SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing RR42_RS22445 FitnessBrowser__Cup4G11:RR42_RS22445 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)

P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
66% identity, 51% coverage: 9:298/568 of query aligns to 3:292/295 of P56839

query
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P56839

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D58 (= D64) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
D85 (= D91) mutation to A: Strongly reduces enzyme activity and increases KM.
D87 (= D93) mutation to A: Strongly reduces enzyme activity.
E114 (= E120) mutation to A: Strongly reduces enzyme activity.
N122 (= N128) mutation N->A,D: Strongly reduces enzyme activity.
R159 (= R165) mutation to A: Strongly reduces enzyme activity.
H190 (= H196) mutation to A: Strongly reduces enzyme activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
67% identity, 50% coverage: 13:298/568 of query aligns to 3:288/291 of 1pymA

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active site: W40 (= W50), S42 (= S52), G43 (= G53), L44 (= L54), D54 (= D64), D81 (= D91), D83 (= D93), C108 (= C118), E110 (= E120), K116 (= K126), N118 (= N128), S119 (= S129), R155 (= R165), H186 (= H196), V211 (= V221)
binding oxalate ion: W40 (= W50), S42 (= S52), G43 (= G53), L44 (= L54), D81 (= D91), R155 (= R165)

1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
67% identity, 50% coverage: 13:298/568 of query aligns to 3:288/291 of 1m1bA

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1m1bA

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active site: W40 (= W50), S42 (= S52), G43 (= G53), L44 (= L54), D54 (= D64), D81 (= D91), D83 (= D93), C108 (= C118), E110 (= E120), K116 (= K126), N118 (= N128), S119 (= S129), R155 (= R165), H186 (= H196), V211 (= V221)
binding magnesium ion: D81 (= D91), R155 (= R165)
binding sulfopyruvate: S42 (= S52), G43 (= G53), L44 (= L54), D81 (= D91), N118 (= N128), S119 (= S129), L120 (≠ F130), R155 (= R165)

5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
45% identity, 51% coverage: 14:300/568 of query aligns to 3:288/289 of 5uncA

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active site: W39 (= W50), S41 (= S52), G42 (= G53), L43 (= L54), D53 (= D64), D80 (= D91), D82 (= D93), T107 (≠ C118), E109 (= E120), K115 (= K126), N117 (= N128), S118 (= S129), R153 (= R165), H184 (= H196), V209 (= V221)
binding alpha-D-xylopyranose: H22 (= H33), N23 (= N34), G26 (≠ S37), L29 (≠ I40), G239 (≠ A251), V243 (≠ M255)

Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
41% identity, 51% coverage: 12:298/568 of query aligns to 2:289/290 of Q84G06

query
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Q84G06

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L

L

E

F

F

T

M

A

M

M

E

A

A

A

H

H

N

N

G

P

L

L

S

V

A

A

R

K

I

L

V

A

R

E

E

Q

A

A

G

G

F

F

K

G

A

G

I

I

W

W

A

G

S

S

G

G

L

F

A

E

I

L

S

S

A

A

Q

S

Y

Y

G

A

V

V

R

P

D

D

N

A

N

N

E

I

A

L

S

S

W

M

T

S

Q

T

V

H

V

L

D

E

T

M

L

M

E

R

F

A

M

I

A

A

D

S

A

T

S

V

D

S

L

I

P

P

I

L

L

I

L

A

D
|
D

G

I

D

D

T

T

G

G

Y

F

G

G

N

N

F

A

N

V

N

N

V

V

R

H

R

Y

L

V

V

V

R

P

K

Q

L

Y

E

E

Q

A

R

A

G

G

I

A

A

S

G

A

V

I

C

V

I

M

E

E

D

D

K

K

Q

T

F

F

P

P

K

K

T

D

N

T

S

S

F

L

I

R

D

T

G

D

E

G

R

R

Q

Q

P

E

L

L

A

V

E

R

I

I

D

E

E

E

F

F

C

Q

G

G

K

K

I

I

K

A

A

A

G

A

K

T

D

A

S

A

Q

R

S

A

D

D

D

R

N

D

F

F

S

V

I

V

V

I

A

A

R

R

V

V

E

E

A

A

L

L

I

I

A

A

G

G

W

L

G

G

M

Q

D

Q

E

E

A

A

L

V

R

R

A

G

E

Q

A

A

Y

Y

R

E

Q

E

A

A

G

G

A

A

D

D

A

A

I

I

L

L

I

I

H

H

S

S

K
x
R

L

Q

S

K

R

T

P

P

D

D

E

E

I

I

L

L

Q

A

F

F

A

V

R

K

E

S

W

W

A

P

G

G

R

K

G

V

P

P

L

L

V

V

I

L

V

V

P

P

T

T

K

A

Y

Y

-

P

-

Q

-

L

Y

T

S

E

T

A

P

D

T

I

E

A

A

A

F

L

R

S

K

K

A

V

G

G

I

I

S

-

V

-

V

V

I

I

W

Y

A

G

N

N

H

H

L

A

I

I

R

R

V

A

A

A

A

V

S

G

S

A

M

V

Q

R

A

E

V

V

A

F

K

A

E

R

I

I

H

R

D

R

S

D

E

G

T

G

L

I

V

R

N

E

V

V

E

D

D

A

R

A

I

L

A

P

T

S

V

V

N

K

E

E

I

I

F

I

R

E

L

L

Q

Q

D

G

A

D

D

E

E

R

Y

M

S

R

T

A

A

V

E

E

K

A

I

R

Y

Y

L

L

D81 (= D91) binding
R188 (≠ K198) mutation to A: Reduced affinity for substrate.

2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
40% identity, 51% coverage: 12:298/568 of query aligns to 2:282/283 of 2hjpA

