SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Pf6N2E2_4497 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_4497 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)

P0A6C5 Amino-acid acetyltransferase; N-acetylglutamate synthase; AGS; NAGS; EC 2.3.1.1 from Escherichia coli (strain K12) (see paper)
52% identity, 99% coverage: 3:428/432 of query aligns to 8:438/443 of P0A6C5

query
sites
P0A6C5

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H15 (= H10) mutation to Y: In EE17.
Y19 (= Y14) mutation to C: In EE51.
S54 (= S49) mutation to N: In PT2M217.
R58 (= R53) mutation to H: In EE11.
G287 (= G277) mutation to S: In PT2M216.
Q432 (= Q422) mutation to R: In PT2M217.

4i49A Structure of ngnags bound with bisubstrate analog coa-NAG (see paper)
40% identity, 99% coverage: 4:432/432 of query aligns to 3:422/424 of 4i49A

query
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4i49A

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binding (2S)-2-({(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14,20-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaicosan-20-yl}amino)pentanedioic acid (non-preferred name): L295 (= L306), I300 (= I311), L301 (= L312), L302 (≠ V313), R304 (= R315), A343 (= A354), C344 (= C355), L345 (= L356), A346 (= A357), V347 (= V358), Q352 (≠ R363), D353 (≠ H364), G354 (= G365), G355 (= G366), Y356 (≠ R367), G357 (= G368), E358 (≠ D369), L379 (= L390), S380 (≠ T391), N382 (≠ R393), T383 (= T394), E385 (≠ H396), W386 (= W397), F387 (= F398), R390 (= R401), R404 (= R415), R413 (= R423), S415 (= S425)

3d2mA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-glutamate (see paper)
40% identity, 99% coverage: 4:432/432 of query aligns to 3:422/424 of 3d2mA

query
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3d2mA

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E

L

I

A
|
A

C
|
C

L
|
L

A
|
A

V
|
V

N

S

P

P

E

Q

Y

A

R
x
Q

H
x
D

G
|
G

G
|
G

R
x
Y

G
|
G

D
x
E

E

R

L

L

L

L

E

A

R

H

I

I

E

I

T

D

R

K

A

A

R

R

A

G

Q

I

G

G

L

I

K

S

T

R

L

L

F

F

V

A

L
|
L

T
x
S

T

T

R

N

T
|
T

A

G

H
x
E

W
|
W

F
|
F

R

A

E

E

R
|
R

G

G

F

F

E

Q

P

T

S

A

S

S

V

E

E

D

R

E

L

L

P

P

A

E

A

T

R
|
R

A

R

S

K

L

D

Y

Y

N

R

Y

S

Q

N

-

G

R
|
R

N

N

S
|
S

K

H

I

I

F

L

E

V

K

R

A

R

L

L

active site: I26 (≠ L27)
binding coenzyme a: L295 (= L306), I300 (= I311), L345 (= L356), A346 (= A357), V347 (= V358), Q352 (≠ R363), D353 (≠ H364), G354 (= G365), G355 (= G366), Y356 (≠ R367), G357 (= G368), E358 (≠ D369), S380 (≠ T391), T383 (= T394), E385 (≠ H396), W386 (= W397), F387 (= F398), R390 (= R401)
binding glutamic acid: I300 (= I311), L301 (= L312), L302 (≠ V313), R304 (= R315), A343 (= A354), C344 (= C355), L379 (= L390), R404 (= R415), R413 (= R423), S415 (= S425)

3b8gA Crysta structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and n-acetyl-glutamate (see paper)
40% identity, 99% coverage: 4:432/432 of query aligns to 3:422/424 of 3b8gA

