SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_106716882.1 NCBI__GCF_003010935.1:WP_106716882.1 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)

6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
40% identity, 93% coverage: 13:310/321 of query aligns to 2:292/293 of 6pnzA

query
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6pnzA

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binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S63), T49 (= T64), R50 (= R65), T51 (= T66), S75 (= S90), K78 (= K93), R100 (= R115), H127 (= H143), R160 (= R176), R210 (= R230), Q212 (= Q232), A253 (≠ G271)

P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
41% identity, 93% coverage: 13:310/321 of query aligns to 2:289/304 of P05654

query
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P05654

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Sites not aligning to the query:

303 modified: Phosphoserine

3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 93% coverage: 13:310/321 of query aligns to 2:289/291 of 3r7fA

query
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active site: R49 (= R65), T50 (= T66), K77 (= K93), R99 (= R115), H127 (= H143), Q130 (= Q146), L210 (= L229), P249 (= P270), G277 (= G298)
binding phosphoric acid mono(formamide)ester: S47 (= S63), T48 (= T64), R49 (= R65), T50 (= T66), R99 (= R115), H127 (= H143), Q130 (= Q146), P249 (= P270), A250 (≠ G271)
binding phosphate ion: S11 (= S22), T12 (≠ P23), Q23 (≠ E34), K26 (≠ Q42), E140 (≠ R156), R171 (≠ A187), K241 (≠ R262), H243 (≠ D264), K272 (≠ E293), K272 (≠ E293), K275 (≠ E296)

3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 93% coverage: 13:310/321 of query aligns to 2:289/291 of 3r7dA

query
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active site: R49 (= R65), T50 (= T66), K77 (= K93), R99 (= R115), H127 (= H143), Q130 (= Q146), L210 (= L229), P249 (= P270), G277 (= G298)
binding phosphate ion: S11 (= S22), T12 (≠ P23), T73 (≠ S89), S74 (= S90), K77 (= K93), R171 (≠ A187)

3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 93% coverage: 13:310/321 of query aligns to 2:289/290 of 3r7lA

query
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3r7lA

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E

D

E

I

I

V

K

Q

D

L

L

D

Q

L

T

A

A

E

Q

S

E

E

-

I

-

A

-

V

-

S

-

R

L

Q

K

S

S

E

G

K

K

K

T

K

D

A

N

T

Q

L

L

R

T

G

G

R

K

T

F

Q

A

I

A

N

N

L

L

F

F

E

E

S

P

S
|
S

T
|
T

R
|
R

T
|
T

Q

R

S

F

S

S

F

F

E

E

L

V

A

A

G

E

K

K

R

K

L

L

G

G

A

M

D

N

V

V

M

L

N

N

M

L

A

D

V

G

S

T

N

S

S

T

S
|
S

V

V

K

Q

K
|
K

G

G

E

E

T

T

L

L

I

Y

D

D

T

T

A

I

M

R

T

T

L

L

N

E

A

S

M

I

R

G

P

V

D

D

I

V

L

C

I

V

I

I

R
|
R

H

H

G

S

S

E

A

D

G

E

A

Y

A

E

L

E

L

L

A

V

Q

S

K

Q

V

V

G

N

C

I

S

P

V

I

V

L

N

N

A

A

G

G

D

D

G

G

A

C

H

G

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

S

L

L

D

D

A

L

L

M

T

T

I

I

R

Y

R

E

A

E

K

F

G

N

R

T

I

F

A

K

R

G

L

L

T

T

V

V

A

S

I

I

C

H

G

G

D

D

V

I

L

K

H

H

S

S

R
|
R

V

V

A

A

R

R

S

S

N

N

I

A

I

E

L

V

L

L

N

T

A

R

L

L

G

G

A

A

R

R

V

V

R

L

V

F

V

S

A

G

P

P

S

S

T

E

L

W

L

Q

P

D

S

E

G

E

I

N

A

T

H

-

M

F

G

G

A

T

E

Y

V

V

F

-

H

-

N

S

M

M

E

D

D

E

G

A

L

V

Q

E

D

S

A

S

D

D

V

V

M

M

M

L

L
|
L

R
|
R

L

I

Q
|
Q

R

N

E

E

R

R

M

H

T

Q

G

S

S

A

F

V

V

-

P

-

S

S

V

Q

R

E

E

G

Y

Y

F

L

R

N

Y

K

H

Y

G

G

L

L

D

T

R

V

E

E

K

R

L

A

R

E

Y

R

A

M

R

K

P

R

D

H

A

A

L

I

V

I

M

M

H

H

P
|
P

G
x
A

P

P

M

V

N

N

R

R

G

G

V

V

E

E

I

I

A

D

S

D

D

S

V

L

A

V

D

E

G

S

S

E

Q

K

S

S

V

R

I

I

Q

F

E

K

Q

Q

V

M

E

K

M

N

G
|
G

V

V

A

F

V

I

R

R

M

M

A

A

V

V

M

I

E

Q

A

R

L

A

L

L

active site: R49 (= R65), T50 (= T66), K77 (= K93), R99 (= R115), H127 (= H143), Q130 (= Q146), L210 (= L229), P249 (= P270), G277 (= G298)
binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S63), T48 (= T64), R49 (= R65), T50 (= T66), S74 (= S90), K77 (= K93), R99 (= R115), H127 (= H143), R160 (= R176), R211 (= R230), Q213 (= Q232), A250 (≠ G271)

4bjhB Crystal structure of the aquifex reactor complex formed by dihydroorotase (h180a, h232a) with dihydroorotate and aspartate transcarbamoylase with n-(phosphonacetyl)-l-aspartate (pala) (see paper)
36% identity, 89% coverage: 26:310/321 of query aligns to 4:290/291 of 4bjhB

