SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 208580 DVU3065 AMP-binding enzyme family protein 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)

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)
39% identity, 98% coverage: 8:545/550 of query aligns to 36:577/590 of Q4WR83

query
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Q4WR83

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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)
30% identity, 97% coverage: 7:541/550 of query aligns to 21:553/561 of P69451

query
sites
P69451

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Y213 (= Y199) mutation to A: Loss of activity.
T214 (= T200) mutation to A: 10% of wild-type activity.
G216 (= G202) mutation to A: Decreases activity.
T217 (= T203) mutation to A: Decreases activity.
G219 (= G205) mutation to A: Decreases activity.
K222 (= K208) mutation to A: Decreases activity.
E361 (= E344) mutation to A: Loss of activity.

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)
30% identity, 98% coverage: 10:546/550 of query aligns to 3:502/503 of P9WQ37

query
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P9WQ37

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M

R

V

L

S

R

D

S

E

A

F

A

R

D

Q

E

R

P

Q

A

D

V

E

E

L

C

D

G

P

G

Y

D

D

D

V

N

V

L

N

F

M

I

Q

M

Y

Y

T

T

S

S

G

G

T

T

G

G

F

H

P

P

K
|
K

G

G

V

V

M

V

L

H

T

T

H

H

V

E

G

S

I

V

G

H

N

S

N

A

G

A

Y

S

W

S

I

W

G

A

R

S

N

T

Q

I

G

D

F

V

T
x
R

E

Y

K
x
R

D

D

R

R

V

L

C

L

L

L

P

P

V

L

P

P

L

M

F

F

H

H

C
x
V

F

A

G
x
A

C

L

V

T

L
x
T

G

V

V

I

M

F

A

S

A

A

I

M

N

-

H

R

G

G

A

V

A

T

L

L

V

I

I

S

L

M

E

P

N

Q

F

F

N

D

P

A

M

T

H

K

V

V

M

W

A

S

S

L

V

I

D

V

Q

E

E

E

K
x
R

C

V

T

C

A

I

L

G

Y

G

G

A

V

V

P

P

T

A

M

I

F

L

L

N

A

F

V

M

L

R

E

Q

H

V

K

P

L

E

F

F

D

A

R

E

F

L

D

D

F

A

S

P

S

D

L

F

R

R

T

Y

G

F

I

I

M

T

A

G

G

G

S

A

V

P

C

M

P

P

E

E

P

A

L

L

M

I

R

K

R

-

V

-

I

I

E

Y

K

A

M

A

N

K

M

N

R

I

E

E

I

V

T

V

I

Q

C

G

Y

Y

G
x
A

L

L

T

T

E

E

G

S

S

C

P

G

V

G

M

G

T

T

Q

L

T

L

L

L

V

S

D

E

D

D

S

A

L

L

E

-

R

R

R

K

V

A

Q

G

T

S

V

A

G

G

R

R

A

A

-

T

-

M

M

F

P

T

G

D

I

V

E

A

V

V

R

R

I

G

V

D

D

D

P

G

E

V

T

I

N

R

E

E

E

-

V

-

P

-

H

H

G

G

T

E

P

-

G

G

E

E

V

V

C

I

R

K

G

S

Y

D

N

I

V

L

M

L

K

K

G

E

Y

Y

Y

W

N

N

M

R

P

P

E

E

A

A

T

T

A

R

K

D

A

A

V

F

D

D

G

-

D

N

G

G

W
|
W

L

F

H

R

S

T

G

G

D
|
D

L

I

G

G

I

E

M

I

D

D

E

D

H

E

G

G

Y

Y

V

L

R

Y

I

I

T

K

G

D

R
|
R

I

L

K

K

D

D

M

M

I

I

R
x
S

G

G

G
|
G

E

E

N

N

I

V

Y

Y

P

P

R

A

E

E

I

I

E

E

E

S

F

V

L

I

Y

I

G

G

M

V

E

P

G

G

V

V

Q

S

D

E

V

V

Q

A

V

V

V

I

G

G

V

L

P

P

S

D

R

E

K

K

Y

W

G

G

E

-

E

E

V

I

G

A

A

A

F

A

I

I

I

V

P

V

K

A

E

D

G

Q

Y

N

D

E

L

V

A

S

P

E

E

Q

D

Q

V

I

R

V

D

E

H

Y

C

C

R

G

G

T

R

R

I

L

S

A

W

R

Y

Y

K

K

V

L

P

P

R

K

H

K

I

V

A

I

F

F

V

A

S

E

E

A

F

I

P

P

M

R

T

N

A

P

S

T

A

G

K
|
K

I

I

Q

L

K

K

Y

T

K

V

L

L

R

R

E

E

M

Q

A

Y

A

S

E

A

L

T

F

V

P

P

R9 (≠ D16) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
R17 (≠ D24) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
K172 (= K208) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
R195 (≠ T231) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
R197 (≠ K233) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
V209 (≠ C245) 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 (≠ G247) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
T214 (≠ L250) 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 (≠ K281) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
A302 (≠ G341) 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 (= W420) 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 (= D425) 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 (= R440) mutation to A: Reduction of binding affinity for fatty acids.
S404 (≠ R447) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
G406 (= G449) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
K487 (= K531) 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)
29% identity, 98% coverage: 10:546/550 of query aligns to 6:502/502 of 3r44A