query
sites
3b8gA

Y

F

V

V

N

A

W

H

L

F

R

R

H

E

A

A

S

A

P

P

Y

Y

I

I

N

R

A

Q

H

M

R

R

D

G

C

T

T

T

F

L

I

V

V

A

M

G

L
x
I

P

D

G

G

D

R

G

L

V

L

E

E

H

G

P

G

N

T

F

L

G

N

N

K

I

L

V

A

H

A

D

D

L

I

V

G

L

L

L

L

H

S

S

Q

L

L

G

G

V

I

R

R

L

L

V

V

L

L

V

I

H

H

G

G

S

A

R

Y

P

H

Q

F

I

L

E

D

T

R

R

L

L

A

A

A

A

A

R

Q

G

G

L

R

T

T

P

P

H

H

Y

Y

H

C

H

R

G

G

M

L

R

R

I

V

T

T

D

D

A

E

A

T

T

S

L

L

E

G

C

Q

V

A

I

Q

D

Q

A

F

V

A

G

G

Q

T

L

V

R

R

I

S

A

R

I

F

E

E

A

A

R

A

L

L

S

C

M

-

D

-

M

-

A

-

S

-

S

-

P

-

M

-

Q

-

G

G

S

S

R

S

L

V

R

P

V

L

A

V

S

S

G

G

N

N

L

F

V

L

T

T

A

A

R

R

P

P

I

I

G

G

V

V

L

I

E

D

G

G

V

T

D

D

Y

M

H

E

H

Y

T

A

G

G

E

V

V

I

R

R

R

K

V

T

D

D

R

T

K

A

G

A

I

L

N

R

R

F

L

Q

L

L

D

D

E

A

R

G

S

N

I

I

V

V

L

W

L

M

S

P

P

P

L

L

G

G

Y

H

S

S

P

Y

T

G

G

G

E

K

I

T

F

F

N

N

L

L

A

D

C

M

E

V

D

Q

V

A

A

A

T

A

R

S

A

V

A

A

I

V

D

S

L

L

A

Q

A

A

D

E

K

K

L

L

L

V

L

Y

F

L

G

T

S

L

E

S

Q

D

G

G

L

I

I

S

G

R

E

P

D

D

G

G

R

T

L

L

V

A

R

E

E

T

L

L

R

S

P

A

Q

Q

Q

E

V

A

P

Q

A

S

H

L

I

A

Q

E

R

H

L

A

G

A

S

S

D

E

Y

T

Q

R

A

-

E

R

L

L

L

I

D

S

A

S

A

A

A

V

Q

A

A

A

C

L

R

E

G

G

G

G

V

V

A

H

R

R

S

V

H

Q

I

I

V

L

S

N

Y

G

V

A

E

A

N

D

G

G

A

S

L

L

L

L

A

Q

E

E

L

L

F

F

T

T

R

R

D

N

G

G

S

I

G

G

T

T

L

S

V

I

A

A

Q

K

E

E

Q

A

F

F

E

V

V

S

V

I

R

R

E

Q

A

A

A

H

I

S

E

G

D

D

V

I

G

P

G

H

L

I

L

A

D

A

L

L

I

I

S

R

P

P

L
|
L

E

E

E

E

Q

Q

G

G

I
|
I

L
|
L

V
x
L

R

H

R
|
R

S

S

R

R

E

E

V

Y

L

L

E

E

R

N

E

H

I

I

E

S

Q

E

F

F

S

S

V

I

V

L

E

E

R

H

E

D

G

G

M

N

I

L

I

Y

A

G

C

C

A

A

A

A

L

L

Y

K

Q

T

I

F

A

A

D

E

S

A

D

D

A

C

G

G

E

E

L

I

A
|
A

C
|
C

L
|
L

A

A

V
|
V

N

S

P

P

E

Q

Y

A

R
x
Q

H
x
D

G
|
G

G
|
G

R
x
Y

G
|
G

D
x
E

E

R

L

L

L

L

E

A

R

H

I

I

E

I

T

D

R

K

A

A

R

R

A

G

Q

I

G

G

L

I

K

S

T

R

L

L

F

F

V

A

L
|
L

T
x
S

T

T

R

N

T
|
T

A

G

H
x
E

W
|
W

F

F

R

A

E

E

R
|
R

G

G

F

F

E

Q

P

T

S

A

S

S

V

E

E

D

R

E

L

L

P

P

A

E

A

T

R

R

A

R

S

K

L

D

Y

Y

N

R

Y

S

Q

N

-

G

R
|
R

N

N

S
|
S

K

H

I

I

F

L

E

V

K

R

A

R

L

L

active site: I26 (≠ L27)
binding coenzyme a: L295 (= L306), I300 (= I311), L301 (= L312), L345 (= L356), V347 (= V358), Q352 (≠ R363), D353 (≠ H364), G354 (= G365), G355 (= G366), Y356 (≠ R367), G357 (= G368), E358 (≠ D369), S380 (≠ T391), T383 (= T394), E385 (≠ H396), W386 (= W397), R390 (= R401)
binding n-acetyl-l-glutamate: I300 (= I311), L301 (= L312), L302 (≠ V313), R304 (= R315), A343 (= A354), C344 (= C355), L345 (= L356), L379 (= L390), S380 (≠ T391), R413 (= R423), S415 (= S425)

2r8vA Native structure of n-acetylglutamate synthase from neisseria gonorrhoeae (see paper)
40% identity, 99% coverage: 4:432/432 of query aligns to 3:422/424 of 2r8vA