query
sites
2hjpA

S

T

R

K

S

N

A

Q

R

A

L

L

R

R

Q

A

M

A

I

L

V

D

G

S

N

G

E

R

L

L

E

F

F

T

M

A

M

M

E

A

A

A

H

H

N

N

G

P

L

L

S

V

A

A

R

K

I

L

V

A

R
x
E

E

Q

A

A

G

G

F

F

K

G

A

G

I

I

W
|
W

A

G

S
|
S

G
|
G

L
x
F

A

E

I

L

S

S

A

A

Q

S

Y

Y

G

A

V

V

R

P

D
|
D

N

A

N

N

E

I

A

L

S

S

W

M

T

S

Q

T

V

H

V

L

D

E

T

M

L

M

E

R

F

A

M

I

A

A

D

S

A

T

S

V

D
x
S

L

I

P

P

I

L

L

I

L

A

D
|
D

G

I

D
|
D

T

T

G

G

Y

F

G

G

N

N

F

A

N

V

N

N

V

V

R

H

R

Y

L

V

V

V

R

P

K

Q

L

Y

E

E

Q

A

R

A

G

G

I

A

A

S

G

A

V

I

C
x
V

I

M

E
|
E

D

D

K

K

Q

T

F

F

P

P

K
|
K

T

-

N

-

S

-

F

-

I

-

D

-

G

-

E

D

R
x
T

Q

Q

P

E

L

L

A

V

E

R

I

I

D

E

E

E

F

F

C

Q

G

G

K

K

I

I

K

A

A

A

G

A

K

T

D

A

S

A

Q

R

S

A

D

D

D

R

N

D

F

F

S

V

I

V

V

I

A

A

R
|
R

V

V

E

E

A

A

L

L

I

I

A

A

G

G

W

L

G

G

M

Q

D

Q

E

E

A

A

L

V

R

R

A

G

E

Q

A

A

Y

Y

R

E

Q

E

A

A

G

G

A

A

D

D

A

A

I

I

L

L

I

I

H
|
H

S

S

K
x
R

L

Q

S

K

R

T

P

P

D

D

E

E

I

I

L

L

Q

A

F

F

A

V

R

K

E

S

W

W

A

P

G

G

R

K

G

V

P

P

L

L

V

V

I

L

V
|
V

P

P

T

T

K

A

Y

Y

-

P

-

Q

-

L

Y

T

S

E

T

A

P

D

T

I

E

A

A

A

F

L

R

S

K

K

A

V

G

G

I

I

S

-

V

-

V

V

I

I

W

Y

A

G

N

N

H

H

L

A

I

I

R

R

V

A

A

A

A

V

S

G

S

A

M

V

Q

R

A

E

V

V

A

F

K

A

E

R

I

I

H

R

D

R

S

D

E

G

T

G

L

I

V

R

N

E

V

V

E

D

D

A

R

A

I

L

A

P

T

S

V

V

N

K

E

E

I

I

F

I

R

E

L

L

Q

Q

D

G

A

D

D

E

E

R

Y

M

S

R

T

A

A

V

E

E

K

A

I

R

Y

Y

L

L

active site: W40 (= W50), S42 (= S52), G43 (= G53), F44 (≠ L54), D54 (= D64), D81 (= D91), D83 (= D93), V108 (≠ C118), E110 (= E120), K116 (= K126), T118 (≠ R135), R148 (= R165), H179 (= H196), V204 (= V221)
binding phosphonopyruvate: W40 (= W50), S42 (= S52), F44 (≠ L54), D81 (= D91), R148 (= R165), H179 (= H196), R181 (≠ K198)
binding alpha-D-xylopyranose: E32 (≠ R42), S75 (≠ D85)

2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
40% identity, 51% coverage: 12:298/568 of query aligns to 2:282/283 of 2duaA

query
sites
2duaA

S

T

R

K

S

N

A

Q

R

A

L

L

R

R

Q

A

M

A

I

L

V

D

G

S

N

G

E

R

L

L

E

F

F

T

M

A

M

M

E

A

A

A

H

H

N

N

G

P

L

L

S

V

A

A

R

K

I

L

V

A

R
x
E

E

Q

A

A

G

G

F

F

K

G

A

G

I

I

W
|
W

A

G

S
|
S

G
|
G

L
x
F

A

E

I

L

S

S

A

A

Q

S

Y

Y

G

A

V

V

R

P

D
|
D

N

A

N

N

E

I

A

L

S

S

W

M

T

S

Q

T

V

H

V

L

D

E

T

M

L

M

E

R

F

A

M

I

A

A

D

S

A

T

S

V

D
x
S

L

I

P

P

I

L

L

I

L

A

D
|
D

G

I

D
|
D

T

T

G

G

Y

F

G

G

N

N

F

A

N

V

N

N

V

V

R

H

R

Y

L

V

V

V

R

P

K

Q

L

Y

E

E

Q

A

R

A

G

G

I

A

A

S

G

A

V

I

C
x
V

I

M

E
|
E

D

D

K

K

Q

T

F

F

P

P

K
|
K

T

-

N

-

S

-

F

-

I

-

D

-

G

-

E

D

R
x
T

Q

Q

P

E

L

L

A

V

E

R

I

I

D

E

E

E

F

F

C

Q

G

G

K

K

I

I

K

A

A

A

G

A

K

T

D

A

S

A

Q

R

S

A

D

D

D

R

N

D

F

F

S

V

I

V

V

I

A

A

R
|
R

V

V

E

E

A

A

L

L

I

I

A

A

G

G

W

L

G

G

M

Q

D

Q

E

E

A

A

L

V

R

R

A

G

E

Q

A

A

Y

Y

R

E

Q

E

A

A

G

G

A

A

D

D

A

A

I

I

L

L

I

I

H
|
H

S

S

K

R

L

Q

S

K

R

T

P

P

D

D

E

E

I

I

L

L

Q

A

F

F

A

V

R

K

E

S

W

W

A

P

G

G

R

K

G

V

P

P

L

L

V

V

I

L

V
|
V

P

P

T

T

K

A

Y

Y

-

P

-

Q

-

L

Y

T

S

E

T

A

P

D

T

I

E

A

A

A

F

L

R

S

K

K

A

V

G

G

I

I

S

-

V

-

V

V

I

I

W

Y

A

G

N

N

H

H

L

A

I

I

R

R

V

A

A

A

A

V

S

G

S

A

M

V

Q

R

A

E

V

V

A

F

K

A

E

R

I

I

H

R

D

R

S

D

E

G

T

G

L

I

V

R

N

E

V

V

E

D

D

A

R

A

I

L

A

P

T

S

V

V

N

K

E

E

I

I

F

I

R

E

L

L

Q

Q

D

G

A

D

D

E

E

R

Y

M

S

R

T

A

A

V

E

E

K

A

I

R

Y

Y

L

L

active site: W40 (= W50), S42 (= S52), G43 (= G53), F44 (≠ L54), D54 (= D64), D81 (= D91), D83 (= D93), V108 (≠ C118), E110 (= E120), K116 (= K126), T118 (≠ R135), R148 (= R165), H179 (= H196), V204 (= V221)
binding oxalate ion: W40 (= W50), S42 (= S52), F44 (≠ L54), D81 (= D91), R148 (= R165)
binding alpha-D-xylopyranose: E32 (≠ R42), S75 (≠ D85)

