SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CCNA_03292 FitnessBrowser__Caulo:CCNA_03292 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)
30% identity, 97% coverage: 13:512/517 of query aligns to 3:498/503 of P9WQ37

query
sites
P9WQ37

T

N

I

I

G

G

D

W

I

M

L

L

R
|
R

E

Q

R

R

A

A

R

T

E

V

N

S

P

P

D

-

R
|
R

L

L

A

Q

V

A

V

Y

M

V

E

E

-

P

-

S

T

T

G

D

E

V

A

R

V

M

T

T

Y

Y

A

A

Q

Q

F

M

D

N

A

A

L

L

V

A

D

N

R

R

V

C

A

A

A

D

A

V

L

L

Q

T

R

A

D

L

G

G

V

I

A

A

P

K

G

G

E

D

A

R

V

V

A

A

V

L

C

L

A

M

L

P

S

N

S

S

I

V

P

E

Y

F

A

C

L

L

F

F

L

Y

G

G

A

A

L

A

R

K

A

L

G

G

V

A

A

V

V

A

A

V

P

P

I

I

A

N

P

T

S

R

S

L

T

A

P

A

E

P

S

E

I

V

A

S

G

F

M

I

V

L

A

S

D

D

C

S

G

G

A

S

K

K

L

V

F

V

F

I

-

Y

-

G

-

A

-

P

-

S

-

A

-

P

-

V

L

I

D

D

A

A

G

I

V

R

A

A

E

Q

A

A

Q

D

K

P

P

P

A

G

P

T

V

V

P

T

V

D

R

W

P

-

I

-

A

-

L

I

D

G

G

A

S

D

S

S

A

L

G

A

Q

E

A

R

F

L

D

R

A

S

W

A

L

A

A

A

P

D

E

E

D

P

A

A

T

-

P

-

T

-

P

-

V

V

E

E

I

C

G

G

P

G

K

D

H

D

P

N

F

L

N

F

I

I

I

M

Y

Y

S

T

S

S

G

G

T

T

G

G

T

H

P

P

K
|
K

G

G

I

V

Q

H

S

T

H

H

-

E

-

S

-

V

-

H

-

S

-

A

G

A

M

S

R

S

W

W

K

-

H

-

I

-

F

-

V

-

G

A

D

S

A

T

I

I

G

D

Y

V

G
x
R

H

Y

T
x
R

P

D

V

R

S

L

L

L

S

P

T

L

P

P

L

M

Y

F

S

H

N
x
V

T

A

T
x
A

L

L

V

T

C
x
T

F

V

F

I

P

F

T

S

L

A

A

M

G

R

G

G

G

V

T

T

V

L

V

I

L

S

M

M

K

P

K

Q

F

F

D

D

V

A

V

T

R

K

Y

V

L

W

E

S

L

L

A

I

A

V

K

E

H

E

R
|
R

I

V

T

C

H

I

T

G

M

G

L

A

V

V

P

P

V

A

Q

I

Y

L

R

N

R

F

L

M

M

R

E

Q

H

V

P

P

D

E

F

F

D

A

R

E

Y

L

D

D

L

A

S

P

S

D

T

F

R

R

M

Y

K

F

F

I

C

T

T

G

S

G

A

A

P

P

F

M

-

P

A

E

A

A

D

L

L

I

K

K

A

I

Q

Y

V

A

L

A

K

K

R

N

W

I

P

E

G

-

L

V

V

V

E

Q

Y

G

F

Y

G
x
A

M

L

T

T

E

E

-

S

-

C

G

G

T

T

C

-

I

L

L

L

M

L

A

S

H

E

E

D

H

A

P

L

D

R

K

K

L

A

H

G

T

S

V

A

G

G

R

R

P

A

A

T

P

M

G

F

H

T

D

D

I

V

R

A

L

V

V

R

D

G

E

D

D

D

G

G

-

V

-

I

R

R

Q

E

V

H

G

G

P

E

G

G

V

-

G

-

E

E

I

V

V

V

G

I

R

K

S

S

A

D

S

I

M

L

N

K

G

E

Y

Y

H

W

G

N

R

R

P

P

D

E

K

A

T

T

A

R

E

D

A

A

T

F

W

-

V

-

S

-

P

D

E

N

G

G

W
|
W

T

-

F

-

I

F

R

R

T

T

G

G

D
|
D

V

I

G

G

R

E

F

I

D

D

E

D

E

E

G

G

F

Y

L

L

T

Y

L

I

M

K

D

D

R
|
R

K

L

K

K

D

D

M

M

I

I

S
|
S

G

G

G
|
G

F

E

N

N

I

V

Y

Y

P

P

S

A

D

E

L

I

E

E

A

S

V

V

L

I

V

I

Q

G

H

V

P

P

A

G

V

V

F

S

E

E

A

V

A

A

V

V

V

I

G

G

V

L

P

P

S

D

D

E

A

K

W

W

G

G

E

E

T

I

P

A

V

A

A

A

F

I

V

V

A

V

L

A

K

D

S

Q

S

N

Q

E

V

V

A

S

E

E

A

Q

D

Q

A

I

I

V

K

E

T

-

F

Y

V

C

N

G

G

T

Q

R

V

L

G

A

K

R

T

Y

Q

K

R

L

L

P

A

K

E

K

V

V

V

I

V

F

V

A

D

E

S

A

L

I

P

P

R

R

S

N

H

P

I

T

G

G

K
|
K

V

I

L

L

K

K

R

T

E

V

L

L

R

R

D

E

S

Q

W

Y

Q

S

R9 (= R19) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
R17 (= R28) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
K172 (= K180) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
R195 (≠ G202) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
R197 (≠ T204) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
V209 (≠ N216) 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 (≠ T218) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
T214 (≠ C221) 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 (= R251) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
A302 (≠ G310) 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 (= W388) 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 (= D395) 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 (= R410) mutation to A: Reduction of binding affinity for fatty acids.
S404 (= S417) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
G406 (= G419) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
K487 (= K501) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.

Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 92% coverage: 34:508/517 of query aligns to 55:542/559 of Q67W82

query
sites
Q67W82

E

Q

T

T

G

G

E

A

A

V

V

Y

T

S

Y

Y

A

G

Q

E

F

V

D

E

A

E

L

L

V

S

D

R

R

R

V

A

A

A

A

G

L

L

Q

R

R

R

D

L

G

G

V

V

A

G

P

K

G

G

E

D

A

V

V

V

A

M

V

S

C

L

A

L

L

R

S

N

S

C

I

P

P

E

Y

F

A

A

A

F

L

T

F

F

L

L

G

G

A

A

L

A

R

R

A

L

G

G

V

A

A

A

V

T

A

T

P

T

I

A

A

N

P

P

S

F

S

Y

T

T

P

P

E

H

S

E

I

I

A

H

G

R

M

Q

V

A

A

S

D

A

C

A

G

G

A

A

K

R

L

V

F

I

F

V

L

T

D

E

A

A

G

C

V

A

A

V

E

E

-

K

-

V

-

R

-

G

-

F

-

A

A

A

Q

D

K

R

P

G

A

I

P

P

V

V

P

-

V

-

R

-

P

-

I

V

A

A

L

V

D

D

G

G

S

D

S

F

A

D

G

G

-

C

-

V

-

G

-

F

-

G

-

E

Q

A

A

M

F

L

D

D

A

A

W

S

L

I

A

E

P

P

E

L

D

D

A

A

T

D

P

E

T

-

P

-

V

-

E

E

I

V

G

H

P

P

K

D

H

D

P

V

F

V

N

A

I

L

I

P

Y

Y

S

S

G

G

T

T

G

G

T

L

P

P

K

K

G

G

I

V

I

M

Q

L

S

T

H

H

G

-

M

-

R

R

W

S

K

L

H

V

I

T

F

S

V

V

G

A

D

Q

A

Q

I

V

G

D

Y

-

G

G

H

E

T

N

P

P

-

N

-

L

-

Y

-

F

-

R

-

E

-

D

V

V

S

V

L

L

L

C

S

L

T

L

P

P

L

L

Y

F

S

H

N

I

T

Y

T

S

L

L

-

N

V

S

C

V

F

L

P

A

T

G

L

L

A

R

G

A

G

G

G

S

T

A

V

I

V

V

L

I

M

M

K

R

K

K

F

F

D

D

V

L

V

G

R

A

Y

L

L

V

E

D

L

L

A

T

A

R

K

R

H

H

R

G

I

V

T

T

H

V

T

A

M

P

L

F

V

V

P

P

V

P

Q

I

Y

V

R

V

R

E

L

I

M

A

E

K

H

S

P

P

D

R

F

V

D

T

R

A

Y

D

D

D

L

L

S

A

S

S

T

I

R

R

M

M

K

V

F

M

C

S

T

G

S

A

A

A

P

P

F

M

A

G

A

K

D

D

L

L

K

Q

A

D

Q

A

V

F

L

M

K

A

R

K

W

I

P

P

G

N

G

A

L

V

V

L

-

G

E

Q

Y

G

F

Y

G

G

M

M

T

T

E

E

G

A

G

G

-

P

-

V

-

L

G

A

T

M

C

C

I

L

L

A

M

F

A

A

H

K

E

E

H

P

P

F

D

E

-

V

K

K

L

S

H

G

T

S

V

C

G

G

R

T

P

V

A

V

P

R

G

N

H

A

D

E

I

L

R

K

L

I

V

V

D

D

E

P

D

D

-

T

G

G

R

A

Q

T

V

L

G

G

P

R

G

N

V

Q

V

S

G
|
G

E

E

I

I

V

C

G

I

R

R

S

G

A

E

S

Q

M

I

M

M

N

K

G

G

Y

Y

H

L

G

N

R

D

P

P

D

E

K

S

T

T

A

K

E

N

A

T

T

-

W

-

V

I

S

D

P

K

E

G

G

G

W

W

T

-

F

-

I

L

R

H

T

T

G

G

D

D

V

I

G

G

R

Y

F

V

D

D

E

D

G

D

F

E

L

I

T

F

L

I

M

V

D

D

R

R

K

L

K

K

D

E

M

I

I

I

I

K

S

Y

G

K

G

G

F

F

N

Q

I

V

Y

P

P

P

S

A

D

E

L

L

E

E

A

A

V

L

L

L

V

I

Q

T

H

H

P

P

A

D

V

I

F

K

E

D

A

A

V

V

G

P

V

M

P

I

S

D

D

E

A

I

W

A

G

G

E

E

T

V

P

P

V

V

A

A

F

F

V

I

A

V

L

R

K

I

S

E

S

G

Q

S

V

A

A

I

E

S

A

E

D

N

A

E

I

I

K

K

T

Q

F

F

V

V

N

A

G

K

Q

E

V

V

G

V

K

F

T

Y

Q

K

R

R

L

L

A

N

E

K

V

V

V

F

V

A

D

D

S

S

L

I

P

P

R

K

S

S

H

P

I

S

G

G

K

K

V

I

L

L

K

R

R

K

E

D

L

L

R

R

G395 (= G357) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.

3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 92% coverage: 35:510/517 of query aligns to 42:528/528 of 3ni2A

