SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_009567142.1 NCBI__GCF_000021485.1:WP_009567142.1 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)

P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
68% identity, 98% coverage: 1:186/190 of query aligns to 1:186/187 of P00903

query
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P00903

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C79 (= C79) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H168) mutation to Q: Loss of activity.
E170 (= E170) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.

Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
51% identity, 97% coverage: 2:186/190 of query aligns to 75:265/276 of Q42565

query
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Q42565

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G150 (= G77) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G102) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
47% identity, 96% coverage: 3:184/190 of query aligns to 7:187/673 of 8hx8A

query
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8hx8A

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binding magnesium ion: I175 (= I172), S177 (= S174)

Sites not aligning to the query:

binding magnesium ion: 521, 655, 658
binding tryptophan: 231, 232, 233, 241, 243, 458, 459, 460, 614

P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
42% identity, 97% coverage: 2:185/190 of query aligns to 4:187/193 of P00900

query
sites
P00900

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C84 (= C79) active site, Nucleophile; for GATase activity

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1i7qB Anthranilate synthase from s. Marcescens (see paper)
42% identity, 97% coverage: 2:185/190 of query aligns to 3:186/192 of 1i7qB

query
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1i7qB

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active site: G58 (≠ C54), C83 (= C79), L84 (= L80), H169 (= H168), E171 (= E170)
binding glutamic acid: P55 (= P51), G56 (= G52), G58 (≠ C54), C83 (= C79), L84 (= L80), Q87 (= Q83), H132 (= H128), S133 (= S129), L134 (= L130)

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
37% identity, 96% coverage: 3:184/190 of query aligns to 6:144/632 of 8hx9A

query
sites
8hx9A

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binding magnesium ion: S134 (= S174), D135 (≠ E175)

Sites not aligning to the query:

binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: 453, 454, 455, 456, 547, 570, 590, 603, 604, 605, 606, 619, 623
binding tryptophan: 189, 190, 191, 199, 201, 419, 420, 421, 574, 575

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
28% identity, 98% coverage: 1:186/190 of query aligns to 1:176/183 of 7yc6A

query
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7yc6A

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-

G

I

I

C

I

I

L

S

S

P

G

G

G

P

P

C

-

T

D

P

I

N

E

E

K

A

A

G

K

I

N

S

C

L

I

E

D

V

I

I

A

R

-

H

-

F

L

A

N

G

A

K

K

I

L

P

P

L

I

L

L

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

A

L

I

I

G

A

Q

L

A

A

F

Y

G

G

K

E

V

V

V

G

R

R

A

A

-

A

-

L

D

T

K

K

V

V

M

Y

H

V

G
x
D

K

K

T

E

S

N

P

P

I

-

F

-

H

-

D

-

G

-

K

-

G

-

L

L

F

F

R

K

D

N

L

V

P

P

D

R

P

E

F

F

A

N

A

A

T

W

R

A

Y

S

H

H

S

K

L

D

I
x
E

V

V

E

K

R

K

A

-

S

-

L

V

P

P

D

E

T

G

L

F

E

E

V

I

T

L

A

A

W
x
H

T

S

A

D

A

I

G
x
C

E

Q

I

V

M

E

G

A

L

M

R

K

H

H

R

K

T

T

L

K

D

P

V

I

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

S

V

I

A

L

H

S

T

E

E

H

Y

G

G

K

N

T

E

L

I

L

L

Q

K

H

N

F

F

L

C

Q

K

binding zinc ion: C76 (= C79), D101 (≠ G102), E123 (≠ I131), E123 (≠ I131), H136 (≠ W146), C140 (≠ G150), C140 (≠ G150), H158 (= H168)

