SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011938749.1 NCBI__GCF_000016745.1:WP_011938749.1 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)

P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
41% identity, 95% coverage: 6:300/311 of query aligns to 2:285/304 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, 95% coverage: 6:300/311 of query aligns to 2:285/291 of 3r7fA

query
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3r7fA

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active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L223), P249 (= P264), G277 (= G292)
binding phosphoric acid mono(formamide)ester: S47 (= S56), T48 (= T57), R49 (= R58), T50 (= T59), R99 (= R108), H127 (= H136), Q130 (= Q139), P249 (= P264), A250 (≠ G265)
binding phosphate ion: S11 (≠ T15), T12 (≠ R16), Q23 (≠ E27), K26 (= K30), E140 (≠ Q149), R171 (= R180), K241 (= K256), H243 (≠ D258), K272 (= K287), K272 (= K287), K275 (≠ E290)

3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 95% coverage: 6:300/311 of query aligns to 2:285/291 of 3r7dA

query
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3r7dA

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active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L223), P249 (= P264), G277 (= G292)
binding phosphate ion: S11 (≠ T15), T12 (≠ R16), T73 (≠ S82), S74 (= S83), K77 (= K86), R171 (= R180)

3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
41% identity, 95% coverage: 6:300/311 of query aligns to 2:285/290 of 3r7lA

query
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3r7lA

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active site: R49 (= R58), T50 (= T59), K77 (= K86), R99 (= R108), H127 (= H136), Q130 (= Q139), L210 (= L223), P249 (= P264), G277 (= G292)
binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S56), T48 (= T57), R49 (= R58), T50 (= T59), S74 (= S83), K77 (= K86), R99 (= R108), H127 (= H136), R160 (= R169), R211 (= R224), Q213 (= Q226), A250 (≠ G265)

6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
38% identity, 94% coverage: 8:300/311 of query aligns to 4:288/293 of 6pnzA