query
sites
3r44A

T
x
N

L
x
I

G

G

R

W

I

M

L

L

D

R

E

Q

T

R

A

A

A

T

K

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F

S

P

P

D

R

N

L

D

Q

A

A

V

Y

V

V

Y

E

V

P

D

S

R

T

D

D

Y

V

R

R

Q

M

T

T

Y

Y

R

A

E

Q

F

M

V

N

S

A

V

L

V

A

D

N

D

R

L

C

A

A

R

D

G

V

L

L

M

T

A

A

L

L

G

G

V

I

K

A

R

K

G

G

D

D

K

R

V

V

A

A

L

L

W

L

A

M

T

P

N

N

V

S

P

V

Y

E

W

F

V

C

A

C

L

L

Q

F

F

Y

A

G

T

A

A

A

K

K

I

L

G

G

A

A

V

V

L

A

L

V

T

P

V

I

N

N

T

T

N

R

Y

L

R

A

E

A

S

P

E

E

L

V

R

S

Y

F

L

I

L

L

E

S

Q

D

S

S

E

G

C

S

E

K

N

-

L

-

F

V

I

V

M

I

D

Y

G

G

F

A

R

P

D

S

H

A

D

P

F

V

V

I

Q

D

T

A

I

I

Y

-

Q

-

V

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I

-

P

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L

-

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-

M

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Q

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G

-

Q

-

L

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R

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A

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Q

G

A

L

D

P

P

H

P

L

G

K

T

R

V

V

T

M

D

F

W

L

I

G

G

A

A

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D

K

-

H

-

R

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G

-

M

-

Y

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L

L

G

A

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M

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A

F

A

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D

Q

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V

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C

D

G

P

G

Y

D

D

D

V

N

V

L

N

F

M

I

Q

M

Y

Y

T
|
T

S

S

G

G

T

-

G

-

F

H

P

P

K

K

G

G

V

V

M

V

L

H

T

T

H
|
H

V
x
E

G

S

I

V

G
x
H

N

S

N
x
A

G

A

Y

S

W

S

I

W

G

A

R

S

N

T

Q

I

G

D

F

V

T

R

E

Y

K

R

D

D

R

R

V

L

C

L

L

L

P

P

V

L

P

P

L

M

F

F

H
|
H

C

V

F

A

G

A

C

L

V

T

L

T

G

V

V

I

M

F

A

S

A

A

I

M

N

-

H

R

G

G

A

V

A

T

L

L

V

I

I

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L

M

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N

Q

F

F

N

D

P

A

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H

K

V

V

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W

A

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S

L

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Q

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K

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C

V

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C

A

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Y

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V

V

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M

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L

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M

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S

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G

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M

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A

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L

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-

I

I

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K

A

M

A

N

K

M

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T

V

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C

G

Y

Y

G

A

L

L

T
|
T

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|
E

G

S

S

C

P

G

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G

M

G

T

T

Q

L

T

L

L

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D

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A

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L

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-

R

R

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K

V

A

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G

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M

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N

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L

M

L

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K

G

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Y

Y

W

N

N

M

R

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P

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E

A

A

T

T

A

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K

D

A

A

V

F

D

D

G

-

D

N

G

G

W

W

L

F

H

R

S

T

G

G

D

D

L

I

G

G

I

E

M

I

D

D

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D

H

E

G

G

Y

Y

V

L

R

Y

I

I

T

K

G

D

R

R

I

L

K

K

D

D

M

M

I

I

I
|
I

R

S

G

G

E

E

N
|
N

I

V

Y

Y

P

P

R

A

E

E

I

I

E

E

E

S

F

V

L

I

Y

I

G

G

M

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G

G

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V

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V

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A

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V

V

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G

G

V

L

P

P

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D

R

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K

K

Y

W

G

G

E

-

E

E

V

I

G

A

A

A

F

A

I

I

I

V

P

V

K

A

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D

G

Q

Y

N

D

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L

V

A

S

P

E

E

Q

D

Q

V

I

R

V

D

E

H

Y

C

C

R

G

G

T

R

R

I

L

S

A

W

R

Y

Y

K

K

V

L

P

P

R

K

H

K

I

V

A

I

F

F

V

A

S

E

E

A

F

I

P

P

M

R

T

N

A

P

S

T

A

G

K
|
K

I

I

Q

L

K

K

Y

T

K

V

L

L

R

R

E

E

M

Q

A

Y

A

S

E

A

L

T

F

V

P

P

active site: T167 (= T200), A184 (≠ N220), H208 (= H244), T304 (= T343), E305 (= E344), I403 (= I446), N408 (= N451), K487 (= K531)
binding histidine: N6 (≠ T10), I7 (≠ L11), H178 (= H214), E179 (≠ V215), H182 (≠ G218)

Sites not aligning to the query:

binding histidine: 4, 5

Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
28% identity, 93% coverage: 29:542/550 of query aligns to 63:551/556 of Q9S725

