SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013009813.1 NCBI__GCF_000025725.1:WP_013009813.1 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)
53% identity, 96% coverage: 5:502/519 of query aligns to 6:501/517 of Q9JZG1

query
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Q9JZG1

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D16 (= D15) binding Mn(2+)
H204 (= H203) binding Mn(2+)
H206 (= H205) binding Mn(2+)
N240 (= N239) 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)
47% identity, 73% coverage: 3:381/519 of query aligns to 15:407/409 of 6e1jA

query
sites
6e1jA

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binding coenzyme a: Q30 (= Q18), F60 (= F48), S63 (= S51), I95 (≠ L74), R97 (= R76), F121 (= F100), K132 (= K111), L133 (= L112), S322 (≠ A299), G323 (= G300), I324 (= I301), D327 (= D304), K331 (= K308), L359 (≠ H333), R362 (= R336), H363 (= H337)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P170), T194 (= T172), H225 (= H203), H227 (= H205)
binding manganese (ii) ion: D27 (= D15), V82 (vs. gap), E84 (vs. gap), H225 (= H203), H227 (= H205)

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)
45% identity, 74% coverage: 3:386/519 of query aligns to 82:479/503 of Q9FN52

query
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Q9FN52

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H

K

K

A

P

I

I

V

V

G

G

K

D

N

N

A

C

F

F

A

V

H

H

E

E

A

S

G

G

I

I

H

H

Q

Q

D

D

G

G

M

I

L

L

K

K

N

N

R

R

T

S

T

T

Y

Y

E

E

I

I

M

L

T

S

P

P

E

E

S

D

V

V

G

G

Y

I

-

V

-

K

-

S

P

E

S

N

T

S

S

G

L

I

V

V

L

L

G

G

K

K

H

L

S

S

G

G

R

R

H

H

A

A

F

V

V

K

Q

D

R

R

I

L

K

K

D

E

L

L

G

G

Y

Y

E

E

I

I

E

S

N

D

D

E

A

K

M

F

Q

N

S

D

A

I

F

F

D

S

E

R

F

Y

K

R

I

E

L

L

A

T

D

K

K

D

K

K

E

R

V

I

F

T

D

D

E

A

D

D

I

L

E

K

S

A

I

L

I

V

F

V

N

N

Q

G

A

A

K

E

G263 (= G174) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
57% identity, 61% coverage: 5:323/519 of query aligns to 3:307/308 of 3rmjB

