SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_092996593.1 NCBI__GCF_900102855.1:WP_092996593.1 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)
64% identity, 97% coverage: 1:192/197 of query aligns to 1:187/187 of P00903

query
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P00903

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C79 (= C79) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H173) mutation to Q: Loss of activity.
E170 (= E175) 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)
50% identity, 96% coverage: 2:191/197 of query aligns to 75:265/276 of Q42565

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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.

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)
46% identity, 96% coverage: 2:190/197 of query aligns to 4:187/193 of P00900

query
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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)
46% identity, 96% coverage: 2:190/197 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 (= H173), E171 (= E175)
binding glutamic acid: P55 (= P51), G56 (= G52), G58 (≠ C54), C83 (= C79), L84 (= L80), Q87 (= Q83), H132 (= H128), S133 (= S129), L134 (= L130)

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
48% identity, 95% coverage: 3:189/197 of query aligns to 7:187/673 of 8hx8A

query
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8hx8A

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binding magnesium ion: I175 (= I177), S177 (≠ T179)

Sites not aligning to the query:

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

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
38% identity, 95% coverage: 3:189/197 of query aligns to 6:144/632 of 8hx9A

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8hx9A

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binding magnesium ion: S134 (≠ T179), D135 (≠ C180)

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

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, 87% coverage: 14:184/197 of query aligns to 254:413/430 of Q9LVW7

query
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Q9LVW7

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Y

G

G

A

C

Q

Q

V

I

E

T

V

V

H

V

R

P

N

S

D

T

Q

F

I

P

S

A

I

A

E

E

A

A

I

L

E

-

R

K

L

M

V

N

P

P

D

D

H

G

L

I

V

L

I

F

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

S

E

A

A

V

G

P

I

Y

S

A

V

V

E

E

A

T

I

V

R

K

H

E

F

L

A

L

G

G

K

K

L

V

P

P

I

V

L

Y

G

G

V

I

C

C

L

M

G

G

H

H

Q

Q

S

L

I

L

G

G

Q

Q

A

A

F

L

G

G

R

K

I

T

V

F

R

K

A

M

G

K

E

F

I

G

M

H

H

H

G

G

K

G

T

N

S

H

L

P

V

V

Y

R

H

N

K

N

D

R

I

T

G

G

V

Q

F

V

A

E

G

-

L

-

D

-

N

-

P

-

F

-

V

I

A

S

T

A

R

Q

Y

N

H

H

S

N

L

Y

V

A

I

V

E

D

Q

P

A

A

S

S

L

L

P

P

A

G

V

G

L

V

E

E

V

V

T

T

A

H

W

V

T

N

G

L

D

N

A

D

G

G

G

-

N

-

M

-

E

-

E

S

I

C

M

A

G

G

I

L

R

S

H

F

V

P

E

E

Y

M

N

N

L

V

E

M

G

S

V

L

Q

Q

F

Y

H

H

P

P

E

E

S

A

I

S

L

P

T

G

C

P

H
|
H

G

D

H

S

D

D

H410 (= H181) mutation to Y: In ven6-1; reticulate leaf phenotype.

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
28% identity, 100% coverage: 1:197/197 of query aligns to 1:188/475 of 2ywcA

