SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Pf1N1B4_5858 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5858 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)

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)
78% identity, 100% coverage: 1:289/289 of query aligns to 1:287/287 of Q9HUU1

query
sites
Q9HUU1

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D88 (= D88) binding
Y212 (= Y212) mutation to F: 25-fold increase in substrate affinity and 23-fold decrease in activity.
H235 (= H235) mutation to A: 2-fold increase in substrate affinity and 15-fold decrease in activity.; mutation to Q: No change in substrate affinity and 3-fold decrease in activity.

3b8iA Crystal structure of oxaloacetate decarboxylase from pseudomonas aeruginosa (pa4872) in complex with oxalate and mg2+. (see paper)
78% identity, 99% coverage: 3:288/289 of query aligns to 1:284/284 of 3b8iA

query
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3b8iA

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active site: I44 (= I46), G46 (= G48), G47 (= G49), S48 (= S50), D59 (= D61), D86 (= D88), D88 (= D90), T113 (= T115), E115 (= E117), A121 (= A123), F123 (= F125), G124 (= G126), R157 (= R159), V186 (= V188), M206 (= M208)
binding oxalate ion: S48 (= S50), D86 (= D88), H233 (= H235)

4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
33% identity, 79% coverage: 5:232/289 of query aligns to 5:233/290 of 4iqdA

query
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4iqdA

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active site: Y46 (≠ I46), S48 (≠ G48), G49 (= G49), A50 (≠ S50), D60 (= D61), D87 (= D88), D89 (= D90), Q114 (≠ T115), E116 (= E117), K122 (≠ A123), C124 (≠ F125), G125 (= G126), H126 (≠ R127), R157 (= R159), E187 (≠ V188), N209 (vs. gap)
binding pyruvic acid: E71 (= E72), R72 (≠ Q73), D75 (≠ R76), G165 (≠ P166), L166 (≠ V167), Y218 (≠ L217), Y219 (≠ R218)

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)
31% identity, 72% coverage: 13:220/289 of query aligns to 10:223/295 of Q56062

query
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Q56062

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SGG 45:47 (≠ GGS 48:50) binding
D58 (= D61) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
D85 (= D88) binding
K121 (≠ A123) mutation to A: 1000-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
R122 (≠ Q124) mutation to K: 2-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
C123 (≠ F125) mutation to A: Inactive. Retains the same oligomeric state of the wild-type.
H125 (vs. gap) mutation to A: 750-fold decrease in the catalytic efficiency. Retains the same oligomeric state of the wild-type.
R158 (= R159) binding

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)
30% identity, 73% coverage: 11:220/289 of query aligns to 8:223/296 of P77541

query
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P77541

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R

K

V

T

D

D

S

P

E

D

M

F

A

V

I

I

I

M

A

A

R
|
R

T

T

N

D

A

A

-

L

G

A

I

V

L

E

P

G

V

L

Q

D

E

A

I

A

I

I

S

E

R

R

T

A

K

Q

Q

A

Y

Y

Q

V

Q

E

A

A

G

G

A

A

D

E

G

M

I

L

C

F

M

P

V
x
E

G

A

V

I

R

T

D

E

F

L

D

A

H

M

L

Y

E

R

Q

Q

I

F

A

A

E

D

H

A

L

V

S

Q

V

V

P

P

L

I

M

L

-

A

-
x
N

L
x
I

V
x
T

T

E

Y

F

G

G

-

A

N

T

P

P

L

L

L

F

R

T

D

T

D

D

SGG 45:47 (≠ GGS 48:50) binding
D85 (= D88) binding
D87 (= D90) binding
C123 (≠ F125) mutation to S: Inactive.
CG 123:124 (≠ FG 125:126) binding
R158 (= R159) binding
E188 (≠ V188) binding
NIT 210:212 (≠ -LV 209:210) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
241 binding
270 binding

1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli (see paper)
30% identity, 73% coverage: 11:220/289 of query aligns to 6:221/289 of 1mumA

query
sites
1mumA

R

K

N

A

F

F

R

R

Q

A

L

A

F

L

A

T

S

K

N

E

A

N

C

P

Y

L

H

Q

T

I

A

V

S

G

V

T

F

I

D

N

P

A

M

N

S

H

A

A

R

L

I

L

A

A

A

Q

D

R

L

A

G

G

F

Y

E

Q

V

A

G

I

I
x
Y

L

L

G
x
S

G
|
G

S
x
G

V

G

A

V

S

A

L

A

Q

G

V

S

L

L

G

G

A

L

P

P

D
|
D

F

L

A

G

L

I

I

S

T

T

L

L

S

D

E

D

F

V

A

L

E

T

Q

D

A

I

T

R

R

R

I

I

G

T

R

D

V

V

A

C

Q

S

L

L

P

P

V

L

I

L

A

V

D
|
D

A

A

D
|
D

H

I

G

G

Y

F

G

G

-

S

N

S

A

A

L

F

N

N

V

V

M

A

R

R

T

T

I

V

V

K

E

S

L

M

E

I

R

K

A

A

G

G

V

A

A

A

A

G

L

L

T
x
H

I

I

E
|
E

D

D

T

Q

L

V

L

G

P

A

A
x
K

Q

R

F
x
C

G
|
G

-
x
H

R

R

K

P

S

N

T

K

D

A

L

I

I

V

T

S

V

K

A

E

E

E

G

M

V

V

G

D

K

R

I

I

R

R

A

A

L

V

E

D

A

A

R

K

V

T

D

D

S

P

E

D

M

F

A

V

I

I

I

M

A

A

R
|
R

T

T

N

D

A

A

-

L

G

A

I

V

L

E

P

G

V

L

Q

D

E

A

I

A

I

I

S

E

R

R

T

A

K

Q

Q

A

Y

Y

Q

V

Q

E

A

A

G

G

A

A

D

E

G

M

I

L

C

F

M

P

V
x
E

G

A

V

I

R

T

D

E

F

L

D

A

H

M

L

Y

E

R

Q

Q

I

F

A

A

E

D

H

A

L

V

S

Q

V

V

P

P

L

I

M

L

-

A

-
x
N

L

I

V

T

T

E

Y

F

G

G

-

A

N
x
T

P

P

L
|
L

L

F

R

T

D

T

D

D

active site: Y41 (≠ I46), S43 (≠ G48), G44 (= G49), G45 (≠ S50), D56 (= D61), D83 (= D88), D85 (= D90), H111 (≠ T115), E113 (= E117), K119 (≠ A123), C121 (≠ F125), G122 (= G126), H123 (vs. gap), R156 (= R159), E186 (≠ V188), N208 (vs. gap), T215 (≠ N214), L217 (= L216)
binding magnesium ion: D56 (= D61), D85 (= D90)