query
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6pnzA

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I

I

E

Y

L

K

L

L

L

I

N

Q

T

K

A

A

E

S

N

Q

L

F

K

K

E

S

I

-

N

G

E

E

R

R

D

-

I

-

K

-

K

Q

V

L

P

P

T

N

L

F

R

E

G

G

K

K

T

Y

I

V

V

A

N

N

L

L

F

F

Y

F

E

E

A

N

S
|
S

T
|
T

R
|
R

T
|
T

R

K

T

C

S

S

F

F

E

E

I

M

A

A

A

E

K

L

R

K

L

L

S

G

A

L

D

K

T

T

I

I

N

S

I

F

T

E

A

T

S

S

T

T

S

S

S
|
S

V

V

T

S

K
|
K

G

G

E

E

T

S

L

L

S

Y

D

D

T

T

A

C

R

K

N

T

V

L

L

E

A

S

M

I

K

G

P

C

D

D

I

L

V

V

M

I

R
|
R

H

H

A

P

V

F

S

N

G

N

A

Y

H

Y

H

E

Y

K

L

L

A

A

Q

N

R

-

V

I

S

N

C

I

S

P

V

I

I

A

N

N

A

A

G

G

D

D

G

G

A

S

H

G

E

Q

H
|
H

P

P

S

T

Q

Q

G

S

L

L

D

D

M

L

L

M

T

T

M

I

R

Y

Q

E

K

E

F

Y

G

G

K

Y

L

F

D

E

G

G

L

L

K

N

V

V

A

L

I

I

V

C

G

G

D

D

I

I

T

K

H

N

S

S

R
|
R

V

V

A

A

R

R

S

S

N

N

I

Y

Y

H

G

S

L

L

T

K

R

A

M

L

G

G

A

A

H

N

V

V

F

M

L

F

A

N

G

S

P

P

P

N

T

A

M

W

M

I

P

D

G

S

I

L

E

E

R

-

L

-

G

-

N

-

V

-

T

A

V

P

C

Y

R

V

D

N

M

I

R

D

A

D

A

V

I

I

T

E

D

T

A

V

D

D

V

I

V

V

M

M

M

L

L

L

R
|
R

I

I

Q
|
Q

L

H

E

E

R

R

Q

H

G

G

-

L

-

A

K

E

T

E

L

T

L

R

P

F

T

A

L

A

K

D

E

D

Y

Y

S

H

R

Q

Y

K

F

H

G

G

L

L

N

N

N

E

H

V

L

R

L

Y

Q

N

L

K

A

L

K

Q

K

E

D

H

A

A

M

I

V

V

M

M

H

H

P

P

G
x
A

P

P

I

V

N

N

R

R

G

G

V

V

E

E

L

I

C

Q

S

S

H

D

V

L

A

V

D

E

G

A

D

S

Q

K

S

S

H

R

I

I

L

F

K

K

Q

Q

V

M

E

E

N

N

G

G

V

V

A

Y

V

L

R

R

M

M

S

A

M

V

L

I

binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S56), T49 (= T57), R50 (= R58), T51 (= T59), S75 (= S83), K78 (= K86), R100 (= R108), H127 (= H136), R160 (= R169), R210 (= R224), Q212 (= Q226), A253 (≠ G265)

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)
38% identity, 95% coverage: 6:299/311 of query aligns to 2:285/291 of 4bjhB

query
sites
4bjhB

K

R

D

S

I

L

I

I

G

S

L

S

Q

L

D

D

L

L

T

T

R

R

E

E

I

V

E

E

L

E

L

I

L

L

N

K

T

Y

A

A

E

K

N

E

L

F

K

K

E

E

I

G

N

K

E

E

R

E

D

T

I

I

K

K

K

A

V

S

P

A

T

V

L

L

R

-

G

-

K

-

T

-

I

-

V

-

N

-

L

F

F

F

Y

S

E

E

A

P

S
|
S

T
|
T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

I

K

A

A

K

R

R

E

L

L

S

G

A

I

D

E

T

T

I

Y

N

L

I

V

T

S

A

G

S

S

T

E

S

S

V

T

T

V

K
|
K

G

G

E

E

T

S

L

F

S

F

D

D

T

T

A

L

R

K

N

T

V

F

L

E

A

G

M

L

K

G

P

F

D

D

I

Y

I

V

V

V

M

F

R
|
R

H

V

A

P

V

F

S

V

G

F

A

F

-

P

H

Y

H

K

Y

E

L

I

A

V

Q

K

R

S

V

L

S

N

C

L

S

R

V

L

I

V

N

N

A

A

G

G

D

D

G

G

A

T

H

H

E

Q

H
|
H

P

P

S

S

Q
|
Q

G

G

L

L

L

I

D

D

M

F

L

F

T

T

M

I

R

K

Q

E

K

H

F

F

G

G

K

E

L

V

D

K

G

D

L

L

K

R

V

V

A

L

I

Y

V

V

G

G

D

D

I

I

T

K

H

H

S

S

R
|
R

V
|
V

A

F

R

R

S

S

N

G

I

A

Y

P

G

L

L

L

T

N

R

M

M

F

G

G

A

A

H

K

V

I

F

G

L

V

A

C

G

G

P

P

P

K

T

T

M

L

M

I

P

P

P

R

G

D

I

V

E

E

R

-

L

V

G

F

N

K

V

V

T

D

V

V

C

F

R

D

D

D

M

V

R

D

A

K

A

G

I

I

T

D

D

W

A

A

D

D

V

V

M

I

M

W

L

L

R
|
R

I

L

Q
|
Q

L

K

E

E

R

R

Q

Q

G

K

K

E

T

N

L

Y

L

I

P

P

T

S

L

E

K

S

E

S

Y

Y

S

F

R

K

Y

Q

F

F

G

G

L

L

N

T

N

K

H

E

L

R

L

F

Q

E

L

K

A

V

K

K

K

-

D

-

A

-

M

L

V

Y

M

M

H

H

P

P

G
|
G

P

P

I

V

N

N

R

R

G

N

V

V

E

D

L

I

C

D

S

H

H

E

V

L

A

V

D

Y

G

T

D

E

Q

K

S

S

H

L

I

I

L

Q

K

E

Q

Q

V

V

E

K

N

N

G

G

V

I

A

P

V

V

R

R

M

K

S

A

M

I

active site: R47 (= R58), T48 (= T59), K75 (= K86), R97 (= R108), H126 (= H136), Q129 (= Q139)
binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S56), T46 (= T57), R47 (= R58), T48 (= T59), R97 (= R108), H126 (= H136), R159 (= R169), V160 (= V170), R213 (= R224), Q215 (= Q226), G251 (= G265)

3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
38% identity, 95% coverage: 6:299/311 of query aligns to 2:285/291 of 3d6nB

query
sites
3d6nB

K

R

D

S

I

L

I

I

G

S

L

S

Q

L

D

D

L

L

T

T

R

R

E

E

I

V

E

E

L

E

L

I

L

L

N

K

T

Y

A

A

E

K

N

E

L

F

K

K

E

E

I

G

N

K

E

E

R

E

D

T

I

I

K

K

K

A

V

S

P

A

T

V

L

L

R

-

G

-

K

-

T

-

I

-

V

-

N

-

L

F

F

F

Y

S

E

E

A

P

S

S

T

T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

I

K

A

A

K

R

R

E

L

L

S

G

A

I

D

E

T

T

I

Y

N

L

I

V

T

S

A

G

S

S

T

E

S

S

V

T

T

V

K
|
K

G

G

E

E

T

S

L

F

S

F

D

D

T

T

A

L

R

K

N

T

V

F

L

E

A

G

M

L

K

G

P

F

D

D

I

Y

I

V

V

V

M

F

R
|
R

H

V

A

P

V

F

S

V

G

F

A

F

-

P

H

Y

H

K

Y

E

L

I

A

V

Q

K

R

S

V

L

S

N

C

L

S

R

V

L

I

V

N

N

A

A

G

G

D

D

G

G

A

T

H

H

E

Q

H
|
H

P

P

S

S

Q
|
Q

G

G

L

L

L

I

D

D

M

F

L

F

T

T

M

I

R

K

Q

E

K

H

F

F

G

G

K

E

L

V

D

K

G

D

L

L

K

R

V

V

A

L

I

Y

V

V

G

G

D

D

I

I

T

K

H

H

S

S

R
|
R

V
|
V

A

F

R

R

S

S

N

G

I

A

Y

P

G

L

L

L

T

N

R

M

M

F

G

G

A

A

H

K

V

I

F

G

L

V

A

C

G

G

P

P

P

K

T

T

M

L

M

I

P

P

P

R

G

D

I

V

E

E

R

-

L

V

G

F

N

K

V

V

T

D

V

V

C

F

R

D

D

D

M

V

R

D

A

K

A

G

I

I

T

D

D

W

A

A

D

D

V

V

M

I

M

W

L

L

R
|
R

I

L

Q

Q

L

K

E

E

R

R

Q

Q

G

K

K

E

T

N

L

Y

L

I

P

P

T

S

L

E

K

S

E

S

Y

Y

S

F

R

K

Y

Q

F

F

G

G

L

L

N

T

N

K

H

E

L

R

L

F

Q

E

L

K

A

V

K

K

K

-

D

-

A

-

M

L

V

Y

M

M

H

H

P

P

G
|
G

P

P

I

V

N

N

R

R

G

N

V

V

E

D

L

I

C

D

S

H

H

E

V

L

A

V

D

Y

G

T

D

E

Q

K

S

S

H

L

I

I

L

Q

K

E

Q

Q

V

V

E

K

N

N

G

G

V

I

A

P

V

V

R

R

M

K

S

A

M

I

active site: R47 (= R58), T48 (= T59), K75 (= K86), R97 (= R108), H126 (= H136), Q129 (= Q139)
binding citrate anion: T48 (= T59), R97 (= R108), H126 (= H136), R159 (= R169), V160 (= V170), R213 (= R224), G251 (= G265)

1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
38% identity, 97% coverage: 3:305/311 of query aligns to 2:305/307 of 1ml4A

query
sites
1ml4A

F

W

K

K

H

G

K

R

D

D

I

V

I

I

G

S

L

I

Q

R

D

D

L

F

T

S

R

K

E

E

E

D

I

I

E

E

L

T

L

V

L

L

N

A

T

T

A

A

E

E

N

R

L

L

K

-

E

-

I

-

N

-

E

E

R

R

D

E

I

L

K

K

K

E

V

K

P

G

T

Q

L

L

-

E

-

Y

-

A

R

K

G

G

K

K

T

I

I

L

V

A

N

T

L

L

F

F

Y

F

E

E

A

P

S
|
S

T
|
T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

I

S

A

A

A

M

K

H

R

R

L

L

S

G

A

G

D

A

T

V

I

I

N

G

I

F

T

A

-

E

A

A

S

S

T

T

S

S

V

V

T

K

K
|
K

G

G

E

E

T

S

L

L

S

R

D

D

T

T

A

I

R

K

N

T

V

V

L

-

A

E

M

Q

K

Y

P

C

D

D

I

V

I

I

V

V

M

I

R
|
R

H

H

A

P

V

K

S

E

G

G

A

A

H

A

H

R

Y

L

L

A

A

A

Q

E

R

V

V

A

S

E

C

V

S

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

A

S

H

N

E

Q

H
|
H

P

P

S

T

Q
|
Q

G

T

L

L

D

D

M

L

L

Y

T

T

M

I

R

K

Q

K

K

E

F

F

G

G

K

R

L

I

D

D

G

G

L

L

K

K

V

I

A

G

I

L

V

L

G

G

D

D

I

L

T

K

H

Y

S

G

R
|
R

V
x
T

A

V

R

H

S

S

N

L

I

A

Y

E

G

A

L

L

T

T

R

F

M

Y

G

D

A

V

H

E

V

L

F

Y

L

L

A

I

G

S

P

P

P

E

T

L

M

L

-

R

M

M

P

P

P

R

G

H

I

I

-

V

-

E

-

L

-

R

E

E

R

K

L

G

G

M

N

K

V

V

T

V

V

E

C

T

R

T

D

T

M

L

R

E

A

D

A

V

I

I

T

G

D

K

A

L

D

D

V

V

V

L

M

Y

M

V

L
x
T

R
|
R

I

I

Q

Q

L

K

E

E

R

R

Q

-

G

-

K

-

T

-

L

-

L

F

P

P

T

D

L

E

K

Q

E

E

Y

Y

S

L

R

K

Y

V

F

K

G

G

-

S

-

Y

-

Q

L

V

N

N

N

L

H

K

L

V

L

L

Q

E

L

K

A

A

K

K

K

D

D

E

A

L

M

R

V

I

M

M

H

H

P
|
P

G
x
L

P

P

I

-

N

-

R

R

G

V

V

D

E

E

L

I

C

H

S

P

H

E

V

V

A

D

D

N

G

T

D

K

Q

H

S

A

H

I

I

Y

L

F

K

R

Q

Q

V

V

E

F

N

N

G
|
G

V

V

A

P

V

V

R

R

M

M

S

A

M

L

L

L

Y

A

H

L

V

V

S

L

G

G

active site: R56 (= R58), T57 (= T59), K85 (= K86), R106 (= R108), H134 (= H136), Q137 (= Q139), T227 (≠ L223), P266 (= P264), G292 (= G292)
binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S56), T55 (= T57), R56 (= R58), T57 (= T59), R106 (= R108), H134 (= H136), R167 (= R169), T168 (≠ V170), R228 (= R224), L267 (≠ G265)

5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
35% identity, 96% coverage: 6:305/311 of query aligns to 6:305/307 of 5g1nE

query
sites
5g1nE

K

Q

D

H

I

I

I

L

G

S

L

V

Q

Q

D

Q

L

F

T

T

R

K

E

D

E

Q

I

M

E

S

L

H

L

L

L

F

N

N

T

V

A

A

E

H

N

T

L

L

K

R

E

M

I

M

N

V

E

Q

R

K

D

E

I

-

K

R

K

S

V

L

P

D

T

I

L

L

R

K

G

G

K

K

T

V

I

M

V

A

N

S

L

M

F

F

Y

Y

E

E

A

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

T

S

S

S

F

F

E

A

I

A

A

A

A

M

K

A

R

R

L

L

S

G

A

G

D

A

T

V

I

L

N

S

I

F

T

S

A

E

S

A

T

T

S

S

S
|
S

V

V

T

Q

K
|
K

G

G

E

E

T

S

L

L

S

A

D

D

T

S

A

V

R

Q

N

T

V

-

L

M

A

S

M

C

K

Y

P

A

D

D

I

V

V

V

M

L

R
|
R

H

H

A

P

V

Q

S

P

G

G

A

A

H

V

H

E

Y

L

L

A

A

A

Q

K

R

H

V

C

S

R

C

R

S

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

A

V

H

G

E

E

H
|
H

P

P

S

T

Q
|
Q

G

A

L

L

D

D

M

I

L

F

T

T

M

I

R

R

Q

E

K

E

F

L

G

G

K

T

L

V

D

N

G

G

L

M

K

T

V

I

A

T

I

M

V

V

G

G

D

D

I

L

T

K

H

H

S

G

R
|
R

V

T

A

V

R

H

S

S

N

L

I

A

Y

C

G

L

L

L

T

T

R

Q

M

Y

G

R

A

V

H

S

V

L

F

R

L

Y

A

V

G

A

P

P

T

S

M

L

-

R

M

M

P

P

G

T

I

V

-

R

-

A

-

F

-

V

-

A

E

S

R

R

L

G

G

T

N

K

V

Q

T

E

V

E

C

F

R

E

D

S

M

I

R

E

A

E

A

A

I

L

T

P

D

D

A

T

D

D

V

V

V

L

M

Y

M

M

L
x
T

R
|
R

I

I

Q
|
Q

L

K

E

E

R

R

Q

F

G

G

K

S

T

T

L

-

P

-

T

-

L

-

K

Q

E

E

Y

Y

S

E

R

A

Y

C

F

F

G

G

-

Q

-

F

-

I

L

L

N

T

N

P

H

H

L

I

L

M

Q

T

L

R

A

A

K

K

D

K

A

M

M

V

V

V

M

M

H

H

P
|
P

G
x
M

P

P

I

-

N

-

R

R

G

V

V

N

E

E

L

I

C

S

S

V

H

E

V

V

A

D

D

S

G

D

D

P

Q

R

S

A

H

A

I

Y

L

F

K

R

Q

Q

V

A

E

E

N

N

G
|
G

V

M

A

Y

V

I

R

R

M

M

S

A

M

L

L

L

Y

A

H

T

V

V

S

L

G

G

active site: R57 (= R58), T58 (= T59), K85 (= K86), R106 (= R108), H134 (= H136), Q137 (= Q139), T227 (≠ L223), P266 (= P264), G292 (= G292)
binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S56), T56 (= T57), R57 (= R58), T58 (= T59), S82 (= S83), K85 (= K86), R106 (= R108), H134 (= H136), R167 (= R169), R228 (= R224), Q230 (= Q226), M267 (≠ G265)

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)
35% identity, 96% coverage: 6:305/311 of query aligns to 1924:2223/2225 of P27708

query
sites
P27708

K
x
Q

D
x
H

I
|
I

I
x
L

G
x
S

L
x
V

Q
|
Q

D
x
Q

L
x
F

T
|
T

R
x
K

E
x
D

E
x
Q

I
x
M

E
x
S

L
x
H

L
|
L

L
x
F

N
|
N

T
x
V

A
|
A

E
x
H

N
x
T

L
|
L

K
x
R

E
x
M

I
x
M

N
x
V

E
x
Q

R
x
K

D
x
E

I

-

K
x
R

K
x
S

V
x
L

P
x
D

T
x
I

L
|
L

R
x
K

G
|
G

K
|
K

T
x
V

I
x
M

V
x
A

N
x
S

L
x
M

F
|
F

Y
|
Y

E
|
E

A
x
V

S
|
S

T
|
T

R
|
R

T
|
T

R
x
S

T
x
S

S
|
S

F
|
F

E
x
A

I
x
A

A
|
A

A
x
M

K
x
A

R
|
R

L
|
L

S
x
G

A
x
G

D
x
A

T
x
V

I
x
L

N
x
S

I
x
F

T
x
S

A
x
E

S
x
A

T
|
T

S
|
S

V
|
V

T
x
Q

K
|
K

G
|
G

E
|
E

T
x
S

L
|
L

S
x
A

D
|
D

T
x
S

A
x
V

R
x
Q

N
x
T

V

-

L
x
M

A
x
S

M
x
C

K
x
Y

P
x
A

D
|
D

I
x
V

V
|
V

M
x
L

R
|
R

H
|
H

A
x
P

V
x
Q

S
x
P

G
|
G

A
|
A

H
x
V

H
x
E

Y
x
L

L
x
A

A
|
A

Q
x
K

R
x
H

V
x
C

S
x
R

C
x
R

S
x
P

V
|
V

I
|
I

N
|
N

A
|
A

G
|
G

D
|
D

G
|
G

A
x
V

H
x
G

E
|
E

H
|
H

P
|
P

S
x
T

Q
|
Q

G
x
A

L
|
L

D
|
D

M
x
I

L
x
F

T
|
T

M
x
I

R
|
R

Q
x
E

K
x
E

F
x
L

G
|
G

K
x
T

L
x
V

D
x
N

G
|
G

L
x
M

K
x
T

V
x
I

A
x
T

I
x
M

V
|
V

G
|
G

D
|
D

I
x
L

T
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

Y
x
C

G
x
L

L
|
L

T
|
T

R
x
Q

M
x
Y

G
x
R

A
x
V

H
x
S

V
x
L

F
x
R

L
x
Y

A
x
V

G
x
A

P
|
P

T
x
S

M
x
L

-
x
R

M
|
M

P
|
P

G
x
T

I
x
V

-
x
R

-
x
A

-
x
F

-
x
V

-
x
A

E
x
S

R
|
R

L
x
G

G
x
T

N
x
K

V
x
Q

T
x
E

V
x
E

C
x
F

R
x
E

D
x
S

M
x
I

R
x
E

A
x
E

A
|
A

I
x
L

T
x
P

D
|
D

A
x
T

D
|
D

V
|
V

V
x
L

M
x
Y

M
|
M

L
x
T

R
|
R

I
|
I

Q
|
Q

L
x
K

E
|
E

R
|
R

Q
x
F

G
|
G

K
x
S

T
|
T

L

-

P

-

T

-

L

-

K
x
Q

E
|
E

Y
|
Y

S
x
E

R
x
A

Y
x
C

F
|
F

G
|
G

-
x
Q

-
x
F

-
x
I

L
|
L

N
x
T

N
x
P

H
|
H

L
x
I

L
x
M

Q
x
T

L
x
R

A
|
A

K
|
K

D
x
K

A
x
M

M
x
V

V
|
V

M
|
M

H
|
H

P
|
P

G
x
M

P
|
P

I

-

N

-

R
|
R

G
x
V

V
x
N

E
|
E

L
x
I

C
x
S

S
x
V

H
x
E

V
|
V

A
x
D

D
x
S

G
x
D

D
x
P

Q
x
R

S
x
A

H
x
A

I
x
Y

L
x
F

K
x
R

Q
|
Q

V
x
A

E
|
E

N
|
N

G
|
G

V
x
M

A
x
Y

V
x
I

R
|
R

M
|
M

S
x
A

M
x
L

L
|
L

Y
x
A

H
x
T

V
|
V

S
x
L

G
|
G

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

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, 96% coverage: 6:305/311 of query aligns to 1924:2223/2225 of P08955

query
sites
P08955

K

Q

D

H

I

I

I

L

G

S

L

V

Q

K

D

Q

L

F

T

T

R

K

E

D

E

Q

I

M

E

S

L

H

L

L

L

F

N

N

T

V

A

A

E

H

N

T

L

L

K

R

E

M

I

M

N

V

E

Q

R

K

D

E

I

-

K

R

K

S

V

L

P

D

T

I

L

L

R

K

G

G

K

K

T

V

I

M

V

A

N

S

L

M

F

F

Y

Y

E

E

A

V

S

S

T

T

R

R

T

T

R

S

T

S

S

S

F

F

E

A

I

A

A

A

A

M

K

A

R

R

L

L

S

G

A

G

D

A

T

V

I

L

N

S

I

F

T

S

A

E

S

A

T

T

S

S

V

V

T

Q

K

K

G

G

E

E

T

S

L

L

S

A

D

D

T

S

A

V

R

Q

N

T

V

-

L

M

A

S

M

C

K

Y

P

A

D

D

I

V

V

V

M

L

R

R

H

H

A

P

V

Q

S

P

G

G

A

A

H

V

H

E

Y

L

L

A

A

A

Q

K

R

H

V

C

S

R

C

R

S

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

A

V

H

G

E

E

H

H

P

P

S

T

Q

Q

G

A

L

L

D

D

M

I

L

F

T

T

M

I

R

R

Q

E

K

E

F

L

G

G

K

T

L

V

D

N

G

G

L

M

K

T

V

I

A

T

I

M

V

V

G

G

D

D

I

L

T

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

A

Y

C

G

L

L

L

T

T

R

Q

M

Y

G

R

A

V

H

S

V

L

F

R

L

Y

A

V

G

A

P

P

T

S

M

L

-

R

M

M

P

P

G

S

I

V

-

W

-

D

-

F

-

V

-

A

E

S

R

R

L

G

G

T

N

K

V

Q

T

E

V

E

C

F

R

E

D

S

M

I

R

E

A

E

A

A

I

L

T

P

D

D

A

T

D

D

V

V

V

L

M

Y

M

M

L

T

R

R

I

I

Q

Q

L

K

E

E

R

R

Q

F

G

G

K

S

T

T

L

-

P

-

T

-

L

-

K

Q

E

E

Y

Y

S

E

R

A

Y

C

F

F

G

G

-

Q

-

F

-

I

L

L

N

T

N

P

H

H

L

I

L

M

Q

T

L

R

A

A

K

K

D

K

A

M

M

V

V

V

M

M

H

H

P

P

G

M

P

P

I

-

N

-

R

R

G

V

V

N

E

E

L

I

C

S

S

V

H

E

V

V

A

D

D

S

G

D

D

P

Q

R

S

A

H

A

I

Y

L

F

K

R

Q

Q

V

A

E

E

N

N

G

G

V

M

A

Y

V

I

R

R

M

M

S

A

M

L

L

L

Y

A

H

T

V

V

S

L

G

G

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.

5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
33% identity, 96% coverage: 6:305/311 of query aligns to 3:290/292 of 5g1pA

query
sites
5g1pA

K

Q

D

H

I

I

I

L

G

S

L

V

Q

Q

D

Q

L

F

T

T

R

K

E

D

E

Q

I

M

E

S

L

H

L

L

L

F

N

N

T

V

A

A

E

H

N

T

L

L

K

R

E

M

I

M

N

V

E

Q

R

K

D

E

I

-

K

R

K

S

V

L

P

D

T

I

L

L

R

K

G

G

K

K

T

V

I

M

V

A

N

S

L

M

F

F

Y

Y

E

E

A

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

T

S

S

S

F

F

E

A

I

A

A

A

A

M

K

A

R

R

L

L

S

G

A

G

D

A

T

V

I

L

N

S

I

F

T

S

A

E

S

A

T

T

S

S

V

V

T

Q

K
|
K

G

G

E

E

T

S

L

L

S

A

D

D

T

S

A

V

R

Q

N

T

V

-

L

M

A

S

M

C

K

Y

P

A

D

D

I

V

V

V

M

L

R
|
R

H

H

A

P

V

Q

S

P

G

G

A

A

H

V

H

E

Y

L

L

A

A

A

Q

K

R

H

V

C

S

R

C

R

S

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

A

V

H

G

E

E

H
|
H

P

P

S

T

Q
|
Q

G

A

L

L

D

D

M

I

L

F

T

T

M

I

R

R

Q

E

K

E

F

L

G

G

K

T

L

V

D

N

G

G

L

M

K

T

V

I

A

T

I

M

V

V

G

G

D

D

I

L

T

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

N

L

I

A

Y

C

G

L

L

L

T

T

R

Q

M

Y

G

R

A

V

H

S

V

L

F

R

L

Y

A

V

G

A

P

P

T

S

M

L

-

R

M

M

P

P

G

T

I

V

E

R

R

A

L

F

G

V

N

A

V

S

T

G

V

T

C

K

R

Q

D

E

-

E

-

F

-

E

-

S

M

I

R

E

A

E

A

A

I

L

T

P

D

D

A

T

D

D

V

V

V

L

M

Y

M

M

L
x
T

R

R

I

I

Q

Q

L

K

E

E

R

R

Q

-

G

-

K

-

T

-

L

-

P

-

T

-

L

-

K

-

E

-

Y

-

S

-

R

F

Y

Q

F

F

G

I

L

L

N

T

N

P

H

H

L

I

L

M

Q

T

L

R

A

A

K

K

D

K

A

M

M

V

V

V

M

M

H

H

P
|
P

G
x
M

P

P

I

-

N

-

R

R

G

V

V

N

E

E

L

I

C

S

S

V

H

E

V

V

A

D

D

S

G

D

D

P

Q

R

S

A

H

A

I

Y

L

F

K

R

Q

Q

V

A

E

E

N

N

G
|
G

V

M

A

Y

V

I

R

R

M

M

S

A

M

L

L

L

Y

A

H

T

V

V

S

L

G

G

active site: R54 (= R58), T55 (= T59), K82 (= K86), R103 (= R108), H131 (= H136), Q134 (= Q139), T223 (≠ L223), P251 (= P264), G277 (= G292)
binding phosphoric acid mono(formamide)ester: S52 (= S56), T53 (= T57), R54 (= R58), T55 (= T59), R103 (= R108), Q134 (= Q139), M252 (≠ G265)