query
sites
3ni2A

T

N

G

G

E

D

A

V

V

Y

T

T

Y

Y

A

A

Q

D

F

V

D

E

A

L

L

T

V

A

D

R

R

R

V

V

A

A

A

S

A

G

L

L

Q

N

R

K

D

I

G

G

V

I

A

Q

P

Q

G

G

E

D

A

V

V

I

A

M

V

L

C

F

A

L

L

P

S

S

I

P

P

E

Y

F

A

V

A

L

L

A

F

F

L

L

G

G

A

A

L

S

R

H

A

R

G

G

V

A

A

I

V

I

A

T

P

A

I

A

A

N

P

P

S

F

S

S

T

T

P

P

E

A

S

E

I

L

A

A

G

K

M

H

V

A

A

K

D

A

C

S

G

R

A

A

K

K

L

L

F

L

F

I

L

T

D

Q

A

A

G

C

V

Y

A

Y

E

E

A

K

Q

V

K

K

-

D

-

F

P

A

A

R

P

E

V

S

P

D

V

V

R

K

P

V

I

M

A

C

L

V

D

D

G

S

S

A

S

P

A

D

G

G

Q

C

A

L

F

H

D

F

A

S

W

E

L

L

A

T

P

Q

E

A

D

D

A

E

T

N

P

E

T

A

P

P

-

Q

V

V

E

D

I

I

G

S

P

P

K

D

H

D

P

V

F

V

N

A

I

L

I

P

Y

Y

S
|
S

S

S

G

G

T

T

G

G

T

L

P

P

K

K

G

G

I

V

I

M

Q

L

S

T

H

H

G

K

M

G

R

L

W

I

K

T

H
x
S

I

V

-

A

-

Q

F

V

V

D

G

G

D

D

A

N

I

P

G

N

-

L

Y

Y

G

F

H

H

T

S

P

E

-

D

V

V

S

I

L

L

L

C

S

V

T

L

P

P

L

M

Y

F

S
x
H

-
x
I

-
x
Y

-

A

-

L

N

N

T
x
S

T

I

L

M

V

L

C

C

F

-

P

-

T

G

L

L

A

R

G

V

G

G

G

A

T

P

V

I

V

L

L

I

M

M

K

P

K

K

F

F

D

E

V

I

V

G

R

S

Y

L

L

L

E

G

L

L

A

I

A

E

K

K

H

Y

R

K

I

V

T

S

H

I

T

A

M

P

L

V

V

V

P

P

V

P

Q

V

Y

M

R

M

R

S

L

I

M

A

E

K

H

S

P

P

D

D

F

L

D

D

R

K

Y

H

D

D

L

L

S

S

T

L

R

R

M

M

K

I

F
x
K

C

S

T
x
G

S
x
G

A
|
A

P
|
P

F

L

A

G

A

K

D

E

L

L

K

E

A

D

Q

T

V

V

L

R

K

A

R

K

W

F

P

P

G

Q

G

A

-

R

L

L

V

G

E
x
Q

Y
x
G

F
x
Y

G
|
G

M
|
M

T
|
T

E
|
E

G

A

G

G

-
x
P

-
x
V

-

L

G

A

T

M

C

C

I

L

L

A

M

F

A

A

H

K

E

E

-

P

-

F

-

D

-

I

H

K

P

P

D

G

K

A

L

C

H

G

T

T

V

V

G

V

R

R

P

N

A

A

P

-

G

-

H

-

D

E

I

M

R

K

L

I

V

V

D

D

-

P

E

E

D

T

G

G

R

A

Q

S

V

L

G

P

P

R

G

N

V

Q

V

P

G

G

E

E

I

I

V

C

G

I

R

R

S

G

A

D

S

Q

M

I

M

M

N

K

G

G

Y

Y

H

L

G

N

R

D

P

P

D

E

K

A

T

T

A

S

E

R

A

T

T

-

W

-

V

I

S

D

P

K

E

E

G

G

W

W

T

L

F

H

I

T

R

G

T
x
D

G

I

D

G

V

Y

G

I

R

D

F

D

D

D

E

D

E

E

G

L

F

F

L
x
I

T

-

L

-

M

V

D

D

R
|
R

K

L

K
|
K

D

E

M

L

I

I

I
x
K

S

Y

G

K

G

G

F

F

N
x
Q

I

V

Y

A

P

P

S

A

D

E

L

L

E

E

A

A

V

L

L

L

V

I

Q

A

H

H

P

P

A

E

V

I

F

S

E

D

A

A

V

V

G

G

V

L

P

K

S

D

D

E

A

D

W

A

G

G

E

E

T

V

P

P

V

V

A

A

F

F

V

V

A

V

L

K

K

S

S

E

S

K

Q

S

V

Q

A

A

E

T

A

E

D

D

A

E

I

I

K

K

T

Q

F

Y

V

I

N

S

G

K

Q

Q

V

V

G

I

K

F

T

Y

Q

K

R

R

L

I

A

K

E

R

V

V

V

F

V

I

D

E

S

A

L

I

P

P

R

K

S

A

H

P

I

S

G

G

K
|
K

V

I

L

L

K

R

R

K

E

N

L

L

R

K

D

E

S

K

active site: S182 (= S172), S202 (≠ H192), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: I231 (vs. gap), Y232 (vs. gap), S236 (≠ T217), K299 (≠ F283), G301 (≠ T285), G302 (≠ S286), A303 (= A287), P304 (= P288), Q324 (≠ E307), G325 (≠ Y308), Y326 (≠ F309), G327 (= G310), M328 (= M311), T329 (= T312), P333 (vs. gap), V334 (vs. gap), D413 (≠ T393), I425 (≠ L405), R428 (= R410), K430 (= K412), K434 (≠ I416), Q439 (≠ N421)

3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
31% identity, 92% coverage: 35:510/517 of query aligns to 42:528/528 of 3a9vA

