H203)
binding zinc ion: D13 (= D13), H205 (= H201), H207 (= H203)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
28% identity, 90% coverage: 3:467/519 of query aligns to 7:472/516 of Q8F3Q1

query
sites
Q8F3Q1

K

R

V

L

Y

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

A

T

P

R

G

G

F

V

S

S

M

F

T

S

S

T

E

S

E

E

K

K

L

L

Q

N

M

I

A

A

-

K

L

F

Q

L

L

L

A

Q

R

K

L

L

G

N

V

V

D

D

V

R

L

V

E

E

A

I

G

A

F

S

A

A

A

R

A

V

S

S

K

K

G

G

D

E

Y

L

E

E

A

T

V

V

K

Q

L

K

I

I

A

M

Q

E

E

W

V

A

K

A

G

T

P

E

V

Q

I

L

C

T

S

E

L

R

A

I

R

E

A

I

L
|
L

-

G

-
x
F

-

V

-

D

-

G

E

N

K

K

D

T

I

V

D

D

L

W

A

I

A

K

E

D

A

S

L

G

A

A

P

-

A

-

E

-

R

-

K

K

R

V

I

L

H

N

T

L

F
x
L

I

T

A

K

T

G

S

S

E

L

I

H

H

H

M

L

R

E

Y

K

K

Q

L

L

R

G

M

K

S

T

P

P

Q

K

D

E

V

F

L

F

E

T

R

D

A

V

K

S

R

F

A

V

V

I

S

E

Y

Y

A

A

R

I

R

K

Y

S

T

G

D

L

D

K

V

I

E

N

F

V

S
x
Y

C

L

E
|
E

D

D

A

W

T

S

-

N

-

G

-

F

R

R

S

N

Q

S

R

P

E

D

F

Y

L

V

Y

K

R

S

V

L

I

V

E

E

E

H

A

L

I

S

K

K

A

E

G

H

A

I

T

E

V

R

I

I

N

F

I

L

P

P

D

D

T
|
T

V

L

G

G

Y

V

S

L

V

S

P

P

E

E

F

T

A

F

Q

Q

L

G

I

V

E

D

D

S

I

L

R

I

N

Q

N

K

V

Y

P

P

N

D

I

I

D

H

K

-

V

-

I

-

I

F

S

E

V

F

H

H

C

G

H

H

D

N

D

D

L

Y

G

D

L

L

A

S

V

V

A

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R16 (= R12) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 12:13) binding pyruvate
D17 (= D13) 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 (= L76) mutation to A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat.; mutation to V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat.
F83 (vs. gap) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ F98) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ S138) 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 (= E140) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T170) 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 (≠ H302) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ P308) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (= L309) 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 (≠ F450) 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 (≠ L455) 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 (≠ A463) mutation to A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.

Sites not aligning to the query:

493 P→A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
495 Q→A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

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: 1:373/519 of query aligns to 1:365/376 of O87198

query
sites
O87198

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R12 (= R12) binding 2-oxoglutarate
E13 (≠ D13) binding Mg(2+)
H72 (≠ S71) 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 (≠ H96) binding L-lysine
R133 (vs. gap) binding 2-oxoglutarate
S135 (= S138) binding L-lysine
T166 (= T170) binding 2-oxoglutarate; binding L-lysine
H195 (= H201) binding Mg(2+)
H197 (= H203) binding Mg(2+)

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
28% identity, 71% coverage: 6:373/519 of query aligns to 32:389/400 of 3ivtB

query
sites
3ivtB

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