6ys6B Arabidopsis aspartate transcarbamoylase complex with pala (see paper)
36% identity, 96% coverage: 3:300/311 of query aligns to 4:305/312 of 6ys6B

query
sites
6ys6B

F

F

K

E

H

L

K

S

D

D

I

V

I

I

G

E

L

G

Q

K

D

Q

L

F

T

D

R

R

E

E

E

M

I

L

E

S

L

A

L

I

L

F

N

D

T

V

A

A

E

R

N

E

L

M

K

E

E

K

I

I

N

-

E

E

R

K

D

S

I

S

K

S

K

Q

V

S

P

E

T

I

L

L

R

K

G

G

K

Y

T

L

I

M

V

A

N

T

L

L

F

F

Y

Y

E

E

A

P

S

S

T

T

R

R

T

T

R

R

T

L

S

S

F

F

E

E

I

S

A

A

A

M

K

K

R

R

L

L

S

G

A

G

D

E

T

V

I

L

N

T

I

T

T

E

A

N

S

A

-

R

-

E

T

F

S

S

S
|
S

V

A

T

A

K
|
K

G

G

E

E

T

T

L

L

S

E

D

D

T

T

A

I

R

R

N

T

V

V

L

E

A

G

M

Y

K

S

P

-

D

D

I

I

V

V

M

M

R
|
R

H

H

A

F

V

E

S

S

G

G

A

A

H

A

H

R

Y

K

L

A

A

A

Q

A

R

T

V

A

S

N

C

I

S

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

A

P

H

G

E

E

H
|
H

P

P

S

T

Q
|
Q

G

A

L

L

D

D

M

V

L

Y

T

T

M

I

R

Q

Q

S

K

E

F

I

G

G

K

K

L

L

D

D

G

G

L

I

K

S

V

V

A

A

I

L

V

V

G

G

D

D

I

L

T

A

H

N

S

G

R

R

V

T

A

V

R

R

S

S

N

L

I

A

Y

Y

G

L

L

L

T

A

R

K

M

F

-

K

G

D

A

V

H

K

V

I

F

Y

L

F

A

V

G

S

P

P

P

E

T

I

-

V

-

K

-

M

-

K

-

D

-

I

-

K

-

D

-

Y

M

L

M

T

P

S

G

G

I

V

E

E

R

-

L

-

G

-

N

-

V

W

T

E

V

E

C

S

R

S

D

D

M

L

R

M

A

E

A

V

I

A

T

S

D

K

A

C

D

D

V

V

M

Y

M

Q

L
x
T

R

R

I

I

Q

Q

L

R

E

E

R

R

Q

F

G

G

K

E

T

R

L

L

L

-

P

-

T

D

L

L

K

Y

E

E

Y

A

S

A

R

R

-

G

Y

K

F

F

G

I

L

V

N

D

N

K

H

D

L

L

Q

G

L

V

A

M

K

Q

K

K

D

K

A

A

M

I

V

I

M

M

H

H

P
|
P

G

L

P

P

I

-

N

-

R

R

G

L

V

D

E

E

L

I

C

T

S

A

H

D

V

V

A

D

D

A

G

D

D

P

Q

R

S

A

H

A

I

Y

L

F

K

R

Q

Q

V

A

E

K

N

N

G
|
G

V

L

A

F

V

I

R

R

M

M

S

A

M

L

L

L

active site: R109 (= R108), H137 (= H136), Q140 (= Q139), T231 (≠ L223), P271 (= P264), G297 (= G292)
binding n-(phosphonacetyl)-l-aspartic acid: S85 (= S83), K88 (= K86)

6ypoA Arabidopsis aspartate transcarbamoylase bound to ump (see paper)
36% identity, 96% coverage: 3:300/311 of query aligns to 4:305/312 of 6ypoA

query
sites
6ypoA

F

F

K

E

H

L

K

S

D

D

I

V

I

I

G

E

L

G

Q

K

D

Q

L

F

T

D

R

R

E

E

E

M

I

L

E

S

L

A

L

I

L

F

N

D

T

V

A

A

E

R

N

E

L

M

K

E

E

K

I

I

N

-

E

E

R

K

D

S

I

S

K

S

K

Q

V

S

P

E

T

I

L

L

R

K

G

G

K

Y

T

L

I

M

V

A

N

T

L

L

F

F

Y

Y

E

E

A

P

S

S

T

T

R
|
R

T
|
T

R

R

T

L

S

S

F

F

E

E

I

S

A

A

A

M

K

K

R

R

L

L

S

G

A

G

D

E

T

V

I

L

N

T

I

T

T

E

A

N

S

A

-

R

-

E

T

F

S

S

V

A

T

A

K

K

G

G

E

E

T

T

L

L

S

E

D

D

T

T

A

I

R

R

N

T

V

V

L

E

A

G

M

Y

K

S

P

-

D

D

I

I