query
sites
3a9vA

T

N

G

G

E

D

A

V

V

Y

T

T

Y

Y

A

A

Q

D

F

V

D

E

A

L

L

T

V

A

D

R

R

R

V

V

A

A

A

S

A

G

L

L

Q

N

R

K

D

I

G

G

V

I

A

Q

P

Q

G

G

E

D

A

V

V

I

A

M

V

L

C

F

A

L

L

P

S

S

I

P

P

E

Y

F

A

V

A

L

L

A

F

F

L

L

G

G

A

A

L

S

R

H

A

R

G

G

V

A

A

I

V

I

A

T

P

A

I

A

A

N

P

P

S

F

S

S

T

T

P

P

E

A

S

E

I

L

A

A

G

K

M

H

V

A

A

K

D

A

C

S

G

R

A

A

K

K

L

L

F

L

F

I

L

T

D

Q

A

A

G

C

V

Y

A

Y

E

E

A

K

Q

V

K

K

-

D

-

F

P

A

A

R

P

E

V

S

P

D

V

V

R

K

P

V

I

M

A

C

L

V

D

D

G

S

S

A

S

P

A

D

G

G

Q

C

A

L

F

H

D

F

A

S

W

E

L

L

A

T

P

Q

E

A

D

D

A

E

T

N

P

E

T

A

P

P

-

Q

V

V

E

D

I

I

G

S

P

P

K

D

H

D

P

V

F

V

N

A

I

L

I

P

Y

Y

S
|
S

S

S

G

G

T

T

G

G

T

L

P

P

K

K

G

G

I

V

I

M

Q

L

S

T

H

H

G

K

M

G

R

L

W

I

K

T

H
x
S

I

V

-

A

-

Q

F

V

V

D

G

G

D

D

A

N

I

P

G

N

-

L

Y

Y

G

F

H

H

T

S

P

E

-

D

V

V

S

I

L

L

L

C

S

V

T

L

P

P

L

M

Y

F

S
x
H

-

I

-

Y

-

A

-

L

N

N

T

S

T

I

L

M

V

L

C

C

F

-

P

-

T

G

L

L

A

R

G

V

G

G

G

A

T

P

V

I

V

L

L

I

M

M

K

P

K

K

F

F

D

E

V

I

V

G

R

S

Y

L

L

L

E

G

L

L

A

I

A

E

K

K

H

Y

R

K

I

V

T

S

H

I

T

A

M

P

L

V

V

V

P

P

V

P

Q

V

Y

M

R

M

R

S

L

I

M

A

E

K

H

S

P

P

D

D

F

L

D

D

R

K

Y

H

D

D

L

L

S

S

T

L

R

R

M

M

K

I

F

K

C

S

T

G

S
x
G

A
|
A

P
|
P

F

L

A

G

A

K

D

E

L

L

K

E

A

D

Q

T

V

V

L

R

K

A

R

K

W

F

P

P

G

Q

G

A

-

R

L

L

V

G

E

Q

Y
x
G

F
x
Y

G
|
G

M
|
M

T
|
T

E
|
E

G

A

G

G

-

P

-

V

-

L

G

A

T

M

C

C

I

L

L

A

M

F

A

A

H

K

E

E

-

P

-

F

-

D

-

I

H

K

P

P

D

G

K

A

L

C

H

G

T

T

V

V

G

V

R

R

P

N

A

A

P

-

G

-

H

-

D

E

I

M

R

K

L

I

V

V

D

D

-

P

E

E

D

T

G

G

R

A

Q

S

V

L

G

P

P

R

G

N

V

Q

V

P

G

G

E

E

I

I

V

C

G

I

R

R

S

G

A

D

S

Q

M

I

M

M

N

K

G

G

Y

Y

H

L

G

N

R

D

P

P

D

E

K

A

T

T

A

S

E

R

A

T

T

-

W

-

V

I

S

D

P

K

E

E

G

G

W

W

T

L

F

H

I

T

R

G

T
x
D

G

I

D

G

V

Y

G

I

R

D

F

D

D

D

E

D

E

E

G

L

F

F

L
x
I

T

-

L

-

M

V

D

D

R
|
R

K

L

K
|
K

D

E

M

L

I

I

I
x
K

S

Y

G

K

G

G

F

F

N
x
Q

I

V

Y

A

P

P

S

A

D

E

L

L

E

E

A

A

V

L

L

L

V

I

Q

A

H

H

P

P

A

E

V

I

F

S

E

D

A

A

V

V

G

G

V

L

P

K

S

D

D

E

A

D

W

A

G

G

E

E

T

V

P

P

V

V

A

A

F

F

V

V

A

V

L

K

K

S

S

E

S

K

Q

S

V

Q

A

A

E

T

A

E

D

D

A

E

I

I

K

K

T

Q

F

Y

V

I

N

S

G

K

Q

Q

V

V

G

I

K

F

T

Y

Q

K

R

R

L

I

A

K

E

R

V

V

V

F

V

I

D

E

S

A

L

I

P

P

R

K

S

A

H

P

I

S

G

G

K
|
K

V

I

L

L

K

R

R

K

E

N

L

L

R

K

D

E

S

K

active site: S182 (= S172), S202 (≠ H192), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
binding adenosine monophosphate: H230 (≠ S215), G302 (≠ S286), A303 (= A287), P304 (= P288), G325 (≠ Y308), Y326 (≠ F309), G327 (= G310), M328 (= M311), T329 (= T312), D413 (≠ T393), I425 (≠ L405), R428 (= R410), K430 (= K412), K434 (≠ I416), Q439 (≠ N421)

3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
30% identity, 97% coverage: 13:512/517 of query aligns to 6:498/502 of 3r44A

query
sites
3r44A

T
x
N

I
|
I

G

G

D

W

I

M

L

L

R

R

E

Q

R

R

A

A

R

T

E

V

N

S

P

P

D

-

R

R

L

L

A

Q

V

A

V

Y

M

V

E

E

-

P

-

S

T

T

G

D

E

V

A

R

V

M

T

T

Y

Y

A

A

Q

Q

F

M

D

N

A

A

L

L

V

A

D

N

R

R

V

C

A

A

A

D

A

V

L

L

Q

T

R

A

D

L

G

G

V

I

A

A

P

K

G

G

E

D

A

R

V

V

A

A

V

L

C

L

A

M

L

P

S

N

S

S

I

V

P

E

Y

F

A

C

L

L

F

F

L

Y

G

G

A

A

L

A

R

K

A

L

G

G

V

A

A

V

V

A

A

V

P

P

I

I

A

N

P

T

S

R

S

L

T

A

P

A

E

P

S

E

I

V

A

S

G

F

M

I

V

L

A

S

D

D

C

S

G

G

A

S

K

K

L

V

F

V

F

I

-

Y

-

G

-

A

-

P

-

S

-

A

-

P

-

V

L

I

D

D

A

A

G

I

V

R

A

A

E

Q

A

A

Q

D

K

P

P

P

A

G

P

T

V

V

P

T

V

D

R

W

P

-

I

-

A

-

L

I

D

G

G

A

S

D

S

S

A

L

G

A

Q

E

A

R

F

L

D

R

A

S

W

A

L

A

A

A

P

D

E

E

D

P

A

A

T

-

P

-

T

-

P

-

V

V

E

E

I

C

G

G

P

G

K

D

H

D

P

N

F

L

N

F

I

I

I

M

Y

Y

S

-

G

-

T
|
T

T

S

G

G

T

H

P

P

K

K

G

G

I

V

Q

H

S

T

H
|
H

-
x
E

-

S

-

V

-
x
H

-

S

-
x
A

G

A

M

S

R

S

W

W

K

-

H

-

I

-

F

-

V

-

G

A

D

S

A

T

I

I

G

D

Y

V

G

R

H

Y

T

R

P

D

V

R

S

L

L

L

S

P

T

L

P

P

L

M

Y

F

S
x
H

N

V

T

A

L

L

V

T

C

T

F

V

F

I

P

F

T

S

L

A

A

M

G

R

G

G

G

V

T

T

V

L

V

I

L

S

M

M

K

P

K

Q

F

F

D

D

V

A

V

T

R

K

Y

V

L

W

E

S

L

L

A

I

A

V

K

E

H

E

R

R

I

V

T

C

H

I

T

G

M

G

L

A

V

V

P

P

V

A

Q

I

Y

L

R

N

R

F

L

M

M

R

E

Q

H

V

P

P

D

E

F

F

D

A

R

E

Y

L

D

D

L

A

S

P

S

D

T

F

R

R

M

Y

K

F

F

I

C

T

T

G

S

G

A

A

P

P

F

M

-

P

A

E

A

A

D

L

L

I

K

K

A

I

Q

Y

V

A

L

A

K

K

R

N

W

I

P

E

G

-

L

V

V

V

E

Q

Y

G

F

Y

G

A

M

L

T
|
T

E
|
E

-

S

-

C

G

G

T

T

C

-

I

L

L

L

M

L

A

S

H

E

E

D

H

A

P

L

D

R

K

K

L

A

H

G

T

S

V

A

G

G

R

R

P

A

A

T

P

M

G

F

H

T

D

D

I

V

R

A

L

V

V

R

D

G

E

D

D

D

G

G

-

V

-

I

R

R

Q

E

V

H

G

G

P

E

G

G

V

-

G

-

E

E

I

V

V

V

G

I

R

K

S

S

A

D

S

I

M

L

N

K

G

E

Y

Y

H

W

G

N

R

R

P

P

D

E

K

A

T

T

A

R

E

D

A

A

T

F

W

-

V

-

S

-

P

D

E

N

G

G

W

W

T

-

F

-

I

F

R

R

T

T

G

G

D

D

V

I

G

G

R

E

F

I

D

D

E

D

E

E

G

G

F

Y

L

L

T

Y

L

I

M

K

D

D

R

R

K

L

K

K

D

D

M

M

I

I

I
|
I

S

S

G

G

F

E

N
|
N

I

V

Y

Y

P

P

S

A

D

E

L

I

E

E

A

S

V

V

L

I

V

I

Q

G

H

V

P

P

A

G

V

V

F

S

E

E

A

V

A

A

V

V

V

I

G

G

V

L

P

P

S

D

D

E

A

K

W

W

G

G

E

E

T

I

P

A

V

A

A

A

F

I

V

V

A

V

L

A

K

D

S

Q

S

N

Q

E

V

V

A

S

E

E

A

Q

D

Q

A

I

I

V

K

E

T

-

F

Y

V

C

N

G

G

T

Q

R

V

L

G

A

K

R

T

Y

Q

K

R

L

L

P

A

K

E

K

V

V

V

I

V

F

V

A

D

E

S

A

L

I

P

P

R

R

S

N

H

P

I

T

G

G

K
|
K

V

I

L

L

K

K

R

T

E

V

L

L

R

R

D

E

S

Q

W

Y

Q

S

active site: T167 (= T175), A184 (vs. gap), H208 (≠ S215), T304 (= T312), E305 (= E313), I403 (= I416), N408 (= N421), K487 (= K501)
binding histidine: N6 (≠ T13), I7 (= I14), H178 (= H186), E179 (vs. gap), H182 (vs. gap)

Sites not aligning to the query:

binding histidine: 4, 5

O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 54:533/542 of O24146

query
sites
O24146

T

T

Y

Y

A

A

Q

D

F

V

D

E

A

L

L

N

V

S

D

R

R

K

V

V

A

A

A

G

L

L

Q

H

R

K

D

Q

G

G

V

I

A

Q

P

P

G

K

E

D

A

T

V

I

A

M

V

I

C

L

A

L

L

P

S

N

S

S

I

P

P

E

Y

F

A

V

A

F

L

A

F

F

L

I

G

G

A

A

L

S

R

Y

A

L

G

G

V

A

A

I

V

S

A

T

P

M

I

A

A

N

P

P

S

L

S

F

T

T

P

P

E

A

S

E

I

V

A

V

G

K

M

Q

V

A

A

K

D

A

C

S

G

S

A

A

K

K

L

I

F

I

F

V

L

T

D

Q

A

A

G

C

V

H

A

V

E

N

A

K

Q

V

K

K

P

D

A

Y

P

A

V

F

P

E

-

N

-

D

V

V

R

K

P

I

I

I

A

C

L

I

D

D

G

S

S

A

S

P

A

E

G

G

Q

C

A

L

F

H

D

F

A

S

W

V

L

L

A

T

P

Q

E

A

D

N

A

E

T

H

P

D

T

I

P

P

-

E

V

V

E

E

I

I

G

Q

P

P

K

D

H

D

P

V

F

V

N

A

I

L

I

P

Y

Y

S
|
S

G
|
G

T
|
T

G

G

T

L

P

P

K
|
K

G

G

I

V

I

M

Q

L

S

T

H

H

-

K

G

G

M

L

R

V

W

T

-

S

-

V

-

A

K

Q

H

Q

I

V

F

D

V

G

G

E

D

N

A

P

I

N

G

L

Y

Y

G

I

H

H

T

S

P

E

-

D

V

V

S

M

L

L

L

C

S

V

T

L

P

P

L

L

Y

F

S
x
H

-

I

-
x
Y

-

S

-

L

N

N

T
x
S

T

V

L

L

V

L

C

C

F

-

P

-

T

G

L

L

A

R

G

V

G

G

G

A

T

A

V

I

V

L

L

I

M

M

K

Q

K
|
K

F

F

D

D

V

I

V

V

R

S

Y

F

L

L

E

E

L

L

A

I

A

Q

K

R

H

Y

R

K

I

V

T

T

H

I

T

G

M

P

L

F

V

V

P

P

V

P

Q

I

Y

V

R

L

R

A

L

I

M

A

E

K

H

S

P

P

D

M

F

V

D

D

R

D

Y

Y

D

D

L

L

S

S

T

V

R

R

M

T

K

V

F

M

C

S

T

G

S
x
A

A

A

P

P

F

L

A

G

A

K

D

E

L

L

K

E

A

D

Q

T

V

V

L

R

K

A

R

K

W

F

P

P

G

N

G

A

-

K

L

L

V

G

E
x
Q

Y
x
G

F

Y

G

G

M

M

T
|
T

E

E

G

A

G

G

-

P

-
x
V

-

L

G

A

T
x
M

C

C

I

L

L

A

M

F

A

A

H

K

E

E

H

-

P

P

D

F

K

E

L

I

H

K

T

S

-

G

-

A

V

C

G

G

R

T

P

V

A

V

P

R

G

N

H

A

D

E

I

M

R

K

L

I

V

V

D

D

-

P

E

K

D

T

G

G

R

N

Q

S

V

L

G

P

P

R

G

N

V

Q

V

S

G

G

E

E

I

I

V

C

G

I

R

R

S

G

A

D

S

Q

M

I

M

M

N

K

G

G

Y

Y

H

L

G

N

R

D

P

P

D

E

K

A

T

T

A

A

E

R

A

T

T

-

W

-

V

I

S

D

P

K

E

E

G

G

W

W

T

L

F

Y

I

T

R

G

T
x
D

G

I

D

G

V

Y

G

I

R

D

F

D

D

D

E

D

E

E

G

L

F

F

L

I

T

-

L

-

M

V

D

D

R
|
R

K

L

K
|
K

D

E

M

L

I

I

I
x
K

S

Y

G
x
K

G
|
G

F

F

N
x
Q

I

V

Y

A

P

P

S

A

D

E

L

L

E

E

A

A

V

L

L

L

V

L

Q

N

H

H

P

P

A

N

V

I

F

S

E

D

A

A

V

V

G

P

V

M

P

K

S

D

D

E

A

Q

W

A

G

G

E

E

T

V

P

P

V

V

A

A

F

F

V

V

A

V

L

R

K

S

S

N

S

G

Q

S

V

T

A

I

E

T

A

E

D

D

A

E

I

V

K

K

T

D

F

F

V

I

N

S

G

K

Q

Q

V

V

G

I

K

F

T

Y

Q

K

R

R

L

I

A

K

E

R

V

V

V

F

V

V

D

D

S

A

L

I

P

P

R

K

S

S

H

P

I

S

G

G

K
|
K

V

I

L

L

K

R

R

K

E

D

L

L

R

R

S189 (= S172) binding
S190 (= S173) binding
G191 (= G174) binding
T192 (= T175) binding
T193 (= T176) binding ; mutation to A: Reduced activity against 4-coumarate.
K197 (= K180) binding ; mutation to A: Reduced activity against 4-coumarate.
H237 (≠ S215) mutation to A: Strongly reduced activity against 4-coumarate.
Y239 (vs. gap) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
S243 (≠ T217) binding ; binding ; binding
K260 (= K237) binding
A309 (≠ S286) binding ; binding ; binding
Q331 (≠ E307) binding
G332 (≠ Y308) binding ; binding ; binding ; binding ; binding
T336 (= T312) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
V341 (vs. gap) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
M344 (≠ T317) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
D420 (≠ T393) binding ; binding ; binding ; binding ; binding
R435 (= R410) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
K437 (= K412) binding ; binding ; binding ; binding
K441 (≠ I416) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
K443 (≠ G418) binding ; mutation to A: Normal activity against 4-coumarate.
G444 (= G419) binding
Q446 (≠ N421) binding
K526 (= K501) binding ; mutation to A: Abolished activity against 4-coumarate.

5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 47:526/530 of 5bsmA

query
sites
5bsmA

T

T

Y

Y

A

A

Q

D

F

V

D

E

A

L

L

N

V

S

D

R

R

K

V

V

A

A

A

G

L

L

Q

H

R

K

D

Q

G

G

V

I

A

Q

P

P

G

K

E

D

A

T

V

I

A

M

V

I

C

L

A

L

L

P

S

N

S

S

I

P

P

E

Y

F

A

V

A

F

L

A

F

F

L

I

G

G

A

A

L

S

R

Y

A

L

G

G

V

A

A

I

V

S

A

T

P

M

I

A

A

N

P

P

S

L

S

F

T

T

P

P

E

A

S

E

I

V

A

V

G

K

M

Q

V

A

A

K

D

A

C

S

G

S

A

A

K

K

L

I

F

I

F

V

L

T

D

Q

A

A

G

C

V

H

A

V

E

N

A

K

Q

V

K

K

P

D

A

Y

P

A

V

F

P

E

-

N

-

D

V

V

R

K

P

I

I

I

A

C

L

I

D

D

G

S

S

A

S

P

A

E

G

G

Q

C

A

L

F

H

D

F

A

S

W

V

L

L

A

T

P

Q

E

A

D

N

A

E

T

H

P

D

T

I

P

P

-

E

V

V

E

E

I

I

G

Q

P

P

K

D

H

D

P

V

F

V

N

A

I

L

I

P

Y

Y

S
|
S

G
|
G

T
|
T

G

G

T

L

P

P

K
|
K

G

G

I

V

I

M

Q

L

S

T

H

H

-

K

G

G

M

L

R

V

W

T

-
x
S

-

V

-

A

K

Q

H

Q

I

V

F

D

V

G

G

E

D

N

A

P

I

N

G

L

Y

Y

G

I

H

H

T

S

P

E

-

D

V

V

S

M

L

L

L

C

S

V

T

L

P

P

L

L

Y

F

S
x
H

-

I

-

Y

-

S

-

L

N

N

T

S

T

V

L

L

V

L

C

C

F

-

P

-

T

G

L

L

A

R

G

V

G

G

G

A

T

A

V

I

V

L

L

I

M

M

K

Q

K

K

F

F

D

D

V

I

V

V

R

S

Y

F

L

L

E

E

L

L

A

I

A

Q

K

R

H

Y

R

K

I

V

T

T

H

I

T

G

M

P

L

F

V

V

P

P

V

P

Q

I

Y

V

R

L

R

A

L

I

M

A

E

K

H

S

P

P

D

M

F

V

D

D

R

D

Y

Y

D

D

L

L

S

S

T

V

R

R

M

T

K

V

F

M

C

S

T

G

S
x
A

A
|
A

P
|
P

F

L

A

G

A

K

D

E

L

L

K

E

A

D

Q

T

V

V

L

R

K

A

R

K

W

F

P

P

G

N

G

A

-

K

L

L

V

G

E
x
Q

Y
x
G

F
x
Y

G
|
G

M
|
M

T
|
T

E
|
E

G

A

G

G

-

P

-

V

-

L

G

A

T

M

C

C

I

L

L

A

M

F

A

A

H

K

E

E

H

-

P

P

D

F

K

E

L

I

H

K

T

S

-

G

-

A

V

C

G

G

R

T

P

V

A

V

P

R

G

N

H

A

D

E

I

M

R

K

L

I

V

V

D

D

-

P

E

K

D

T

G

G

R

N

Q

S

V

L

G

P

P

R

G

N

V

Q

V

S

G

G

E

E

I

I

V

C

G

I

R

R

S

G

A

D

S

Q

M

I

M

M

N

K

G

G

Y

Y

H

L

G

N

R

D

P

P

D

E

K

A

T

T

A

A

E

R

A

T

T

-

W

-

V

I

S

D

P

K

E

E

G

G

W

W

T

L

F

Y

I

T

R

G

T
x
D

G

I

D

G

V

Y

G

I

R

D

F

D

D

D

E

D

E

E

G

L

F

F

L
x
I

T

-

L

-

M

V

D

D

R
|
R

K

L

K

K

D

E

M

L

I

I

I
x
K

S

Y

G

K

G

G

F

F

N
x
Q

I

V

Y

A

P

P

S

A

D

E

L

L

E

E

A

A

V

L

L

L

V

L

Q

N

H

H

P

P

A

N

V

I

F

S

E

D

A

A

V

V

G

P

V

M

P

K

S

D

D

E

A

Q

W

A

G

G

E

E

T

V

P

P

V

V

A

A

F

F

V

V

A

V

L

R

K

S

S

N

S

G

Q

S

V

T

A

I

E

T

A

E

D

D

A

E

I

V

K

K

T

D

F

F

V

I

N

S

G

K

Q

Q

V

V

G

I

K

F

T

Y

Q

K

R

R

L

I

A

K

E

R

V

V

V

F

V

V

D

D

S

A

L

I

P

P

R

K

S

S

H

P

I

S

G

G

K
|
K

V

I

L

L

K

R

R

K

E

D

L

L

R

R

active site: S182 (= S172), S202 (vs. gap), H230 (≠ S215), T329 (= T312), E330 (= E313), K434 (≠ I416), Q439 (≠ N421), K519 (= K501)
binding adenosine-5'-triphosphate: S182 (= S172), S183 (= S173), G184 (= G174), T185 (= T175), T186 (= T176), K190 (= K180), H230 (≠ S215), A302 (≠ S286), A303 (= A287), P304 (= P288), Q324 (≠ E307), G325 (≠ Y308), Y326 (≠ F309), G327 (= G310), M328 (= M311), T329 (= T312), D413 (≠ T393), I425 (≠ L405), R428 (= R410), K519 (= K501)

5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 46:525/528 of 5bsrA

query
sites
5bsrA

T

T

Y

Y

A

A

Q

D

F

V

D

E

A

L

L

N

V

S

D

R

R

K

V

V

A

A

A

G

L

L

Q

H

R

K

D

Q

G

G

V

I

A

Q

P

P

G

K

E

D

A

T

V

I

A

M

V

I

C

L

A

L

L

P

S

N

S

S

I

P

P

E

Y

F

A

V

A

F

L

A

F

F

L

I

G

G

A

A

L

S

R

Y

A

L

G

G

V

A

A

I

V

S

A

T

P

M

I

A

A

N

P

P

S
x
L

S

F

T

T

P

P

E

A

S

E

I

V

A

V

G

K

M

Q

V

A

A

K

D

A

C

S

G

S

A

A

K

K

L

I

F

I

F

V

L

T

D

Q

A

A

G

C

V

H

A

V

E

N

A

K

Q

V

K

K

P

D

A

Y

P

A

V

F

P

E

-

N

-

D

V

V

R

K

P

I

I

I

A

C

L

I

D

D

G

S

S

A

S

P

A

E

G

G

Q

C

A

L

F

H

D

F

A

S

W

V

L

L

A

T

P

Q

E

A

D

N

A

E

T

H

P

D

T

I

P

P

-

E

V

V

E

E

I

I

G

Q

P

P

K

D

H

D

P

V

F

V

N

A

I

L

I

P

Y

Y

S
|
S

S

S

G

G

T

T

G

G

T

L

P

P

K

K

G

G

I

V

I

M

Q

L

S

T

H

H

-

K

G

G

M

L

R

V

W

T

-
x
S

-

V

-

A

K

Q

H

Q

I

V

F

D

V

G

G

E

D

N

A

P

I

N

G

L

Y

Y

G

I

H

H

T

S

P

E

-

D

V

V

S

M

L

L

L

C

S

V

T
x
L

P
|
P

L

L

Y

F

S
x
H

-

I

-
x
Y

-

S

-

L

N

N

T

S

T

V

L

L

V

L

C

C

F

-

P

-

T

G

L

L

A

R

G

V

G

G

G

A

T

A

V

I

V

L

L

I

M

M

K

Q

K
|
K

F
|
F

D

D

V

I

V

V

R

S

Y

F

L

L

E

E

L

L

A

I

A

Q

K

R

H

Y

R

K

I

V

T

T

H

I

T

G

M

P

L

F

V
|
V

P

P

V

P

Q
x
I

Y

V

R

L

R

A

L

I

M

A

E

K

H

S

P

P

D

M

F

V

D

D

R

D

Y

Y

D

D

L

L

S

S

T

V

R

R

M

T

K

V

F

M

C

S

T

G

S
x
A

A
|
A

P
|
P

F

L

A

G

A

K

D

E

L

L

K

E

A

D

Q

T

V

V

L

R

K

A

R

K

W

F

P

P

G

N

G

A

-

K

L

L

V

G

E

Q

Y
x
G

F
x
Y

G
|
G

M
|
M

T
|
T

E
|
E

G

A

G

G

-

P

-

V

-

L

G

A

T

M

C

C

I

L

L

A

M

F

A

A

H

K

E

E

H

-

P

P

D

F

K

E

L

I

H

K

T

S

-

G

-

A

V

C

G

G

R

T

P

V

A

V

P

R

G

N

H

A

D

E

I

M

R

K

L

I

V

V

D

D

-

P

E

K

D

T

G

G

R

N

Q

S

V

L

G

P

P

R

G

N

V

Q

V

S

G

G

E

E

I

I

V

C

G

I

R

R

S

G

A

D

S

Q

M

I

M

M

N

K

G

G

Y

Y

H

L

G

N

R

D

P

P

D

E

K

A

T

T

A

A

E

R

A

T

T

-

W

-

V

I

S

D

P

K

E

E

G

G

W

W

T

L

F

Y

I

T

R

G

T
x
D

G

I

D

G

V

Y

G

I

R

D

F

D

D

D

E

D

E

E

G

L

F

F

L
x
I

T

-

L

-

M

V

D

D

R
|
R

K

L

K
|
K

D

E

M

L

I

I

I
x
K

S

Y

G
x
K

G
|
G

F
|
F

N
x
Q

I

V

Y

A

P

P

S

A

D

E

L

L

E

E

A

A

V

L

L

L

V

L

Q

N

H

H

P

P

A

N

V

I

F

S

E

D

A

A

V

V

G

P

V

M

P

K

S

D

D

E

A

Q

W

A

G

G

E

E

T

V

P

P

V

V

A

A

F

F

V

V

A

V

L

R

K

S

S

N

S

G

Q

S

V

T

A

I

E

T

A

E

D

D

A

E

I

V

K

K

T

D

F

F

V

I

N

S

G

K

Q

Q

V

V

G

I

K
x
F

T

Y

Q

K

R

R

L

I

A

K

E

R

V

V

V

F

V

V

D

D

S

A

L

I

P

P

R

K

S

S

H

P

I

S

G

G

K
|
K

V

I

L

L

K

R

R

K

E

D

L

L

R

R

active site: S181 (= S172), S201 (vs. gap), H229 (≠ S215), T328 (= T312), E329 (= E313), K433 (≠ I416), Q438 (≠ N421), K518 (= K501)
binding adenosine monophosphate: A301 (≠ S286), A302 (= A287), P303 (= P288), G324 (≠ Y308), Y325 (≠ F309), G326 (= G310), M327 (= M311), T328 (= T312), D412 (≠ T393), I424 (≠ L405), R427 (= R410), K429 (= K412), K433 (≠ I416), Q438 (≠ N421)
binding coenzyme a: L102 (≠ S96), L225 (≠ T211), P226 (= P212), H229 (≠ S215), Y231 (vs. gap), K252 (= K237), F253 (= F238), V273 (= V258), I276 (≠ Q261), K435 (≠ G418), G436 (= G419), F437 (= F420), F498 (≠ K481)

5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 91% coverage: 40:508/517 of query aligns to 47:526/529 of 5bsvA

query
sites
5bsvA

T

T

Y

Y

A

A

Q

D

F

V

D

E

A

L

L

N

V

S

D

R

R

K

V

V

A

A

A

G

L

L

Q

H

R

K

D

Q

G

G

V

I

A

Q

P

P

G

K

E

D

A

T

V

I

A

M

V

I

C

L

A

L

L

P

S

N

S

S

I

P

P

E

Y

F

A

V

A

F

L

A

F

F

L

I

G

G

A

A

L

S

R

Y

A

L

G

G

V

A

A

I

V

S

A

T

P

M

I

A

A

N

P

P

S

L

S

F

T

T

P

P

E

A

S

E

I

V

A

V

G

K

M

Q

V

A

A

K

D

A

C

S

G

S

A

A

K

K

L

I

F

I

F

V

L

T

D

Q

A

A

G

C

V

H

A

V

E

N

A

K

Q

V

K

K

P

D

A

Y

P

A

V

F

P

E

-

N

-

D

V

V

R

K

P

I

I

I

A

C

L

I

D

D

G

S

S

A

S

P

A

E

G

G

Q

C

A

L

F

H

D

F

A

S

W

V

L

L

A

T

P

Q

E

A

D

N

A

E

T

H

P

D

T

I

P

P

-

E

V

V

E

E

I

I

G

Q

P

P

K

D

H

D

P

V

F

V

N

A

I

L

I

P

Y

Y

S
|
S

S

S

G

G

T

T

G

G

T

L

P

P

K

K

G

G

I

V

I

M

Q

L

S

T

H

H

-

K

G

G

M

L

R

V

W

T

-
x
S

-

V

-

A

K

Q

H

Q

I

V

F

D

V

G

G

E

D

N

A

P

I

N

G

L

Y

Y

G

I

H

H

T

S

P

E

-

D

V

V

S

M

L

L

L

C

S

V

T

L

P

P

L

L

Y

F

S
x
H

-

I

-
x
Y

-

S

-

L

N

N

T
x
S

T

V

L

L

V

L

C

C

F

-

P

-

T

G

L

L

A

R

G

V

G

G

G

A

T

A

V

I

V

L

L

I

M

M

K

Q

K

K

F

F

D

D

V

I

V

V

R

S

Y

F

L

L

E

E

L

L

A

I

A

Q

K

R

H

Y

R

K

I

V

T

T

H

I

T

G

M

P

L

F

V

V

P

P

V

P

Q

I

Y

V

R

L

R

A

L

I

M

A

E

K

H

S

P

P

D

M

F

V

D

D

R

D

Y

Y

D

D

L

L

S

S

T

V

R

R

M

T

K

V

F

M

C
x
S

T
x
G

S
x
A

A
|
A

P
|
P

F

L

A

G

A

K

D

E

L

L

K

E

A

D

Q

T

V

V

L

R

K

A

R

K

W

F

P

P

G

N

G

A

-

K

L

L

V

G

E
x
Q

Y
x
G

F
x
Y

G
|
G

M
|
M

T
|
T

E
|
E

G

A

G

G

-
x
P

-
x
V

-

L

G

A

T
x
M

C

C

I

L

L

A

M

F

A

A

H

K

E

E

H

-

P

P

D

F

K

E

L

I

H

K

T

S

-

G

-

A

V

C

G

G

R

T

P

V

A

V

P

R

G

N

H

A

D

E

I

M

R

K

L

I

V

V

D

D

-

P

E

K

D

T

G

G

R

N

Q

S

V

L

G

P

P

R

G

N

V

Q

V

S

G

G

E

E

I

I

V

C

G

I

R

R

S

G

A

D

S

Q

M

I

M

M

N

K

G

G

Y

Y

H

L

G

N

R

D

P

P

D

E

K

A

T

T

A

A

E

R

A

T

T

-

W

-

V

I

S

D

P

K

E

E

G

G

W

W

T

L

F

Y

I

T

R

G

T
x
D

G

I

D

G

V

Y

G

I

R

D

F

D

D

D

E

D

E

E

G

L

F

F

L
x
I

T

-

L

-

M

V

D

D

R
|
R

K

L

K
|
K

D

E

M

L

I

I

I
x
K

S

Y

G

K