query
sites
Q9S725

V

V

Y

Y

V

T

D

Y

R

A

D

D

Y

V

R

H

Q

V

T

T

Y

S

R

R

E

K

F

-

V

-

S

-

V

-

D

-

L

L

A

A

R

A

G

G

L

L

M

H

A

N

L

L

G

G

V

V

K

K

R

Q

G

H

D

D

K

V

V

V

A

M

L

I

W

L

A

L

T

P

N

N

V

S

P

P

Y

E

W

V

V

V

A

L

L

T

Q

F

F

L

A

A

T

A

A

S

K

F

I

I

G

G

A

A

V

I

L

T

T

S

V

A

N

N

T

P

N

F

Y

F

R

T

E

P

S

A

E

E

L

I

R

S

Y

K

L

Q

L

A

E

K

Q

A

S

S

E

A

C

A

E

K

N

-

L

-

F

L

I

I

M

V

D

T

G

Q

F

S

R

R

D

Y

H

V

D

D

F

K

V

I

Q

K

T

N

I

L

Y

Q

Q

N

-

D

-

G

-

V

-

L

-

I

V

V

I

T

P

T

E

D

L

S

R

D

M

A

Q

I

P

P

R

E

G

N

Q

C

L

L

R

R

C

F

E

S

G

E

L

L

P

T

H

Q

L

-

K

-

R

-

V

-

M

-

F

-

L

-

G

-

A

S

E

E

K

E

H

P

R

R

G

-

M

V

Y

D

S

S

V

I

P

P

E

E

I

K

V

I

S

S

L

-

G

-

V

-

M

-

V

-

S

-

D

-

E

-

F

-

R

-

Q

-

R

-

Q

-

D

-

E

-

L

-

D

-

P

P

Y

E

D

D

V

V

N

A

M

L

Q

P

Y

F

T

S

S

S

G

G

T

T

G

G

F

L

P

P

K
|
K

G

G

V

V

M

M

L

L

T

T

H

H

V

K

G

G

I

L

G

V

N

T

N

S

-

V

-

A

G

Q

Y

Q

W

V

I

D

G

G

R

E

N

N

Q

P

G

N

-

L

-

Y

F

F

T

N

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R

K

D

D

D

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V

V

I

C

L

L

C

P

V

V

L

P

P

L

M

F

F

H

H

C

I

F

Y

G

A

C

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N

L

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G

I

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M

L

A

C

A

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G

G

A

A

A

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I

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F

F

N

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Q

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I

D

Q

Q

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C

K

K

C

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T

T

A

V

L

A

Y
x
M

G

V

V

V

P

P

T

P

M

I

F

V

L

L

A

A

V

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A

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K

H

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K

P

L

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D

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F

Y

D

D

F

L

S

S

L

V

R

R

T

M

G

V

I
x
K

M

S

A

G

G

A

S

A

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C

L

P

G

E

K

P

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L

L

M

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D

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I

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A

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K

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P

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N

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C

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Y

Y

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G

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T

T

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G

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P

V

V

M

L

T

A

Q

M

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L

L

-

G

-

F

V

A

D

K

D

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|
E

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C

C

I

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G

G

Y

N

N

Q

V

I

M

M

K

K

G

G

Y

Y

Y

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N

N

M

D

P

P

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A

A

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S

A

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V

I

D

D

G

K

D

D

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G

W

W

L

L

H

H

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G

G

D

D

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V

G

G

I

F

M

I

D

D

E

D

H

D

G

D

Y

E

V

L

R

F

I

I

T

V

G

D

R
|
R

I

L

K

K

D

E

M

L

I

I

I

K

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Y

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x
K

G

G

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Q

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Y

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P

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A

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L

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F

L

L

L

Y

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D

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A

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N

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D

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H

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K

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W

F

Y

Y

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K

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I

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N

H

K

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A

F

F

F

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T

S

D

E

S

F

I

P

P

M

K

T

A

A

P

S

S

A

G

K
|
K

I

I

Q

L

K

R

Y

K

K

D

L

L

R

R

E

A

M

R

A

L

A

A

K211 (= K208) mutation to S: Drastically reduces the activity.
M293 (≠ Y286) mutation M->A,P: Affects the substrate specificity.
K320 (≠ I313) mutation K->L,A: Affects the substrate specificity.
E401 (= E392) mutation to Q: Slighlty reduces the substrate specificity.
C403 (≠ V394) mutation to A: Significantly reduces the substrate specificity.
R449 (= R440) mutation to Q: Drastically reduces the activity.
K457 (≠ G448) mutation to S: Drastically reduces the activity.
K540 (= K531) mutation to N: Abolishes the activity.

O74976 Oxalate--CoA ligase; Oxalyl-CoA synthetase; Peroxisomal-coenzyme A synthetase; EC 6.2.1.8 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 92% coverage: 27:534/550 of query aligns to 18:497/512 of O74976

query
sites
O74976

A

A

V

L

V

V

Y

A

V

P

D

S

R

L

D

N

Y

A

R

E

Q

L

T

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Y

F

R

S

E

E

F

L

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R

S

I

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A

V

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D

M

D

D

L

L

A

Q

R

R

G

Q

L

I

M

A

A

S

L

L

G

G

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I

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K

R

V

G

G

D

D

K

P

V

V

A

N

L

I

W

A

A

I

T

P

N

N

V

G

P

L

Y

E

W

F

V

V

A

V

L

A

Q

F

F

Y

A

A

T

V

A

S

K

W

I

Q

G

R

A

A

V

I

L

C

L

G

T

P

V

L

N

N

T

S

N

N

Y

Y

R

K

E

Q

S

S

E

E

L

F

R

E

Y

F

L

Y

L

I

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D

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D

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K

C

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N

L

L

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F

I

I

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G

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A

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A

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N

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-

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-

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-

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A

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T

K

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L

Y

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A

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L

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A

M

W

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P

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G

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R

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L

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C

-

E

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G

-

L

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P

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H

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F

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G

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A

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S283 (≠ P320) modified: Phosphoserine
S284 (≠ E321) modified: Phosphoserine

4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 64% coverage: 193:545/550 of query aligns to 156:505/506 of 4gxqA