query
sites
4bjhB

I

L

V

I

Q

S

L

S

L

L

D

D

L

L

A

T

E

R

S

E

E

E

I

V

-

E

-

I

-

L

-

K

A

Y

V

A

S

K

R

E

Q

F

S

K

E

E

K

G

K

K

K

E

A

E

T

T

L

I

R

K

G

A

R

-

T

S

Q

A

I

V

N

L

L

F

F

F

F

S

E

E

S

P

S
|
S

T
|
T

R
|
R

T
|
T

Q

R

S

L

S

S

F

F

E

E

L

K

A

A

G

A

K

R

R

E

L

L

G

G

A

I

D

E

V

T

M

Y

N

L

M

V

A

S

V

G

S

S

N

E

S

S

V

T

K

V

K
|
K

G

G

E

E

T

S

L

F

I

F

D

D

T

T

A

L

M

K

T

T

L

F

N

E

A

G

M

L

R

G

P

F

D

D

I

Y

L

V

I

V

I

F

R
|
R

H

V

G

P

S

F

A

V

G

F

A

F

A

P

A

Y

L

K

-

E

L

I

A

V

Q

K

K

S

V

L

G

N

C

L

S

R

V

L

V

V

N

N

A

A

G

G

D

D

G

G

A

T

H

H

E

Q

H
|
H

P

P

T

S

Q
|
Q

A

G

L

L

L

I

D

D

A

F

L

F

T

T

I

I

R

K

R

E

A

H

K

F

G

G

R

E

I

V

A

K

R

D

L

L

T

R

V

V

A

L

I

Y

C

V

G

G

D

D

V

I

L

K

H

H

S

S

R
|
R

V
|
V

A

F

R

R

S

S

N

G

I

A

I

P

L

L

N

N

A

M

L

F

G

G

A

A

R

K

V

I

R

G

V

V

V

C

A

G

P

P

S

K

T

T

L

L

L

I

P

P

S

R

G

D

I

V

A

E

H

V

M

F

G

K

A

V

E

D

V

V

F

F

H

D

N

D

M

V

E

D

D

K

G

G

L

I

Q

D

D

W

A

A

D

D

V

V

M

I

M

W

L

L

R
|
R

L

L

Q
|
Q

R

K

E

E

R

R

M

Q

T

K

G

E

S

N

F

Y

V

I

P

P

S

S

V

E

R

S

E

S

Y

Y

F

F

R

K

Y

Q

H

F

G

G

L

L

D

T

R

K

E

E

K

R

L

F

R

E

Y

K

A

V

R

K

P

-

D

-

A

-

L

L

V

Y

M

M

H

H

P

P

G
|
G

P

P

M

V

N

N

R

R

G

N

V

V

E

D

I

I

A

D

S

H

D

E

V

L

A

V

D

Y

G

T

S

E

Q

K

S

S

V

L

I

I

Q

Q

E

E

Q

Q

V

V

E

K

M

N

G

G

V

I

A

P

V

V

R

R

M

K

A

A

V

I

M

Y

E

K

A

F

L

L

L

W

active site: R47 (= R65), T48 (= T66), K75 (= K93), R97 (= R115), H126 (= H143), Q129 (= Q146)
binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S63), T46 (= T64), R47 (= R65), T48 (= T66), R97 (= R115), H126 (= H143), R159 (= R176), V160 (= V177), R213 (= R230), Q215 (= Q232), G251 (= G271)

3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
36% identity, 89% coverage: 26:310/321 of query aligns to 4:290/291 of 3d6nB

query
sites
3d6nB

I

L

V

I

Q

S

L

S

L

L

D

D

L

L

A

T

E

R

S

E

E

E

I

V

-

E

-

I

-

L

-

K

A

Y

V

A

S

K

R

E

Q

F

S

K

E

E

K

G

K

K

K

E

A

E

T

T

L

I

R

K

G

A

R

-

T

S

Q

A

I

V

N

L

L

F

F

F

F

S

E

E

S

P

S

S

T

T

R
|
R

T
|
T

Q

R

S

L

S

S

F

F

E

E

L

K

A

A

G

A

K

R

R

E

L

L

G

G

A

I

D

E

V

T

M

Y

N

L

M

V

A

S

V

G

S

S

N

E

S

S

V

T

K

V

K
|
K

G

G

E

E

T

S

L

F

I

F

D

D

T

T

A

L

M

K

T

T

L

F

N

E

A

G

M

L

R

G

P

F

D

D

I

Y

L

V

I

V

I

F

R
|
R

H

V

G

P

S

F

A

V

G

F

A

F

A

P

A

Y

L

K

-

E

L

I

A

V

Q

K

K

S

V

L

G

N

C

L

S

R

V

L

V

V

N

N

A

A

G

G

D

D

G

G

A

T

H

H

E

Q

H
|
H

P

P

T

S

Q
|
Q

A

G

L

L

L

I

D

D

A

F

L

F

T

T

I

I

R

K

R

E

A

H

K

F

G

G

R

E

I

V

A

K

R

D

L

L

T

R

V

V

A

L

I

Y

C

V

G

G

D

D

V

I

L

K

H

H

S

S

R
|
R

V
|
V

A

F

R

R

S

S

N

G

I

A

I

P

L

L

N

N

A

M

L

F

G

G

A

A

R

K

V

I

R

G

V

V

V

C

A

G

P

P

S

K

T

T

L

L

L

I

P

P

S

R

G

D

I

V

A

E

H

V

M

F

G

K

A

V

E

D

V

V

F

F

H

D

N

D

M

V

E

D

D

K

G

G

L

I

Q

D

D

W

A

A

D

D

V

V

M

I

M

W

L

L

R
|
R

L

L

Q

Q

R

K

E

E

R

R

M

Q

T

K

G

E

S

N

F

Y

V

I

P

P

S

S

V

E

R

S

E

S

Y

Y

F

F

R

K

Y

Q

H

F

G

G

L

L

D

T

R

K

E

E

K

R

L

F

R

E

Y

K

A

V

R

K

P

-

D

-

A

-

L

L

V

Y

M

M

H

H

P

P

G
|
G

P

P

M

V

N

N

R

R

G

N

V

V

E

D

I

I

A

D

S

H

D

E

V

L

A

V

D

Y

G

T

S

E

Q

K

S

S

V

L

I

I

Q

Q

E

E

Q

Q

V

V

E

K

M

N

G

G

V

I

A

P

V

V

R

R

M

K

A

A

V

I

M

Y

E

K

A

F

L

L

L

W

active site: R47 (= R65), T48 (= T66), K75 (= K93), R97 (= R115), H126 (= H143), Q129 (= Q146)
binding citrate anion: T48 (= T66), R97 (= R115), H126 (= H143), R159 (= R176), V160 (= V177), R213 (= R230), G251 (= G271)

P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
35% identity, 93% coverage: 13:310/321 of query aligns to 1924:2222/2225 of P08955

query
sites
P08955

R

Q

H

H

L

I

L

L

G

S

I

V

K

K

G

Q

L

F

S

T

P

K

Q

D

D

Q

I

M

V

S

Q

H

L

L

L

F

D

N

L

V

A

A

E

H

S

T

E

-

I

L

A

R

V

M

S

M

R

V

Q

Q

S

K

E

E

K

R

K

S

K

L

A

D

T

I

L

L

R

K

G

G

R

K

T

V

Q

M

I

A

N

S

L

M

F

F

F

Y

E

E

S

V

S

S

T

T

R

R

T

T

Q

S

S

S

F

F

E

A

L

A

A

A

G

M

K

A

R

R

L

L

G

G

A

G

D

A

V

V

M

L

N

S

M

F

A

S

V

E

S

A

N

T

S

S

V

V

K

Q

K

K

G

G

E

E

T

S

L

L

I

A

D

D

T

S

A

V

M

Q

T

T

L

M

N

S

A

C

M

Y

R

A

P

-

D

D

I

V

L

V

I

V

I

L

R

R

H

H

G

P

S

Q

A

P

G

G

A

A

A

V

A

E

L

L

L

A

A

A

Q

K

K

H

V

C

G

R

C

R

S

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

A

V

H

G

E

E

H

H

P

P

T

T

Q

Q

A

A

L

L

D

D

A

I

L

F

T

T

I

I

R

R

R

E

A

E

K

L

G

G

R

T

I

V

A

N

R

G

L

M

T

T

V

I

A

T

I

M

C

V

G

G

D

D

V

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

A

I

C

L

L

N

T

A

Q

L

Y

G

R

A

V

R

S

V

L

R

R

V

Y

V

V

A

A

P

P

S

P

T

S

L

L

-

R

L

M

P

P

S

P

G

S

I

V

A

W

H

D

M

F

G

V

A

A

-

S

-

R

-

G

-

T

-

K

-

Q

E

E

V

E

F

F

H

E

N

S

M

I

E

E

D

E

G

A

L

L

Q

P

D

D

A

T

D

D

V

V

V

L

M

Y

M

M

L

T

R

R

L

I

Q

Q

R

K

E

E

R

R

M

F

T

G

G

-

S

-

F

-

V

-

P

-

S

S

V

T

R

Q

E

E

Y

Y

F

E

R

A

Y

C

H

F

G

G

-

Q

-

F

-

I

L

L

D

T

R

P

E

H

K

I

L

M

R

T

Y

R

A

A

R

K

P

K

D

K

A

M

L

V

V

V

M

M

H

H

P

-

G

-

P

P

M

M

N

P

R

R

G

V

V

N

E

E

I

I

A

S

S

V

D

E

V

V

A

D

D

S

G

D

S

P

Q

R

S

A

V

A

I

Y

Q

F

E

R

Q

Q

V

A

E

E

M

N

G

G

V

M

A

Y

V

I

R

R

M

M

A

A

V

L

M

L

E

A

A

T

L

V

L

L

Sites not aligning to the query:

1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.