5uncA The crystal structure of phosphoenolpyruvate phosphomutase from streptomyces platensis subsp. Rosaceus
36% identity, 52% coverage: 12:162/289 of query aligns to 5:156/289 of 5uncA

query
sites
5uncA

N

Q

F

L

R

R

Q

A

L

L

F

F

A

D

S

A

N

P

A

G

C

T

Y

V

H

R

T

I

A

A

S

G

V

A

F
x
H

D
x
N

P

P

M

L

S
x
G

A

A

R

R

I
x
L

A

A

A

E

D

R

L

A

G

G

F

F

E

D

V

-

G

G

I

I

L
x
W

G

S

G
x
S

S
x
G

V
x
L

A

E

S

I

L

S

Q

A

V

S

L

Q

G

G

A

L

P

P

D
|
D

F

A

A

D

L

I

I

L

T

T

L

M

S

T

E

E

F

L

A

L

E

G

Q

V

A

A

T

G

R

S

I

M

G

A

R

S

V

A

A

V

Q

G

L

V

P

P

V

V

I

V

A

A

D
|
D

A

C

D
|
D

H

T

G

G

Y

Y

G

G

N

N

A

A

L

N

N

N

V

V

M

M

R

H

T

M

I

V

V

R

E

R

L

Y

E

E

R

A

A

A

G

G

V

I

A

A

L

V

T
|
T

I

I

E
|
E

D

D

T

K

L

R

L

F

P

P

A
x
K

-

V

-
x
N

Q
x
S

F

F

G

I

R

P

K

G

S

R

T

Q

D

E

L

L

I

A

T

S

V

V

A

P

E

E

G

F

V

C

G

G

K

R

I

I

R

E

A

A

L

K

E

D

A

A

R

Q

V

R

D

D

S

P

E

D

M

F

A

M

I

V

I

I

A

A

R
|
R

T

I

N

E

A

A

active site: W39 (≠ L47), S41 (≠ G49), G42 (≠ S50), L43 (≠ V51), D53 (= D61), D80 (= D88), D82 (= D90), T107 (= T115), E109 (= E117), K115 (≠ A123), N117 (vs. gap), S118 (≠ Q124), R153 (= R159)
binding alpha-D-xylopyranose: H22 (≠ F29), N23 (≠ D30), G26 (≠ S33), L29 (≠ I36)

Sites not aligning to the query:

active site: 184, 209
binding alpha-D-xylopyranose: 239, 243

3fa4A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form (see paper)
32% identity, 79% coverage: 28:254/289 of query aligns to 25:252/284 of 3fa4A

query
sites
3fa4A

V

V

F

Y

D

D

P

G

M

L

S

S

A

A

R

R

I

V

A

A

A

L

D

S

L

A

G

G

F

F

E

D

V

A

G

L

I
x
Y

L

M

G
x
T

G
|
G

S
x
A

V

G

A

T

S

A

L

A

Q

S

V

V

L

H

G

G

A

Q

P

A

D
|
D

F

L

A

G

L

I

I

C

T

T

L

L

S

N

E

D

F

M

A

R

E

A

Q

N

A

A

T

E

R

M

I

I

G

S

R

N

V

I

A

S

-

P

Q

S

L

T

P

P

V

V

I

I

A

A

D
|
D

A

A

D
|
D

H

T

G

G

Y

Y

G

G

N

G

A

P

L

I

N

M

V

V

M

A

R

R

T

T

I

T

V

E

E

Q

L

Y

E

S

R

R

A

S

G

G

V

V

A

A

L

F

T
x
H

I

I

E
|
E

D

D

T

Q

L

V

L

-

P

-

A

-

Q

Q

F

T

G

G

R

K

K

I

S

L

T

V

D

D

L

T

I

D

T

T

V

Y

A

-

E

-

G

-

V

V

G

T

K

R

I

I

R

R

A

A

L

V

E

Q

A

A

-

R

-

Q

R

R

V

I

D

G

S

S

E

D

M

I

A

V

I

V

I

I

A

A

R
|
R

T

T

N

D

A

S

-

L

G

Q

I

T

L

H

P

G

V

Y

Q

E

E

E

I

S

I

V

S

A

R

R

T

L

K

R

Q

A

Y

A

Q

R

Q

D

A

A

G

G

A

A

D

D

G

V

I

G

C

F

M

L

V
x
E

G

G

V

I

R

T

D

S

F

R

D

E

H

M

L

A

E

R

Q

Q

I

V

A

I

E

Q

H

D

L

L

S

A

-

G

V

W

P

P

L

L

M

L

L

L

-
x
N

-

M

V

V

T

E

Y

H

G

G

N

A

P
x
T

L

P

L
x
S

R

I

D

S

D

A

N

A

R

E

L

A

A

K

E

E

L

M

G

G

V

F

R

R

V

I

T

I

I

I

D

F

G

P

H

F

G

A

A

A

Y

L

F

G

A

P

A

A

I

V

K

A

A

A

T

M

Y

R

D

E

S

A

L

M

R

E

E

K

Q

L

R

K

Q

R

active site: Y43 (≠ I46), T45 (≠ G48), G46 (= G49), A47 (≠ S50), D58 (= D61), D86 (= D88), D88 (= D90), H113 (≠ T115), E115 (= E117), R153 (= R159), E183 (≠ V188), N206 (vs. gap), T213 (≠ P215), S215 (≠ L217)
binding magnesium ion: D86 (= D88), D88 (= D90)