query
sites
4gxqA

D

D

V

L

V

A

N

A

M

I

Q

L

Y

Y

T
|
T

S
|
S

G
|
G

T
|
T

G

G

F

R

P

S

K
|
K

G

G

V

A

M

M

L

L

T

S

H

H

V

D

G

N

I

L

G

A

N

S

N
|
N

G

S

Y

L

W

T

I

L

G

V

R

D

N

Y

Q

W

G

R

F

F

T

T

E

P

K

D

D

D

R

V

V

L

C

I

L

H

P

A

V

L

P

P

L

I

F

Y

H
|
H

C
x
T

F
x
H

G

G

C

L

V

F

L

V

G

A

V

S

M

N

A

V

A

T

I

L

N

F

H

A

G

R

A

G

A

S

L

M

V

I

I

F

L

L

E

P

N

K

F

F

N

D

P

P

M

D

H

K

V

I

M

L

A

D

S

L

V

M

D

-

Q

-

E

A

K

R

C

A

T

T

A

V

L

L

Y

M

G

G

V

V

P

P

T

T

M

F

F

Y

L

T

A

R

V

L

L

L

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Q

H

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K

P

L

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L

D

T

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K

F

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D

T

F

T

S

G

S

H

L

M

R

R

T

L

G

-

I

F

M

I

A

S

G

G

S
|
S

V
x
A

C
x
P

P

L

E

L

P

A

L

D

M

T

R

H

R

R

V

E

I

W

E

S

K

A

M

K

N

T

M

G

R

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A

I

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T

L

I
x
E

C
x
R

Y
|
Y

G
|
G

L
x
M

T
|
T

E
|
E

G

-

S

T

P

N

V
x
M

M

N

T

T

Q

S

T

N

L

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Y

D

D

D

G

S

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L

-

E

D

R

R

R

V

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Q

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A

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|
V

G

G

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A

A

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L

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D

D

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P

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G

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K

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G

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D

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I

G

G

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M

V

I

V

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C

V

R

K

G

G

Y

P

N

N

V

V

M

F

K

K

G

G

Y

Y

Y

W

N

R

M

M

P

P

E

E

A

K

T

T

A

K

K

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A

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V

F

D

R

G

D

D

D

G

G

W

F

L

F

H

I

S

T

G

G

D
|
D

L

L

G

G

I

K

M

I

D

D

E

E

H

R

G

G

Y

Y

V

V

R

H

I
|
I

T

L

G

G

R
|
R

I

G

K

K

D

D

M

L

I

V

I
|
I

R

T

G

G

E

F

N
|
N

I

V

Y

Y

P

P

R

K

E

E

I

I

E

E

E

S

F

E

L

I

Y

D

G

A

M

M

E

P

G

G

V

V

Q

V

D

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V

S

Q

A

V

V

V

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G

G

V

V

P

P

S

H

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A

K

D

Y

F

G

G

E

E

E

G

V

V

G

T

A

A

F

F

I

V

P

L

K

K

E

R

G

E

Y

F

-

A

-

P

-

S

D

E

L

I

A

L

P

A

E

E

D

E

V

L

R

K

D

A

H

F

C

V

R

K

G

D

R

R

I

L

S

A

W

K

Y

F

K

K

V

M

P

P

R

K

H

K

I

V

A

I

F

F

V

V

S

D

E

D

F

L

P

P

M

R

T

N

A

T

S

M

A

G

K
x
A

I

V

Q

Q

K

K

Y

N

K

V

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R

R

E

E

M

T

A

Y

A

K

E

D

L

I

F

Y

active site: T163 (= T200), N183 (= N220), H207 (= H244), T303 (= T343), E304 (= E344), I403 (= I446), N408 (= N451), A491 (≠ K531)
binding adenosine-5'-triphosphate: T163 (= T200), S164 (= S201), G165 (= G202), T166 (= T203), T167 (= T204), K171 (= K208), H207 (= H244), S277 (= S317), A278 (≠ V318), P279 (≠ C319), E298 (≠ I338), R299 (≠ C339), Y300 (= Y340), G301 (= G341), M302 (≠ L342), T303 (= T343), V322 (= V365), D382 (= D425), I394 (= I437), R397 (= R440)
binding carbonate ion: H207 (= H244), T208 (≠ C245), H209 (≠ F246), S277 (= S317), R299 (≠ C339), G301 (= G341), M302 (≠ L342), M307 (≠ V348)

Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
29% identity, 98% coverage: 2:539/550 of query aligns to 11:532/541 of Q5SKN9

query
sites
Q5SKN9

D

S

T

T

F

M

A

M

I

D

R

E

E

E

M

L

T

N

L

L

G

W

R

D

I

F

L

L

D

E

E

R

T

A

A

A

K

L

F

F

P

G

D

R

N

K

D

E

A

V

V

V

-

S

-

R

V

L

Y

H

V

T

D

G

R

E

D

V

Y

H

R

R

Q

T

T

T

Y

Y

R

A

E

E

F

V

V

Y

S

Q

V

R

V

A

D

R

L

L

A

M

R

G

G

G

L

L

M

R

A

A

L

L

G

G

V

V

K

G

R

V

G

G

D

D

K

R

V

V

A

A

L

T

W

L

A

G

T

F

N

N

V

H

P

F

Y

R

W

H

V

L

A

E

L

A

Q

Y

F

F

A

A

T

V

A

P

K

G

I

M

G

G

A

A

V

V

L

L

L

H

T

T

V

A

N

N

T

P

N

R

Y

L

R

S

E

P

S

K

E

E

L

I

R

A

Y

Y

L

I

L

L

E

N

Q

H

S

A

E

E

C

D

E

K

N

V

L

L

F

L

I

F

M

-

D

-

G

-

F

-

R

-

D

D

H

P

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T184 (= T200) binding
W234 (≠ C248) binding
G323 (≠ C339) binding
T327 (= T343) binding
E328 (= E344) binding
D418 (= D425) binding
K435 (= K442) binding
K439 (≠ I446) binding
W444 (≠ N451) binding

6qjzA Identificationand characterization of an oxalylfrom grass pea (lathyrus sativuscoa-synthetase l.) (see paper)
28% identity, 94% coverage: 10:525/550 of query aligns to 5:493/504 of 6qjzA

query
sites
6qjzA

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