query
sites
2r8vA

Y

F

V

V

N

A

W

H

L

F

R

R

H

E

A

A

S

A

P

P

Y

Y

I

I

N

R

A

Q

H

M

R

R

D

G

C

T

T

T

F

L

I

V

V

A

M

G

L
x
I

P

D

G

G

D

R

G

L

V

L

E

E

H

G

P

G

N

T

F

L

G

N

N

K

I

L

V

A

H

A

D

D

L

I

V

G

L

L

L

L

H

S

S

Q

L

L

G

G

V

I

R

R

L

L

V

V

L

L

V

I

H

H

G

G

S

A

R

Y

P

H

Q

F

I

L

E

D

T

R

R

L

L

A

A

A

A

A

R

Q

G

G

L

R

T

T

P

P

H

H

Y

Y

H

C

H

R

G

G

M

L

R

R

I

V

T

T

D

D

A

E

A

T

T

S

L

L

E

G

C

Q

V

A

I

Q

D

Q

A

F

V

A

G

G

Q

T

L

V

R

R

I

S

A

R

I

F

E

E

A

A

R

A

L

L

S

C

M

-

D

-

M

-

A

-

S

-

S

-

P

-

M

-

Q

-

G

G

S

S

R

S

L

V

R

P

V

L

A

V

S

S

G

G

N

N

L

F

V

L

T

T

A

A

R

R

P

P

I

I

G

G

V

V

L

I

E

D

G

G

V

T

D

D

Y

M

H

E

H

Y

T

A

G

G

E

V

V

I

R

R

R

K

V

T

D

D

R

T

K

A

G

A

I

L

N

R

R

F

L

Q

L

L

D

D

E

A

R

G

S

N

I

I

V

V

L

W

L

M

S

P

P

P

L

L

G

G

Y

H

S

S

P

Y

T

G

G

G

E

K

I

T

F

F

N

N

L

L

A

D

C

M

E

V

D

Q

V

A

A

A

T

A

R

S

A

V

A

A

I

V

D

S

L

L

A

Q

A

A

D

E

K

K

L

L

L

V

L

Y

F

L

G

T

S

L

E

S

Q

D

G

G

L

I

I

S

G

R

E

P

D

D

G

G

R

T

L

L

V

A

R

E

E

T

L

L

R

S

P

A

Q

Q

Q

E

V

A

P

Q

A

S

H

L

I

A

Q

E

R

H

L

A

G

A

S

S

D

E

Y

T

Q

R

A

-

E

R

L

L

L

I

D

S

A

S

A

A

A

V

Q

A

A

A

C

L

R

E

G

G

G

G

V

V

A

H

R

R

S

V

H

Q

I

I

V

L

S

N

Y

G

V

A

E

A

N

D

G

G

A

S

L

L

L

L

A

Q

E

E

L

L

F

F

T

T

R

R

D

N

G

G

S

I

G

G

T

T

L

S

V

I

A

A

Q

K

E

E

Q

A

F

F

E

V

V

S

V

I

R

R

E

Q

A

A

A

H

I

S

E

G

D

D

V

I

G

P

G

H

L

I

L

A

D

A

L

L

I

I

S

R

P

P

L
|
L

E

E

E

E

Q

Q

G

G

I
|
I

L
|
L

V

L

R

H

R

R

S

S

R

R

E

E

V

Y

L

L

E

E

R

N

E

H

I

I

E

S

Q

E

F

F

S

S

V

I

V

L

E

E

R

H

E

D

G

G

M

N

I

L

I

Y

A

G

C

C

A

A

A

A

L

L

Y

K

Q

T

I

F

A

A

D

E

S

A

D

D

A

C

G

G

E

E

L

I

A
|
A

C
|
C

L
|
L

A
|
A

V
|
V

N

S

P

P

E

Q

Y

A

R
x
Q

H
x
D

G
|
G

G
|
G

R
x
Y

G
|
G

D
x
E

E

R

L

L

L

L

E

A

R

H

I

I

E

I

T

D

R

K

A

A

R

R

A

G

Q

I

G

G

L

I

K

S

T

R

L

L

F

F

V

A

L
|
L

T
x
S

T

T

R

N

T
|
T

A

G

H
x
E

W
|
W

F
|
F

R

A

E

E

R

R

G

G

F

F

E

Q

P

T

S

A

S

S

V

E

E

D

R

E

L

L

P

P

A

E

A

T

R

R

A

R

S

K

L

D

Y

Y

N

R

Y

S

Q

N

-

G

R

R

N

N

S

S

K

H

I

I

F

L

E

V

K

R

A

R

L

L

active site: I26 (≠ L27)
binding acetyl coenzyme *a: L295 (= L306), I300 (= I311), L301 (= L312), A343 (= A354), C344 (= C355), L345 (= L356), A346 (= A357), V347 (= V358), Q352 (≠ R363), D353 (≠ H364), G354 (= G365), G355 (= G366), Y356 (≠ R367), G357 (= G368), E358 (≠ D369), L379 (= L390), S380 (≠ T391), T383 (= T394), E385 (≠ H396), W386 (= W397), F387 (= F398)

3d2pA Crystal structure of n-acetylglutamate synthase from neisseria gonorrhoeae complexed with coenzyme a and l-arginine (see paper)
38% identity, 99% coverage: 4:432/432 of query aligns to 3:422/424 of 3d2pA

