SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing SMc00261 FitnessBrowser__Smeli:SMc00261 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)

P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
33% identity, 93% coverage: 19:527/549 of query aligns to 3:496/503 of P9WQ37

query
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P9WQ37

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R9 (≠ S25) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
R17 (≠ D33) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
K172 (= K191) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
R195 (≠ T216) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
R197 (= R218) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
V209 (≠ G230) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
A211 (≠ G232) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
T214 (≠ Q235) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
R244 (= R266) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
A302 (≠ G325) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
W377 (= W407) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
D382 (= D412) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
R397 (= R427) mutation to A: Reduction of binding affinity for fatty acids.
S404 (= S434) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
G406 (= G436) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
K487 (= K518) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.

3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
33% identity, 93% coverage: 16:527/549 of query aligns to 3:496/502 of 3r44A

query
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3r44A

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active site: T167 (= T183), A184 (≠ V203), H208 (= H229), T304 (≠ G327), E305 (= E328), I403 (= I433), N408 (= N438), K487 (= K518)
binding histidine: M4 (≠ V17), K5 (≠ M18), N6 (= N19), I7 (≠ L20), H178 (= H197), E179 (≠ G198), H182 (≠ A201)

Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
31% identity, 89% coverage: 43:531/549 of query aligns to 64:580/590 of Q4WR83

query
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Q4WR83

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-

S

S

P

H

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A

A

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D

D

R

R

D

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-

A

-

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-

L

-

H

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T

D

D

P

V

C

C

W

N

Y

L

F

Q

Y

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S

G

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G

G

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N

P

P

K

K

A

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T

H

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M

L

A

-

F

-

V

-

I

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-

F

I

I

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G

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D

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I

I

A

G

G

P

Y

A

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L

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A

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G

G

Y

Y

Y

W

R

N

N

N

P

P

E

E

A

K

N

T

A

A

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A

A

F

L

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I

N

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D

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T

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-

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G

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Sites not aligning to the query:

6:14 PTS2-type peroxisomal targeting signal

P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
29% identity, 95% coverage: 16:535/549 of query aligns to 21:558/561 of P69451

query
sites
P69451

R

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K

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W

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G

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-

G

A

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K

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Y213 (= Y182) mutation to A: Loss of activity.
T214 (= T183) mutation to A: 10% of wild-type activity.
G216 (= G185) mutation to A: Decreases activity.
T217 (= T186) mutation to A: Decreases activity.
G219 (= G188) mutation to A: Decreases activity.
K222 (= K191) mutation to A: Decreases activity.
E361 (= E328) mutation to A: Loss of activity.

5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
30% identity, 93% coverage: 22:534/549 of query aligns to 6:484/485 of 5x8fB

query
sites
5x8fB

N

N

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A

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A

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L

G

G

A

V

V

K

W

A

V

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T

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N

N

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R
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K