Q9LVW7 Carbamoyl phosphate synthase small chain, chloroplastic; Carbamoyl phosphate synthetase glutamine chain; Protein VENOSA 6; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 86% coverage: 14:176/190 of query aligns to 254:410/430 of Q9LVW7

query
sites
Q9LVW7

N

N

L

I

V

L

Q

R

Y

R

F

L

G

S

E

S

L

Y

G

G

A

C

E

Q

V

I

R

T

V

V

E

V

R

P

N

S

D

-

S

T

I

F

D

P

V

A

A

A

A

E

I

A

E

L

Q

K

L

M

A

N

P

P

S

D

R

G

I

I

C

L

I

F

S

S

P

N

G

G

P

P

C

G

T

D

P

P

N

S

E

A

A

V

G

P

I

Y

S

A

L

V

E

E

V

T

I

V

R

K

H

E

F

L

A

L

G

G

K

K

I

V

P

P

L

V

L

Y

G

G

V

I

C

C

L

M

G

G

H

H

Q

Q

A

L

I

L

G

G

Q

Q

A

A

F

L

G

G

K

K

V

T

V

F

R

K

A

M

D

K

K

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

I

V

F

R

H

N

D

N

G

R

K

T

G

G

L

Q

F

V

R

E

D

-

L

-

P

-

D

-

P

-

F

-

A

I

A

S

T

A

R

Q

Y

N

H

H

S

N

L

Y

I

A

V

V

E

D

R

P

A

A

S

S

L

L

P

P

D

G

T

G

L

V

E

E

V

V

T

T

A

H

W

V

T

N

-

L

A

N

A

D

G

G

E

S

I

C

M

A

G

G

L

L

R

S

H

F

R

P

T

E

L

M

D

N

V

V

E

M

G

S

V

L

Q

Q

F

Y

H

H

P

P

E

E

S

A

I

S

L

P

S

G

E

P

H
|
H

H410 (= H176) mutation to Y: In ven6-1; reticulate leaf phenotype.

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
28% identity, 98% coverage: 1:186/190 of query aligns to 1:182/475 of 2ywcA

query
sites
2ywcA

M

M

L

V

L

L

M

V

I

L

D

D

N

F

Y

G

D

S

S

Q

F

Y

T

T

Y

R

N

L

L

I

V

A

Q

R

Y

R

F

L

G

R

E

E

L

L

G

R

A

A

E

F

V

S

R

L

V

I

E

L

R

P

N

G

D

D

S

A

I

-

D

P

V

L

A

E

I

V

E

L

Q

K

L

H

A

R

P

P

S

Q

R

A

I

L

C

I

I

L

S

S

P

G

G
|
G

P

P

C
x
R

T

S

P

V

N

F

E

D

A

P

G

D

I

A

S

P

L

R

E

P

V

D

I

P

R

R

H

L

F

F

A

S

G

S

K

G

I

L

P

P

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

A

L

I

L

G

A

Q

Q

A

E

F

L

G

G

K

R

V

V

V

E

R

R

A

A

D

G

K

R

V

A

M

E

H

Y

G

G

K

K

T

A

S

L

P

L

I

T

F

R

H

H

D

E

G

G

K

P

G

-

L

L

F

F

R

R

D

G

L

L

P

E

D

G

P

E

F

V

A

Q

A

V

T

W

R

M

Y

S

H

H

S

Q

L

D

I

A

V

V

E

-

R

-

A

T

S

A

L

P

P

P

D

P

T

G

L

W

E

R

V

V

T

V

A

A

W

E

T

T

A

E

G

N

E

P

I

V

M

A

G

A

L

I

R

A

H

S

R

P

T

D

L

G

D

R

V

A

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

S

T

E

P

H

K

G

G

K

M

T

Q

L

I

L

L

Q

E

H

N

F

F

L

L

Q

E

active site: G51 (= G52), R53 (≠ C54), C78 (= C79), Y79 (≠ L80), H164 (= H168), E166 (= E170)

Sites not aligning to the query:

active site: 221, 343
binding xanthosine-5'-monophosphate: 288, 366, 367, 368, 408, 467, 471, 472, 473

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
28% identity, 77% coverage: 41:186/190 of query aligns to 229:371/379 of 1ce8B

query
sites
1ce8B

Q

K

L

M

A

N

P

P

S

D

R

G

I

I

C

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

N

A

E

P

A

C

G

D

I

Y

S

A

L

I

E

T

V

A

I

I

R

Q

H

K

F

F

-

L

A

E

G

T

K

D

I

I

P

P

L

V

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

A

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

K

K

V

T

V

V

R

K

A

M

D

K

K

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

I

V

F

K

H

D

D

V

G

E

K

K

G

N

L

V

F

V

R

-

D

-

L

-

P

-

D

-

P

-

F

M

A

I

A

T

T

A

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

E

D

R

E

A

A

S

T

L

L

P

P

D

A

T

N

L

L

E

R

V

V

T

T

A

H

W

K

T

S

A

L

-

F

A

D

G

G

E

T

I

L

M

Q

G

G

L

I

R

H

H

R

R

T

T

D

L

K

D

P

V

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

I

S

L

P

S

G

E

P

H

H

-

D

G

A

K

A

T

P

L

L

L

F

Q

D

H

H

F

F

L

I

Q

E

active site: C268 (= C79), H352 (= H168), E354 (= E170)