query
sites
3d2pA

Y

F

V

V

N

A

W

H

L

F

R

R

H

E

A

A

S

A

P

P

Y
|
Y

I

I

N

R

A

Q

H

M

R

R

D

G

C

T

T

T

F

L

I

V

V

A

M

G

L
x
I

P

D

G

G

D

R

G

L

V

L

E

E

H

G

P

G

N

T

F

L

G

N

N

K

I

L

V

A

H

A

D

D

L

I

V

G

L

L

L

L

H

S

S

Q

L

L

G

G

V

I

R

R

L

L

V

V

L

L

V

I

H

H

G

G

S

A

R

Y

P

H

Q

F

I

L

E

D

T

R

R

L

L

A

A

A

A

A

R

Q

G

G

L

R

T

T

P

P

H

H

Y

Y

H

C

H

R

G

G

M

L

R

R

I

V

T

T

D

D

A

E

A

T

T

S

L

L

E

G

C

Q

V

A

I

Q

D

Q

A

F

V

A

G

G

Q

T

L

V

R

R

I

S

A

R

I

F

E

E

A

A

R

A

L

L

S

C

M

G

D

S

M

V

A

-

S

S

S

G

P

F

M

A

Q

R

G

A

S

P

R

S

L

V

R

P

V

L

A

V

S

S

G

G

N

N

L

F

V

L

T

T

A

A

R

R

P

P

I

I

G

G

V

V

L

I

E

D

G

G

V

T

D

D

Y

M

H

E

H

Y

T

A

G

G

E

V

V

I

R

R

R

K

V

T

D

D

R

T

K

A

G

A

I

L

N

R

R

F

L

Q

L

L

D

D

E

A

R

G

S

N

I

I

V

V

L

W

L

M

S

P

P

P

L

L

G

G

Y

H

S

S

P

Y

T

G

G

G

E

K

I

T

F

F

N

N

L

L

A

D

C

M

E

V

D

Q

V

A

A

A

T

A

R

S

A

V

A

A

I

V

D

S

L

L

A

Q

A

A

D

E

K
|
K

L

L

L

V

L

Y

F

L

G

T

S

L

E

S

Q

D

G

G

L

I

I

S

G

R

E

P

D

D

G

G

R

T

L

L

V

A

R
x
E

E

T

L

L

R

S

P

A

Q

Q

Q

E

V

A

P

Q

A

S

H

L

I

A

Q

E

R

H

L

A

G

A

S

S

D

E

Y

T

Q

R

A

-

E

R

L

L

L

I

D

S

A

S

A

A

A

V

Q

A

A

A

C

L

R

E

G

G

G

G

V

V

A

H

R

R

S

V

H
x
Q

I

I

V

L

S

N

Y

G

V

A

E

A

N

D

G

G

A

S

L

L

L

L

A

Q

E
|
E

L
|
L

F

F

T
|
T

R
|
R

D
x
N

G
|
G

S
x
I

G
|
G

T
|
T

L
x
S

V

I

A

A

Q

K

E

E

Q

A

F

F

E

V

V

S

V

I

R

R

E

Q

A

A

A

H

I

S

E

G

D

D

V

I

G

P

G

H

L

I

L

A

D

A

L

L

I

I

S

R

P

P

L
|
L

E

-

E

-

Q

-

G

-

I

I

L

L

V

L

R

H

R

R

S

S

R

R

E

E

V

Y

L

L

E

E

R

N

E

H

I

I

E

S

Q

E

F

F

S

S

V

I

V

L

E

E

R

H

E
x
D

G

G

M

N

I

L

I

Y

A

G

C

C

A

A

A

A

L

L

Y

K

Q

T

I

F

A

A

D

E

S

A

D

D

A

C

G

G

E

E

L

I

A

A

C

C

L
|
L

A
|
A

V
|
V

N

S

P

P

E

Q

Y

A

R
x
Q

H
x
D

G
|
G

G
|
G

R
x
Y

G
|
G

D
x
E

E

R

L

L

L

L

E

A

R

H

I

I

E

I

T

D

R

K

A

A

R

R

A

G

Q

I

G

G

L

I

K

S

T

R

L

L

F

F

V

A

L

L

T

S

T

T

R
x
N

T
|
T

A

G

H
x
E

W
|
W

F

F

R

A

E

E

R
|
R

G

G

F

F

E

Q

P

T

S

A

S

S

V

E

E

D

R

E

L

L

P

P

A

E

A

T

R

R

A

R

S

K

L

D

Y

Y

N

-

Y

-

Q

-

R

R

N

N

S

S

K

H

I

I

F

L

E

V

K

R

A

R

L

L

active site: I26 (≠ L27)
binding arginine: Y13 (= Y14), K197 (= K199), E216 (≠ R218), Q253 (≠ H256), E266 (= E269), L267 (= L270), T269 (= T272), R270 (= R273), N271 (≠ D274), G272 (= G275), I273 (≠ S276), G274 (= G277), T275 (= T278), S276 (≠ L279), D326 (≠ E333)
binding coenzyme a: L303 (= L306), L349 (= L356), A350 (= A357), V351 (= V358), Q356 (≠ R363), D357 (≠ H364), G358 (= G365), G359 (= G366), Y360 (≠ R367), G361 (= G368), E362 (≠ D369), N386 (≠ R393), T387 (= T394), E389 (≠ H396), W390 (= W397), R394 (= R401)

2bufA Arginine feed-back inhibitable acetylglutamate kinase (see paper)
29% identity, 64% coverage: 8:284/432 of query aligns to 14:290/292 of 2bufA