P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
34% identity, 93% coverage: 13:310/321 of query aligns to 1924:2222/2225 of P27708

query
sites
P27708

R
x
Q

H
|
H

L
x
I

L
|
L

G
x
S

I
x
V

K
x
Q

G
x
Q

L
x
F

S
x
T

P
x
K

Q
x
D

D
x
Q

I
x
M

V
x
S

Q
x
H

L
|
L

L
x
F

D
x
N

L
x
V

A
|
A

E
x
H

S
x
T

E

-

I
x
L

A
x
R

V
x
M

S
x
M

R
x
V

Q
|
Q

S
x
K

E
|
E

K
x
R

K
x
S

K
x
L

A
x
D

T
x
I

L
|
L

R
x
K

G
|
G

R
x
K

T
x
V

Q
x
M

I
x
A

N
x
S

L
x
M

F
|
F

F
x
Y

E
|
E

S
x
V

S
|
S

T
|
T

R
|
R

T
|
T

Q
x
S

S
|
S

F
|
F

E
x
A

L
x
A

A
|
A

G
x
M

K
x
A

R
|
R

L
|
L

G
|
G

A
x
G

D
x
A

V
|
V

M
x
L

N
x
S

M
x
F

A
x
S

V
x
E

S
x
A

N
x
T

S
|
S

V
|
V

K
x
Q

K
|
K

G
|
G

E
|
E

T
x
S

L
|
L

I
x
A

D
|
D

T
x
S

A
x
V

M
x
Q

T
|
T

L
x
M

N
x
S

A
x
C

M
x
Y

R
x
A

P

-

D
|
D

I
x
V

L
x
V

I
x
V

I
x
L

R
|
R

H
|
H

G
x
P

S
x
Q

A
x
P

G
|
G

A
|
A

A
x
V

A
x
E

L
|
L

L
x
A

A
|
A

Q
x
K

K
x
H

V
x
C

G
x
R

C
x
R

S
x
P

V
|
V

V
x
I

N
|
N

A
|
A

G
|
G

D
|
D

G
|
G

A
x
V

H
x
G

E
|
E

H
|
H

P
|
P

T
|
T

Q
|
Q

A
|
A

L
|
L

D
|
D

A
x
I

L
x
F

T
|
T

I
|
I

R
|
R

R
x
E

A
x
E

K
x
L

G
|
G

R
x
T

I
x
V

A
x
N

R
x
G

L
x
M

T
|
T

V
x
I

A
x
T

I
x
M

C
x
V

G
|
G

D
|
D

V
x
L

L
x
K

H
|
H

S
x
G

R
|
R

V
x
T

A
x
V

R
x
H

S
|
S

N
x
L

I
x
A

I
x
C

L
|
L

N
x
T

A
x
Q

L
x
Y

G
x
R

A
x
V

R
x
S

V
x
L

R
|
R

V
x
Y

V
|
V

A
|
A

P
|
P

S
x
P

T
x
S

L
|
L

-
x
R

L
x
M

P
|
P

S
x
P

G
x
T

I
x
V

A
x
R

H
x
A

M
x
F

G
x
V

A
|
A

-
x
S

-
x
R

-
x
G

-
x
T

-
x
K

-
x
Q

E
|
E

V
x
E

F
|
F

H
x
E

N
x
S

M
x
I

E
|
E

D
x
E

G
x
A

L
|
L

Q
x
P

D
|
D

A
x
T

D
|
D

V
|
V

V
x
L

M
x
Y

M
|
M

L
x
T

R
|
R

L
x
I

Q
|
Q

R
x
K

E
|
E

R
|
R

M
x
F

T
x
G

G

-

S

-

F

-

V

-

P

-

S
|
S

V
x
T

R
x
Q

E
|
E

Y
|
Y

F
x
E

R
x
A

Y
x
C

H
x
F

G
|
G

-
x
Q

-
x
F

-
x
I

L
|
L

D
x
T

R
x
P

E
x
H

K
x
I

L
x
M

R
x
T

Y
x
R

A
|
A

R
x
K

P
x
K

D
x
K

A
x
M

L
x
V

V
|
V

M
|
M

H
|
H

P

-

G

-

P
|
P

M
|
M

N
x
P

R
|
R

G
x
V

V
x
N

E
|
E

I
|
I

A
x
S

S
x
V

D
x
E

V
|
V

A
x
D

D
x
S

G
x
D

S
x
P

Q
x
R

S
x
A

V
x
A

I
x
Y

Q
x
F

E
x
R

Q
|
Q

V
x
A

E
|
E

M
x
N

G
|
G

V
x
M

A
x
Y

V
x
I

R
|
R

M
|
M

A
|
A

V
x
L

M
x
L

E
x
A

A
x
T

L
x
V

L
|
L

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
456 modified: Phosphothreonine; by MAPK1
735 Y → C: in a colorectal cancer sample; somatic mutation
1406 modified: Phosphoserine; by PKA
1471 binding Zn(2+); binding Zn(2+); H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
1473 binding Zn(2+); H→A: No zinc-binding and no catalytic activity.
1475 binding (S)-dihydroorotate
1505 binding (S)-dihydroorotate
1512 D→N: No change in catalytic activity.
1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
1562 T→A: Abolishes dihydroorotase activity.
1563 F→A: Abolishes dihydroorotase activity.
1590 binding Zn(2+); H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
1613 binding Zn(2+); C→S: Reduces dihydroorotase activity.
1614 binding Zn(2+); H→A: Abolishes dihydroorotase activity.
1637 binding Zn(2+); E→T: Abolishes dihydroorotase activity.
1642 H→N: 11.5% of wild-type catalytic activity.
1661 binding (S)-dihydroorotate
1686 binding Zn(2+); D→N: Abolishes dihydroorotase activity.
1690 binding (S)-dihydroorotate; H→N: 3% of wild-type catalytic activity.
1702 binding (S)-dihydroorotate
1789:2225 natural variant: Missing (in DEE50; uncertain significance)
1859 modified: Phosphoserine; by RPS6KB1 and PKA
1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
1900 modified: Phosphoserine