Sites not aligning to the query:

binding L-ornithine: 119, 122

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
28% identity, 77% coverage: 41:186/190 of query aligns to 230:372/382 of P0A6F1

query
sites
P0A6F1

Q

K

L

M

A

N

P

P

S

D

R

G

I

I

C

F

I

L

S

S

P

N

G
|
G

P

P

C
x
G

T

D

P

P

N

A

E

P

A

C

G

D

I

Y

S

A

L

I

E

T

V

A

I

I

R

Q

H

K

F

F

-

L

A

E

G

T

K

D

I

I

P

P

L

V

L

F

G

G

V

I

C

C

L
|
L

G

G

H

H

Q
|
Q

A

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

K

K

V

T

V

V

R

K

A

M

D

K

K

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

I

V

F

K

H

D

D

V

G

E

K

K

G

N

L

V

F

V

R

-

D

-

L

-

P

-

D

-

P

-

F

M

A

I

A

T

T

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

I

A

V

V

E

D

R

E

A

A

S

T

L

L

P

P

D

A

T

N

L

L

E

R

V

V

T

T

A

H

W

K

T

S

A

L

-

F

A

D

G

G

E

T

I

L

M

Q

G

G

L

I

R

H

H

R

R

T

T

D

L

K

D

P

V

A

E

F

G

S

V

F

Q

Q

F

G

H

H

P

P

E

E

S

A

I

S

L

P

S

G

E

P

H

H

-

D

G

A

K

A

T

P

L

L

L

F

Q

D

H

H

F

F

L

I

Q

E

G241 (= G52) binding L-glutamine
G243 (≠ C54) binding L-glutamine
L270 (= L80) binding L-glutamine
Q273 (= Q83) binding L-glutamine
N311 (≠ Y127) binding L-glutamine
G313 (≠ S129) binding L-glutamine
F314 (≠ L130) binding L-glutamine

Sites not aligning to the query:

47 binding L-glutamine

2vxoB Human gmp synthetase in complex with xmp (see paper)
31% identity, 59% coverage: 74:185/190 of query aligns to 77:182/658 of 2vxoB

query
sites
2vxoB

P

P

L

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

A

M

I

M

G

N

Q

K

A

V

F

F

G

G

K

T

V

V

V

-

R

-

A

-

D

-

K

-

V

-

M

-

H

H

G

K

K

K

T

S

S

D

P

G

I

V

F

F

H

N

-

I

-

S

-

V

-

D

D

N

G

T

K

C

G

S

L

L

F

F

R

R

D

G

L

L

P

Q

D

K

P

E

F

E

A

V

T

L

R

L

Y

T

H

H

S

G

L

D

I

S

V

V

E

D

R

K

A

V

S

A

L

-

P

-

D

D

T

G

L

F

E

K

V

V

T

V

A

A

W

-

T

R

A

S

A

G

G

N

E

I

I

V

M

A

G

G

L

I

R

A

H

N

R

E

T

S

L

K

D

K

V

L

E

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

S

T

E

E

H

N

G

G

K

K

T

V

L

I

L

L

Q

K

H

N

F

F

L

L

active site: C82 (= C79), Y83 (≠ L80), H165 (= H168), E167 (= E170)

Sites not aligning to the query:

active site: 55, 223, 381
binding xanthosine-5'-monophosphate: 302, 348, 349, 404, 405, 406, 489, 575, 610, 650, 654, 655, 656