query
sites
2bufA

L

L

R

S

H

E

A

A

S

L

P

P

Y

Y

I

I

N

R

A

R

H

F

R

V

D

G

C

K

T

T

F

L

I

V

V

I

M
x
K

L

Y

P

G

G
|
G

D

N

G

A

V

M

E

E

H

S

P

E

N

E

F

L

-

K

G

A

N

G

I

F

V

A

H

R

D

D

L

V

V

V

L

L

L

M

H

K

S

A

L

V

G

G

V

I

R

N

L

P

V

V

L

V

V

V

H

H

G
|
G

S
x
G

R
x
G

P

P

Q

Q

I
|
I

E

G

T

D

R

L

L

L

A

K

A

R

R

L

G

S

L

I

T

E

P

S

H

H

Y

F

H

I

H

D

G

G

M
|
M

R
|
R

I

V

T

T

D

D

A

A

A

A

T

T

L

M

E

D

C

V

V

V

I

-

D

-

A

-

V

-

G

-

Q

-

L

-

R

E

I

M

A

V

I

L

E

G

A

G

R

Q

L

V

S

N

M

K

D

D

M

I

A

V

S

N

-

L

-

I

S

N

P

R

M

H

Q

G

G

G

S

S

R

A

L

I

R

G

V

L

A

T

S

G

G

K

N

D

-

A

-

E

L

L

V

I

T

R

A

A

R

K

P

K

I

L

G

T

V

V

L

T

-

R

E

Q

G

I

V

I

D

D

Y

I

H

G

H

H

T

V

G

G

E

E

V

V

R

T

R

G

V

V

D

N

R

V

K

G

G

L

I

L

N

N

R

M

L

L

L

V

D

K

E

G

R

D

S

F

I

I

V

P

L

V

L

I

S

A

P

P

L

I

G

G

Y

V

S

G

P

S

T

N

G

G

E

E

I

S

F

Y

N
|
N

L

I

A

N

C
x
A

E
x
D

D

L

V

V

A

A

T

G

R

K

A

V

A

A

I

E

D

A

L

L

A

K

A

A

D

E

K

K

L

L

L

M

L

L

F

L

G

T

S

N

E

I

Q

A

G

G

L

L

I

M

G

D

E

K

D

Q

G

G

R

Q

L

V

V

L

R

T

E

G

L

L

R

S

P

T

Q

E

Q

Q

V

V

P

N

A

E

H

L

I

I

Q

A

R

D

L

-

G

G

S

T

D

I

Y

Y

Q

G

A

G

E

M

L

L

-

P

-
x
K

L

I

D

R

A

C

A

A

A

L

Q

E

A

A

C

V

R

Q

G

G

G

G

V

V

A

T

R

S

S

A

H

H

I

I

V

I

S

D

Y

G

V

R

E

V

N

P

G

N

A

A

L

V

L

L

A

L

E

E

L

I

F

F

T

T

R

D

D

S

G

G

S

V

G

G

T

T

L

L

V

I

A

S

Q

N

E

R

Q

K

active site: K32 (≠ M26), G35 (= G29), G68 (≠ R61), D190 (≠ E185), K246 (vs. gap)
binding n-acetyl-l-glutamate: G66 (= G59), G67 (≠ S60), I71 (= I64), M88 (= M81), R89 (= R82), N186 (= N181), A189 (≠ C184)

2bufC Arginine feed-back inhibitable acetylglutamate kinase (see paper)
29% identity, 64% coverage: 8:284/432 of query aligns to 14:298/298 of 2bufC

query
sites
2bufC

L

L

R

S

H

E

A

A

S

L

P

P

Y

Y

I

I

N

R

A

R

H

F

R

V

D

G

C

K

T

T

F

L

I

V

V

I

M
x
K

L

Y

P

G

G
|
G

D
x
N

G

A

V

M

E

E

H

S

P

E

N

E

F

L

-

K

G

A

N

G

I

F

V

A

H

R

D

D

L

V

V

V

L

L

L

M

H

K

S

A

L

V

G

G

V

I

R

N

L

P

V

V

L

V

V

V

H

H

G

G

S

G

R
x
G

P

P

Q

Q

I

I

E

G

T

D

R

L

L

L

A

K

A

R

R

L

G

S

L

I

T

E

P

S

H

H

Y

F

H

I

H

D

G

G

M

M

R

R

I

V

T

T

D

D

A

A

A

A

T

T

L

M

E

D

C

V

V

V

I

-

D

-

A

-

V

-

G

-

Q

-

L

-

R

E

I

M

A

V

I

L

E

G

A

G

R

Q

L

V

S

N

M

K

D

D

M

I

A

V

S

N

-

L

-

I

S

N

P

R

M

H

Q

G

G

G

S

S

R

A

L

I

R

G

V

L

A

T

S

G

G

K

N

D

-

A

-

E

L

L

V

I

T

R

A

A

R

K

P

K

I

L

G

T

V

V

L

T

-

R

-

Q

-

T

-

P

-

E

-

M

-

T

-

K

-

P

E

E

G

I

V

I

D

D

Y

I

H

G

H

H

T

V

G

G

E

E

V

V

R

T

R

G

V

V

D

N

R

V

K

G

G

L

I

L

N

N

R

M

L

L

L

V

D

K

E

G

R

D

S

F

I

I

V

P

L

V

L

I

S

A

P

P

L

I

G

G

Y

V

S

G

P

S

T

N

G

G

E

E

I

S

F

Y

N

N

L

I

A

N

C

A

E
x
D

D

L

V

V

A

A

T

G

R

K

A

V

A

A

I

E

D

A

L

L

A

K

A

A

D

E

K

K

L

L

L

M

L

L

F

L

G
x
T

S
x
N

E
x
I

Q

A

G

G

L
|
L

I
x
M

G

D

E

K

D

Q

G

G

R

Q

L

V

V

L

R

T

E

G

L

L

R

S

P

T

Q

E

Q

Q

V

V

P

N

A

E

H

L

I

I

Q

A

R

D

L

-

G

G

S
x
T

D
x
I

Y
|
Y

Q

G

A
x
G

E
x
M

L

L

-

P

-
x
K

L

I

D

R

A

C

A

A

A

L

Q

E

A

A

C

V

R

Q

G

G

G

G

V

V

A

T

R

S

S

A

H

H

I

I

V

I

S

D

Y

G

V

R

E

V

N

P

G

N

A

A

L

V

L

L

A

L

E

E

L

I

F

F

T

T

R

D

D

S

G

G

S

V

G

G

T

T

L

L

V

I

A

S

Q

N

E

R

Q

K

active site: K32 (≠ M26), G35 (= G29), G68 (≠ R61), D198 (≠ E185), K254 (vs. gap)
binding adenosine-5'-diphosphate: N36 (≠ D30), T217 (≠ G204), N218 (≠ S205), I219 (≠ E206), L222 (= L209), M223 (≠ I210), T246 (≠ S234), I247 (≠ D235), Y248 (= Y236), G250 (≠ A238), M251 (≠ E239), K254 (vs. gap)

2btyA Acetylglutamate kinase from thermotoga maritima complexed with its inhibitor arginine (see paper)
27% identity, 65% coverage: 3:282/432 of query aligns to 4:279/282 of 2btyA

query
sites
2btyA

E

D

Y

T

V

V

N

N

W

V

L

L

R

L

H

E

A

A

S

L

P

P

Y
|
Y

I

I

N

K

A

E

H
x
F

R

Y

D

G

C

K

T

T

F

F

I

V

V

I

M
x
K

L

F

P
x
G

G
|
G

D

S

G

A

V

M

E

K

H

Q

P

E

N

N

F

A

G

K

N

K

-

A

I

F

V

I

H

Q

D

D

L

I

V

I

L

L

L

L

H

K

S

Y

L

T

G

G

V

I

R

K

L

P

V

I

L

I

V

V

H

H

G
|
G

S
x
G

R
x
G

P

P

Q

A

I

I

E

S

T

Q

R

M

L

M

A

K

A

D

R

L

G

G

L

I

T

E

P

P

H

V

Y

F

H

K

H

N

G

G

M

H

R

R

I

V

T

T

D

D

A

E

A

K

T

T

L

M

E

E

C

-

V

I

I

V

D

E

A

M

V

V

G

L

Q

V

L

G

R

K

I

I

A

N

I

K

E

E

A

I

R

V

L

M

S

N

M

L

D

N

M

L

A

H

S

G

S

G

P

R

M

A

Q

V

G

G

-

I

-

C

-

G

-

K

-

D

S

S

R

K

L

L

R

I

V

V

A

A

S

E

G

K

N

E

L

T

V

K

T

H

A

G

R

-

P

-

I

-

G

-

V

-

L

-

E

-

G

-

V

-

D

D

Y

I

H

G

H

Y

T

V

G

G

E

K

V

V

R

K

R

K

V

V

D

N

R

P

K

E

G

I

I

L

N

H

R

A

L

L

L

I

D

E

E

N

R

D

S

Y

I

I

V

P

L

V

L

I

S

A

P

P

L

V

G

G

Y

I

S

G

P

E

T

D

G

G

E

H

I

S

F

Y

N

N

L

I

A
x
N

C

A

E
x
D

D

T

V

A

A

A

T

A

R

E

A

I

A

A

I

K

D

S

L

L

A

M

A

A

D

E

K
|
K

L

L

L

I

L

L

F

L

G

T

S

D

E

V

Q

D

G

G

L

V

I

L

G

-

E

K

D

D

G

G

R

K

L

L

V

I

R
x
S

E

T

L

L

R

T

P

P

Q

D

Q

E

V

A

P

E

A

E

H

L

I

I

Q

-

R

R

L

D

G

G

S

T

D

V

Y

T

Q

G

A

G

E

M

L

I

-

P

-
x
K

L

V

D

E

A

C

A

A

A

V

Q

S

A

A

C

V

R

R

G

G

G

G

V

V

A

G

R

A

S

V

H
|
H

I

I

V

I

S

N

Y

G

V

G

E

L

N

E

G

H

A

A

L

I

L

L

A

L

E
|
E

L
x
I

F

F

T
x
S

R
|
R

D
x
K

G
|
G

S

I

G
|
G

T
|
T

L
x
M

V

I

A

K

Q

E

active site: K27 (≠ M26), G30 (= G29), G63 (≠ R61), D182 (≠ E185), K237 (vs. gap)
binding arginine: Y15 (= Y14), F19 (≠ H18), K196 (= K199), S214 (≠ R218), H253 (= H256), E266 (= E269), I267 (≠ L270), S269 (≠ T272), R270 (= R273), K271 (≠ D274), G272 (= G275), G274 (= G277), T275 (= T278), M276 (≠ L279)
binding n-acetyl-l-glutamate: K27 (≠ M26), G29 (≠ P28), G30 (= G29), G61 (= G59), G62 (≠ S60), G63 (≠ R61), N180 (≠ A183), D182 (≠ E185)

Q9X2A4 Acetylglutamate kinase; N-acetyl-L-glutamate 5-phosphotransferase; NAG kinase; NAGK; EC 2.7.2.8 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
27% identity, 65% coverage: 3:282/432 of query aligns to 4:279/282 of Q9X2A4

query
sites
Q9X2A4

E

D

Y

T

V

V

N

N

W

V

L

L

R

L

H

E

A

A

S

L

P

P

Y

Y

I

I

N

K

A

E

H

F

R

Y

D

G

C

K

T

T

F

F

I

V

V

I

M

K

L

F

P

G

G

G

D

S

G

A

V

M

E

K

H

Q

P

E

N

N

F

A

G

K

N

K

-

A

I

F

V

I

H

Q

D

D

L

I

V

I

L

L

L

L

H

K

S

Y

L

T

G

G

V

I

R

K

L

P

V

I

L

I

V

V

H

H

G

G

S

G

R

G

P

P

Q

A

I

I

E

S

T

Q

R

M

L

M

A

K

A

D

R

L

G

G

L

I

T

E

P

P

H

V

Y

F

H

K

H

N

G

G

M

H

R

R

I

V

T

T

D

D

A

E

A

K

T

T

L

M

E

E

C

-

V

I

I

V

D

E

A

M

V

V

G

L

Q

V

L

G

R

K

I

I

A

N

I

K

E

E

A

I

R

V

L

M

S

N

M

L

D

N

M

L

A

H

S

G

S

G

P

R

M

A

Q

V

G

G

-

I

-

C

-

G

-

K

-

D

S

S

R

K

L

L

R

I

V

V

A

A

S

E

G

K

N

E

L

T

V

K

T

H

A

G

R

-

P

-

I

-

G

-

V

-

L

-

E

-

G

-

V

-

D

D

Y

I

H

G

H

Y

T

V

G

G

E

K

V

V

R

K

R

K

V

V

D

N

R

P

K

E

G

I

I

L

N

H

R

A

L

L

L

I

D

E

E

N

R

D

S

Y

I

I

V

P

L

V

L

I

S

A

P

P

L

V

G

G

Y

I

S

G

P

E

T

D

G

G

E

H

I

S

F

Y

N
|
N

L

I

A

N

C

A

E

D

D

T

V

A

A

A

T

A

R

E

A

I

A

A

I

K

D

S

L

L

A

M

A

A

D

E

K
|
K

L

L

L

I

L

L

F

L

G

T

S

D

E

V

Q

D

G

G

L

V

I

L

G

-

E

K

D

D

G

G

R

K

L

L

V

I

R
x
S

E

T

L

L

R

T

P

P

Q

D

Q

E

V

A

P

E

A

E

H

L

I

I

Q

-

R

R

L

D

G

G

S

T

D

V

Y

T

Q

G

A

G

E

M

L

I

-

P

-

K

L

V

D

E

A

C

A

A

A

V

Q

S

A

A

C

V

R

R

G

G

G

G

V

V

A

G

R

A

S

V

H

H

I

I

V

I

S

N

Y

G

V

G

E

L

N

E

G

H

A

A

L

I

L

L

A

L

E
|
E

L
x
I

F
|
F

T
x
S

R

R

D

K

G

G

S

I

G

G

T

T

L

M

V

I

A

K

Q

E

N178 (= N181) binding
K196 (= K199) binding
S214 (≠ R218) binding
EIFS 266:269 (≠ ELFT 269:272) binding

Q9HTN2 Acetylglutamate kinase; N-acetyl-L-glutamate 5-phosphotransferase; NAG kinase; NAGK; EC 2.7.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
29% identity, 64% coverage: 8:284/432 of query aligns to 15:299/301 of Q9HTN2