5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
34% identity, 93% coverage: 13:310/321 of query aligns to 3:289/292 of 5g1pA

query
sites
5g1pA

R

Q

H

H

L

I

L

L

G

S

I

V

K

Q

G

Q

L

F

S

T

P

K

Q

D

D

Q

I

M

V

S

Q

H

L

L

L

F

D

N

L

V

A

A

E

H

S

T

E

-

I

L

A

R

V

M

S

M

R

V

Q

Q

S

K

E

E

K

R

K

S

K

L

A

D

T

I

L

L

R

K

G

G

R

K

T

V

Q

M

I

A

N

S

L

M

F

F

F

Y

E

E

S

V

S
|
S

T
|
T

R
|
R

T
|
T

Q

S

S

S

F

F

E

A

L

A

A

A

G

M

K

A

R

R

L

L

G

G

A

G

D

A

V

V

M

L

N

S

M

F

A

S

V

E

S

A

N

T

S

S

V

V

K

Q

K
|
K

G

G

E

E

T

S

L

L

I

A

D

D

T

S

A

V

M

Q

T

T

L

M

N

S

A

C

M

Y

R

-

P

A

D

D

I

V

L

V

I

V

I

L

R
|
R

H

H

G

P

S

Q

A

P

G

G

A

A

A

V

A

E

L

L

L

A

A

A

Q

K

K

H

V

C

G

R

C

R

S

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

A

V

H

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

A

I

L

F

T

T

I

I

R

R

R

E

A

E

K

L

G

G

R

T

I

V

A

N

R

G

L

M

T

T

V

I

A

T

I

M

C

V

G

G

D

D

V

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

A

I

C

L

L

N

T

A

Q

L

Y

G

R

A

V

R

S

V

L

R

R

V

Y

V

V

A

A

P

P

S

P

T

S

L

L

-

R

L

M

P

P

S

P

G

T

I

V

A

R

H

A

M

F

G

V

A

A

-

S

-

G

-

T

-

K

-

Q

E

E

V

E

F

F

H

E

N

S

M

I

E

E

D

E

G

A

L

L

Q

P

D

D

A

T

D

D

V

V

V

L

M

Y

M

M

L
x
T

R

R

L

I

Q

Q

R

K

E

E

R

R

M

F

T

Q

G

F

S

I

F

L

V

T

P

P

S

-

V

-

R

-

E

-

Y

-

F

-

R

-

Y

-

H

H

G

I

L

M

D

T

R

R

E

-

K

-

L

-

R

-

Y

-

A

A

R

K

P

K

D

K

A

M

L

V

V

V

M

M

H

H

P
|
P

G
x
M

P

P

M

-

N

-

R

R

G

V

V

N

E

E

I

I

A

S

S

V

D

E

V

V

A

D

D

S

G

D

S

P

Q

R

S

A

V

A

I

Y

Q

F

E

R

Q

Q

V

A

E

E

M

N

G
|
G

V

M

A

Y

V

I

R

R

M

M

A

A

V

L

M

L

E

A

A

T

L

V

L

L

active site: R54 (= R65), T55 (= T66), K82 (= K93), R103 (= R115), H131 (= H143), Q134 (= Q146), T223 (≠ L229), P251 (= P270), G277 (= G298)
binding phosphoric acid mono(formamide)ester: S52 (= S63), T53 (= T64), R54 (= R65), T55 (= T66), R103 (= R115), Q134 (= Q146), M252 (≠ G271)

5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
34% identity, 93% coverage: 13:310/321 of query aligns to 6:304/307 of 5g1nE

query
sites
5g1nE

R

Q

H

H

L

I

L

L

G

S

I

V

K

Q

G

Q

L

F

S

T

P

K

Q

D

D

Q

I

M

V

S

Q

H

L

L

L

F

D

N

L

V

A

A

E

H

S

T

E

-

I

L

A

R

V

M

S

M

R

V

Q

Q

S

K

E

E

K

R

K

S

K

L

A

D

T

I

L

L

R

K

G

G

R

K

T

V

Q

M

I

A

N

S

L

M

F

F

F

Y

E

E

S

V

S
|
S

T
|
T

R
|
R

T
|
T

Q

S

S

S

F

F

E

A

L

A

A

A

G

M

K

A

R

R

L

L

G

G

A

G

D

A

V

V

M

L

N

S

M

F

A

S

V

E

S

A

N

T

S

S

S
|
S

V

V

K

Q

K
|
K

G

G

E

E

T

S

L

L

I

A

D

D

T

S

A

V

M

Q

T

T

L

M

N

S

A

C

M

Y

R

-

P

A

D

D

I

V

L

V

I

V

I

L

R
|
R

H

H

G

P

S

Q

A

P

G

G

A

A

A

V

A

E

L

L

L

A

A

A

Q

K

K

H

V

C

G

R

C

R

S

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

A

V

H

G

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

L

D

D

A

I

L

F

T

T

I

I

R

R

R

E

A

E

K

L

G

G

R

T

I

V

A

N

R

G

L

M

T

T

V

I

A

T

I

M

C

V

G

G

D

D

V

L

L

K

H

H

S

G

R
|
R

V

T

A

V

R

H

S

S

N

L

I

A

I

C

L

L

N

T

A

Q

L

Y

G

R

A

V

R

S

V

L

R

R

V

Y

V

V

A

A

P

P

S

P

T

S

L

L

-

R

L

M

P

P

S

P

G

T

I

V

A

R

H

A

M

F

G

V

A

A

-

S

-

R

-

G

-

T

-

K

-

Q

E

E

V

E

F

F

H

E

N

S

M

I

E

E

D

E

G

A

L

L

Q

P

D

D

A

T

D

D

V

V

V

L

M

Y

M

M

L
x
T

R
|
R

L

I

Q
|
Q

R

K

E

E

R

R

M

F

T

G

G

-

S

-

F

-

V

-

P

-

S

S

V

T

R

Q

E

E

Y

Y

-

E

-

A

-

C

F

F

R

G

Y

Q

H

F

G

I

L

L

D

T

R

P

E

H

K

I

L

M

R

T

Y

R

A

A

R

K

P

K

D

K

A

M

L

V

V

V

M

M

H

H

P
|
P

G
x
M

P

P

M

-

N

-

R

R

G

V

V

N

E

E

I

I

A

S

S

V

D

E

V

V

A

D

D

S

G

D

S

P

Q

R

S

A

V

A

I

Y

Q

F

E

R

Q

Q

V

A

E

E

M

N

G
|
G

V

M

A

Y

V

I

R

R

M

M

A

A

V

L

M

L

E

A

A

T

L

V

L

L

active site: R57 (= R65), T58 (= T66), K85 (= K93), R106 (= R115), H134 (= H143), Q137 (= Q146), T227 (≠ L229), P266 (= P270), G292 (= G298)
binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S63), T56 (= T64), R57 (= R65), T58 (= T66), S82 (= S90), K85 (= K93), R106 (= R115), H134 (= H143), R167 (= R176), R228 (= R230), Q230 (= Q232), M267 (≠ G271)