3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
31% identity, 78% coverage: 28:251/289 of query aligns to 25:252/302 of 3fa3B

query
sites
3fa3B

V

V

F

Y

D

D

P

G

M

L

S

S

A

A

R

R

I

V

A

A

A

L

D

S

L

A

G

G

F

F

E

D

V

A

G

L

I
x
Y

L

M

G
x
T

G
|
G

S
x
A

V

G

A

T

S

A

L

A

Q

S

V

V

L

H

G

G

A

Q

P

A

D
|
D

F

L

A

G

L

I

I

C

T

T

L

L

S

N

E

D

F

M

A

R

E

A

Q

N

A

A

T

E

R

M

I

I

G

S

R

N

V

I

A

S

-

P

Q

S

L

T

P

P

V

V

I

I

A

A

D
|
D

A

A

D
|
D

H

T

G

G

Y

Y

G

G

N

G

A

P

L

I

N

M

V

V

M

A

R

R

T

T

I

T

V

E

E

Q

L

Y

E

S

R

R

A

S

G

G

V

V

A

A

L

F

T
x
H

I

I

E
|
E

D

D

T

Q

L

V

L

Q

P

T

A
x
K

Q

R

F
x
C

G
|
G

R
x
H

K

L

S

A

T

G

D

K

L

I

I

L

T

V

V

D

A

T

E

D

G

T

-

Y

V

V

G

T

K

R

I

I

R

R

A

A

L

V

E

Q

A

A

-

R

-

Q

R

R

V

I

D

G

S

S

E

D

M

I

A

V

I

V

I

I

A

A

R
|
R

T

T

N

D

A

S

-

L

G

Q

I

T

L

H

P

G

V

Y

Q

E

E

E

I

S

I

V

S

A

R

R

T

L

K

R

Q

A

Y

A

Q

R

Q

D

A

A

G

G

A

A

D

D

G

V

I

G

C

F

M

L

V
x
E

G

G

V

I

R

T

D

S

F

R

D

E

H

M

L

A

E

R

Q

Q

I

V

A

I

E

Q

H

D

L

L

S

A

-

G

V

W

P

P

L

L

M

L

L

L

-
x
N

-

M

V

V

T

E

Y

H

G

G

N

A

P
x
T

L

P

L
x
S

R

I

D

S

D

A

N

A

R

E

L

A

A

K

E

E

L

M

G

G

V

F

R

R

V

I

T

I

I

I

D

-

G

-

H

-

G

-

A

F

Y
x
P

F

F

A

A

I

L

K

G

A

P

T

A

Y

V

D

A

S

A

L

M

R

R

E

E

active site: Y43 (≠ I46), T45 (≠ G48), G46 (= G49), A47 (≠ S50), D58 (= D61), D86 (= D88), D88 (= D90), H113 (≠ T115), E115 (= E117), K121 (≠ A123), C123 (≠ F125), G124 (= G126), H125 (≠ R127), R160 (= R159), E190 (≠ V188), N213 (vs. gap), T220 (≠ P215), S222 (≠ L217)
binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y43 (≠ I46), T45 (≠ G48), G46 (= G49), A47 (≠ S50), D86 (= D88), G124 (= G126), R160 (= R159), E190 (≠ V188), N213 (vs. gap), P239 (≠ Y238)

2hjpA Crystal structure of phosphonopyruvate hydrolase complex with phosphonopyruvate and mg++ (see paper)
31% identity, 85% coverage: 13:258/289 of query aligns to 7:245/283 of 2hjpA