query
sites
2ywcA

M

M

I

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

Q

F

V

S

E

L

V

I

H

L

R

P

N

G

D

D

Q

A

I

-

S

P

I

L

E

E

A

E

I

V

E

L

R

K

L

H

V

R

P

P

D

Q

H

A

L

L

V

I

I

L

S

S

P

G

G
|
G

P

P

C
x
R

T

S

P

V

T

F

E

D

A

P

G

D

I

A

S

P

V

R

E

P

A

D

I

P

R

R

H

L

F

F

A

S

G

S

K

G

L

L

P

P

I

L

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

L

I

L

G

A

Q

Q

A

E

F

L

G

G

R

R

I

V

V

E

R

R

A

A

G

G

E

R

I

A

M

E

H

Y

G

G

K

K

T

A

S

L

L

L

V

T

Y

R

H

H

K

E

D

G

I

-

G

P

V

L

F

F

A

R

G

G

L

L

D

E

N

G

P

E

F

V

V

Q

A

V

T

W

R

M

Y

S

H

H

S

Q

L

D

V

A

I

V

E

T

Q

A

A

P

S

P

L

-

P

-

A

-

V

-

L

-

E

-

V

-

T

P

A

G

W

W

T

R

G

V

D

V

A

A

G

E

G

T

N

E

M

E

E

N

E

P

I

V

M

A

G

A

I

I

R

A

H

S

V

P

E

D

Y

G

N

R

L

A

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

T

T

C

P

H

K

G

G

H

M

D

Q

L

I

L

L

A

E

N

N

F

F

L

L

K

E

Q

L

S

A

G

G

G

V

V

K

R

R

active site: G51 (= G52), R53 (≠ C54), C78 (= C79), Y79 (≠ L80), H164 (= H173), E166 (= E175)

Sites not aligning to the query:

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

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
27% identity, 98% coverage: 1:194/197 of query aligns to 1:179/183 of 7yc6A

query
sites
7yc6A

M

M

I

I

L

V

M

I

I

L

D

D

N

N

Y

G

D

G

S

Q

F

Y

T

V

Y

H

N

R

L

I

V

H

Q

R

Y

S

F

L

G

K

E

Y

L

I

G

G

A

V

Q

S

V

S

E

K

V

I

H

V

R

P

N

N

D

T

Q

T

I

P

S

L

I

E

E

E

A

I

I

E

E

S

R

N

L

K

V

E

P

V

D

K

H

G

L

I

V

I

I

L

S

S

P

G

G

G

P

P

C

D

T

I

P

E

T

K

E

A

A

K

G

N

I

C

S

I

V

D

E

I

A

A

I

L

R

N

H

-

F

-

A

-

G

A

K

K

L

L

P

P

I

I

L

L

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

L

I

I

G

A

Q

L

A

A

F

Y

G

G

R

E

I

V

V

G

R

R

A

A

G

-

E

-

I

-

M

-

H

-

G

A

K

L

T

T

S

K

L

V

V

Y

Y

V

H
x
D

K

K

D

E

I

N

G

P

V

L

F

F

A

K

G

N

L

V

D

P

N

R

P

E

F

F

V

N

A

A

T

W

R

A

Y

S

H

H

S

K

L

-

V

-

I

D

E
|
E

Q

V

A

K

S

K

L

V

P

P

A

E

V

G

L

F

E

E

V

I

T

L

A

A

W
x
H

T

S

G

-

D

-

A

-

G

-

N

D

M

I

E
x
C

E

Q

I

V

M

E

G

A

I

M

R

K

H

H

V

K

E

T

Y

K

N

P

L

I

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

S

V

I

A

L

H

T

T

C

E

H

Y

G

G

H

N

D

E

L

I

L

L

A

K

N

N

F

F

L

C

K

K

Q

V

S

C

G

G

binding zinc ion: C76 (= C79), D101 (≠ H109), E123 (= E133), E123 (= E133), H136 (≠ W146), C140 (≠ E155), C140 (≠ E155), H158 (= H173)

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, 73% coverage: 33:176/197 of query aligns to 222:356/382 of P0A6F1

query
sites
P0A6F1

Q

Q

I

T

S

S

I

A

E

E

A

D

I

V

E

L

R

K

L

M

V

N

P

P

D

D

H

G

L

I

V

F

I

L

S

S

P

N

G
|
G

P

P

C
x
G

T

D

P

P

T

A

E

P

A

C

G

D

I

Y

S

A

V

I

E

T

A

A

I

I

R

Q

H

K

F

F

-

L

A

E

G

T

K

D

L

I

P

P

I

V

L

F

G

G

V

I

C

C

L
|
L

G

G

H

H

Q
|
Q

S

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

R

K

I

T

V

V

R

K

A

M

G

K

E

F

I

G

M

H

H

H

G

G

K

G

T

N

S

H

L

P

V

V

Y

K

H

D

K

V

D

E

I

K

G

N

V

V

F

V

A

-

G

-

L

-

D

-

N

-

P

-

F

M

V

I

A

T

T

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

V

A

I

V

E

D

Q

E

A

A

S

T

L

L

P

P

A

A

V

N

L

L

E

R

V

V

T

T

A

H

W

K

T

S

G

L

D

F

A

D

G

G

G

-

N

-

M

-

E

-

E

T

I

L

M

Q

G

G

I

I

R

H

H

R

V

T

E

D

Y

K

N

P

L

A

E

F

G

S

V

F

Q

Q

F

G

H

H

P

P

E

E

S

A

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

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
28% identity, 73% coverage: 33:176/197 of query aligns to 221:355/379 of 1ce8B