8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
33% identity, 93% coverage: 7:306/321 of query aligns to 10:311/316 of 8bplA

query
sites
8bplA

P

P

L

S

F

F

P

K

H

K

R

S

H

H

L

V

L

L

G

S

I

V

K

T

G

Q

L

F

S

T

P

R

Q

A

D

D

I

L

V

H

Q

L

L

L

L

F

D

Q

L

I

A

A

E

Q

S

-

E

E

I

M

A

R

V

L

S

G

R

V

Q

Q

S

R

E

E

K

G

K

V

K

L

A

D

T

I

L

L

R

R

G

G

R

K

T

V

Q

L

I

C

N

T

L

L

F

F

F

Y

E

E

S

P

S
|
S

T
|
T

R
|
R

T
|
T

Q

S

S

A

S

S

F

F

E

D

L

A

A

A

G

M

K

Q

R

R

L

L

G

G

A

G

D

R

V

T

M

I

N

P

M

I

A

Q

V

T

S

S

N

T

S

S

V

V

K

Q

K

K

G

G

E

E

T

T

L

L

I

Q

D

D

T

T

A

L

M

R

T

T

L

L

N

-

A

A

M

C

R

Y

P

S

D

D

I

A

L

I

I

V

I

L

R
|
R

H

H

G

P

S

D

A

E

G

K

A

C

A

V

A

D

L

V

L

A

A

K

Q

K

K

Y

V

C

G

P

C

V

S

P

V

V

V

I

N

N

A

G

G

G

D

N

G

G

A

S

H

K

E

E

H
|
H

P

P

T

T

Q
|
Q

A

A

L

F

L

L

D

D

A

L

L

F

T

T

I

I

R

R

R

E

A

E

K

L

G

G

R

T

I

M

A

Q

R

G

L

L

T

T

V

I

A

T

I

F

C

V

G

G

D

D

V

L

L

L

H

Y

S

G

R

R

V

P

A

V

R

H

S

S

N

L

I

V

I

Y

L

L

N

R

A

H

L

Y

G

Q

A

V

R

K

V

V

R

Q

V

L

V

V

A

S

P

P

S

K

T

A

L

L

-

R

L

L

P

P

S

P

G

A

I

V

-

R

-

Q

-

L

-

V

-

D

-

A

A

G

H

Q

M

L

G

L

A

C

E

E

V

S

F

E

H

A

N

L

M

T

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P

D

E

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I

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L

Q

G

D

R

A

T

D

D

V

V

V

L

M

Y

M

C

L

T

R

R

L

V

Q

Q

R

K

E

E

R

R

M

F

T

P

G

S

-

L

S

A

F

E

V

F

P

E

S

A

V

V

R

K

E

D

Y

S

F

Y

R

R

Y

-

H

-

G

-

L

I

D

D

R

Y

E

S

K

T

L

L

R

K

Y

Y

A

A

R

K

P

P

D

T

A

T

L

V

V

V

M

M

H

H

P

P

G
x
L

P

P

M

R

N

N

R

E

G

-

V

-

E

E

I

V

A

A

S

E

D

E

V

V

A

D

D

F

G

D

S

Q

Q

R

S

A

V

A

I

Y

Q

F

E

R

Q

Q

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M

E

C

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Y

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G

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A

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M

A

A

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L

M

L

binding phosphoric acid mono(formamide)ester: S65 (= S63), T66 (= T64), R67 (= R65), T68 (= T66), R116 (= R115), H144 (= H143), Q147 (= Q146), L278 (≠ G271)

1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
36% identity, 93% coverage: 13:310/321 of query aligns to 5:304/307 of 1ml4A

query
sites
1ml4A

R

R

H

D

L

V

L

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G

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I

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R

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D

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F

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K

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D

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D

A

L

T

A

A

E

E

S

R

E

-

I

-

A

-

V

L

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E

R

R

Q

E

S

L

E

-

K

K

K

E

K

K

A

G

T

Q

L

L

-

E

-

Y

-

A

R

K

G

G

R

K

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I

Q

L

I

A

N

T

L

L

F

F

E

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S
|
S

T
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T

R
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R

T
|
T

Q

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S

F

F

E

E

L

S

A

A

G

M

K

H

R

R

L

L

G

G

A

G

D

A

V

V

M

I

N

G

M

F

A

A

-

E

V

A

S

S

N

T

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S

V

V

K

K

K
|
K

G

G

E

E

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L

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D

D

T

T

A

I

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T

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N

E

A

Q

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R

-

P

C

D

D

I

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L

I

I

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I

I

R
|
R

H

H

G

P

S

K

A

E

G

G

A

A

A

R

L

L

L

A

A

A

Q

E

K

V

V

A

G

E

C

V

S

P

V

V

V

I

N

N

A

A

G

G

D

D

G

G

A

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E

Q

H
|
H

P

P

T

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Q

A

T

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L

D

D

A

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Y

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I

I

R

K

A

E

K

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G

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I

A

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A

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C

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G

D

D

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L

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S

G

R
|
R

V
x
T

A

V

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S

N

L

I

A

I

E

L

A

L

L

N

T

A

F

L

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G

D

A

V

R

E

V

L

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Y

V

L

V

I

A

S

P

P

S

E

T

L

L

L

-

R

L

M

P

P

S

R

G

H

I

I

A

V

-

E

-

L

-

R

H

E

M

K

G

G

A

M

E

K

V

V

F

V

H

E

-

T

N

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M

L

E

E

D

D

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D

K

A

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D

V

V

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M

Y

M

V

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x
T

R
|
R

L

I

Q

Q

R

K

E

E

R

R

M

F

T

-

G

-

S

-

F

-

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-

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P

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E

R

Q

E

E

Y

Y

F

L

R

K

Y

V

H

K

G

G

-

S

-

Y

-

Q

L

V

D

N

R

L

E

K

K

V

L

L

R

E

Y

K

A

A

R

K

P

D

D

E

A

L

L

R

V

I

M

M

H

H

P
|
P

G
x
L

P

P

M

-

N

-

R

R

G

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V

D

E

E

I

I

A

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P

D

E

V

V

A

D

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G

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S

K

Q

H

S

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I

I

Y

Q

F

E

R

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Q

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G

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A

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M

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E

A

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L

active site: R56 (= R65), T57 (= T66), K85 (= K93), R106 (= R115), H134 (= H143), Q137 (= Q146), T227 (≠ L229), P266 (= P270), G292 (= G298)
binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S63), T55 (= T64), R56 (= R65), T57 (= T66), R106 (= R115), H134 (= H143), R167 (= R176), T168 (≠ V177), R228 (= R230), L267 (≠ G271)

4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
35% identity, 93% coverage: 13:311/321 of query aligns to 2:301/304 of 4eknB