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
28% identity, 77% coverage: 41:186/190 of query aligns to 229:371/379 of 1c3oB

query
sites
1c3oB

Q

K

L

M

A

N

P

P

S

D

R

G

I

I

C

F

I

L

S

S

P
x
N

G
|
G

P

P

C
x
G

T

D

P

P

N

A

E

P

A

C

G

D

I

Y

S

A

L

I

E

T

V

A

I

I

R

Q

H

K

F

F

-

L

A

E

G

T

K

D

I

I

P

P

L

V

L

F

G

G

V

I

C
x
S

L
|
L

G

G

H

H

Q

Q

A

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

K

K

V

T

V

V

R

K

A

M

D

K

K

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

I

V

F

K

H

D

D

V

G

E

K

K

G

N

L

V

F

V

R

-

D

-

L

-

P

-

D

-

P

-

F

M

A

I

A

T

T

A

R

Q

Y
x
N

H
|
H

S
x
G

L
x
F

I

A

V

V

E

D

R

E

A

A

S

T

L

L

P

P

D

A

T

N

L

L

E

R

V

V

T

T

A

H

W

K

T

S

A

L

-

F

A

D

G

G

E

T

I

L

M

Q

G

G

L

I

R

H

H

R

R

T

T

D

L

K

D

P

V

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

I

S

L

P

S

G

E

P

H

H

-

D

G

A

K

A

T

P

L

L

L

F

Q

D

H

H

F

F

L

I

Q

E

active site: S268 (≠ C79), H352 (= H168), E354 (= E170)
binding glutamine: N239 (≠ P51), G240 (= G52), G242 (≠ C54), S268 (≠ C79), L269 (= L80), N310 (≠ Y127), H311 (= H128), G312 (≠ S129), F313 (≠ L130)

Sites not aligning to the query:

active site: 201
binding glutamine: 46

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
30% identity, 59% coverage: 74:185/190 of query aligns to 99:207/693 of P49915

query
sites
P49915

P

P

L

V

L

L

G

G

V

I

C
|
C

L

Y

G

G

H

M

Q

Q

A

M

I

M

G

N

Q

K

A

V

F

F

G

G

K

T

V

V

V

H

R

K

A

K

D

S

K

V

V

R

M

E

H

D

G

G

K

V

T

F

S

N

P

I

I

S

F

V

H

D

D

N

G

T

K

C

G

S

L

L

F

F

R

R

D

G

L

L

P

Q

D

K

P

E

F

E

A

V

T

L

R

L

Y

T

H

H

S

G

L

D

I

S

V

V

E

D

R

K

A

V

S

A

L

-

P

-

D

D

T

G

L

F

E

K

V

V

T

V

A

A

W

-

T

R

A

S

A

G

G

N

E

I

I

V

M

A

G

G

L

I

R

A

H

N

R

E

T

S

L

K

D

K

V

L

E

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

S

T

E

E

H

N

G

G

K

K

T

V

L

I

L

L

Q

K

H

N

F

F

L

L

C104 (= C79) active site, For GATase activity
H190 (= H168) active site, For GATase activity
E192 (= E170) active site, For GATase activity

Sites not aligning to the query:

337 binding XMP
522 binding XMP
610 binding XMP
685 binding XMP
691 binding XMP

1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
24% identity, 97% coverage: 2:186/190 of query aligns to 8:197/501 of 1gpmA

query
sites
1gpmA

L

I

L

L

M

I

I

L

D

D

N

F

Y

G

D

S

S

Q

F

Y

T

T

Y

Q

N

L

L

V

V

A

Q

R

Y

R

F

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G

R

E

E

L

L

G

G

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V

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L

E

W

R

A

N

W

D

D

S

V

I

T

D

E

V

-

A

A

A

Q

I

I

E

R

Q

D

L

F

A

N

P

P

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S

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I

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I

I

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G

G
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G

P

P

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E

T

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T

N

T

E

E

A

E

G

N

I

S

S

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R

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F

F

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E

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A

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C
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C

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x
Y

G

G

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M

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I

M

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A

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M

A

Q

F

L

G

G

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R

A

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N

K

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N

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G

L

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P

E

D

D

P

A

F

L

A

T

A

A

T

D

R

G

Y

K

H

P

S

L

L

L

I

D

V

V

-

W

-

M

-

S

-

H

-

G

-

D

E

K

R

V

A

T

S

A

L

I

P

P

D

S

T

D

L

F

E

I

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T

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V

A

A

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S

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T

A

E

A

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C

E

P

I

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A

G

I

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M

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R

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E

Y

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G

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F

H
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H

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E

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L

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F

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R

active site: G57 (= G52), C84 (= C79), Y85 (≠ L80), H179 (= H168), E181 (= E170)

Sites not aligning to the query:

active site: 237, 357
binding adenosine monophosphate: 231, 232, 233, 258, 313
binding pyrophosphate 2-: 233, 235, 236, 237, 238, 357

5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
27% identity, 77% coverage: 39:185/190 of query aligns to 42:188/490 of 5tw7F

query
sites
5tw7F

I

I

E

K

Q

A

L

F

A

N

P

P

S

K

R

G

I

I

C

I

I

L

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G
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G

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P

C

N

T

S

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N

Y

E

E

A

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I

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S

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A

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D

V

T

I

-

R

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D

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G

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I

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C

L
x
Y

G

G

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M

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Q

A

F

I

M

G

A

Q

H

A

H

F

L

G

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K

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N

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G

K

Y

T

A

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K

F

T

H

I

D

D

G

S

-

G

-

L

-

T

K

R

G

G

L

I

F

Q

R

D

D

D

L

A

P

P

D

N

P

T

F

L

A

D

A

V

T

W

R

M

Y

S

H

H

S

G

L

D

I

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V

V

E

S

R

K

A

-

S

-

L

L

P

P

D

D

T

G

L

F

E

A

V

V

T

I

A

G

W

D

T

T

A

P

A

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C

E

P

I

I

M

A

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H

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H
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H

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E
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E

S

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I

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A

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R

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F

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V

active site: G55 (= G52), C81 (= C79), Y82 (≠ L80), H171 (= H168), E173 (= E170)

Sites not aligning to the query:

active site: 229, 345
binding magnesium ion: 466, 469, 472

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)
29% identity, 84% coverage: 11:170/190 of query aligns to 185:338/2225 of P27708

query
sites
P27708

F

L

T

K

Y

Y

N

N

L

Q

V

I

Q

R

Y

C

F

L

G

C

E

Q

L

R

G

G

A

A

E

E

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V

E

V

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P

N

W

D

D

-

H

S

A

I

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D

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S

A

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A

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I

Y

E

E

Q

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L

L

A

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L

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S

R

N

I

-

C

-

I

-

S

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G

G

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D

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C

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A

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A

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L

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I

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G

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C

R

-

D

-

L

-

P

-

D

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P

-

F

F

A

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A

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T

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R

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Y

N

H

H

S

G

L

F

I

A

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E

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T

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S

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L

P

P

-

A

D

D

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W

L

A

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P

V

L

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F

A

T

W

N

T

A

A

N

A

D

G

G

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Q

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F

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H

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P

E

E

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)
29% identity, 84% coverage: 11:170/190 of query aligns to 185:338/2225 of P08955

query
sites
P08955

F

L

T

K

Y

Y

N

N

L

Q

V

I

Q

R

Y

C

F

L

G

C

E

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L

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G

A

A

E

E

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V

-

V

E

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R

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N

N

D

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E

I

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D

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S

A

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A

K

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G

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L

A

-

P

-

S

-

R

-

I

-

C

F

I

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S

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P

N

G

G

P

P

C

G

T

D

P

P

-

A

N

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E

Y

A

P

G

G

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-

V

-

A

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T

L

L

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N

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K

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C

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G

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H

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Q

A

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L

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A

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L

A

A

F

I

G

G

G

A

K

K

V

T

V

Y

R

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A

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D

R

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M

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R

G

G

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N

S

Q

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P

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C

F

L

H

L

D

V

G

G

K

T

G

G

L

R

F

C

R

-

D

-

L

-

P

-

D

-

P

-

F

F

A

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

E

D

R

A

A

D

S

S

L

L

P

P

-

A

-

G

-

W

D

T

T

P

L

L

E

F

V

T

T

N

A

A

W

N

T

D

A

C

A

S

G

N

E

E

I

-

M

-

G

G

L

I

R

V

H

H

R

D

T

S

L

L

D

P

V

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

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.

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)
27% identity, 64% coverage: 49:170/190 of query aligns to 237:355/2224 of P05990

query
sites
P05990

I

L

S

S

P

N

G

G

P

P

C

G

T

N

P

P

N

E

E

S

A

C

G

D

I

Q

S

I

L

V

E

Q

V

Q

I

V

R

R

H

K

F

V

-

I

-

E

A

E

G

G

K

Q

I

K

P

P

L

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

A

L

I

L

G

A

Q

K

A

A

F

I

G

G

G

C

K

S

V

T

V

Y

R

K

A

M

D

K

K

Y

V

G

M

N

H

R

G

G

K

H

T

N

S

L

P

P

I

C

F

L

H

H

D

R

G

A

K

T

G

G

L

R

F

C

R

-

D

-

L

-

P

-

D

-

P

-

F

L

A

M

A

T

T

S

R

Q

Y

N

H

H

S

G

L

Y

I

A

V

V

E

D

R

L

A

E

S

Q

L

L

P

P

D

D

T

G

L

W

-

S

E

E

V

L

T

F

A

V

W

N

T

A

A

N

A

D

G

G

E

T

I

N

M

E

G

G

L

I

R

V

H

H

R

A

T

S

L

K

D

P

V

Y

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

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

3r75B Crystal structure of 2-amino-2-desoxyisochorismate synthase (adic) synthase phze from burkholderia lata 383 in complex with benzoate, pyruvate, glutamine and contaminating zn2+ (see paper)
27% identity, 94% coverage: 3:181/190 of query aligns to 434:610/622 of 3r75B

query
sites
3r75B

L

L

M

I

I

V

D

D

N

A

Y

E

D

D

S

H

F

F

T

T

Y

A

N

M

L

I

V

A

Q

Q

Y

Q

F

L

G

S

E

S

L

L

G

G

A

L

E

A

V

T

R

E

V

V

-

C

E

G

R

V

N

H

D

D

S

A

I

V

D

D

V

L

A

A

A

R

I

Y

E

D

Q

V

L

-

A

-

P

-

S

-

R

-

I

V

C

V

I

M

S

G

P

P

G

G

P

P

C

G

T

D

P

P

N

S

E

D

A

A

G

G

I

-

S

D

L

P

E

R

V

I

I

A

R

R

H

L

F

Y

A

A

-

W

-

L

-

R

-

H

-

L

-

I

-

D

-

E

G

G

K

K

I

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P

P

L

F

L

M

G

A

V

V

C
|
C

L

L

G

S

H

H

Q

Q

A

I

I

L

G

N

Q

A

A

I

F

L

G

G

G

I

K

P

V

L

V

V

R

R

A

R

D

E

K

V

V

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M

N

H

Q

G

G

K

I

T

Q

S

V

P

E

I

I

F

D

H

L

D

F

G

G

K

Q

-

R

-

E

-

R

-

V

G

G

L

F

F
x
Y

R

N

D

T

L

Y

P

-

D

-

P

-

F

V

A

A

A

Q

T

T

R

V

Y

R

H

D

S

E

L

M

I

D

V

V

E

D

R

G

A

V

S

G

L

-

P

-

D

-

T

T

L

V

E

A

V

I

T

S

A

R

W

D

T

P

A

R

A

T

G

G

E

E

I

V

M

H

G

A

L

L

R

R

H

G

R

P

T

T

L

F

D

-

V

-

E

S

G

S

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M

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Q

F

F

H
|
H

P

A

E

E

S

S

I

V

L

L

S

T

E

V

H

D

G

G

K

P

T

R

L

I

L

L

binding zinc ion: C512 (= C79), Y552 (≠ F115), H597 (= H168)

Sites not aligning to the query:

active site: 143, 195, 238, 273, 298, 322, 346, 363, 376, 380
binding magnesium ion: 238, 376
binding pyruvic acid: 322, 346, 360, 361, 380

Query Sequence

>WP_009567142.1 NCBI__GCF_000021485.1:WP_009567142.1
MLLMIDNYDSFTYNLVQYFGELGAEVRVERNDSIDVAAIEQLAPSRICISPGPCTPNEAG
ISLEVIRHFAGKIPLLGVCLGHQAIGQAFGGKVVRADKVMHGKTSPIFHDGKGLFRDLPD
PFAATRYHSLIVERASLPDTLEVTAWTAAGEIMGLRHRTLDVEGVQFHPESILSEHGKTL
LQHFLQGGAR

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