query
sites
1ce8B

Q

Q

I

T

S

S

I

A

E

E

A

D

I

V

E

L

R

K

L

M

V

N

P

P

D

D

H

G

L

I

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

A

E

P

A

C

G

D

I

Y

S

A

V

I

E

T

A

A

I

I

R

Q

H

K

F

F

-

L

A

E

G

T

K

D

L

I

P

P

I

V

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

R

K

I

T

V

V

R

K

A

M

G

K

E

F

I

G

M

H

H

H

G

G

K

G

T

N

S

H

L

P

V

V

Y

K

H

D

K

V

D

E

I

K

G

N

V

V

F

V

A

-

G

-

L

-

D

-

N

-

P

-

F

M

V

I

A

T

T

A

R

Q

Y

N

H

H

S

G

L

F

V

A

I

V

E

D

Q

E

A

A

S

T

L

L

P

P

A

A

V

N

L

L

E

R

V

V

T

T

A

H

W

K

T

S

G

L

D

F

A

D

G

G

G

-

N

-

M

-

E

-

E

T

I

L

M

Q

G

G

I

I

R

H

H

R

V

T

E

D

Y

K

N

P

L

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

active site: C268 (= C79), H352 (= H173), E354 (= E175)

Sites not aligning to the query:

binding L-ornithine: 119, 122

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
28% identity, 73% coverage: 33:176/197 of query aligns to 221:355/379 of 1c3oB

query
sites
1c3oB

Q

Q

I

T

S

S

I

A

E

E

A

D

I

V

E

L

R

K

L

M

V

N

P

P

D

D

H

G

L

I

V

F

I

L

S

S

P
x
N

G
|
G

P

P

C
x
G

T

D

P

P

T

A

E

P

A

C

G

D

I

Y

S

A

V

I

E

T

A

A

I

I

R

Q

H

K

F

F

-

L

A

E

G

T

K

D

L

I

P

P

I

V

L

F

G

G

V

I

C
x
S

L
|
L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

R

K

I

T

V

V

R

K

A

M

G

K

E

F

I

G

M

H

H

H

G

G

K

G

T

N

S

H

L

P

V

V

Y

K

H

D

K

V

D

E

I

K

G

N

V

V

F

V

A

-

G

-

L

-

D

-

N

-

P

-

F

M

V

I

A

T

T

A

R

Q

Y
x
N

H
|
H

S
x
G

L
x
F

V

A

I

V

E

D

Q

E

A

A

S

T

L

L

P

P

A

A

V

N

L

L

E

R

V

V

T

T

A

H

W

K

T

S

G

L

D

F

A

D

G

G

G

-

N

-

M

-

E

-

E

T

I

L

M

Q

G

G

I

I

R

H

H

R

V

T

E

D

Y

K

N

P

L

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

active site: S268 (≠ C79), H352 (= H173), E354 (= E175)
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

1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
23% identity, 97% coverage: 2:192/197 of query aligns to 8:198/501 of 1gpmA