query
sites
4eknB

R

K

H

H

L

L

L

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S

I

M

K

K

G

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E

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D

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A

A

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K

-

M

-

E

E

E

I

L

A

L

V

N

S

T

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K

Q

R

S

P

E

L

K

K

K

-

A

-

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L

L

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E

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G

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K

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I

Q

L

I

A

N

T

L

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F

F

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A

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M

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K

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R

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L

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G

A

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M

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A

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A

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G

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T

S

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L

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I

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D

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T

A

I

M

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T

V

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N

S

A

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M

Y

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A

D

D

I

I

L

I

I

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I

L

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R

H

H

G

P

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S

A

E

G

G

A

A

A

R

L

L

L

A

A

S

Q

E

K

Y

V

S

G

Q

C

V

S

P

V

I

N

N

A

A

G

G

D

D

G

G

A

S

H

N

E

Q

H

H

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P

T

T

Q

Q

A

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L

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D

A

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M

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A

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K

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G

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I

I

A

D

R

G

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K

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I

A

A

I

F

C

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G

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x
G

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x
T

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N

L

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I

Y

L

A

L

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S

A

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N

A

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K

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E

L

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K

G

D

I

I

A

I

H

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-

D

M

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A

A

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K

-

N

-

I

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K

F

F

H

Y

N

E

M

K

E

E

D

S

-

L

-

D

G

L

L

D

Q

D

D

D

A

I

D

D

V

V

V

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M

Y

M

V

L
x
T

R
|
R

L

I

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Q

R

K

E

E

R

R

M

F

T

-

G

-

S

-

F

-

V

-

P

P

S

D

V

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R

N

E

E

Y

Y

F

E

R

K

Y

V

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K

G

G

L

S

D

Y

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K

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I

K

K

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E

Y

Y

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V

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E

-

G

P

K

D

K

A

F

L

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M

M

H

H

P
|
P

G

L

P

P

M

-

N

-

R

R

G

V

V

D

E

E

I

I

A

D

S

Y

D

D

V

V

A

D

D

D

G

L

S

P

Q

Q

S

A

V

K

I

Y

Q

F

E

K

Q

Q

V

S

E

F

M

Y

G
|
G

V

I

A

P

V

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R

M

M

A

A

V

I

M

L

E

K

A

K

L

L

L

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D

E

active site: T225 (≠ L229), P262 (= P270), G288 (= G298)
binding sulfate ion: G163 (≠ S175), R164 (= R176), T165 (≠ V177), R226 (= R230)

P20054 Multifunctional protein pyr1-3; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Dictyostelium discoideum (Social amoeba)
33% identity, 92% coverage: 13:306/321 of query aligns to 1923:2217/2225 of P20054

query
sites
P20054

R

K

H

H

L

I

L

F

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S

I

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K

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S

N

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A

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D

G

L

I

A

A

-

H

E

E

S

M

E

R

I

I

A

L

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V

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R

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E

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K

-

A

-

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T

L

L

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F

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E

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T

T

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R

T

T

Q

Q

S

C

S

S

F

F

E

T

L

A

A

A

G

M

K

Q

R

R

L

L

G

G

A

G

D

S

V

V

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N

T

M

V

A

D

V

N

S

V

N

S

S

S

V

V

K

A

K

K

G

G

E

E

T

S

L

I

I

A

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D

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T

A

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Q

T

T

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L

N

E

A

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-

P

C

D

D

I

A

L

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I

C

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R

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P

S

A

A

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A

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A

E

L

S

L

A

A

I

Q

Q

K

V

V

A

G

K

C

K

S

P

V

I

N

N

A

A

G

G

D

D

G

G

A

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H

G

E

E

H

H

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P

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T

Q

Q

A

A

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D

A

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F

T

T

I

I

R

R

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E

A

E

K

L

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G

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A

N

R

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I

A

T

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C

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G

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G

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V

T

A

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S

S

N

L

I

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I

R

L

L

N

A

A

N

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G

Q

A

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K

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I

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N

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Y

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V

A

S

P

P

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T

S

L

L

-

S

L

M

P

P

S

T

G

E

I

I

A

I

H

K

-

E

-

L

-

N

-

E

-

K

-

G

M

I

G

E

A

Q

E

K

V

E

F

Y

H

T

N

N

M

I

E

E

D

S

G

I

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Q

P

D

T

A

T

D

N

V

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Y

M

V

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R

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Q

Q

R

K

E

E

R

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M

F

T

Q

G

-

S

-

F

-

V

-

P

-

S

S

V

I

R

E

E

E

Y

Y

F

E

R

K

Y

V

H

K

G

D

-

S

-

F

-

I

L

I

D

T

R

P

E

H

K

T

L

L

R

T

Y

K

A

A

R

S

P

D

D

N

A

M

L

I

V

V

M

M

H

H

P

P

G

L

P

P

M

-

N

-

R

R

G

I

V

N

E

E

I

I

A

S

S

P

D

E

V

V

A

D

D

S

G

D

S

P

Q

R

S

A

V

A

I

Y

Q

F

E

R

Q

Q

V

M

E

E

M

N

G

G

V

L

A

Y

V

V

R

R

M

M

A

S

V

L

M

L

Sites not aligning to the query:

1 modified: N-acetylmethionine

P05990 Multifunctional protein r; Protein rudimentary; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
32% identity, 95% coverage: 13:316/321 of query aligns to 1918:2223/2224 of P05990

query
sites
P05990

R

K

H

H

L

I

L

L

G

A

I

V

K

D

G

M

L

F

S

N

P

K

Q

D

D

H

I

L

V

N

Q

D

L

I

L

F

D

N

L

L

A

A

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Q

S

L

E

L

I

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A

L

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R

K

P

K

V

K

D

A

E

T

L

L

L

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P

G

G

R

K

T

I

Q

M

I

A

N

S

L

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F

F

F

Y

E

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S

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T

R

R

T

T

Q

Q

S

C

S

S

F

F

E

A

L

A

A

A

G

M

K

L

R

R

L

L

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G

A

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M

M

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G

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N

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P

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G

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A

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A

A

A

Q

T

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L

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I

N

N

A

A

G

G

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D

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G

A

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G

E

E

H

H

P

P

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T

Q

Q

A

A

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D

D

A

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I

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E

A

E

K

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N

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A

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S

S

N

L

I

A

I

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T

A

L

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Y

G

N

A

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R

N

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L

R

Q

V

Y

V

V

A

A

P

P

S

N

T

S

L

L

-

Q

L

M

P

P

S

D

G

E

I

V

A

V

H

Q

M

F

-

V

-

H

-

Q

-

R

-

G

G

V

A

K

E

Q

V

L

F

F

-

A

H

R

N

D

M

L

E

K

D

N

G

V

L

L

Q

P

D

D

A

T

D

D

V

V

V

L

M

Y

M

M

L

T

R

R

L

I

Q

Q

R

R

E

E

R

R

M

F

T

D

G

-

S

-

F

-

V

-

P

-

S

N

V

V

R

E

E

D

Y

Y

F

E

R

K

Y

C

H

C

G

G

-

H

-

L

-

V

L

L

D

T

R

P

E

E

K

H

L

M

R

M

Y

R

A

A

R

K

P

K

D

R

A

S

L

I

V

V

M

L

H

H

P

P

G

L

P

P

M

-

N

-

R

R

G

L

V

N

E

E

I

I

A

S

S

R

D

E

V

I

A

D

D

S

G

D

S

P

Q

R

S

A

V

A

I

Y

Q

F

E

R

Q

Q

V

A

E

E

M

Y

G

G

V

M

A

Y

V

I

R

R

M

M

A

A

V

L

M

L

E

A

A

M

L

V

D

G

P

G

R

R

R

N

N

T

A

A

Sites not aligning to the query:

1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
1883 modified: Phosphoserine
1885 modified: Phosphoserine
1892 modified: Phosphoserine
1894 modified: Phosphoserine