Q

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G

E

E

I

I

C

M

V

V

I

K

G

G

P

P

A

N

V

V

F

M

A

K

G

S

Y

Y

Y

F

R

N

N

R

P

E

E

S

A

A

N

N

A

E

K

A

A

S

F

F

R

Q

N

N

G

G

W

W

F

L

R

K

T

T

G

G

D

D

L

L

G

G

H

Y

V

L

D

D

A

N

Q

E

G

G

F

F

L

L

Y

Y

I

V

T

L

G

D

R

R

A

R

S

S

D

D

M

L

Y

I

I
|
I

S
|
S

G
|
G

S
x
E

N
|
N

V

I

Y

Y

P

P

R

A

E

E

I

V

E

E

E

S

K

V

L

L

M

S

H

H

P

P

D

A

I

V

S

A

E

E

A

A

A

G

I

V

V

S

G

G

V

A

P

E

D

D

P

K

V
x
K

W
|
W

G

G

E

K

V

V

G

P

I

H

A

A

V

Y

C

L

V

V

A

L

R

H

G

-

A

K

T

P

V

V

G

S

A

A

A

G

A

E

L

L

R

T

E

D

W

Y

L

C

D

K

G

E

K

R

I

L

A

A

R
x
K

Y
|
Y

K

K

L

R

P

P

K

K

I

F

V

F

F

V

W

L

S

D

E

R

M

L

P

P

K

R

S

N

A

A

Y

-

G

-

K

-

I

-

T

S

K

N

K
|
K

L

L

I

L

R

R

E

N

E

Q

L

L

E

K

-

D

-

A

R

R

R

K

G

G

E

E

L

L

active site: T151 (= T183), S171 (≠ V203), H195 (= H229), T288 (≠ G327), E289 (= E328), I387 (= I433), N392 (= N438), K470 (= K522)
binding magnesium ion: Y23 (≠ H39), E24 (≠ G40), H70 (≠ F87), N178 (≠ D210), L202 (= L236), L214 (= L247), F282 (≠ V321), T296 (≠ V335), L297 (= L336), S298 (≠ P337)
binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R102), L191 (≠ A225), P192 (= P226), H195 (= H229), I196 (≠ G230), S197 (≠ A231), F218 (≠ L253), S236 (≠ F271), A237 (= A272), V238 (= V273), M241 (≠ I276), L260 (≠ I298), G262 (≠ A300), G263 (= G301), G286 (= G325), M287 (≠ L326), S292 (≠ G331), Q293 (≠ A332), S388 (= S434), G389 (= G435), G390 (= G436), E391 (≠ S437), K420 (≠ V466), W421 (= W467), K450 (≠ R498), Y451 (= Y499)

5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
30% identity, 93% coverage: 22:534/549 of query aligns to 6:484/484 of 5gtdA