query
sites
1gpmA

I

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

V

G

R

E

E

L

L

G

G

A

V

Q

Y

V

C

E

E

V

L

H

W

R

A

N

W

D

D

Q

-

I

V

S

T

I

E

E

A

A

Q

I

I

E

R

R

D

L

F

V

N

P

P

D

S

H

G

L

I

V

I

I

L

S

S

P

G

G
|
G

P

P

C

E

T

S

P

T

T

T

E

E

A

E

G

N

I

S

S

P

V

R

E

A

A

P

I

Q

R

Y

H

V

F

F

A

E

G

A

K

G

L

V

P

P

I

V

L

F

G

G

V

V

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

T

I

M

G

A

Q

M

A

Q

F

L

G

G

R

H

I

V

V

E

R

A

A

S

G

N

E

E

I

R

M

E

H

F

G

G

K

Y

T

A

S

Q

L

V

V

E

Y

V

H

V

K

N

D

D

I

S

G

A

V

L

F

V

A

R

G

G

L

I

D

E

N

D

P

A

F

L

V

T

A

A

T

D

R

G

Y

K

H

P

S

L

L

L

V

D

I

V

E

W

Q

M

A

S

-

H

-

G

-

D

-

K

-

V

-

T

S

A

L

I

P

P

A

S

V

D

L

F

E

I

V

T

T

V

A

A

W

S

T

T

G

E

D

S

A

C

G

P

G

F

N

A

M

I

E

-

I

-

M

-

G

-

I

M

R

A

H

N

V

E

E

E

Y

K

N

R

L

F

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

C

R

H

Q

G

G

H

M

D

R

L

M

L

L

A

E

N

R

F

F

L

V

K

R

Q

D

active site: G57 (= G52), C84 (= C79), Y85 (≠ L80), H179 (= H173), E181 (= E175)

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

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
29% identity, 62% coverage: 74:195/197 of query aligns to 99:212/693 of P49915

query
sites
P49915

P

P

I

V

L

L

G

G

V

I

C
|
C

L

Y

G

G

H

M

Q

Q

S

M

I

M

G

N

Q

K

A

V

F

F

G

G

R

T

I

V

V

H

R

K

A

K

G

S

E

V

I

R

M

E

H

D

G

G

K

V

T

F

S

N

L

I

V

S

Y

V

H

D

K

N

D

T

I

C

G

S

V

L

F

F

A

R

G

G

L

L

D

Q

N

K

P

E

F

E

V

V

A

V

T

L

R

L

Y

T

H

H

S

G

L

D

V

S

I

V

E

D

Q

K

A

V

S

A

L

-

P

-

A

D

V

G

L

F

E

K

V

V

T

V

A

A

W

R

T

S

G

G

D

N

A

I

G

-

N

-

M

-

E

-

I

V

M

A

G

G

I

I

R

A

H

N

V

E

E

S

Y

K

N

K

L

L

E

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

T

T

C

E

H

N

G

G

H

K

D

V

L

I

L

L

A

K

N

N

F

F

L

L

K

Y

Q

D

S

I

G

A

G

G

C104 (= C79) active site, For GATase activity
H190 (= H173) active site, For GATase activity
E192 (= E175) 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

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)
27% identity, 84% coverage: 11:175/197 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

Q

E

V

V

E

T

V

V

H

V

R

P

N

W

D

D

Q

H

I

-

S

-

I

-

E

-

A

A

I

L

E

D

R

S

L

Q

V

E

P

Y

D

E

H

G

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

A

E

S

A

Y

G

P

I

S

S

V

V

V

E

S

A

T

I

L

R

S

H

R

F

V

A

L

G

S

K

E

-

P

-

N

-

P

L

R

P

P

I

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

I

G

G

G

A

R

K

I

T

-

Y

-

K

V

M

R

R

A

Y

G

G

E

N

I

R

M

G

H

H

G

N

K

Q

T

P

S

C

L

L

V

-

Y

-

H

-

K

-

D

-

I

-

G

-

V

-

F

L

A

V

G

G

L

S

D

G

N

R

P

C

F

F

V

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

I

V

E

E

Q

T

A

D

S

S

L

L

P

P

A

A

V

D

L

W

E

A

V

P

T

L

A

F

W

T

T

N

G

A

D

N

A

D

G

G

G

S

N

N

M

-

E

-

I

-

M

E

G

G

I

I

R

V

H

H

V

N

E

S

Y

L

N

P

L

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

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

2vxoB Human gmp synthetase in complex with xmp (see paper)
29% identity, 62% coverage: 74:195/197 of query aligns to 77:187/658 of 2vxoB