P07259 Multifunctional protein URA2; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
35% identity, 93% coverage: 10:306/321 of query aligns to 1908:2206/2214 of P07259

query
sites
P07259

F

F

P

R

H

G

R

R

H

H

L

I

L

L

G

S

I

I

K

K

G

Q

L

F

S

K

P

R

Q

S

D

D

I

F

V

H

Q

V

L

L

L

F

D

A

L

V

A

A

-

Q

E

E

S

L

E

R

I

A

A

A

V

V

S

A

R

R

Q

-

S

-

E

E

K

G

K

V

K

L

A

D

T

L

L

M

R

K

G

G

R

H

T

V

Q

I

I

T

N

T

L

I

F

F

E

E

S

P

S

S

T

T

R

R

T

T

Q

C

S

S

F

F

E

I

L

A

A

A

G

M

K

E

R

R

L

L

G

G

A

G

D

R

V

I

M

V

N

N

M

V

A

N

V

P

S

L

N

V

S

S

V

V

K

K

G

G

E

E

T

T

L

L

I

Q

D

D

T

T

A

I

M

R

T

T

L

L

N

-

A

A

M

C

R

Y

P

S

D

D

I

A

L

I

I

V

I

M

R

R

H

H

G

S

S

E

A

E

G

M

A

S

A

V

A

H

L

I

L

A

A

A

Q

K

K

Y

V

S

G

P

C

V

S

P

V

I

N

N

A

G

G

G

D

N

G

G

A

S

H

R

E

E

H

H

P

P

T

T

Q

Q

A

A

L

F

L

L

D

D

A

L

L

F

T

T

I

I

R

R

R

E

A

E

K

I

G

G

R

T

I

V

A

N

R

G

L

I

T

T

V

V

A

T

I

F

C

M

G

G

D

D

V

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

C

I

R

L

L

N

M

A

H

L

Y

G

Q

A

V

R

R

V

I

R

N

V

L

V

V

A

S

P

P

S

P

T

E

L

L

-

R

L

L

P

P

S

E

G

G

I

L

A

R

H

E

-

E

-

L

-

R

-

K

-

A

-

G

-

L

M

L

G

G

A

V

E

E

V

S

F

I

H

E

N

L

M

T

E

P

D

H

G

I

L

I

Q

S

D

K

A

T

D

D

V

V

V

L

M

Y

M

C

L

T

R

R

L

V

Q

Q

R

E

E

E

R

R

M

F

T

N

G

-

S

-

F

-

V

-

P

-

S

S

V

P

R

E

E

E

Y

Y

F

A

R

R

Y

L

-

K

-

D

-

T

H

Y

G

I

L

V

D

D

R

N

E

K

K

I

L

L

R

A

Y

H

A

A

R

K

P

E

D

N

A

M

L

A

V

I

M

M

H

H

P

P

G

L

P

P

M

-

N

-

R

R

G

V

V

N

E

E

I

I

A

K

S

E

D

E

V

V

A

D

D

Y

G

D

S

H

Q

R

S

A

V

A

I

Y

Q

F

E

R

Q

Q

V

M

E

K

M

Y

G

G

V

L

A

F

V

V

R

R

M

M

A

A

V

L

M

L

Sites not aligning to the query:

1857 modified: Phosphoserine; by PKA

2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
35% identity, 93% coverage: 13:311/321 of query aligns to 7:305/310 of 2hseA

query
sites
2hseA

R

K

H

H

L

I

G

S

I

I

K

N

G

D

L

L

S

S

P

R

Q

D

D

D

I

L

V

N

Q

L

L

V

L

L

D

A

L

T

A

A

E

-

S

A

E

K

I

L

A

K

V

A

S

N

R

P

Q

Q

S

P

E

E

K

-

A

-

T

L

L

L

R

K

G

H

R

K

T

V

Q

I

I

A

N

S

L

C

F

F

E

E

S

A

S
|
S

T
|
T

R
|
R

T
|
T

Q

R

S

L

S
|
S

F

F

E

E

L

T

A

S

G

M

K

H

R

R

L

L

G

G

A

A

D

S

V

V

M

V

N

G

M

F

A

S

V

D

S

S

-

A

N

N

S

T

S

S

V

L

-

G

K

K

K
|
K

G

G

E

E

T

T

L

L

I

A

D

D

T

T

A

-

M

I

T

S

L

V

N

I

A

S

M

T

R

Y

P

V

D

D

I

A

L

I

I

V

I

M

R
|
R

H

H

G

P

S

Q

A

E

G

G

A

A

A

R

L

L

L

A

A

T

Q

E

K

F

V

S

G

G

-

N

C

V

S

P

V

V

V

L

N

N

A

A

G

G

D

D

G

G

A

S

H

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

A

L

L

F

T

T

I

I

R

Q

R

E

A

T

K

Q

G

G

R

R

I

L

A

D

R

N

L

L

T

H

V

V

A

A

I

M

C

V

G

G

D

D

V

L

L

K

H

Y

S

G

R
|
R

V

T

A

V

R

H

S

S

N

-

I

-

L

L

L

T

N

Q

A

A

L

L

-

A

-

K

-

F

-

D

G

G

A

N

R

R

V

F

R

Y

V

F

V

I

A

A

P

P

S

D

T

A

L

L

-

A

L

M

P

P

S

Q

G

Y

I

I

A

L

H

D

M

M

G

L

A

D

E

E

-

K

-

G

-

I

-

A

-

W

-

S

V

L

F

H

H

S

N

S

M

I

E

E

D

E

G

V

L

M

Q

A

D

E

A

V

D

D

V

I

V

L

M

Y

M

M

L
x
T

R
|
R

L

V

Q
|
Q

R

K

E

E

R

R

M

L

T

A

G

P

S

S

F

E

V

Y

P

A

S

N

V

V

R

K

E

A

Y

Q

F

F

R

V

Y

L

H

R

G

A

L

S

D

D

R

-

E

-

K

-

L

L

R

H

Y

N

A

A

R

K

P

A

D

N

A

M

L

K

V

V

M

L

H

H

P
|
P

G
x
L

P
|
P

M

-

N

-

R

R

G

V

V

D

E

E

I

I

A

A

S

T

D

D

V

V

A

D

D

K

G

T

S

P

Q

H

S

A

V

W

I

Y

Q

F

E

Q

Q

Q

V
x
A

E

G

M

N

G
|
G

V

I

A

F

V

A

R
|
R

M

Q

A

A

V

L

M

L

E

A

A

L

L

V

L

L

D

N

active site: R54 (= R65), T55 (= T66), K84 (= K93), R105 (= R115), H134 (= H143), Q137 (= Q146), T228 (≠ L229), P266 (= P270), G292 (= G298)
binding aspartic acid: R54 (= R65), T55 (= T66), S58 (= S69), R105 (= R115), H134 (= H143), Q137 (= Q146), R167 (= R176), R229 (= R230), Q231 (= Q232), L267 (≠ G271), P268 (= P272), A289 (≠ V295), R296 (= R302)
binding phosphonoacetamide: S52 (= S63), T53 (= T64), R54 (= R65), T55 (= T66), R105 (= R115), L267 (≠ G271)