query
sites
3rmjB

R

R

V

V

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

N

T

T

K

D

E

E

E

K

K

I

I

Q

R

L

V

A

A

L

R

Q

Q

L

L

E

E

R

K

L

L

G

G

V

V

D

D

V

I

M

I

E

E

A

A

G

G

F

F

P

A

I

A

S

A

S

S

P

P

G

G

D

D

F

F

E

E

A

A

V

V

T

N

R

A

V

I

A

A

K

K

V

T

I

I

K

T

N

K

S

S

G

T

V

V

A

C

G

S

L

L

C

S

R

R

A

A

N

I

E

E

K

R

D

D

I

I

S

R

V

Q

G

A

W

G

D

E

A

A

L

V

Q

A

H

P

A

A

V

P

R

K

P

K

R

R

I

I

H

H

T

T

F

F

I

I

A

A

T

T

S

S

D

P

I

I

H

H

L

M

Q

E

H

Y

K

K

L

L

K

K

K

M

T

K

R

P

E

K

E

Q

A

V

L

I

E

E

I

A

A

A

V

V

K

K

A

A

V

V

K

K

F

I

A

A

R

R

N

E

L

Y

C

T

D

D

V

V

E

E

F

F

S

S

A

C

E

E

D

D

A

A

M

L

R

R

S

S

D

E

V

I

D

D

Y

F

L

L

C

A

Q

E

V

I

V

C

E

G

A

A

V

V

I

I

A

E

A

A

G

G

A

A

N

T

T

T

V

I

N

N

L

I

P

P

D

D

T

T

V

V

G

G

Y

Y

K

S

M

I

P

P

F

Y

E

K

I

T

D

E

K

E

V

F

I

F

S

R

E

E

V

L

I

I

N

A

R

K

V

T

P

P

N

N

V

G

D

G

K

K

A

V

R

V

I

W

S

S

V

A

H
|
H

C

C

H
|
H

N

N

D

D

L

L

G

G

L

L

S

A

V

V

A

A

N

N

S

S

L

L

M

A

A

A

V

L

N

K

A

G

G

G

A

A

S

R

Q

Q

I

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

C

A

S

S

L

V

E

E

V

I

V

V

M

M

G

A

L

L

T

K

V

V

R

R

K

H

D

D

V

L

F

F

D

-

D

G

I

L

E

E

I

T

G

G

V

I

K

D

T

T

N

T

E

Q

I

I

Y

V

R

P

A

S

S

S

K

K

M

L

L

V

T

S

T

T

I

I

T

T

G

G

V

Y

G

P

V

V

Q

Q

P

P

N

N

K

K

A

A

I

I

V

V

G

G

K

A

N

N

A

A

F

F

A

S

H

H

E

E

A

-

G

-

I

-

H

-

Q

-

D

-

G

-

M

-

L

-

K

-

N

-

R

-

T

-

T

T

Y

Y

E

E

I

I

M

M

T

S

P

A

E

E

S

S

V

V

G

G

Y

W

active site: Q16 (= Q18)
binding manganese (ii) ion: D13 (= D15), H201 (= H203), H203 (= H205), N237 (= N239)

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
44% identity, 78% coverage: 6:411/519 of query aligns to 85:502/506 of Q9FG67

query
sites
Q9FG67

V

V

I

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

N

T

T

P

D

P

E

Q

K

K

I

L

Q

E

L

I

A

A

L

R

Q

Q

L

L

E

A

R

K

L

L

G

R

V

V

D

D

V

I

M

M

E

E

A

V

G

G

F

F

P

P

I

G

S

S

P

E

G

E

D

E

F

L

E

E

A

T

V

I

T

K

R

T

V

I

A

A

K

K

V

T

I

V

K

G

N

N

-

E

-

V

-

D

-

E

S

T

G

G

-

Y

-

V

-

P

-

V

V

I

A

C

G

A

L

I

C

A

R

R

A

C

N

K

E

H

K

R

D

D

I

I

S

E

V

A

G

T

W

W

D

E

A

A

L

L

Q

K

H

Y

A

A

V

K

R

R

P

P

R

R

I

I

H

L

T

V

F

F

I

T

A

S

T

T

S

S

D

D

I

I

H

H

L

M

Q

K

H

Y

K

K

L

L

K

K

T

T

R

Q

E

E

A

V

L

I

E

E

I

M

A

A

V

V

K

S

A

S

V

I

K

R

F

F

A

A

R

K

N

S

L

L

-

G

C

F

D

N

D

D

V

I

E

Q

F

F

S

G

A

C

E

E

D

D

A

G

M

G

R

R

S

S

D

D

V

K

D

D

Y

F

L

L

C

C

Q

K

V

I

V

L

E

G

A

E

V

A

I

I

A

K

A

A

G

G

A

V

N

T

T

V

V

V

N

T

L

I

P

G

D

D

T

T

V

V

G

G

Y

I

K

N

M

M

P

P

F

H

E

E

I

Y

D

G

K

E

V

L

I

V

S

T

E

Y

V

L

I

K

N

A

R

N

V

T

P

P

N

G

V

I

D

D

K

D

A

V

R

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

M

A

A

G

V

I

N

R

A

A

G

G

A

A

S

R

Q

Q

I

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

V

V

M

M

G

A

L

L

T

K

V

C

R

R

K

G

D

A

-

Y

V

V

F

I

D

N

D

G

I

V

E

Y

I

T

G

K

V

I

K

D

T

T

N

R

E

Q

I

I

Y

M

R

A

A

T

S

S

K

K

M

M

L

V

T

Q

T

E

I

Y

T

T

G

G

V

L

G

Y

V

V

Q

Q

P

A

N

H

K

K

A

P

I

I

V

V

G

G

K

A

N

N

A

C

F

F

A

V

H

H

E

E

A

S

G

G

I

I

H

H

Q

Q

D

D

G

G

M

I

L

L

K

K

N

N

R

R

T

S

T

T

Y

Y

E

E

I

I

M

L

T

S

P

P

E

E

S

D

V

I

G

G

Y

I

-

V

-

K

-

S

P

Q

S

N

T

S

S

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

V

K

Q

D

R

R

I

L

K

K

D

E

L

L

G

G

Y

Y

E

E

I

L

E

D

N

D

D

E

A

K

M

L

Q

N

S

A

A

V

F

F

D

S

E

L

F

F

K

R

I

D

L

L

A

T

D

K

K

N

K

K

E

R

V

I

F

T

D

D

E

A

D

D

I

L

E

K

S

A

I

L

I

V

F

-

N

-

Q

T

A

S

K

S

D

D

E

E

Q

I

F

S

A

L

Y

E

V

K

M

L

E

N

S

G

V

A

N

N

I

G

L

L

S

K

G

S

D

N

T

G

A

Y

I

I

P

P

T

V

A

P

T

Q

I

V

S102 (= S23) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ S201) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
36% identity, 69% coverage: 5:363/519 of query aligns to 21:370/399 of 6ktqA

query
sites
6ktqA

R

K

V

V

I

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

N

T

T

T

D

D

E

Q

K

R

I

V

Q

E

L

I

A

A

L

K

Q

A

L

L

E

S

R

D

L

I

G

G

V

V

D

Q

V

M

M

I

E

E

A

A

G

G

F

H

P

P

I

A

S
x
V

S

S

P

P

G

D

D

I

F

Y

E

E

A

G

V

I

T

R

R

R

V

I

A

I

K

K

-

L

-

K

-

R

-

E

-

G

V

V

I

I

K

K

N

S

S

E

G

I

V

V

A

A

G

H

L

-

C

S

R
|
R

A
|
A

N

V

E

K

K

R

D

D

I

I

S

E

V

V

G

G

W

A

D

E

A

I

L

E

Q

A

H

-

A

-

V

-

R

-

P

D

R

R

I

I

H

A

T

I

F
|
F

I

Y

A

G

T

I

S

S

D

D

I

T

H

H

L

L

Q

K

H

A

K

K

L
x
H

K

H

K

T

T

T

R

R

E

D

E

E

A

A

L

L

E

R

I

S

A

I

V

A

K

E

A

T

V

V

K

S

F

Y

A

A

R

K

N

S

L

H

C

G

D

V

D

K

V

V

E
x
R

F

F

S
x
T

A

A

E
|
E

D

D

A

A

M

T

R

R

S

A

D

D

V

Y

D

Q

Y

Y

L

L

C

L

Q

E

V

V

V

I

E

K

A

T

V

V

I

R

A

D

A

A

G

G

A

A

N

D

T

R

V

V

N
x
S

L

I

P

A

D

D

T
|
T

V

V

G

G

Y

V

K

L

M

Y

P

P

F

S

E

R

I

T

D

R

K

E

V

L

I

F

S

K

E

D

V

L

I

T

N

S

R

R

V

F

P

P

N

D

V

I

D

E

K

-

A

-

R

-

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

M

A

A

A

V

A

N

E

A

G

G

G

A

A

S

T

Q

I

I

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

V

V

V

A

M

A

G

A

L

L

T

K

V

Y

R

H

K

F

D

-

V

-

F

-

D

-

D

G

I

I

E

E

I

V

G

-

V

V

K

D

T

L

N

K

E

K

I

L

Y

S

R

E

A

V

S

A

K

S

M

L

L

V

T

E

T

K

I

Y

T

S

G

G

V

I

G

A

V

L

Q

P

P

P

N

N

K

F

A

P

I

I

V

T

G

G

K

D

N

Y

A

A

F

F

A

V

H

H

E

K

A

A

G

G

I

V

H

H

Q

V

D

A

G

G

M

V

L

L

K

N

N

D

R

P

T

K

T

T

Y

Y

E

E

I

F

M

L

T

P

P

P

E

E

S

T

V

F

G

G

Y

R

P

-

S

S

T

R

S

D

L

Y

V

V

L

I

G

D

K

K

H

Y

S

T

G

G

R

K

H

H

A

A

F

V

V

K

Q

D

R

R

I

F

K

D

D

R

L

L

G

G

Y

V

E

K

I

L

E

T

N

D

D

S

A

E

M

I

Q

D

S

Q

A

V

F

L

D

A

E

K

F

I

K

K

binding 2-oxoglutaric acid: R30 (= R14), R154 (≠ E138), T156 (≠ S140), E158 (= E142), S184 (≠ N168), T188 (= T172), H216 (= H203), H218 (= H205)
binding coenzyme a: V67 (≠ S51), R96 (= R76), A97 (= A77), F116 (= F100), H128 (≠ L112), E158 (= E142)
binding zinc ion: E31 (≠ D15), H216 (= H203), H218 (= H205)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
32% identity, 71% coverage: 4:369/519 of query aligns to 2:366/380 of 4ov9A

query
sites
4ov9A

R

K

R

T

V

I

I

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

N

T

T

I

D

D

E

E

K

K

I

I

Q

E

L

V

A

F

L

D

Q

L

L

L

E

V

R

E

L

L

G

N

V

V

D

D

V

G

M

I

E

E

A

V

G

G

F

F

P

P

I

S

S

S

S

N

P

E

G

T

D

E

F

F

E

H

A

T

V

C

T

Q

R

V

V

L

A

S

K

K

-

R

V

A

I

P

K

K

N

G

S

K

G

P

V

I

A

A

G

A

L
|
L

C

S

R

R

A

A

N

N

E

Q

K

N

D

E

I

I

S

A

V

V

G

T

W

W

D

E

A

A

L

I

Q

Q

H

K

A

A

V

D

R

C

P

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

L

I

Q

K

H

H

K

V

L

L

K

K

K

I

T

S

R

E

E

K

E

E

A

V

L

L

E

Q

I

K

A

I

V

R

K

N

A

S

V

I

K

S

F

F

A

A

R

R

N

S

L

I

C

V

D

G

-

P

-

G

-

I

D

E

V

I

E

Q

F

F

S

S

A

G

E

E

-

H

-

F

-

G

D

D

A

A

M

I

R

E

S

-

D

N

V

F

D

A

Y

F

L

T

C

K

Q

E

V

A

V

F

E

L

A

T

V

A

I

I

A

E

A

A

G

G

A

A

N

N

T

I

V

I

N

N

L

L

P

P

D

N

T
|
T

V

V

G

E

Y

R

K

Y

M

R

P

P

F

M

E

V

I

F

D

V

K

N

V

M

I

V

S

K

E

E

V

I

I

K

N

D

R

V

V

V

P

K

N

-

V

-

D

D

K

K

A

A

R

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

M

E

A

S

V

V

N

Y

A

V

G

G

A

A

S

E

Q

Q

I

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

V

T

V

A

M

I

G

A

L

L

T

H

V

Q

R

N

K

G

D

E

V

-

F

-

D

-

I

-

E

N

I

L

G

N

V

I

K

N

T

F

N

Q

E

R

I

I

Y

Y

R

P

A

T

S

A

K

K

M

R

L

I

T

S

T

E

I

L

T

T

G

G

V

I

G

P

V

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

K

E

N

D

A

I

F

F

A

S

H

H

E

R

A

S

G

G

I

I

H

H

Q

Q

D

T

G

-

M

L

L

H

K

Q

N

S

R

K

T

G

T

A

Y

Y

E

R

I

T

M

F

T

S

P

P

E

E

S

F

V

V

G

G

-

R

Y

M

P

D

S

K

T

E

S

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

V

E

Q

F

R

L

I

L

K

H

D

Q

L

R

G

G

Y

I

E

Q

I

V

E

S

N

K

D

E

A

G

M

I

Q

H

S

H

A

L

F

F

D

S

E

L

F

A

K

K

I

S

L

I

A

S

D

S

K

R

K

E

active site: Q16 (= Q18)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R14), L73 (= L74), T176 (= T172), H205 (= H203), H207 (= H205)
binding zinc ion: D13 (= D15), H205 (= H203), H207 (= H205)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
32% identity, 71% coverage: 4:369/519 of query aligns to 2:364/379 of 4ov4A

query
sites
4ov4A

R

K

R

T

V

I

I

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

N

T

T

I

D

D

E

E

K

K

I

I

Q

E

L

V

A

F

L

D

Q

L

L

L

E

V

R

E

L

L

G

N

V

V

D

D

V

G

M

I

E

E

A

V

G

G

F

F

P

P

I

S

S

S

S

N

P

E

G

T

D

E

F

F

E

H

A

T

V

C

T

Q

R

V

V

L

A

S

K

K

-

R

V

A

I

P

K

K

N

G

S

K

G

P

V

I

A

A

G

A

L

L

C

S

R

R

A

A

N

N

E

Q

K

N

D

E

I

I

S

A

V

V

G

T

W

W

D

E

A

A

L

I

Q

Q

H

K

A

A

V

D

R

C

P

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

L

I

Q

K

H

H

K

V

L

L

K

K

K

I

T

S

R

E

E

K

E

E

A

V

L

L

E

Q

I

K

A

I

V

R

K

N

A

S

V

I

K

S

F

F

A

A

R

R

N

S

L

I

C

V

D

G

-

P

-

G

-

I

D

E

V

I

E

Q

F

F

S

S

A

G

E

E

-

H

-

F

-

G

D

D

A

A

M

I

R

E

S

-

D

N

V

F

D

A

Y

F

L

T

C

K

Q

E

V

A

V

F

E

L

A

T

V

A

I

I

A

E

A

A

G

G

A

A

N

N

T

I

V

I

N

N

L

L

P
|
P

D

N

T
|
T

V

V

G

E

Y

R

K

Y

M

R

P

P

F

M

E

V

I

F

D

V

K

N

V

M

I

V

S

K

E

E

V

I

I

K

N

D

R

V

V

V

P

K

N

-

V

-

D

D

K

K

A

A

R

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

M

E

A

S

V

V

N

Y

A

V

G

G

A

A

S

E

Q

Q

I

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

V

T

V

A

M

I

G

A

L

L

T

H

V

Q

R

N

K

G

D

E

V

-

F

-

D

-

I

-

E

N

I

L

G

N

V

I

K

N

T

F

N

Q

E

R

I

I

Y

Y

R

P

A

T

S

A

K

K

M

R

L

I

T

S

T

E

I

L

T

T

G

G

V

I

G

P

V

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

K

E

N

D

A

I

F

F

A

S

H

H

E

R

A

S

G

G

I

I

H

H

Q

Q

D

H

G

-

M

-

L

-

K

Q

N

S

R

K

T

G

T

A

Y

Y

E

R

I

T

M

F

T

S

P

P

E

E

S

F

V

V

G

G

-

R

Y

M

P

D

S

K

T

E

S

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

V

E

Q

F

R

L

I

L

K

H

D

Q

L

R

G

G

Y

I

E

Q

I

V

E

S

N

K

D

E

A

G

M

I

Q

H

S

H

A

L

F

F

D

S

E

L

F

A

K

K

I

S

L

I

A

S

D

S

K

R

K

E

active site: Q16 (= Q18)
binding 3-methyl-2-oxobutanoic acid: R12 (= R14), P174 (= P170), T176 (= T172), H205 (= H203), H207 (= H205)
binding zinc ion: D13 (= D15), H205 (= H203), H207 (= H205)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
30% identity, 96% coverage: 5:502/519 of query aligns to 7:509/516 of Q8F3Q1

query
sites
Q8F3Q1

R

R

V

L

I

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

A

T

P

R

G

G

F

V

S

S

M

F

N

S

T

T

D

S

E

E

K

K

I

L

Q

N

L

I

A

A

-

K

L

F

Q

L

L

L

E

Q

R

K

L

L

G

N

V

V

D

D

V

R

M

V

E

E

A

I

G

A

F

S

P

A

I

R

S

V

S

S

P

K

G

G

D

E

F

L

E

E

A

T

V

V

T

Q

R

K

V

I

A

M

-

E

-

W

-

A

-

T

-

E

K

Q

V

L

I

T

K

E

N

R

S

I

G

E

V

I

A
x
L

G

G

L
x
F

C

V

R

D

A

G

N

N

E

K

K

-

D

-

I

-

S

T

V

V

G

D

W

W

D

-

A

-

L

I

Q

K

H

D

A

S

V

G

R

A

P

K

R

V

I

L

H

N

T

L

F
x
L

I

T

A

K

T

G

S

S

D

L

I

H

H

H

L

L

Q

E

H

K

K

Q

L

L

K

G

K

K

T

T

R

P

E

K

E

E

A

F

L

F

E

T

I

D

A

V

V

S

K

F

A

V

V

I

K

E

F

Y

A

A

R

I

N

K

L

S

C

G

D

L

D

K

V

I

E

N

F

V

S
x
Y

A

L

E
|
E

D

D

-

W

-

S

-

N

A

G

M

F

R

R

S

N

D

S

V

P

D

D

Y

Y

L

V

C

K

Q

S

V

L

V

V

E

E

A

H

V

L

I

S

A

K

A

E

G

H

A

I

N

E

T

R

V

I

N

F

L

L

P

P

D

D

T
|
T

V

L

G

G

Y

V

K

L

M

S

P

P

F

E

E

E

I

T

D

F

K

Q

V

G

I

V

S

D

E

S

V

L

I

I

N

Q

R

K

V

Y

P

P

N

D

V

I

D

-

K

-

A

-

R

H

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

M

Q

A

A

V

I

N

R

A

A

G

G

A

V

S

K

Q

G

I

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

V

L

V

V

M

T

G

T

L

I

T

H

V

D

R

K

K

S

D

N

V

S

F

K

D

T

D

N

I

I

-

N

E

E

I

I

G

A

V

-

K

-

T

-

N

-

E

-

I

I

Y

T

R

E

A

A

S

S

K

R

M

L

L

V

T

E

T

V

I

F

T

S

G

G

V

K

G

R

V

I

Q

S

P

A

N

N

K

R

A

P

I

I

V

V

G

G

K

E

N

D

A

V

F

F

A

T

H

Q

E

T

A

A

G

G

I

V

H
|
H

Q

A

D
|
D

G

G

M

D

L

K

K

K

N

G

R
x
N

T
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

Y

R

P

-

S

K

T

R

S

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

V

S

Q

E

R

N

I

V

K

K

D

Q

L

L

G

G

Y

M

E

V

I

L

E

S

N

E

D

V

A

V

M

L

Q

Q

S

K

A

V

F

L

D

E

E

R

F

V

K

I

I

E

L

L

A

G

D

D

K

Q

K

N

K

K

E

L

V

V

F

T

D

P

E

E

D

D

I

L

E

P

S

F

I

I

F

A

N

D

-

V

Q

S

A

G

K

R

D

T

E

G

Q

E

F

K

A

V

Y

L

V

T

M

I

E

K

S

S

V

C

N

N

I

I

L

H

S

S

G

G

D

I

T

G

A

I

I

R

P

P

T

H

A

A

T

Q

I

I

K

E

L

L

A

-

D

E

K

Y

D

Q

G

G

N

K

E

I

F

H

V

K

D

E

A

I

S

S

T

E

G

G

D

D

G

G

P

G

V
x
Y

D
|
D

A

A

V

F

M

M

K

N

A

A

I

L

E

T

R

K

I

I

A

T

G

N

V

R

G

L

G

G

-

I

-

S

-

I

-

P

K

K

L
|
L

K

I

S

D

Y
|
Y

Q

E

I

V

K

R

A
x
I

L

P

T

P

A

G

G

G

K

K

-
x
T

D

D

A

A

Q

L

G
x
V

E

E

V

T

V

R

L

I

-

T

-

W

-

N

-

K

S

S

A

L

E

D

F

L

E

E

C

-

G

D

Y

Q

D

T

V

F

R

K

G

T

R

M

G

G

S

V

D

H

T
x
P

D

D

V
x
Q

V

T

V

V

A

A

S

A

A

V

K

H

A

A

Y

T

L

E

D

K

A

M

L

L

N

N

K

Q

R16 (= R14) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 14:15) binding pyruvate
D17 (= D15) 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 (≠ A72) 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 (≠ L74) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ F100) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ S140) 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 (= E142) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T172) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H302) mutation H->A,N: Loss of activity.
D304 (= D304) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ R310) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ T311) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ T312) mutation to A: Loss of activity.
Y430 (≠ V431) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (= D432) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L448) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y451) mutation to A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
I458 (≠ A455) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (vs. gap) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (≠ G464) mutation to A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
P493 (≠ T486) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
Q495 (≠ V488) mutation to 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: 4:375/519 of query aligns to 2:365/376 of O87198

query
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O87198

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R12 (= R14) binding 2-oxoglutarate
E13 (≠ D15) binding Mg(2+)
H72 (≠ N68) 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 (= D87) binding L-lysine
R133 (vs. gap) binding 2-oxoglutarate
S135 (= S140) binding L-lysine
T166 (= T172) binding 2-oxoglutarate; binding L-lysine
H195 (= H203) binding Mg(2+)
H197 (= H205) binding Mg(2+)

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
29% identity, 71% coverage: 8:375/519 of query aligns to 32:389/400 of 3ivtB

query
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3ivtB

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