query
sites
5gtdA

N

N

F

W

L

L

S

M

Q

Q

A

R

A

A

R

Q

R

L

N

T

P

P

D

E

E

R

I

I

A

A

L

L

V

I

H

Y

G

E

D

D

R

Q

R

T

W

V

R

T

W

F

S

A

E

E

M

L

E

F

A

A

R

A

V

S

D

K

A

R

M

M

A

A

Y

E

A

Q

L

L

V

A

H

A

E

H

F

-

G

S

V

V

R

R

K

K

G

G

D

D

R

T

I

A

L

A

V

I

H

L

S

L

A

Q

N

N

C

R

N

A

Q

E

M

M

F

V

E

Y

S

A

M

V

F

H

A

A

A

C

F

F

R

L

A

L

G

G

A

V

V

K

W

A

V

V

P

L

T

L

N

N

F

T

R

K

Q

L

L

S

P

T

E

H

E

E

V

R

A

L

Y

F

L

Q

A

L

E

E

S

D

S

S

G

G

A

S

R

G

L

F

V

L

I

L

F

T

Q

D

A

S

F

F

E

E

A

-

H

-

A

-

E

-

A

-

C

-

R

K

A

K

A

E

G

Y

E

E

Q

H

I

I

G

V

S

Q

C

T

I

I

P

-

I

-

G

-

S

-

R

-

V

-

G

-

E

-

D

D

Y

V

D

D

A

E

I

L

V

M

A

K

R

E

N

A

L

A

G

E

R

E

S

I

V

E

S

I

P

E

V

A

A

Y

V

M

D

Q

R

M

D

D

D

A

P

T

C

A

W

T

Y

L

F

M

Y

Y

T
|
T

S

S

G

G

T

T

G

G

R

K

P

P

K

K

A

G

A

V

V

Q

L

Q

T

T

H

F

G

G

Q

N

M

H

A

Y

F

F

V
x
S

I

A

N

V

N

S

H

S

I

A

G

L

D

N

L

L

F

-

P

-

A

G

T

I

T

T

H

E

R

Q

D

D

R

R

S

W

I

L

V

I

V

A

A
x
L

P

P

L

L

S

F

H
|
H

G
x
I

A
x
S

G

G

I

L

H

S

Q

A

L

L

C

F

Q

K

-

S

V

V

A

I

R

Y

G

G

A

M

T

T

T

V

I

V

L

L

L

-

P

-

S

H

E

Q

K

R

L

F

D

S

I

V

P

S

Q

D

F

V

W

L

A

H

L

S

V

I

E

N

K

R

W

H

R

E

V

V

N

T

N

M

L

I

F
x
S

A
|
A

V

V

P

Q

T

T

I

M

V

L

K

A

L

S

L

L

I

L

E

E

D

E

P

-

S

-

V

T

D

N

R

R

Y

C

D

P

H

E

S

S

S

-

L

I

R

R

Y

C

V

I

I
x
L

Y

L

A
x
G

G
|
G

A
x
G

P
|
P

M

A

Y

P

R

L

A

P

D

L

Q

L

K

E

A

C

L

R

E

E

K

K

L

-

G

G

A

F

V

P

L

V

V

F

Q

Q

Y
x
S

F
x
Y

G
|
G

L
x
M

G
x
T

E
|
E

V

T

T

C

G
x
S

A
x
Q

I

I

T

V

V

T

L

L

P

S

P

P

A

E

F

F

H

S

S

M

S

E

E

-

D

-

G

-

P

-

D

-

A

-

R

K

I

L

G

G

T

S

C

A

G

G

F

K

E

P

R

L

T
x
F

G
x
S

M

C

Q

E

L

I

Q

K

I

I

Q

-

D

E

E

R

D

D

G

G

N

Q

E

V

V

C

P

E

A

P

G

Y

A

E

T

H

G

G

E

E

I

I

C

M

V

V

I

K

G

G

P

P

A

N

V

V

F

M

A

K

G

S

Y

Y

Y

F

R

N

N

R

P

E

E

S

A

A

N

N

A

E

K

A

A

S

F

F

R

Q

N

N

G

G

W

W

F

L

R

K

T

T

G

G

D
|
D

L

L

G

G

H

Y

V

L

D

D

A

N

Q

E

G

G

F

F

L

L

Y

Y

I
x
V

T

L

G

D

R
|
R

A

R

S

S

D

D

M

L

Y

I

I

I

S

S

G

G

S

E

N

N

V

I

Y

Y

P

P

R

A

E

E

I

V

E

E

E

S

K

V

L

L

M

S

H

H

P

P

D

A

I

V

S

A

E

E

A

A

A

G

I

V

V

S

G

G

V

A

P

E

D

D

P

K

V

K

W

W

G

G

E

K

V

V

G

P

I

H

A

A

V

Y

C

L

V

V

A

L

R

H

G

-

A

K

T

P

V

V

G

S

A

A

A

G

A

E

L

L

R

T

E

D

W

Y

L

C

D

K

G

E

K

R

I

L

A

A

R

K

Y

Y

K

K

L

I

P

P

K

A

K

K

I

F

V

F

F

V

W

L

S

D

E

R

M

L

P

P

K

R

S

N

A

A

Y

-

G

-

K

-

I

-

T

S

K

N

K
|
K

L

L

I

L

R

R

E

N

E

Q

L

L

E

K

-

D

-

A

R

R

R

K

G

G

E

E

L

L

active site: T151 (= T183), S171 (≠ V203), H195 (= H229), T288 (≠ G327), E289 (= E328)
binding adenosine-5'-monophosphate: H195 (= H229), G263 (= G301), G264 (≠ A302), P265 (= P303), S284 (≠ Y323), Y285 (≠ F324), G286 (= G325), M287 (≠ L326), T288 (≠ G327), D366 (= D412), V378 (≠ I424), R381 (= R427), K470 (= K522)
binding magnesium ion: F314 (≠ T359), S315 (≠ G360)
binding 2-succinylbenzoate: L191 (≠ A225), H195 (= H229), I196 (≠ G230), S197 (≠ A231), S236 (≠ F271), A237 (= A272), L260 (≠ I298), G262 (≠ A300), G263 (= G301), G286 (= G325), M287 (≠ L326), T288 (≠ G327), S292 (≠ G331), Q293 (≠ A332)