query
sites
Q9HTN2

L

L

R

S

H

E

A

A

S

L

P

P

Y

Y

I

I

N

R

A

R

H

F

R

V

D

G

C

K

T

T

F

L

I

V

V

I

M

K

L

Y

P

G

G

G

D

N

G

A

V

M

E

E

H

S

P

E

N

E

F

L

-

K

G

A

N

G

I

F

V

A

H

R

D

D

L

V

V

V

L

L

L

M

H

K

S

A

L

V

G

G

V

I

R

N

L

P

V

V

L

V

V

V

H

H

G

G

S

G

R

G

P

P

Q

Q

I

I

E

G

T

D

R

L

L

L

A

K

A

R

R

L

G

S

L

I

T

E

P

S

H

H

Y

F

H

I

H

D

G

G

M

M

R
|
R

I

V

T

T

D

D

A

A

A

A

T

T

L

M

E

D

C

V

V

V

I

-

D

-

A

-

V

-

G

-

Q

-

L

-

R

E

I

M

A

V

I

L

E

G

A

G

R

Q

L

V

S

N

M

K

D

D

M

I

A

V

S

N

-

L

-

I

S

N

P

R

M

H

Q

G

G

G

S

S

R

A

L

I

R

G

V

L

A

T

S

G

G

K

N

D

-

A

-

E

L

L

V

I

T

R

A

A

R

K

P

K

I

L

G

T

V

V

L

T

-

R

-

Q

-

T

-

P

-

E

-

M

-

T

-

K

-

P

E

E

G

I

V

I

D

D

Y

I

H

G

H

H

T

V

G

G

E

E

V

V

R

T

R

G

V

V

D

N

R

V

K

G

G

L

I

L

N

N

R

M

L

L

L

V

D

K

E

G

R

D

S

F

I

I

V

P

L

V

L

I

S

A

P

P

L

I

G

G

Y

V

S

G

P

S

T

N

G

G

E

E

I

S

F

Y

N
|
N

L

I

A

N

C

A

E

D

D

L

V

V

A

A

T

G

R

K

A

V

A

A

I

E

D

A

L

L

A

K

A

A

D

E

K

K

L

L

L

M

L

L

F

L

G

T

S

N

E

I

Q

A

G

G

L

L

I

M

G

D

E

K

D

Q

G

G

R

Q

L

V

V

L

R

T

E

G

L

L

R

S

P

T

Q

E

Q

Q

V

V

P

N

A

E

H

L

I

I

Q

A

R

D

L

-

G

G

S

T

D

I

Y

Y

Q

G

A

G

E

M

L

L

-

P

-

K

L

I

D

R

A

C

A

A

A

L

Q

E

A

A

C

V

R

Q

G

G

G

G

V

V

A

T

R

S

S

A

H

H

I

I

V

I

S

D

Y

G

V

R

E

V

N

P

G

N

A

A

L

V

L

L

A

L

E

E

L

I

F

F

T

T

R

D

D

S

G

G

S

V

G

G

T

T

L

L

V

I

A

S

Q

N

E

R

Q

K

R90 (= R82) binding
N195 (= N181) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

2v5hB Controlling the storage of nitrogen as arginine: the complex of pii and acetylglutamate kinase from synechococcus elongatus pcc 7942 (see paper)
29% identity, 66% coverage: 3:285/432 of query aligns to 5:286/289 of 2v5hB

query
sites
2v5hB

E

D

Y

R

V

V

N

R

W

I

L

L

R

S

H

E

A

A

S

L

P

P

Y

Y

I

L

N

Q

A

Q

H

F

R

A

D

G

C

R

T

T

F

V

I

V

V

V

M
x
K

L

Y

P

G

G
|
G

D

A

G

A

V

M

E

K

H

Q

P

E

N

E

F

L

G

K

N

E

-

A

I

V

V

M

H

R

D

D

L

I

V

V

L

F

L

L

H

A

S

C

L

V

G

G

V

M

R

R

L

P

V

V

L

V

V

V

H

H

G
|
G

S
x
G

R
x
G

P

P

Q

E

I
|
I

E

N

T

A

R

W

L

L

A

G

A

R

R

V

G

G

L

I

T

E

P

P

H

Q

Y

F

H

H

H

N

G

G

M
x
L

R
|
R

I

V

T

T

D

D

A

A

A

D

T

T

L

M

E

E

C

V

V

V

-

E

I

M

D

V

A

L

V

V

G

G

Q

R

L

V

R

N

I

K

A

D

I

I

E

V

A

S

R

R

L

I

S

N

M

-

D

-

M

-

A

-

S

T

S

T

P

G

M

G

Q

R

G

A

S

V

R

G

L

F

R

C

V

G

A

T

S

D

G

G

N

R

L

L

V

V

T

L

A

A

R

R

P

P

I

H

G

D

V

-

L

Q

E

E

G

G

V

I

D

G

Y

F

H

-

H

-

T

V

G

G

E

E

V

V

R

N

R

S

V

V

D

N

R

S

K

E

G

V

I

I

N

E

R

P

L

L

L

L

D

E

E

R

R

G

S

Y

I

I

V

P

L

V

L

I

S

S

P

S

L

V

G

A

Y

A

S

D

P

E

T

N

G

G

E

Q

I

S

F

F

N
|
N

L
x
I

A
x
N

C
x
A

E
x
D

D

T

V

V

A

A

T

G

R

E

A

I

A

A

I

A

D

A

L

L

A

N

A

A

D

E

K

K

L

L

L

I

L

L

F

L

G

T

S

D

E

T

Q

R

G

G

L

I

I

L

G

E

E

D

D

P

G

K

R

R

-

P

-

E

-

S

L

L

V

I

R

P

E

R

L

L

R

N

-

I

P

P

Q

Q

Q

S

V

R

P

E

A

L

H

I

I

A

Q

Q

R

G

L

I

G

V

S

G

D

G

Y

G

Q

M

A

I

E

P

L
x
K

L

V

D

D

A

C

A

C

A

I

Q

R

A

S

C

L

R

A

G

Q

G

G

V

V

A

R

R

A

S

A

H

H

I

I

V

I

S

D

Y

G

V

R

E

I

N

P

G

H

A

A

L

L

L

L

A

L

E

E

L

I

F

F

T

T

R

D

D

A

G

G

S

I

G

G

T

T

L

M

V

I

A

V

Q

G

E

S

Q

G

F

Y

active site: K28 (≠ M26), G31 (= G29), G64 (≠ R61), D182 (≠ E185), K241 (≠ L240)
binding n-acetyl-l-glutamate: G62 (= G59), G63 (≠ S60),