P96074 Fosfomycin biosynthesis bifunctional protein Fom1; EC 2.7.7.104; EC 5.4.2.9 from Streptomyces wedmorensis (see paper)
34% identity, 44% coverage: 29:280/568 of query aligns to 162:432/435 of P96074

query
sites
P96074

M

I

M

L

E

E

A

V

H

H

N

N

G

G

L

L

S

T

A

G

R

L

I

I

V

I

R

E

E

N

A

S

G

K

-

V

-

T

-

V

-

D

-

N

-

Q

-

A

-

R

-

E

F

F

K

D

A

G

I

M

W

W

A

S

S

S

G

S

L

L

A

T

I

D

S

S

A

L

Q

A

Y

R

G

G

V

K

R

P

D

D

N

T

N

E

E

A

A

V

S

D

W

V

T

S

Q

S

V

R

V

L

D

Q

T

M

L

V

E

N

F

E

M

L

A

F

D

E

A

V

S

T

D

T

L

K

P

P

I

L

L

V

L

F

D

D

G

G

D

D

T

T

G

G

Y

-

G

G

N

K

F

P

N

E

N

H

V

F

R

G

R

F

L

T

V

V

R

R

K

S

L

L

E

E

Q

R

R

L

G

G

I

V

A

S

G

A

V

V

C

I

I

V

E

E

D

D

K

K

Q

E

F

G

P

L

K

K

T

R

N

N

S

S

F

L

I

F

D

G

G

T

E

D

-

V

R

P

Q

Q

P

T

L

Q

A

S

E

S

I

V

D

E

E

D

F

F

C

S

G

E

K

R

I

I

K

R

A

I

G

G

K

K

D

R

S

A

Q

Q

S

I

D

T

D

D

N

D

F

F

S

M

I

V

V

I

A

A

R

R

V

I

E

E

A

S

L

L

I

I

A

L

G

E

W

K

G

G

M

M

D

A

E

D

A

A

L

V

R

H

R

R

A

A

E

E

A

A

Y

Y

R

V

Q

D

A

A

G

G

A

A

D

D

A

G

I

I

L

M

I

I

H

H

S

S

K

R

L

Q

S

S

R

D

P

P

D

A

E

E

I

I

L

F

Q

E

F

F

A

C

R

R

-

Y

-

F

-

D

E

K

W

L

A

P

G

R

R

R

G

V

P

P

L

L

V

V

I

V

V

V

P

P

T

T

K

S

Y

Y

Y

S

S

S

T

V

P

R

T

E

E

S

A

E

F

L

R

A

K

D

A

A

G

G

I

V

S

N

V

M

V

V

I

I

W

Y

A

A

N

N

H

H

L

L

I

M

R

R

V

A

A

V

A

Y

S

P

S

Q

M

V

Q

T

A

K

V

V

A

V

K

Q

E

S

I

I

-

L

-

Q

-

H

-

G

-

R

-

A

H

H

D

E

S

A

E

E

T

S

-

M

L

L

V

A

N

S

V

I

E

K

D

D

R

A

I

L

A

S

T

I

V

I

N

P

E

E

Sites not aligning to the query:

11:12 binding
45:46 binding
77 binding
91:94 binding
100 binding
124:127 binding

4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
33% identity, 49% coverage: 16:292/568 of query aligns to 12:286/290 of 4iqdA

query
sites
4iqdA

R

R

L

F

R

R

Q

A

M

L

I

V

V

E

G

A

N

N

E

E

L

I

E

L

F

Q

M

I

M

P

E

G

A

A

H

H

N

D

G

A

L

M

S

A

A

A

R

L

I

V

V

A

R

R

E

N

A

T

G

G

F

F

K

L

A

A

I

L

W
x
Y

A

L

S
|
S

G
|
G

L
x
A

A

A

I

Y

S

T

A

A

Q

S

Y

K

G

G

V

L

R

P

D
|
D

N

L

N

G

E

I

A

V

S

T

W

S

T

T

Q

E

V

V

V

A

D
x
E

T
x
R

L

A

E

R

F
x
D

M

L

A

V

D

R

A

A

S

T

D

D

L

L

P

P

I

V

L

L

L

V

D
|
D

G

I

D
|
D

T

T

G

G

Y

F

G

G

N

G

F

V

N

L

N

N

V

V

R

A

R

R

L

T

V

A

R

V

K

E

L

M

E

V

Q

E

R

A

G

K

I

V

A

A

G

A

V

V

C
x
Q

I

I

E
|
E

D

D

K

Q

Q

Q

F

L

P

P

K
|
K

T

K

N
x
C

S
x
G

F
x
H

I

L

D

N

G

G

E

K

R

K

Q

-

P

-

L

L

A

V

E

T

I

T

D

E

E

E

F

L

C

V

G

Q

K

K

I

I

K

K

A

A

G

I

K

K

D

E

S

V

Q

A

S

P

D

-

N

S

F

L

S

Y

I

I

V

V

A

A

R
|
R

V

T

E

D

A

A

L

R

I

-

A

G

G

V

W

E

G
|
G

M
x
L

D

D

E

E

A

A

L

I

R

E

R

R

A

A

E

N

A

A

Y

Y

R

V

Q

K

A

A

G

G

A

A

D

D

A

A

I

I

L

F

I

P

H
x
E

S

A

K

-

L

L

S

Q

R

S

P

E

D

E

E

E

I

F

L

R

Q

L

F

F

A

N

R

S

E

K

W

V

A

-

G

-

R

N

G

A

P

P

L

L

V

L

I

A

V
x
N

P

M

T

T

K

E

Y

F

Y

G

S

K

T

T

P

P

-
x
Y

-

S

T

A

E

E

A

E

F

F

R

A

K

N

A

M

G

G

I

F

S

Q

V

M

V

V

I

I

W

Y

A

P

N

V

H

T

L

S

I

L

R

R

V

V

A

A

S

K

S

A

M

Y

Q

E

A

N

V

V

A

F

K

T

E

L

I

I

H

K

D

E

S

T

-

G

-

S

-

Q

-

K

E

D

T

A

L

L

V

S

N

N

V

M

E

Q

D

T

R

R

I

-

A

S

T

E

V

L

N

Y

E

E

I

T

F

I

R

S

L

Y

Q

H

D

D

A

F

D

E

E

E

Y

L

S

D

T

T

active site: Y46 (≠ W50), S48 (= S52), G49 (= G53), A50 (≠ L54), D60 (= D64), D87 (= D91), D89 (= D93), Q114 (≠ C118), E116 (= E120), K122 (= K126), C124 (≠ N128), G125 (≠ S129), H126 (≠ F130), R157 (= R165), E187 (≠ H196), N209 (≠ V221)
binding pyruvic acid: E71 (≠ D75), R72 (≠ T76), D75 (≠ F79), G165 (= G174), L166 (≠ M175), Y218 (vs. gap), Y219 (vs. gap)