5ie2A Crystal structure of a plant enzyme (see paper)
28% identity, 93% coverage: 19:528/549 of query aligns to 5:505/506 of 5ie2A

query
sites
5ie2A

N

T

L

L

A

S

N

G

F

L

L

L

S

E

Q

N

A

V

A

A

R

K

N

F

P

P

D

D

E

R

I

R

A

A

L

L

-

S

V

V

H

S

G

G

D

K

R

F

R

N

W

L

R

T

W

H

S

A

E

R

M

L

E

H

A

D

R

L

V

I

D

E

A

R

M

A

A

A

Y

S

A

R

L

L

V

V

H

S

E

D

F

A

G

G

V

I

R

K

K

P

G

G

D

D

R

V

I

V

L

A

V

L

H

T

S

F

A

P

N

N

C

T

N

V

Q

E

M

F

F

V

E

I

S

M

M

F

F

L

A

A

A

V

F

I

R

R

A

A

G

R

A

A

V

T

W

A

V

A

P

P

T

L

N

N

F

A

R

A

Q

Y

L

T

P

A

E

E

V

F

A

E

Y

F

L

Y

A

L

E

S

S

D

S

S

G

D

A

S

R

K

L

L

V

L

I

L

F

-

Q

-

A

T

A

S

F

K

E

E

A

G

H

N

A

A

E

P

A

A

C

Q

R

E

A

A

G

S

E

K

Q

L

I

K

G

I

S

S

C

H

I

V

P

T

I

A

G

T

S

L

R

D

V

A

G

G

E

S

D

D

Y

L

D

V

A

L

I

S

V

V

A

A

R

D

N

D

L

-

G

-

R

-

S

S

V

A

S

T

P

E

V

L

A

V

V

N

D

H

R

P

D

D

P

G

C

A

W

L

Y

F

F

L

Y

H

T
|
T

S
|
S

G
|
G

T
|
T

G

S

R

R

P

P

K

K

A

G

A

V

V

P

L

L

T

T

H

Q

G

L

Q

N

M

L

A

A

F

S

V
x
S

I

V

N

K

N

N

H

-

I

I

G

K

D

A

L

V

F

Y

P

-

A

K

T

L

T

T

H

E

R

S

D

D

R

S

S

T

I

V

V

I

V

V

A

L

P

P

L

L

S

F

H
|
H

-

V

G

H

A

G

G

L

I

L

H

A

Q

G

L

L

C

L

Q

S

V

S

A

L

R

G

G

A

A

G

T

A

I

V

L

T

L

L

P

P

S

A

E

A

-

G

K

R

L

F

D

S

I

A

P

T

Q

T

F

F

W

W

A

P

L

D

V

M

E

K

K

K

W

Y

R

N

V

A

N

T

N

W

L

Y

F

T

A

A

V

V

P

P

T

T

I

I

V

H

K

Q

L

I

I

L

E

D

-

R

D

H

P

A

S

S

V

H

D

P

R

E

Y

T

D

E

H

Y

S

P

S

K

L

L

R

R

Y

F

V

I

I

R

Y

S

A

C

G
x
S

A
|
A

P
x
S

M

L

Y

A

R

P

A

V

D

I

Q

L

K

S

K

R

A

L

L

E

E

E

K

A

L

F

G

G

A

A

V

P

L

V

V

L

Q
x
E

Y
x
A

F
x
Y

G
x
A

L
x
M

G
x
T

E
|
E

V

A

T

T

G

H

A

L

I

M

T

S

V

S

L

N

P

P

P

-

A

-

F

-

H

-

S

L

S

P

E

E

D

E

G

G

P

P

D

H

A

-

R

K

I

P

G

G

T

S

C
x
V

G

G

F

-

E

K

R

P

T

V

G

G

M

Q

Q

E

L

M

Q

A

I

I

Q

L

D

N

E

E

D

K

G

G

N

E

E

I

V

Q

P

E

A

P

G

N

A

N

T

K

G

G

E

E

I

V

C

C

V

I

I

R

G

G

P

P

A

N

V

V

F

T

A

K

G

G

Y

Y

Y

K

R

N

N

N

P

P

E

E

A

A

N

N

A

K

K

A