query
sites
2vxoB

P

P

I

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

M

I

M

G

N

Q

K

A

V

F

F

G

G

R

T

I

V

V

-

R

-

A

-

G

-

E

-

I

-

M

-

H

H

G

K

K

K

T

S

S

D

L

G

V

V

Y

F

H

N

K

I

D

S

I

V

-

D

-

N

-

T

-

C

G

S

V

L

F

F

A

R

G

G

L

L

D

Q

N

K

P

E

F

E

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V

A

V

T

L

R

L

Y

T

H

H

S

G

L

D

V

S

I

V

E

D

Q

K

A

V

S

A

L

-

P

-

A

D

V

G

L

F

E

K

V

V

T

V

A

A

W

R

T

S

G

G

D

N

A

I

G

-

N

-

M

-

E

-

I

V

M

A

G

G

I

I

R

A

H

N

V

E

E

S

Y

K

N

K

L

L

E

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

T

T

C

E

H

N

G

G

H

K

D

V

L

I

L

L

A

K

N

N

F

F

L

L

K

Y

Q

D

S

I

G

A

G

G

active site: C82 (= C79), Y83 (≠ L80), H165 (= H173), E167 (= E175)

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

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)
27% identity, 84% coverage: 11:175/197 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

Q

L

L

G

G

A

A

Q

E

V

V

E

T

V

V

-

V

H

P

R

W

N

N

D

H

Q

E

I

L

S

D

I

S

E

Q

A

K

I

Y

E

-

R

-

L

-

V

-

P

-

D

D

H

G

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

A

E

S

-

Y

A

P

G

G

I

V

-

V

-

A

S

T

V

L

E

N

A

R

I

V

R

L

H

S

F

E

A

P

G

N

K

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V

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F

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G

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I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

I

G

G

G

A

R

K

I

T

-

Y

-

K

V

M

R

R

A

Y

G

G

E

N

I

R

M

G

H

H

G

N

K

Q

T

P

S

C

L

L

V

-

Y

-

H

-

K

-

D

-

I

-

G

-

V

-

F

L

A

V

G

G

L

T

D

G

N

R

P

C

F

F

V

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

I

V

E

D

Q

A

A

D

S

S

L

L

P

P

A

A

V

-

L

-

E

-

V

-

T

-

A

G

W

W

T

T

G

P

-

L

D

F

A

T

G

N

G

A

N

N

M

D

E

C

E

S

I

N

M

E

G

G

I

I

R

V

H

H

V

D

E

S

Y

L

N

P

L

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.

Q18990 Multifunctional protein pyr-1; 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 Caenorhabditis elegans (see 3 papers)
28% identity, 66% coverage: 45:175/197 of query aligns to 219:341/2198 of Q18990

query
sites
Q18990

D

D

H

G

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

E

E

I

A

C

G

A

I

P

S

L

V

V

E

D

A

R

I

L

R

A

H

K

F

V

-

I

-

A

A

R

G

G

K

D

L

K

P

P

I

I

L

F

G

G

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I

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C

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L

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H

Q

Q

S

I

I

L

G

S

Q

R

A

A

F

I

G

G

G

A

R

K

I

T

V

Y

R

K

A

L

G

K

E

Y

I

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M

N

H

R

G

G

K

H

T

N

S

Q

L

P

V

C

Y

T

H

H

K

Y

D

A

I

T

G

G

V

-

F

-

A

-

G

-

L

-

D

-

N

R

P

C

F

Y

V

I

A

T

T

S

R

Q

Y

N

H

H

S

G

L

Y

V

A

I

V

E

D

Q

P

A

D

S

S

L

L

P

P

A

A

V

D

L

W

E

K

V

A

T

L

A

-

W

F

T

T

G

N

D

E

A

N

G

D

G

K

N

T

M

N

E

E

E

-

I

-

M

-

G

G

I

I

R

V

H

H

V

S

E

S

Y

K

N

P

L

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

1602 H→Q: In cu8; probable loss of dihydroorotase activity. Severe late stage embryonic lethality in 50% of animals. The few surviving mutants have a shorter and thicker pharyngeal isthmus, an abnormal knobbed tail, mild egg-laying defects, moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background, prevents the formation of abnormally enlarged gut granules in embryos. Complete embryonic lethality in a rnst-2 qx245 mutant background.

5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
26% identity, 96% coverage: 2:190/197 of query aligns to 6:188/490 of 5tw7F

query
sites
5tw7F

I

I

L

L

M

I

I

L

D

D

N

F

Y

G

D

S

S

Q

F

V

T

T

Y

R

N

L

L

I

V

A

Q

R

Y

R

F

V

G

R

E

E

L

A

G

H

A

V

Q

Y

V

C

E

E

V

L

H

H

R

S

N

F

D

D

Q

-

I

M

S

P

I

L

E

D

A

E

I

I

E

K

R

A

L

F

V

N

P

P

D

K

H

G

L

I

V

I

I

L

S

S

P

G

G
|
G

P

P

C

N

T

S

P

V

T

Y

E

E

A

S

G

D

I

Y

S

Q

V

A

E

D

A

T

I

-

R

G

H

I

F

F

A

D

G

L

K

G

L

I

P

P

I

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

F

I

M

G

A

Q

H

A

H

F

L

G

G

R

E

I

-

V

V

R

Q

A

P

G

G

E

N

I

Q

M

R

H

E

G

F

K

G

T

Y

S

A

L

Q

V

V

Y

K

H

T

K

I

D

D

I

S

G

G

V

L

F

T

A

R

G

G

L

I

-

Q

-

D

D

D

N

A

P

P

F

N

V

T

A

L

T

D

R

V

Y

W

H

M

S

S

L

H

V

G

I

D

E

K

Q

V

A

S

S

K

L

L

P

P

A

D

V

G

L

F

E

A

V

V

T

I

A

G

W

D

T

T

G

P

D

S

A

C

G

P

G

I

N

A

M

M

E

M

E

E

I

-

M

-

G

-

I

-

R

-

H

N

V

T

E

E

Y

K

N

Q

L

F

E

Y

G

G

V

I

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

C

K

H

Q

G

G

H

R

D

A

L

L

A

N

N

R

F

F

L

V

active site: G55 (= G52), C81 (= C79), Y82 (≠ L80), H171 (= H173), E173 (= E175)

Sites not aligning to the query:

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

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)
30% identity, 68% coverage: 45:177/197 of query aligns to 238:365/2225 of P20054

query
sites
P20054

D

D

H

G

L

V

V

F

I

I

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

S

E

L

A

C

G

G

I

K

S

A

V

I

E

E

A

N

I

I

R

R

H

K

F

V

A

L

G

A

K

-

L

L

P

P

I

V

-

A

-

K

-

A

-

V

L

F

G

G

V

V

C

C

L

M

G

G

H

N

Q

Q

S

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I

L

G

G

Q

L

A

A

F

A

G

G

G

A

R

Q

I

T

V

-

R

-

A

-

G

-

E

-

I

-

M

-

H

-

G

-

K

-

T

-

S

-

L

-

V

-

Y

-

H

H

K

K

D

M

I

A

G

F

V

G

F

N

A

R

G

G

L

L

D

N

N

Q

P

P

F

C

V

V

-

D

-

Q

-

I

-

S

-

G

-

R

-

C

-

H

-

I

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

V

I

I

E

D

Q

S

A

N

S

S

L

L

P

P

A

A

V

G

L

S

E

G

V

W

T

K

A

T

W

Y

T

F

G

I

D

N

A

A

G

N

G

D

N

A

M

S

E

N

E

E

I

-

M

-

G

G

I

I

R

Y

H

H

V

E

E

S

Y

K

N

P

L

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E

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G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

A

I

M

Sites not aligning to the query:

1 modified: N-acetylmethionine

Query Sequence

>WP_092996593.1 NCBI__GCF_900102855.1:WP_092996593.1
MILMIDNYDSFTYNLVQYFGELGAQVEVHRNDQISIEAIERLVPDHLVISPGPCTPTEAG
ISVEAIRHFAGKLPILGVCLGHQSIGQAFGGRIVRAGEIMHGKTSLVYHKDIGVFAGLDN
PFVATRYHSLVIEQASLPAVLEVTAWTGDAGGNMEEIMGIRHVEYNLEGVQFHPESILTC
HGHDLLANFLKQSGGVR

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