P77541 2-methylisocitrate lyase; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 46% coverage: 34:296/568 of query aligns to 27:286/296 of P77541

query
sites
P77541

N

N

G

A

L

N

S

H

A

A

R

L

I

L

V

A

R

Q

E

R

A

A

G

G

F

Y

K

Q

A

A

I

I

W

Y

A

L

S
|
S

G
|
G

L
x
G

A

G

I

V

S

A

A

A

-

G

Q

S

Y

L

G

G

V

L

R

P

D

D

N

L

N

G

E

I

A

S

S

T

W

L

T

D

Q

D

V

V

V

L

D

T

T

D

L

I

E

R

F

R

M

I

A

T

D

D

A

V

S

C

D

S

L

L

P

P

I

L

L

L

L

V

D
|
D

G

A

D
|
D

T

I

G

G

Y

F

G

G

N

S

F

S

N

A

-

F

N

N

V

V

R

A

R

R

L

T

V

V

R

K

K

S

L

M

E

I

Q

K

R

A

G

G

I

A

A

A

G

G

V

L

C

H

I

I

E

E

D

D

K

Q

Q

V

F

G

P

A

K

K

T

R

N
x
C

S

-

F

-

I

-

D

-

G
|
G

E

H

R

R

-

P

-

N

Q

K

P

A

L

I

A

V

E

S

I

K

D

E

E

E

F

M

C

V

G

D

K

R

I

I

K

R

A

A

G

A

K

V

D

D

S

A

Q

K

S

T

D

D

D

P

N

D

F

F

S

V

I

I

V

M

A

A

R
|
R

V

T

E

D

A

A

L

L

I

-

A

A

G

V

W

E

G

G

M

L

D

D

E

A

A

A

L

I

R

E

R

R

A

A

E

Q

A

A

Y

Y

R

V

Q

E

A

A

G

G

A

A

D

E

A

M

I

L

L

F

I

-

H

-

S

-

K

-

L

-

S

-

R

-

P

P

D
x
E

E

A

I

I

L

T

Q

E

F

L

A

A

-

M

-

Y

R

R

E

Q

W

F

A

A

G

D

-

A

-

V

R

Q

G

V

P

P

L

I

V

L

I

A

V
x
N

P
x
I

T
|
T

K

E

Y

F

Y

G

S

A

T

T

P

P

-

L

-

F

-

T

T

T

E

D

A

E

F

L

R

R

K

S

A

A

G

H

I

V

S

A

V

M

V

A

I

L

W

Y

A

P

N

L

H

S

L

A

I

F

R
|
R

V

A

A

M

A

N

S

R

S

A

M

A

Q

E

A

H

V

V

A

Y

K

N

E

V

I

L

H

R

D

Q

S

E

E

G

T

T

L

Q

V

K

N

S

V

V

E

I

D

D

R

T

I

M

A

Q

T

T

V
x
R

N

N

E

E

I

L

F

Y

R

-

L

-

Q

E

D

S

A

I

D

N

E

Y

Y

Y

S

Q

T

Y

A

E

E

E

K

K

I

L

SGG 45:47 (≠ SGL 52:54) binding
D85 (= D91) binding
D87 (= D93) binding
C123 (≠ N128) mutation to S: Inactive.
C----G 123:124 (≠ NSFIDG 128:133) binding
R158 (= R165) binding
E188 (≠ D203) binding
NIT 210:212 (≠ VPT 221:223) binding
R241 (= R249) binding
R270 (≠ V278) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
28% identity, 46% coverage: 34:296/568 of query aligns to 25:284/289 of 1mumA

query
sites
1mumA

N

N

G

A

L

N

S

H

A

A

R

L

I

L

V

A

R

Q

E

R

A

A

G

G

F

Y

K

Q

A

A

I

I

W
x
Y

A

L

S
|
S

G
|
G

L
x
G

A

G

I

V

S

A

A

A

-

G

Q

S

Y

L

G

G

V

L

R

P

D
|
D

N

L

N

G

E

I

A

S

S

T

W

L

T

D

Q

D

V

V

V

L

D

T

T

D

L

I

E

R

F

R

M

I

A

T

D

D

A

V

S

C

D

S

L

L

P

P

I

L

L

L

L

V

D
|
D

G

A

D
|
D

T

I

G

G

Y

F

G

G

N

S

F

S

N

A

-

F

N

N

V

V

R

A

R

R

L

T

V

V

R

K

K

S

L

M

E

I

Q

K

R

A

G

G

I

A

A

A

G

G

V

L

C
x
H

I

I

E
|
E

D

D

K

Q

Q

V

F

G

P

A

K
|
K

T

R

N
x
C

S

-

F

-

I

-

D

-

G
|
G

E
x
H

R

R

-

P

-

N

Q

K

P

A

L

I

A

V

E

S

I

K

D

E

E

E

F

M

C

V

G

D

K

R

I

I

K

R

A

A

G

A

K

V

D

D

S

A

Q

K

S

T

D

D

D

P

N

D

F

F

S

V

I

I

V

M

A

A

R
|
R

V

T

E

D

A

A

L

L

I

-

A

A

G

V

W

E

G

G

M

L

D

D

E

A

A

A

L

I

R

E

R

R

A

A

E

Q

A

A

Y

Y

R

V

Q

E

A

A

G

G

A

A

D

E

A

M

I

L

L

F

I

-

H

-

S

-

K

-

L

-

S

-

R

-

P

P

D
x
E

E

A

I

I

L

T

Q

E

F

L

A

A

-

M

-

Y

R

R

E

Q

W

F

A

A

G

D

-

A

-

V

R

Q

G

V

P

P

L

I

V

L

I

A

V
x
N

P

I

T

T

K

E

Y

F

Y

G

S

A

T
|
T

P

P

-
x
L

-

F

-

T

T

T

E

D

A

E

F

L

R

R

K

S

A

A

G

H

I

V

S

A

V

M

V

A

I

L

W

Y

A

P

N

L

H

S

L

A

I

F

R

R

V

A

A

M

A

N

S

R

S

A

M

A

Q

E

A

H

V

V

A

Y

K

N

E

V

I

L

H

R

D

Q

S

E

E

G

T

T

L

Q

V

K

N

S

V

V

E

I

D

D

R

T

I

M

A

Q

T

T

V

R

N

N

E

E

I

L

F

Y

R

-

L

-

Q

E

D

S

A

I

D

N

E

Y

Y

Y

S

Q

T

Y

A

E

E

E

K

K

I

L

active site: Y41 (≠ W50), S43 (= S52), G44 (= G53), G45 (≠ L54), D56 (= D64), D83 (= D91), D85 (= D93), H111 (≠ C118), E113 (= E120), K119 (= K126), C121 (≠ N128), G122 (= G133), H123 (≠ E134), R156 (= R165), E186 (≠ D203), N208 (≠ V221), T215 (= T228), L217 (vs. gap)
binding magnesium ion: D56 (= D64), D85 (= D93)

Q56062 2-methylisocitrate lyase; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
29% identity, 47% coverage: 32:296/568 of query aligns to 25:286/295 of Q56062

query
sites
Q56062

A

A

H

I

N

N

G

A

L

N

S

H

A

A

R

L

I

L

V

A

R

Q

E

R

A

A

G

G

F

Y

K

Q

A

A

I

I

W

Y

A

L

S
|
S

G
|
G

L
x
G

A

G

I

V

S

A

A

A

-

G

Q

S

Y

L

G

G

V

L

R

P

D
|
D

N

L

N

G

E

I

A

S

S

T

W

L

T

D

Q

D

V

V

V

L

D

T

T

D

L

I

E

R

F

R

M

I

A

T

D

D

A

V

S

C

D

P

L

L

P

P

I

L

L

L

L

V

D
|
D

G

A

D

D

T

I

G

G

Y

F

G

G

N

S

F

S

N

A

-

F

N

N

V

V

R

A

R

R

L

T

V

V

R

K

K

S

L

I

E

A

Q

K

R

A

G

G

I

A

A

A

G

A

V

L

C

H

I

I

E

E

D

D

K

Q

Q

V

F

G

P

A

K
|
K

T
x
R

N
x
C

S

-

F

-

I

-

D

-

G

G

E
x
H

R

R

-

P

-

N

Q

K

P

A

L

I

A

V

E

S

I

K

D

E

E

E

F

M

C

V

G

D

K

R

I

I

K

R

A

A

G

A

K

V

D

D

S

A

Q

R

S

T

D

D

D

P

N

N

F

F

S

V

I

I

V

M

A

A

R
|
R

V

T

E

D

A

A

L

L

I

-

A

A

G

V

W

E

G

G

M

L

D

E

E

A

A

A

L

L

R

D

R

R

A

A

E

Q

A

A

Y

Y

R

V

Q

D

A

A

G

G

A

A

D

D

A

M

I

L

L

F

I

-

H

-

S

-

K

-

L

-

S

-

R

-

P

P

D

E

E

A

I

I

-

T

-

E

L

L

Q

S

F

M

A

Y

R

R

E

R

W

F

A

A

-

D

-

V

G

A

R

Q

G

V

P

P

L

I

V

L

I

A

V

N

P

I

T

T

K

E

Y

F

Y

G

S

A

T

T

P

P

-

L

-

F

-

T

T

T

E

D

A

E

F

L

R

R

K

S

A

A

G

H

I

V

S

A

V

M

V

A

I

L

W

Y

A

P

N

L

H

S

L

A

I

F

R

R

V

A

A

M

A

N

S

R

S

A

M

A

Q

E

A

K

V

V

A

Y

K

T

E

V

I

L

H

R

D

Q

S

E

E

G

T

T

L

Q

V

K

N

N

V

V

E

I

D

D

R

I

I

M

A

Q

T

T

V

R

N

N

E

E

I

L

F

Y

R

-

L

-

Q

E

D

S

A

I

D

N

E

Y

Y

Y

S

Q

T

F

A

E

E

E

K

K

I

L

SGG 45:47 (≠ SGL 52:54) binding
D58 (= D64) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
D85 (= D91) binding
K121 (= K126) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
R122 (≠ T127) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
C123 (≠ N128) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
H125 (≠ E134) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
R158 (= R165) binding

6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
31% identity, 44% coverage: 34:282/568 of query aligns to 25:261/277 of 6t4vC

query
sites
6t4vC

N

N

G

A

L

N

S

H

A

A

R

L

I

L

V

A

R

K

E

R

A

A

G

G

F

F

K

K

A

A

I

I

W
x
Y

A

L

S
|
S

G
|
G

L
x
G

A

G

I

V

S

A

A

A

-

G

Q

S

Y

L

G

G

V

L

R

P

D
|
D

N

L

N

G

E

I

A

S

S

G

W

L

T

D

Q

D

V

V

V

L

D

T

T

D

L

V

E

R

F

R

M

I

A

T

D

D

A

V

S

C

D

D

L

L

P

P

I

L

L

L

L

V

D
|
D

G

V

D
|
D

T

T

G

G

Y
x
F

G

G

N

S

F

S

N

A

-

F

N
|
N

V

V

R

A

R

R

L

T

V

V

R

K

K

S

L

M

E

I

Q

K

R

F

G

G

I

A

A

A

G

A

V

M

C
x
H

I

I

E
|
E

D

D

K

Q

Q

V

F

-

P

-

K

-

T

-

N

-

S

-

F

-

I

-

D

-

G

-

E

-

R

-

Q

-

P

E

L

I

A

V

E

S

I

Q

D

Q

E

E

F

M

C

V

G

D

K

R

I

I

K

K

A

A

G

A

K

V

D

D

S

A

Q

R

S

S

D

D

N

S

F

F

S

V

I

I

V

M

A

A

R
|
R

V

T

E

D

A

A

L

L

I

-

A

A

G

V

W

E

G

G

M

L

D

Q

E

A

A

A

L

I

R

D

R

R

A

A

E

C

A

A

Y

C

R

V

Q

E

A

A

G

G

A

A

D

D

A

M

I

I

L

F

I

-

H

-

S

-

K

-

L

-

S

-

R

-

P

P

D
x
E

E

A

I

M

L

T

Q

E

F

L

A

A

-

M

-

Y

R

K

E

E

W

F

A

A

G

A

-

A

-

V

R

K

G

V

P

P

L

V

V

L

I

A

V
x
N

P

I

T

T

K

E

Y

F

Y

G

S

A

T
|
T

P

P

-
x
L

-

F

-

T

T

T

E

D

A

E

F

L

R

A

K

S

A

A

G

D

I

V

S

S

V

L

V

V

I

L

W

Y

A

P

N

L

H

S

L

A

I

F

R

R

V

A

A

M

A

N

S

K

S

A

M

A

Q

E

A

N

V

V

A

Y

K

T

E

A

I

I

H

R

D

R

S

D

E

G

T

T

L

Q

V

K

N

N

V

V

E

I

D

D

R

T

I

M

A

Q

T

T

V

R

N

M

E

E

I

L

F

Y

active site: Y41 (≠ W50), S43 (= S52), G44 (= G53), G45 (≠ L54), D56 (= D64), D83 (= D91), D85 (= D93), H111 (≠ C118), E113 (= E120), R145 (= R165), E175 (≠ D203), N197 (≠ V221), T204 (= T228), L206 (vs. gap)
binding pyruvic acid: F88 (≠ Y96), N94 (= N101)

1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
28% identity, 47% coverage: 32:296/568 of query aligns to 21:271/271 of 1o5qA

query
sites
1o5qA

A

A

H

I

N

N

G

A

L

N

S

H

A

A

R

L

I

L

V

A

R

Q

E

R

A

A

G

G

F

Y

K

Q

A

A

I

I

W
x
Y

A

L

S
|
S

G
|
G

L
x
G

A

G

I

V

S

A

A

A

-

G

Q

S

Y

L

G

G

V

L

R

P

D
|
D

N

L

N

G

E

I

A

S

S

T

W

L

T

D

Q

D

V

V

V

L

D

T

T

D

L

I

E

R

F

R

M

I

A

T

D

D

A

V

S

C

D

P

L

L

P

P

I

L

L

L

L

V

D
|
D

G

A

D
|
D

T

I

G

G

Y

F

G

G

N

S

F

S

N

A

-

F

N

N

V

V

R

A

R

R

L

T

V

V

R

K

K

S

L

I

E

A

Q

K

R

A

G

G

I

A

A

A

G

A

V

L

C
x
H

I

I

E
|
E

D

D

K

Q

Q

-

F

-

P

-

K

-

T

-

N

-

S

-

F

-

I

-

D

-

G

-

E

-

R

-

Q

V

P

A

L

I

A

V

E

S

I

K

D

E

E

E

F

M

C

V

G

D

K

R

I

I

K

R

A

A

G

A

K

V

D

D

S

A

Q

R

S

T

D

D

D

P

N

N

F

F

S

V

I

I

V

M

A

A

R
|
R

V

T

E

D

A

A

L

L

I

-

A

A

G

V

W

E

G

G

M

L

D

E

E

A

A

A

L

L

R

D

R

R

A

A

E

Q

A

A

Y

Y

R

V

Q

D

A

A

G

G

A

A

D

D

A

M

I

L

L

F

I

-

H

-

S

-

K

-

L

-

S

-

R

-

P

P

D
x
E

E

A

I

I

-

T

-

E

L

L

Q

S

F

M

A

Y

R

R

E

R

W

F

A

A

-

D

-

V

G

A

R

Q

G

V

P

P

L

I

V

L

I

A

V
x
N

P

I

T

T

K

E

Y

F

Y

G

S

A

T
|
T

P

P

-
x
L

-

F

-

T

T

T

E

D

A

E

F

L

R

R

K

S

A

A

G

H

I

V

S

A

V

M

V

A

I

L

W

Y

A

P

N

L

H

S

L

A

I

F

R

R

V

A

A

M

A

N

S

R

S

A

M

A

Q

E

A

K

V

V

A

Y

K

T

E

V

I

L

H

R

D

Q

S

E

E

G

T

T

L

Q

V

K

N

N

V

V

E

I

D

D

R

I

I

M

A

Q

T

T

V

R

N

N

E

E

I

L

F

Y

R

-

L

-

Q

E

D

S

A

I

D

N

E

Y

Y

Y

S

Q

T

F

A

E

E

E

K

K

I

L

active site: Y39 (≠ W50), S41 (= S52), G42 (= G53), G43 (≠ L54), D54 (= D64), D81 (= D91), D83 (= D93), H109 (≠ C118), E111 (= E120), R143 (= R165), E173 (≠ D203), N195 (≠ V221), T202 (= T228), L204 (vs. gap)
binding pyruvic acid: Y39 (≠ W50), S41 (= S52), G43 (≠ L54), D81 (= D91), R143 (= R165)

Q05957 Petal death protein; (R)-2-methylmalate lyase; D-citramalate lyase; Oxalacetic hydrolase; PSR132; EC 3.7.1.1; EC 4.1.3.- from Dianthus caryophyllus (Carnation) (Clove pink) (see 2 papers)
29% identity, 48% coverage: 10:284/568 of query aligns to 24:297/318 of Q05957

query
sites
Q05957

T

S

A

T

S

G

R

R

S

K

A

T

R

T

L

M

R

H

Q

R

M

L

I

I

V

E

G

E

N

H

E

G

L

S

E

V

F

L

M

M

M

P

E

G

A

V

H

Q

N

D

G

A

L

L

S

S

A

A

R

A

I

V

V

V

R

E

E

K

A

T

G

G

F

F

K

H

A

A

I

A

W

F

A

V

S

S

G

G

L

Y

A

S

I

V

S

S

-

A

A

A

Q

M

Y

L

G

G

V

L

R

P

D
|
D

N

F

N

G

E

L

A

L

S

T

W

T

T

T

Q

E

V

V

D

E

-

A

T

T

L

R

E

R

F

I

M

T

A

A

D

A

A

A

S

P

D

N

L

L

P

C

I

V

L

V

D
|
D

G

G

D
|
D

T

T

G

G

Y

G

G

G

N

G

F

P

N

L

N

N

V

V

R

Q

R

R

L

F

V

I

R

R

K

E

L

L

E

I

Q

S

R

A

G

G

I

A

A

K

G

G

V

V

C

F

I

L

E

E

D

D

K

Q

Q

V

F

W

P

P

K
|
K

T

K

N
x
C

S

G

F

H

I

M

D

R

G

G

E

-

R

-

Q

K

P

A

L

V

A

V

E

P

I

A

D

E

E

E

F

H

C

A

G

L

K

K

I

I

K

A

A

A

G

A

K

R

D

E

S

A

Q

I

S

G

D

D

D

S

N

D

F

F

S

F

I

L

V

V

A

A

R

R

V

T

E

D

A

A

L

R

I

-

A

A

G

P

W

H

G

G

M

L

D

E

E

E

A

G

L

I

R

R

A

A

E

N

A

L

Y

Y

R

K

Q

E

A

A

G

G

A

A

D

D

A

A

I

T

L

F

I

V

H

E

S

A

K

P

L

-

S

A

R

N

P

V

D

D

E

E

I

L

L

K

Q

E

F

V

A

S

R

A

E

K

W

T

A

K

G

G

-

L

R

R

G

I

P

A

L

N

V

M

I

I

V

E

P

G

T

G

K

K

Y

T

Y

P

S

L

T

H

P

T

T

P

E

E

A

E

F

F

R

K

K

E

A

M

G

G

I

F

S

H

V

L

V

I

I

A

W

H

A

S

N

L

H

T

L

A

I

V

R

Y

V

A

A

T

A

A

S

R

S

A

M

L

Q

V

A

N

V

I

A

M

K

K

E

I

I

L

H

K

D

E

S

K

E

G

T

T

L

T

V

R

N

D

V

D

E

L

D

D

R

Q

I

M

A

A

T

T

V

F

N

S

E

E

I

F

F

N

R

E

L

L

D79 (= D64) mutation to A: Reduces catalytic efficiency 1000-fold.
D107 (= D91) binding
D109 (= D93) binding
K142 (= K126) binding
C144 (≠ N128) mutation to A: Loss of catalytic activity.

Sites not aligning to the query:

1:3 modified: propeptide, Removed in mature form

1zlpA Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
29% identity, 48% coverage: 28:297/568 of query aligns to 15:283/284 of 1zlpA

query
sites
1zlpA

F

L

M

M

M

P

E

G

A

V

H

Q

N

D

G

A

L

L

S

S

A

A

R

A

I

V

V

V

R

E

E

K

A

T

G

G

F

F

K

H

A

A

I

A

W
x
F

A

V

S
|
S

G
|
G

L
x
Y

A

S

I

V

S

S

-

A

A

A

Q

M

Y

L

G

G

V

L

R

P

D
|
D

N

F

N

G

E

L

A

L

S

T

W

T

T

T

Q

E

V

V

D

E

-

A

T

T

L

R

E

R

F

I

M

T

A

A

D

A

A

A

S

P

D

N

L

L

P

C

I

V

L

V

D
|
D

G

G

D
|
D

T

T

G

G

Y

G

G

G

N

G

F

P

N

L

N

N

V

V

R

Q

R

R

L

F

V

I

R

R

K

E

L

L

E

I

Q

S

R

A

G

G

I

A

A

K

G

G

V

V

C
x
F

I

L

E
|
E

D

D

K

Q

Q

V

F

W

P

P

K
|
K

T

K

N
x
C

S
x
G

F
x
H

I

M

D

R

G

G

E

-

R

-

Q

K

P

A

L

V

A

V

E

P

I

A

D

E

E

E

F

H

C

A

G

L

K

K

I

I

K

A

A

A

G

A

K

R

D

E

S

A

Q

I

S

G

D

D

D

S

N

D

F

F

S

F

I

L

V

V

A

A

R
|
R

V

T

E

D

A

A

L

R

I

-

A

A

G

P

W

H

G

G

M

L

D

E

E

E

A

G

L

I

R

R

A

A

E

N

A

L

Y

Y

R

K

Q

E

A

A

G

G

A

A

D

D

A

A

I

T

L

F

I

V

H
x
E

S

A

K

P

L

-

S

A

R

N

P

V

D

D

E

E

I

L

L

K

Q

E

F

V

A

S

R

A

E

K

W

T

A

K

G

G

-

L

R

R

G

I

P

A

L
x
N

V

M

I
|
I

V

E

P

G

T

G

K

K

Y
x
T

Y

P

S
x
L

T

H

P

T

T

P

E

E

A

E

F

F

R

K

K

E

A

M

G

G

I

F

S

H

V

L

V

I

I

A

W

H

A

S

N

L

H

T

L

A

I

V

R

Y

V

A

A

T

A

A

S

R

S

A

M

L

Q

V

A

N

V

I

A

M

K

K

E

I

I

L

H

K

D

E

S

K

E

G

T

T

L

T

V

R

N

D

V

D

E

L

D

D

R

Q

I

M

A

A

T

T

V

F

N

S

E

E

I

F

F

N

R

E

L

L

Q

I

D

S

A

L

D

E

E

S

Y

W

S

Y

T

E

A

M

E

E

K

S

I

K

Y

F

active site: F37 (≠ W50), S39 (= S52), G40 (= G53), Y41 (≠ L54), D52 (= D64), D80 (= D91), D82 (= D93), F107 (≠ C118), E109 (= E120), K115 (= K126), C117 (≠ N128), G118 (≠ S129), H119 (≠ F130), R152 (= R165), E182 (≠ H196), N204 (≠ L218), T211 (≠ Y225), L213 (≠ S227)
binding 5-hydroxypentanal: C117 (≠ N128), G118 (≠ S129), R152 (= R165), I206 (= I220)
binding magnesium ion: D80 (= D91), K115 (= K126)

1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct (see paper)
29% identity, 48% coverage: 28:297/568 of query aligns to 15:283/285 of 1zlpB

query
sites
1zlpB

F

L

M

M

M

P

E

G

A

V

H

Q

N

D

G

A

L

L

S

S

A

A

R

A

I

V

V

V

R

E

E

K

A

T

G

G

F

F

K

H

A

A

I

A

W
x
F

A

V

S
|
S

G
|
G

L
x
Y

A

S

I

V

S

S

-

A

A

A

Q

M

Y

L

G

G

V

L

R

P

D
|
D

N

F

N

G

E

L

A

L

S

T

W

T

T

T

Q

E

V

V

D

E

-

A

T

T

L

R

E

R

F

I

M

T

A

A

D

A

A

A

S

P

D

N

L

L

P

C

I

V

L

V

D
|
D

G

G

D
|
D

T

T

G

G

Y

G

G

G

N

G

F

P

N

L

N

N

V

V

R

Q

R

R

L

F

V

I

R

R

K

E

L

L

E

I

Q

S

R

A

G

G

I

A

A

K

G

G

V

V

C
x
F

I

L

E
|
E

D

D

K

Q

Q

V

F

W

P

P

K
|
K

T

K

N
x
C

S
x
G

F
x
H

I

M

D

R

G

G

E

-

R

-

Q

K

P

A

L

V

A

V

E

P

I

A

D

E

E

E

F

H

C

A

G

L

K

K

I

I

K

A

A

A

G

A

K

R

D

E

S

A

Q

I

S

G

D

D

D

S

N

D

F

F

S

F

I

L

V

V

A

A

R
|
R

V

T

E

D

A

A

L

R

I

-

A

A

G

P

W

H

G

G

M

L

D

E

E

E

A

G

L

I

R

R

A

A

E

N

A

L

Y

Y

R

K

Q

E

A

A

G

G

A

A

D

D

A

A

I

T

L

F

I

V

H
x
E

S

A

K

P

L

-

S

A

R

N

P

V

D

D

E

E

I

L

L

K

Q

E

F

V

A

S

R

A

E

K

W

T

A

K

G

G

-

L

R

R

G

I

P

A

L
x
N

V

M

I
|
I

V

E

P

G

T

G

K

K

Y
x
T

Y

P

S
x
L

T

H

P

T

T

P

E

E

A

E

F

F

R

K

K

E

A

M

G

G

I

F

S

H

V

L

V

I

I

A

W

H

A

S

N

L

H

T

L

A

I

V

R

Y

V

A

A

T

A

A

S

R

S

A

M

L

Q

V

A

N

V

I

A

M

K

K

E

I

I

L

H

K

D

E

S

K

E

G

T

T

L

T

V

R

N

D

V

D

E

L

D

D

R

Q

I

M

A

A

T

T

V

F

N

S

E

E

I

F

F

N

R

E

L

L

Q

I

D

S

A

L

D

E

E

S

Y

W

S

Y

T

E

A

M

E

E

K

S

I

K

Y

F

active site: F37 (≠ W50), S39 (= S52), G40 (= G53), Y41 (≠ L54), D52 (= D64), D80 (= D91), D82 (= D93), F107 (≠ C118), E109 (= E120), K115 (= K126), C117 (≠ N128), G118 (≠ S129), H119 (≠ F130), R152 (= R165), E182 (≠ H196), N204 (≠ L218), T211 (≠ Y225), L213 (≠ S227)
binding 5-hydroxypentanal: Y41 (≠ L54), C117 (≠ N128), R152 (= R165), I206 (= I220)

1jylA Catalytic mechanism of ctp:phosphocholine cytidylyltransferase from streptococcus pneumoniae (licc) (see paper)
37% identity, 21% coverage: 307:423/568 of query aligns to 5:124/228 of 1jylA

query
sites
1jylA

A

A

V

I

L
|
L

A
|
A

G
|
G

R

L

G

G

T

T

G

R

L

L

E

R

P

P

L

L

T

T

E

E

D

N

R

T

P

P

K

K

V

A

M

L

L

V

P

Q

V

V

A

N

G

Q

K

K

P

P

L

L

L

I

R

E

W

Y

L

Q

V

I

D

E

A

F

F

L

K

K

K

E

Q

K

S

G

I

I

N

N

D

D

I

I

T

I

V

I

G

V

G

G

Y

Y

Q

L

A

K

K

E

A

Q

I

F

D

D

-

Y

-

L

-

K

-

E

T

K

A

Y

G

G

I

V

K

R

L

L

V

V

V

F

N

N

E

D

Q

K

Y

Y

A

A

Q

D

T

Y

G
x
N

E
x
N

L

F

A

Y

S
|
S

L

L

A

Y

C

L

A

V

V

K

D

E

G

E

L

L

Q

A

T

N

D

S

T

Y

V

V

I

I

A

D

Y
x
A

G
x
D

D

N

L

Y

L

L

F

F

R

K

S

N

Y

M

I

F

L

R

R

N

D

D

L

L

L

T

E

R

S

S

D

-

A

T

P

Y

F

F

S

S

V

V

binding [2-cytidylate-o'-phosphonyloxyl]-ethyl-trimethyl-ammonium: L8 (= L310), A9 (= A311), A10 (= A312), G11 (= G313), N83 (≠ G381), N84 (≠ E382), S87 (= S385), A103 (≠ Y401), D104 (≠ G402)
binding magnesium ion: D104 (≠ G402)

Sites not aligning to the query:

3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
30% identity, 32% coverage: 15:195/568 of query aligns to 9:185/284 of 3b8iA

query
sites
3b8iA

A

A

R

M

L

F

R

R

Q

A

M

L

I

L

V

D

G

S

N

S

E

R

L

C

E

Y

F

H

M

T

M

A

E

S

A

V

H

F

N

D

G

P

L

M

S

S

A

A

R

R

I

I

V

A

R

A

E

D

A

L

G

G

F

F

K

E

A

C

I

G

W
x
I

A

L

S
x
G

G
|
G

L
x
S

A

V

I

A

S

S

A

L

Q

Q

-

V

Y

L

G

A

V

A

R

P

D
|
D

N

F

N

A

E

L

A

I

S

T

W

L

T

S

Q

E

V

F

V

V

D

E

T

Q

L

A

E

T

F

R

M

I

A

G

D

R

A

V

S

A

D

R

L

L

P

P

I

V

L

I

L

A

D
|
D

G

A

D
|
D

T

H

G

G

Y

Y

G

G

N

N

F

A

N

L

N

N

V

V

R

M

R

R

L

T

V

V

R

V

K

E

L

L

E

E

Q

R

R

A

G

G

I

I

A

A

G

A

V

L

C
x
T

I

I

E
|
E

D

D

K

T

Q

L

F

L

P

P

K
x
A

T

Q

N

-

S

-

F

-

I
x
F

D
x
G

G

R

E

K

R

S

Q

T

P

D

L

L

A

I

E

C

I

V

D

E

E

E

F

G

C

V

G

G

K

K

I

I

K

R

A

A

G

A

K

L

D

E

S

A

Q

R

S

V

D

D

D

P

N

A

F

L

S

T

I

I

V

I

A

A

R
|
R

V

T

E

N

A

A

L

E

I

L

A

-

G

-

W

I

G

D

M

V

D

D

E

A

A

V

L

I

R

Q

R

R

A

T

E

L

A

A

Y

Y

R

Q

Q

E

A

A

G

G

A

A

D

D

A

G

I

I

L

C

I

L

active site: I44 (≠ W50), G46 (≠ S52), G47 (= G53), S48 (≠ L54), D59 (= D64), D86 (= D91), D88 (= D93), T113 (≠ C118), E115 (= E120), A121 (≠ K126), F123 (≠ I131), G124 (≠ D132), R157 (= R165)
binding oxalate ion: S48 (≠ L54), D86 (= D91)

Sites not aligning to the query:

active site: 186, 206
binding oxalate ion: 233

Q9HUU1 Oxaloacetate decarboxylase; EC 4.1.1.112 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
32% identity, 28% coverage: 36:195/568 of query aligns to 32:187/287 of Q9HUU1

query
sites
Q9HUU1

L

M

S

S

A

A

R

R

I

I

V

A

R

A

E

D

A

L

G

G

F

F

K

E

A

C

I

G

W

I

A

L

S

G

G

G

L

S

A

V

I

A

S

S

A

L

Q

Q

-

V

Y

L

G

A

V

A

R

P

D

D

N

F

N

A

E

L

A

I

S

T

W

L

T

S

Q

E

V

F

V

V

D

E

T

Q

L

A

E

T

F

R

M

I

A

G

D

R

A

V

S

A

D

R

L

L

P

P

I

V

L

I

L

A

D
|
D

G

A

D

D

T

H

G

G

Y

Y

G

G

N

N

F

A

N

L

N

N

V

V

R

M

R

R

L

T

V

V

R

V

K

E

L

L

E

E

Q

R

R

A

G

G

I

I

A

A

G

A

V

L

C

T

I

I

E

E

D

D

K

T

Q

L

F

L

P

P

K

A

T

Q

N

-

S

-

F

-

I

F

D

G

G

R

E

K

R

S

Q

T

P

D

L

L

A

I

E

C

I

V

D

E

E

E

F

G

C

V

G

G

K

K

I

I

K

R

A

A

G

A

K

L

D

E

S

A

Q

R

S

V

D

D

D

P

N

A

F

L

S

T

I

I

V

I

A

A

R

R

V

T

E

N

A

A

L

E

I

L

A

-

G

-

W

I

G

D

M

V

D

D

E

A

A

V

L

I

R

Q

R

R

A

T

E

L

A

A

Y

Y

R

Q

Q

E

A

A

G

G

A

A

D

D

A

G

I

I

L

C

I

L

D88 (= D91) binding

Sites not aligning to the query:

212 Y→F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
235 H→A: 2-fold increase in substrate affinity and 15-fold decrease in activity.; H→Q: No change in substrate affinity and 3-fold decrease in activity.

Query Sequence

>RR42_RS22445 FitnessBrowser__Cup4G11:RR42_RS22445
MNAIDPIFSTASRSARLRQMIVGNELEFMMEAHNGLSARIVREAGFKAIWASGLAISAQY
GVRDNNEASWTQVVDTLEFMADASDLPILLDGDTGYGNFNNVRRLVRKLEQRGIAGVCIE
DKQFPKTNSFIDGERQPLAEIDEFCGKIKAGKDSQSDDNFSIVARVEALIAGWGMDEALR
RAEAYRQAGADAILIHSKLSRPDEILQFAREWAGRGPLVIVPTKYYSTPTEAFRKAGISV
VIWANHLIRVAASSMQAVAKEIHDSETLVNVEDRIATVNEIFRLQDADEYSTAEKIYLSG
SQAPGAAVVLAAGRGTGLEPLTEDRPKVMLPVAGKPLLRWLVDAFKKQSINDITVVGGYQ
AKAIDTAGIKLVVNEQYAQTGELASLACAVDGLQTDTVIAYGDLLFRSYILRDLLESDAP
FSVVVDSSLTTESNQSVRDFAYCSAPDDRDLFGQKILLRHVSSKGQEPGAGQAQAPHGRW
IGLLNVRGEGRVRLQKLVAELRKRDDFNTLDMPALLNALVEAGEQIEVKYVHGHWRGVND
LDDFRRAGDFAHTQTPFAVGGTDAEEAR

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