query
sites
2hjpA

F

L

R

R

Q

A

L

A

F

L

A

D

S

S

N

G

A

R

C

L

Y

F

H

T

T

A

A

M

S

A

V

A

F

H

D

N

P

P

M

L

S

V

A

A

R

K

I

L

A

A

A
x
E

D

Q

L

A

G

G

F

F

E

G

V

-

G

G

I

I

L
x
W

G

G

G
x
S

S
x
G

V
x
F

A

E

S

L

L

S

Q

A

V

S

L

Y

G

A

A

V

P

P

D
|
D

F

A

A

N

L

I

I

L

T

S

L

M

S

S

E

T

F

H

A

L

E

E

Q

M

A

M

T

R

R

A

I

I

G

A

R

S

V

T

A

V

Q
x
S

L

I

P

P

V

L

I

I

A

A

D
|
D

A

I

D
|
D

H

T

G

G

Y

F

G

G

N

N

A

A

L

V

N

N

V

V

M

H

R

Y

T

V

I

V

V

P

E

Q

L

Y

E

E

R

A

A

A

G

G

V

A

A

S

A

A

L

I

T
x
V

I

M

E
|
E

D

D

T

K

L

T

L

F

P

P

A

-

Q

-

F

-

G

-

R
x
K

K

D

S
x
T

T

Q

D

E

L

L

I

V

T

R

V

I

A

E

E

E

G

F

V

Q

G

G

K

K

I

I

R

A

A

A

L

T

E

A

A

A

R

R

V

A

D

D

S

R

E

D

M

F

A

V

I

V

I

I

A

A

R
|
R

T

V

N

E

A

A

G

L

I

I

-

A

-

G

L

L

P

G

V

Q

Q

Q

E

E

I

A

I

V

S

R

R

R

T

G

K

Q

Q

A

Y

Y

Q

E

A

A

G

G

A

A

D

D

G

A

I

I

C

-

M

L

V

I

G
x
H

V

S

R
|
R

D

Q

F

K

D

T

H

P

L

D

E

E

Q

I

I

L

A

A

E

F

H

V

L

K

S

S

-

W

-

P

-

G

-

K

V

V

P

P

L

L

M

V

L

L

V
|
V

T

P

Y

T

G

A

N

Y

P

P

L

Q

L

L

R

T

D

E

D

A

N

D

R

I

L

A

A

A

E

L

L

S

G

K

V

V

R

G

V

I

T

V

I

I

D

Y

G

G

H

N

G

H

A

A

Y

I

F

R

A

A

I

V

K

G

A

A

T

V

Y

-

D

-

S

-

L

-

R

-

E

-

Q

-

R

R

Q

E

I

V

F

F

T

A

Q

R

active site: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), F44 (≠ V51), D54 (= D61), D81 (= D88), D83 (= D90), V108 (≠ T115), E110 (= E117), K116 (≠ R127), T118 (≠ S129), R148 (= R159), H179 (≠ G189), V204 (= V210)
binding phosphonopyruvate: W40 (≠ L47), S42 (≠ G49), F44 (≠ V51), D81 (= D88), R148 (= R159), H179 (≠ G189), R181 (= R191)
binding alpha-D-xylopyranose: E32 (≠ A38), S75 (≠ Q82)

2duaA Crystal structure of phosphonopyruvate hydrolase complex with oxalate and mg++ (see paper)
31% identity, 85% coverage: 13:258/289 of query aligns to 7:245/283 of 2duaA

query
sites
2duaA

F

L

R

R

Q

A

L

A

F

L

A

D

S

S

N

G

A

R

C

L

Y

F

H

T

T

A

A

M

S

A

V

A

F

H

D

N

P

P

M

L

S

V

A

A

R

K

I

L

A

A

A
x
E

D

Q

L

A

G

G

F

F

E

G

V

-

G

G

I

I

L
x
W

G

G

G
x
S

S
x
G

V
x
F

A

E

S

L

L

S

Q

A

V

S

L

Y

G

A

A

V

P

P

D
|
D

F

A

A

N

L

I

I

L

T

S

L

M

S

S

E

T

F

H

A

L

E

E

Q

M

A

M

T

R

R

A

I

I

G

A

R

S

V

T

A

V

Q
x
S

L

I

P

P

V

L

I

I

A

A

D
|
D

A

I

D
|
D

H

T

G

G

Y

F

G

G

N

N

A

A

L

V

N

N

V

V

M

H

R

Y

T

V

I

V

V

P

E

Q

L

Y

E

E

R

A

A

A

G

G

V

A

A

S

A

A

L

I

T
x
V

I

M

E
|
E

D

D

T

K

L

T

L

F

P

P

A

-

Q

-

F

-

G

-

R
x
K

K

D

S
x
T

T

Q

D

E

L

L

I

V

T

R

V

I

A

E

E

E

G

F

V

Q

G

G

K

K

I

I

R

A

A

A

L

T

E

A

A

A

R

R

V

A

D

D

S

R

E

D

M

F

A

V

I

V

I

I

A

A

R
|
R

T

V

N

E

A

A

G

L

I

I

-

A

-

G

L

L

P

G

V

Q

Q

Q

E

E

I

A

I

V

S

R

R

R

T

G

K

Q

Q

A

Y

Y

Q

E

A

A

G

G

A

A

D

D

G

A

I

I

C

-

M

L

V

I

G
x
H

V

S

R

R

D

Q

F

K

D

T

H

P

L

D

E

E

Q

I

I

L

A

A

E

F

H

V

L

K

S

S

-

W

-

P

-

G

-

K

V

V

P

P

L

L

M

V

L

L

V
|
V

T

P

Y

T

G

A

N

Y

P

P

L

Q

L

L

R

T

D

E

D

A

N

D

R

I

L

A

A

A

E

L

L

S

G

K

V

V

R

G

V

I

T

V

I

I

D

Y

G

G

H

N

G

H

A

A

Y

I

F

R

A

A

I

V

K

G

A

A

T

V

Y

-

D

-

S

-

L

-

R

-

E

-

Q

-

R

R

Q

E

I

V

F

F

T

A

Q

R

active site: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), F44 (≠ V51), D54 (= D61), D81 (= D88), D83 (= D90), V108 (≠ T115), E110 (= E117), K116 (≠ R127), T118 (≠ S129), R148 (= R159), H179 (≠ G189), V204 (= V210)
binding oxalate ion: W40 (≠ L47), S42 (≠ G49), F44 (≠ V51), D81 (= D88), R148 (= R159)
binding alpha-D-xylopyranose: E32 (≠ A38), S75 (≠ Q82)

3fa3J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form (see paper)
32% identity, 78% coverage: 28:251/289 of query aligns to 24:243/292 of 3fa3J

query
sites
3fa3J

V

V

F

Y

D

D

P

G

M

L

S

S

A

A

R

R

I

V

A

A

A

L

D

S

L

A

G

G

F

F

E

D

V

A

G

L

I
x
Y

L

M

G
x
T

G
|
G

S
x
A

V

G

A

T

S

A

L

A

Q

S

V

V

L

H

G

G

A

Q

P

A

D
|
D

F

L

A

G

L

I

I

C

T

T

L

L

S

N

E

D

F

M

A

R

E

A

Q

N

A

A

T

E

R

M

I

I

G

S

R

N

V

I

A

S

-

P

Q

S

L

T

P

P

V

V

I

I

A

A

D
|
D

A

A

D
|
D

H

T

G

G

Y

Y

G

G

N

G

A

P

L

I

N

M

V

V

M

A

R

R

T

T

I

T

V

E

E

Q

L

Y

E

S

R

R

A

S

G

G

V

V

A

A

L

F

T
x
H

I

I

E
|
E

D

D

T

Q

L

V

L

-

P

-

A

-

Q

-

F

-

G

-

R

-

K

Q

S

T

T

K

D

I

L

L

I

V

T

D

V

T

A

D

E

T

G

Y

V

V

G

T

K

R

I

I

R

R

A

A

L

V

E

Q

A

A

-

R

-

Q

R

R

V

I

D

G

S

S

E

D

M

I

A

V

I

V

I

I

A

A

R
|
R

T

T

N

D

A

S

-

L

G

Q

I

T

L

H

P

G

V

Y

Q

E

E

E

I

S

I

V

S

A

R

R

T

L

K

R

Q

A

Y

A

Q

R

Q

D

A

A

G

G

A

A

D

D

G

V

I

G

C

F

M

L

V
x
E

G

G

V

I

R

T

D

S

F

R

D

E

H

M

L

A

E

R

Q

Q

I

V

A

I

E

Q

H

D

L

L

S

A

-

G

V

W

P

P

L

L

M

L

L

L

-
x
N

-

M

V

V

T

E

Y

H

G

G

N

A

P
x
T

L

P

L
x
S

R

I

D

S

D

A

N

A

R

E

L

A

A

K

E

E

L

M

G

G

V

F

R

R

V

I

T

I

I

I

D

-

G

-

H

-

G

-

A

F

Y

P

F

F

A

A

I

L

K

G

A

P

T

A

Y

V

D

A

S

A

L

M

R

R

E

E

active site: Y42 (≠ I46), T44 (≠ G48), G45 (= G49), A46 (≠ S50), D57 (= D61), D85 (= D88), D87 (= D90), H112 (≠ T115), E114 (= E117), R151 (= R159), E181 (≠ V188), N204 (vs. gap), T211 (≠ P215), S213 (≠ L217)
binding manganese (ii) ion: D85 (= D88), D87 (= D90)

1o5qA Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium (see paper)
30% identity, 72% coverage: 13:220/289 of query aligns to 6:208/271 of 1o5qA

query
sites
1o5qA

F

F

R

R

Q

A

L

A

F

L

A

A

S

K

N

E

A

N

C

P

Y

L

H

Q

T

I

A

V

S

G

V

A

F

I

D

N

P

A

M

N

S

H

A

A

R

L

I

L

A

A

A

Q

D

R

L

A

G

G

F

Y

E

Q

V

A

G

I

I
x
Y

L

L

G
x
S

G
|
G

S
x
G

V

G

A

V

S

A

L

A

Q

G

V

S

L

L

G

G

A

L

P

P

D
|
D

F

L

A

G

L

I

I

S

T

T

L

L

S

D

E

D

F

V

A

L

E

T

Q

D

A

I

T

R

R

R

I

I

G

T

R

D

V

V

A

C

Q

P

L

L

P

P

V

L

I

L

A

V

D
|
D

A

A

D
|
D

H

I

G

G

Y

F

G

G

-

S

N

S

A

A

L

F

N

N

V

V

M

A

R

R

T

T

I

V

V

K

E

S

L

I

E

A

R

K

A

A

G

G

V

A

A

A

L

L

T
x
H

I

I

E
|
E

D

D

T

Q

L

V

L

A

P

-

A

-

Q

-

F

-

G

-

R

-

K

-

S

-

T

-

D

-

L

I

I

V

T

S

V

K

A

E

E

E

G

M

V

V

G

D

K

R

I

I

R

R

A

A

L

V

E

D

A

A

R

R

V

T

D

D

S

P

E

N

M

F

A

V

I

I

I

M

A

A

R
|
R

T

T

N

D

A

A

-

L

G

A

I

V

L

E

P

G

V

L

Q

E

E

A

I

A

I

L

S

D

R

R

T

A

K

Q

Q

A

Y

Y

Q

V

Q

D

A

A

G

G

A

A

D

D

G

M

I

L

C

F

M

P

V
x
E

G

A

V

I

R

T

D

E

F

L

D

S

H

M

L

Y

E

R

Q

R

I

F

A

A

E

D

H

V

L

A

S

Q

V

V

P

P

L

I

M

L

-

A

-
x
N

L

I

V

T

T

E

Y

F

G

G

-

A

N
x
T

P

P

L
|
L

L

F

R

T

D

T

D

D

active site: Y39 (≠ I46), S41 (≠ G48), G42 (= G49), G43 (≠ S50), D54 (= D61), D81 (= D88), D83 (= D90), H109 (≠ T115), E111 (= E117), R143 (= R159), E173 (≠ V188), N195 (vs. gap), T202 (≠ N214), L204 (= L216)
binding pyruvic acid: Y39 (≠ I46), S41 (≠ G48), G43 (≠ S50), D81 (= D88), R143 (= R159)

Q84G06 Phosphonopyruvate hydrolase; PPH; EC 3.11.1.3 from Variovorax sp. (strain Pal2) (see paper)
31% identity, 85% coverage: 13:258/289 of query aligns to 7:252/290 of Q84G06

query
sites
Q84G06

F

L

R

R

Q

A

L

A

F

L

A

D

S

S

N

G

A

R

C

L

Y

F

H

T

T

A

A

M

S

A

V

A

F

H

D

N

P

P

M

L

S

V

A

A

R

K

I

L

A

A

A

E

D

Q

L

A

G

G

F

F

E

G

V

-

G

G

I

I

L

W

G

G

G

S

S

G

V

F

A

E

S

L

L

S

Q

A

V

S

L

Y

G

A

A

V

P

P

D

D

F

A

A

N

L

I

I

L

T

S

L

M

S

S

E

T

F

H

A

L

E

E

Q

M

A

M

T

R

R

A

I

I

G

A

R

S

V

T

A

V

Q

S

L

I

P

P

V

L

I

I

A

A

D
|
D

A

I

D

D

H

T

G

G

Y

F

G

G

N

N

A

A

L

V

N

N

V

V

M

H

R

Y

T

V

I

V

V

P

E

Q

L

Y

E

E

R

A

A

A

G

G

V

A

A

S

A

A

L

I

T

V

I

M

E

E

D

D

T

K

L

T

L

F

P

P

A

K

Q

D

F

T

G

S

R

L

K

R

S

T

-

D

-

G

-

R

T

Q

D

E

L

L

I

V

T

R

V

I

A

E

E

E

G

F

V

Q

G

G

K

K

I

I

R

A

A

A

L

T

E

A

A

A

R

R

V

A

D

D

S

R

E

D

M

F

A

V

I

V

I

I

A

A

R

R

T

V

N

E

A

A

G

L

I

I

-

A

-

G

L

L

P

G

V

Q

Q

Q

E

E

I

A

I

V

S

R

R

R

T

G

K

Q

Q

A

Y

Y

Q

E

A

A

G

G

A

A

D

D

G

A

I

I

C

-

M

L

V

I

G

H

V

S

R
|
R

D

Q

F

K

D

T

H

P

L

D

E

E

Q

I

I

L

A

A

E

F

H

V

L

K

S

S

-

W

-

P

-

G

-

K

V

V

P

P

L

L

M

V

L

L

V

V

T

P

Y

T

G

A

N

Y

P

P

L

Q

L

L

R

T

D

E

D

A

N

D

R

I

L

A

A

A

E

L

L

S

G

K

V

V

R

G

V

I

T

V

I

I

D

Y

G

G

H

N

G

H

A

A

Y

I

F

R

A

A

I

V

K

G

A

A

T

V

Y

-

D

-

S

-

L

-

R

-

E

-

Q

-

R

R

Q

E

I

V

F

F

T

A

Q

R

D81 (= D88) binding
R188 (= R191) mutation to A: Reduced affinity for substrate.

3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate (see paper)
32% identity, 78% coverage: 27:251/289 of query aligns to 25:254/297 of 3m0jA

query
sites
3m0jA

S

G

V

V

F

Y

D

D

P

G

M

L

S

S

A

A

R

R

I

T

A

A

A

M

D

E

L

L

G

G

F

F

E

K

V

S

G

L

I
x
Y

L

M

G
x
T

G
|
G

S
x
A

V

G

A

T

S

T

L

A

Q

S

V

R

L

L

G

G

A

Q

P

P

D

D

F

L

A

A

L

I

I

A

T

Q

L

L

S

H

E

D

F

M

A

R

E

D

Q

N

A

A

T

D

R

M

I

I

G

A

R

N

V

L

A

D

Q

P

L

F

-

G

-

P

P

P

V

L

I

I

A

A

D
|
D

A

M

D

D

H

T

G

G

Y

Y

G

G

N

G

A

P

L

I

N

M

V

V

M

A

R

R

T

T

I

V

V

E

E

H

L

Y

E

I

R

R

A

S

G

G

V

V

A

A

A

G

L

A

T

H

I

L

E

E

D

D

T

Q

L

I

L

L

P

T

A

K

Q

R

F

C

G
|
G

R

H

K

L

S

S

-

G

T

K

D

K

L

V

I

V

T

S

V

R

A

D

E

E

G

Y

V

L

G

V

K

R

I

I

R

R

A

A

L

V

-

A

-

T

E

K

A

R

R

R

V

L

D

R

S

S

E

D

M

F

A

V

I

L

I

I

A

A

R
|
R

T

T

N

D

A

A

-

L

G

Q

I

S

L

L

P

G

V

Y

Q

E

E

E

I

C

I

I

S

E

R

R

T

L

K

R

Q

A

Y

A

Q

R

Q

D

A

E

G

G

A

A

D

D

G

V

I

G

C

L

M

L

V
x
E

G

G

V

F

R

R

D

S

F

K

D

E

H

Q

-

A

L

A

E

A

Q

A

I

V

A

A

E

A

H

L

L

A

S

P

V

W

P

P

L

L

M

L

L

L

V
x
N

T

S

Y

V

G
x
E

N
|
N

-

G

-

H

-

S

P

P

L

L

L

I

R

T

D

V

D

E

N

E

R

A

L

K

A

A

E

-

L

M

G

G

V

F

R

R

V

I

T

M

I

I

D

-

G

-

H

-

G

-

A

F

Y
x
S

F

F

A

A

A

T

I

L

K

A

A

P

T

A

Y

Y

D

A

S

A

L

I

R

R

E

E

binding calcium ion: E218 (≠ G213), N219 (= N214)
binding 2,2-difluoro-3,3-dihydroxybutanedioic acid: Y44 (≠ I46), T46 (≠ G48), G47 (= G49), A48 (≠ S50), D88 (= D88), G126 (= G126), R162 (= R159), E192 (≠ V188), N215 (≠ V210), S241 (≠ Y238)

6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
28% identity, 86% coverage: 11:258/289 of query aligns to 6:247/277 of 6t4vC

query
sites
6t4vC

R

Q

N

R

F

F

R

R

Q

E

L

A

F

V

A

A

S

T

N

E

A

H

C

P

Y

L

H

Q

T

V

A

V

S

G

V

T

F

I

D

N

P

A

M

N

S

H

A

A

R

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I

L

A

A

A

K

D

R

L

A

G

G

F

F

E

K

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A

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I

I
x
Y

L

L

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x
S

G
|
G

S
x
G

V

G

A

V

S

A

L

A

Q

G

V

S

L

L

G

G

A

L

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P

D
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D

F

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A

G

L

I

I

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T

G

L

L

S

D

E

D

F

V

A

L

E

T

Q

D

A

V

T

R

R

R

I

I

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T

R

D

V

V

A

C

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D

L

L

P

P

V

L

I

L

A

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D
|
D

A

V

D
|
D

H

T

G

G

Y
x
F

G

G

-

S

N

S

A

A

L

F

N
|
N

V

V

M

A

R

R

T

T

I

V

V

K

E

S

L

M

E

I

R

K

A

F

G

G

V

A

A

A

L

M

T
x
H

I

I

E
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E

D

D

T

Q

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L

-

P

-

A

-

Q

-

F

-

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-

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-

K

-

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-

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-

D

E

L

I

I

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A

Q

E

E

G

M

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G

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I

I

R

K

A

A

L

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D

A

A

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D

D

S

D

E

S

M

F

A

V

I

I

I

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A

A

R
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R

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T

N

D

A

A

-

L

G

A

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E

P

G

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L

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Q

E

A

I

A

I

I

S

D

R

R

T

A

K

C

Q

A

Y

C

Q

V

Q

E

A

A

G

G

A

A

D

D

G

M

I

I

C

F

M

P

V
x
E

G

A

V

M

R

T

D

E

F

L

D

A

H

M

L

Y

E

K

Q

E

I

F

A

A

E

A

H

A

L

V

S

K

V

V

P

P

L

V

M

L

-

A

-
x
N

L

I

V

T

T

E

Y

F

G

G

N

A

P
x
T

L

P

L
|
L

R

F

D

T

N

D

R

E

L

L

A

A

E

S

L

A

G

D

V

V

R

S

V

L

T

V

I

L

D

Y

G

P

H

L

G

S

A

A

Y

F

F

R

A

A

A

M

I

N

K

K

A

A

T

A

Y

E

D

N

S

V

L

Y

R

T

E

A

Q

I

R

R

Q

R

I

D

F

G

T

T

Q

Q

active site: Y41 (≠ I46), S43 (≠ G48), G44 (= G49), G45 (≠ S50), D56 (= D61), D83 (= D88), D85 (= D90), H111 (≠ T115), E113 (= E117), R145 (= R159), E175 (≠ V188), N197 (vs. gap), T204 (≠ P215), L206 (= L217)
binding pyruvic acid: F88 (≠ Y93), N94 (= N98)

3m0kA Structure of oxaloacetate acetylhydrolase in complex with the product oxalate (see paper)
31% identity, 78% coverage: 27:251/289 of query aligns to 25:249/289 of 3m0kA

query
sites
3m0kA

S

G

V

V

F

Y

D

D

P

G

M

L

S

S

A

A

R

R

I

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A

A

A

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E

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L

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G

F

F

E

K

V

S

G

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I
x
Y

L

M

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x
T

G
|
G

S

A

V

G

A

T

S

T

L

A

Q

S

V

R

L

L

G

G

A

Q

P

P

D

D

F

L

A

A

L

I

I

A

T

Q

L

L

S

H

E

D

F

M

A

R

E

D

Q

N

A

A

T

D

R

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I

I

G

A

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N

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L

A

D

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L

F

-

G

-

P

P

P

V

L

I

I

A

A

D

D

A

M

D

D

H

T

G

G

Y

Y

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G

N

G

A

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I

N

M

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V

M

A

R

R

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I

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E

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E

I

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R

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G

G

V

V

A

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A

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E

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D

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I

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-

F

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-

R

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K

R

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E

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Y

V

L

G

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I

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R

A

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-

A

-

T

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K

A

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S

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A

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R
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R

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A

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L

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L

L

P

G

V

Y

Q

E

E

E

I

C

I

I

S

E

R

R

T

L

K

R

Q

A

Y

A

Q

R

Q

D

A

E

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G

A

A

D

D

G

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I

G

C

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M

L

V

E

G

G

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R

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S

F

K

D

E

H

Q

-

A

L

A

E

A

Q

A

I

V

A

A

E

A

H

L

L

A

S

P

V

W

P

P

L

L

M

L

L

L

V

N

T

S

Y

V

G
x
E

N
|
N

-

G

-

H

-

S

P

P

L

L

L

I

R

T

D

V

D

E

N

E

R

A

L

K

A

A

E

-

L

M

G

G

V

F

R

R

V

I

T

M

I

I

D

-

G

-

H

-

G

-

A

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x
S

F

F

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A

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L

K

A

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P

T

A

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Y

D

A

S

A

L

I

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R

E

E

binding calcium ion: E213 (≠ G213), N214 (= N214)
binding oxalate ion: Y44 (≠ I46), T46 (≠ G48), G47 (= G49), R157 (= R159), S236 (≠ Y238)

P56839 Phosphoenolpyruvate phosphomutase; PEP mutase; PEP phosphomutase; Phosphoenolpyruvate mutase; EC 5.4.2.9 from Mytilus edulis (Blue mussel) (see 2 papers)
31% identity, 61% coverage: 13:187/289 of query aligns to 11:189/295 of P56839

query
sites
P56839

F

L

R

K

Q

Q

L

M

F

L

A

N

S

S

N

K

A

D

C

L

Y

E

H

F

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I

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E

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A

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S

A

A

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I

A

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A

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F

E

K

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-

G

G

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I

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G

G

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G

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L

A

S

S

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A

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L

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G

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D
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D

F

S

A

N

L

E

I

A

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S

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S

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E

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F

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A

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E

E

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A

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I

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G

S

R

D

V

A

A

S

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D

L

V

P

P

V

I

I

L

A

L

D
|
D

A

A

D
|
D

H

T

G

G

Y

Y

G

G

N

N

A

F

L

N

N

N

V

A

M

R

R

R

T

L

I

V

V

R

E

K

L

L

E

E

R

D

A

R

G

G

V

V

A

A

A

G

L

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I

L

E
|
E

D

D

T

K

L

L

L

F

P

P

A

K

-

T

-
x
N

-

S

-

L

Q

H

F

D

G

G

R

R

K

-

S

A

T

Q

D

P

L

L

I

A

T

D

V

I

A

E

E

E

G

F

V

A

G

L

K

K

I

I

R

K

A

A

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C

L

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A

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P

E

D

M

F

A

C

I

I

I

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A

A

R
|
R

T

V

N

E

A

A

G

F

I

I

-

A

-

G

L

W

P

G

V

L

Q

D

E

E

I

A

I

L

S

K

R

R

T

A

K

E

Q

A

Y

Y

Q

R

Q

N

A

A

G

G

A

A

D

D

G

A

I

I

C

L

M

M

D58 (= D61) mutation D->A,S: Abolishes enzyme activity.; mutation to N: Strongly reduces enzyme activity.
D85 (= D88) mutation to A: Strongly reduces enzyme activity and increases KM.
D87 (= D90) mutation to A: Strongly reduces enzyme activity.
E114 (= E117) mutation to A: Strongly reduces enzyme activity.
N122 (vs. gap) mutation N->A,D: Strongly reduces enzyme activity.
R159 (= R159) mutation to A: Strongly reduces enzyme activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
190 H→A: Strongly reduces enzyme activity.

1pymA Phosphoenolpyruvate mutase from mollusk in with bound mg2-oxalate (see paper)
31% identity, 61% coverage: 13:187/289 of query aligns to 7:185/291 of 1pymA

query
sites
1pymA

F

L

R

K

Q

Q

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M

F

L

A

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S

N

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A

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S

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I

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L

A

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G

F

F

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K

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-

G

G

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I

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x
W

G

G

G
x
S

S
x
G

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x
L

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S

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A

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L

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D

F

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L

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I

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E

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V

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A

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D

L

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P

V

I

I

L

A

L

D
|
D

A

A

D
|
D

H

T

G

G

Y

Y

G

G

N

N

A

F

L

N

N

N

V

A

M

R

R

R

T

L

I

V

V

R

E

K

L

L

E

E

R

D

A

R

G

G

V

V

A

A

A

G

L

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x
C

I

L

E
|
E

D

D

T

K

L

L

L

F

P

P

A
x
K

-

T

-
x
N

-
x
S

-

L

Q

H

F

D

G

G

R

R

K

-

S

A

T

Q

D

P

L

L

I

A

T

D

V

I

A

E

E

E

G

F

V

A

G

L

K

K

I

I

R

K

A

A

A

C

L

K

E

D

A

S

R

Q

V

T

D

D

S

P

E

D

M

F

A

C

I

I

I

V

A

A

R
|
R

T

V

N

E

A

A

G

F

I

I

-

A

-

G

L

W

P

G

V

L

Q

D

E

E

I

A

I

L

S

K

R

R

T

A

K

E

Q

A

Y

Y

Q

R

Q

N

A

A

G

G

A

A

D

D

G

A

I

I

C

L

M

M

active site: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), L44 (≠ V51), D54 (= D61), D81 (= D88), D83 (= D90), C108 (≠ T115), E110 (= E117), K116 (≠ A123), N118 (vs. gap), S119 (vs. gap), R155 (= R159)
binding oxalate ion: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), L44 (≠ V51), D81 (= D88), R155 (= R159)

Sites not aligning to the query:

active site: 186, 211

1m1bA Crystal structure of phosphoenolpyruvate mutase complexed with sulfopyruvate (see paper)
31% identity, 61% coverage: 13:187/289 of query aligns to 7:185/291 of 1m1bA

query
sites
1m1bA

F

L

R

K

Q

Q

L

M

F

L

A

N

S

S

N

K

A

D

C

L

Y

E

H

F

T

I

A

M

S

E

V

A

F

H

D

N

P

G

M

L

S

S

A

A

R

R

I

I

A

V

A

Q

D

E

L

A

G

G

F

F

E

K

V

-

G

G

I

I

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x
W

G

G

G
x
S

S
x
G

V
x
L

A

S

S

V

L

S

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A

V

Q

L

L

G

G

A

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D
|
D

F

S

A

N

L

E

I

A

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S

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E

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F

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A

V

E

E

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A

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D

V

A

A

S

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D

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P

V

I

I

L

A

L

D
|
D

A

A

D
|
D

H

T

G

G

Y

Y

G

G

N

N

A

F

L

N

N

N

V

A

M

R

R

R

T

L

I

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V

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K

L

L

E

E

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A

R

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G

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A

A

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x
C

I

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|
E

D

D

T

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L

L

F

P

P

A
x
K

-

T

-
x
N

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x
S

-
x
L

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F

D

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G

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K

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S

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L

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I

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E

E

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F

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G

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K

I

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R

K

A

A

A

C

L

K

E

D

A

S

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Q

V

T

D

D

S

P

E

D

M

F

A

C

I

I

I

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A

A

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R

T

V

N

E

A

A

G

F

I

I

-

A

-

G

L

W

P

G

V

L

Q

D

E

E

I

A

I

L

S

K

R

R

T

A

K

E

Q

A

Y

Y

Q

R

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N

A

A

G

G

A

A

D

D

G

A

I

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L

M

M

active site: W40 (≠ L47), S42 (≠ G49), G43 (≠ S50), L44 (≠ V51), D54 (= D61), D81 (= D88), D83 (= D90), C108 (≠ T115), E110 (= E117), K116 (≠ A123), N118 (vs. gap), S119 (vs. gap), R155 (= R159)
binding magnesium ion: D81 (= D88), R155 (= R159)
binding sulfopyruvate: S42 (≠ G49), G43 (≠ S50), L44 (≠ V51), D81 (= D88), N118 (vs. gap), S119 (vs. gap), L120 (vs. gap), R155 (= R159)

Sites not aligning to the query:

active site: 186, 211

Query Sequence

>Pf1N1B4_5858 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5858
MPRLSHQDLRRNFRQLFASNACYHTASVFDPMSARIAADLGFEVGILGGSVASLQVLGAP
DFALITLSEFAEQATRIGRVAQLPVIADADHGYGNALNVMRTIVELERAGVAALTIEDTL
LPAQFGRKSTDLITVAEGVGKIRAALEARVDSEMAIIARTNAGILPVQEIISRTKQYQQA
GADGICMVGVRDFDHLEQIAEHLSVPLMLVTYGNPLLRDDNRLAELGVRVTIDGHGAYFA
AIKATYDSLREQRQIFTQASDLSATELTHTYTQPEEYIVWAKEYMSVKE

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