A

G

F

F

R

E

N

F

G

G

W

W

F

F

R

H

T

T

G

G

D
|
D

L

I

G

G

H

Y

V

F

D

D

A

T

Q

D

G

G

F

Y

L

L

Y

H

I
x
L

T

V

G

G

R
|
R

A

I

S

K

D

E

M

L

Y

I

I
x
N

S

R

G

G

S

E

N
x
K

V

I

Y

S

P

P

R

I

E

E

I

V

E

D

E

A

K

V

L

L

M

T

H

H

P

P

D

D

I

V

S

S

E

Q

A

G

A

V

I

A

V

F

G

G

V

V

P

P

D

D

P

E

V

K

W

Y

G

G

E

E

V

E

G

I

I

N

A

C

V

A

C

V

V

I

A

P

R

R

G

E

G

G

A

T

T

T

V

V

G

T

A

E

A

D

L

I

R

K

E

A

W

F

L

C

D

K

G

K

K

N

I

L

A

A

R

A

Y

F

K

K

L

V

P

P

K

K

K

R

I

V

V

F

F

I

W

T

S

D

E

N

M

L

P

P

K

K

S

T

A

A

Y

S

G

G

K
|
K

I

I

T

Q

K

R

L

I

I

V

R

A

E

Q

E

H

L

F

active site: T165 (= T183), S185 (≠ V203), H209 (= H229), T310 (≠ G327), E311 (= E328), N410 (≠ I433), K415 (≠ N438), K495 (= K518)
binding adenosine-5'-triphosphate: T165 (= T183), S166 (= S184), G167 (= G185), T168 (= T186), T169 (= T187), H209 (= H229), S284 (≠ G301), A285 (= A302), S286 (≠ P303), E305 (≠ Q322), A306 (≠ Y323), Y307 (≠ F324), A308 (≠ G325), M309 (≠ L326), T310 (≠ G327), V332 (≠ C354), D389 (= D412), L401 (≠ I424), R404 (= R427), K495 (= K518)

Q9SMT7 Oxalate--CoA ligase; 4-coumarate--CoA ligase isoform 8; At4CL8; 4-coumarate--CoA ligase-like 10; Acyl-activating enzyme 3; Adenosine monophosphate binding protein 3; AtMPBP3; Oxalyl-CoA synthetase; EC 6.2.1.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 93% coverage: 19:528/549 of query aligns to 5:510/514 of Q9SMT7

query
sites
Q9SMT7

N

T

L

L

A

S

N

G

F

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E

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N

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TSGTT 170:174 (= TSGTT 183:187) binding
H214 (= H229) binding ; mutation to A: Abolished activity.
S289 (≠ G301) binding ; mutation to A: Abolished activity.
SAS 289:291 (≠ GAP 301:303) binding
EA 310:311 (≠ QY 322:323) binding
M314 (≠ L326) binding
T315 (≠ G327) binding
H319 (≠ G331) binding ; mutation to A: Abolished activity.
D394 (= D412) binding
R409 (= R427) binding ; mutation to A: Abolished activity.
K500 (= K518) binding ; binding ; mutation to A: Abolished activity.

5ie3A Crystal structure of a plant enzyme (see paper)
28% identity, 93% coverage: 19:528/549 of query aligns to 5:503/504 of 5ie3A

query
sites
5ie3A

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