2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
35% identity, 93% coverage: 13:311/321 of query aligns to 7:305/310 of 2a0fA

query
sites
2a0fA

R

K

H

H

L

I

G

S

I

I

K

N

G

D

L

L

S

S

P

R

Q

D

D

D

I

L

V

N

Q

L

L

V

L

L

D

A

L

T

A

A

E

-

S

A

E

K

I

L

A

K

V

A

S

N

R

P

Q

Q

S

P

E

E

K

-

A

-

T

L

L

L

R

K

G

H

R

K

T

V

Q

I

I

A

N

S

L

C

F

F

E

E

S

A

S

S

T

T

R
|
R

T
|
T

Q

R

S

L

S

S

F

F

E

E

L

T

A

S

G

M

K

H

R

R

L

L

G

G

A

A

D

S

V

V

M

V

N

G

M

F

A

S

V

D

S

S

-

A

N

N

S

T

S

S

V

L

-

G

K

K

K
|
K

G

G

E

E

T

T

L

L

I

A

D

D

T

T

A

-

M

I

T

S

L

V

N

I

A

S

M

T

R

Y

P

V

D

D

I

A

L

I

I

V

I

M

R
|
R

H

H

G

P

S

Q

A

E

G

G

A

A

A

R

L

L

L

A

A

T

Q

E

K

F

V

S

G

G

-

N

C

V

S

P

V

V

V

L

N

N

A

A

G

G

D

D

G

G

A

S

H

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

A

L

L

F

T

T

I

I

R

Q

R

E

A

T

K

Q

G

G

R

R

I

L

A

D

R

N

L

L

T

H

V

V

A

A

I

M

C

V

G

G

D

D

V

L

L

K

H

Y

S

G

R

R

V

T

A

V

R

H

S

S

N

-

I

-

L

L

L

T

N

Q

A

A

L

L

-

A

-

K

-

F

-

D

G

G

A

N

R

R

V

F

R

Y

V

F

V

I

A

A

P

P

S

D

T

A

L

L

-

A

L

M

P

P

S

Q

G

Y

I

I

A

L

H

D

M

M

G

L

A

D

E

E

-

K

-

G

-

I

-

A

-

W

-

S

V

L

F

H

H

S

N

S

M

I

E

E

D

E

G

V

L

M

Q

A

D

E

A

V

D

D

V

I

V

L

M

Y

M

M

L
x
T

R

R

L

V

Q

Q

R

K

E

E

R

R

M

L

T

A

G

P

S

S

F

E

V

Y

P

A

S

N

V

V

R

K

E

A

Y

Q

F

F

R

V

Y

L

H

R

G

A

L

S

D

D

R

-

E

-

K

-

L

L

R

H

Y

N

A

A

R

K

P

A

D

N

A

M

L

K

V

V

M

L

H

H

P
|
P

G
x
L

P

P

M

-

N

-

R

R

G

V

V

D

E

E

I

I

A

A

S

T

D

D

V

V

A

D

D

K

G

T

S

P

Q

H

S

A

V

W

I

Y

Q

F

E

Q

Q

Q

V

A

E

G

M

N

G
|
G

V

I

A

F

V

A

R

R

M

Q

A

A

V

L

M

L

E

A

A

L

L

V

L

L

D

N

active site: R54 (= R65), T55 (= T66), K84 (= K93), R105 (= R115), H134 (= H143), Q137 (= Q146), T228 (≠ L229), P266 (= P270), G292 (= G298)
binding phosphonoacetamide: R54 (= R65), T55 (= T66), H134 (= H143), Q137 (= Q146), L267 (≠ G271)

P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
35% identity, 93% coverage: 13:311/321 of query aligns to 8:306/311 of P0A786

query
sites
P0A786

R

K

H

H

L

I

G

S

I

I

K

N

G

D

L

L

S

S

P

R

Q

D

D

D

I

L

V

N

Q

L

L

V

L

L

D

A

L

T

A

A

E

-

S

A

E

K

I

L

A

K

V

A

S

N

R

P

Q

Q

S

P

E

E

K

-

A

-

T

L

L

L

R

K

G

H

R

K

T

V

Q

I

I

A

N

S

L

C

F

F

E

E

S

A

S

S

T

T

R
|
R

T
|
T

Q

R

S

L

S

S

F

F

E

E

L

T

A

S

G

M

K

H

R

R

L

L

G

G

A

A

D

S

V

V

M

V

N

G

M

F

A

S

V

D

S

S

-

A

N

N

S

T

S

S

V

L

-

G

K

K

G

G

E

E

T

T

L

L

I

A

D

D

T

T

A

-

M

I

T

S

L

V

N

I

A

S

M

T

R

Y

P

V

D

D

I

A

L

I

I

V

I

M

R
|
R

H

H

G

P

S

Q

A

E

G

G

A

A

A

R

L

L

L

A

A

T

Q

E

K

F

V

S

G

G

-

N

C

V

S

P

V

V

V

L

N

N

A

A

G

G

D

D

G

G

A

S

H

N

E

Q

H
|
H

P

P

T

T

Q
|
Q

A

T

L

L

D

D

A

L

L

F

T

T

I

I

R

Q

R

E

A

T

K

Q

G

G

R

R

I

L

A

D

R

N

L

L

T

H

V

V

A

A

I

M

C

V

G

G

D

D

V

L

L

K

H

Y

S

G

R

R

V

T

A

V

R

H

S

S

N

-

I

-

L

L

L

T

N

Q

A

A

L

L

-

A

-

K

-

F

-

D

G

G

A

N

R

R

V

F

R

Y

V

F

V

I

A

A

P

P

S

D

T

A

L

L

-

A

L

M

P

P

S

Q

G

Y

I

I

A

L

H

D

M

M

G

L

A

D

E

E

-

K

-

G

-

I

-

A

-

W

-

S

V

L

F

H

H

S

N

S

M

I

E

E

D

E

G

V

L

M

Q

A

D

E

A

V

D

D

V

I

V

L

M

Y

M

M

L

T

R

R

L

V

Q

Q

R

K

E

E

R

R

M

L

T

D

G

P

S

S

F

E

V

Y

P

A

S

N

V

V

R

K

E

A

Y

Q

F

F

R

V

Y

L

H

R

G

A

L

S

D

D

R

-

E

-

K

-

L

L

R

H

Y

N

A

A

R

K

P

A

D

N

A

M

L

K

V

V

M

L

H

H

P

P

G
x
L

P
|
P

M

-

N

-

R

R

G

V

V

D

E

E

I

I

A

A

S

T

D

D

V

V

A

D

D

K

G

T

S

P

Q

H

S

A

V

W

I

Y

Q

F

E

Q

Q

Q

V

A

E

G

M

N

G

G

V

I

A

F

V

A

R

R

M

Q

A

A

V

L

M

L

E

A

A

L

L

V

L

L

D

N

R55 (= R65) binding carbamoyl phosphate
T56 (= T66) binding carbamoyl phosphate
R106 (= R115) binding carbamoyl phosphate
H135 (= H143) binding carbamoyl phosphate
Q138 (= Q146) binding carbamoyl phosphate
L268 (≠ G271) binding carbamoyl phosphate
P269 (= P272) binding carbamoyl phosphate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

Query Sequence

>WP_106716882.1 NCBI__GCF_003010935.1:WP_106716882.1
MTSKEPPLLFPHRHLLGIKGLSPQDIVQLLDLAESEIAVSRQSEKKKATLRGRTQINLFF
ESSTRTQSSFELAGKRLGADVMNMAVSNSSVKKGETLIDTAMTLNAMRPDILIIRHGSAG
AAALLAQKVGCSVVNAGDGAHEHPTQALLDALTIRRAKGRIARLTVAICGDVLHSRVARS
NIILLNALGARVRVVAPSTLLPSGIAHMGAEVFHNMEDGLQDADVVMMLRLQRERMTGSF
VPSVREYFRYHGLDREKLRYARPDALVMHPGPMNRGVEIASDVADGSQSVIQEQVEMGVA
VRMAVMEALLDPRRNAEGVAG

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory