SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012470589.1 NCBI__GCF_000020385.1:WP_012470589.1 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)
61% identity, 95% coverage: 1:185/195 of query aligns to 1:185/187 of P00903

query
sites
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, 95% coverage: 2:187/195 of query aligns to 75:266/276 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)
50% identity, 95% coverage: 3:188/195 of query aligns to 7:191/673 of 8hx8A

query
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8hx8A

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binding magnesium ion: I175 (= I172), S177 (≠ T174)

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)
40% identity, 94% coverage: 2:185/195 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)
40% identity, 94% coverage: 2:185/195 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)
41% identity, 95% coverage: 3:188/195 of query aligns to 6:148/632 of 8hx9A

query
sites
8hx9A

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binding magnesium ion: S134 (≠ T174), 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
33% identity, 96% coverage: 1:187/195 of query aligns to 1:177/183 of 7yc6A

query
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7yc6A

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-

L

D

E

E

E

I

I

-

E

S

S

V

N

A

K

D

E

I

V

A

K

G

G

L

-

R

-

P

-

D

-

R

-

I

I

V

I

V

L

S

S

P

G

G

G

P

P

-

D

C

I

S

E

P

K

E

A

E

K

A

N

G

C

I

I

S

D

V

I

A

A

A

-

I

-

K

-

E

-

Y

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

S

L

I

I

G

A

A

L

A

A

F

Y

G

G

K

E

V

V

V

G

R

R

S

A

-

A

-

L

V

T

S

K

L

V

M

Y

H

V

G
x
D

K

K

T

E

S

N

P

P

I

-

H

-

D

-

G

-

K

-

E

-

L

L

F

F

S

K

G

N

L

V

P

P

N

R

P

E

F

F

N

N

A

A

T

W

R

A

Y

S

H

H

S

K

L

D

V
x
E

V

V

E

K

R

K

A

-

T

-

L

V

P

P

D

E

C

G

L

F

E

E

M

I

T

L

A

A

W
x
H

V

S

D

D

N

I

G
x
C

E

Q

I

V

M

E

G

A

L

M

R

K

H

H

R

K

D

T

L

K

P

P

V

I

W

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

S

V

I

A

L

H

T

T

E

E

G

Y

G

G

M

N

E

E

L

I

L

L

D

K

N

N

F

F

L

C

K

K

L

V

binding zinc ion: C76 (= C79), D101 (≠ G102), E123 (≠ V131), E123 (≠ V131), 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)
31% identity, 81% coverage: 14:171/195 of query aligns to 254:405/430 of Q9LVW7

query
sites
Q9LVW7

N

N

I

I

V

L

Q

R

Y

R

L

L

A

S

Q

S

L

Y

G

G

E

C

E

Q

V

I

K

T

V

V

R

P

N

S

D

-

E

T

I

F

S

P

V

A

A

A

D

E

I

A

A

L

G

K

L

M

R

N

P

P

D

D

R

G

I

I

V

L

V

F

S

S

P

N

G

G

P

P

C

G

S

D

P

P

E

S

E

A

A

V

G

P

I

Y

S

A

V

V

A

E

A

T

I

V

K

K

E

E

Y

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

S

L

I

L

G

G

A

Q

A

A

F

L

G

G

K

K

V

T

V

F

R

K

S

M

V

K

S

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

I

V

H

R

H

N

D

N

-

R

-

T

G

G

K

Q

E

V

L

E

F

I

S

S

G

A

L

-

P

-

N

-

P

-

F

-

N

-

A

-

T

-

R

Q

Y

N

H

H

S

N

L

Y

V

A

V

V

E

D

R

P

A

A

T

S

L

L

P

P

D

G

C

G

L

V

E

E

M

V

T

T

-

H

A

V

W

N

V

L

D

N

N

D

G

G

E

S

I

C

M

A

G

G

L

L

R

S

H

F

R

P

D

E

L

M

P

N

V

V

W

M

G

S

V

L

Q

Q

F

Y

H

H

P

P

E

E

S

A

Sites not aligning to the query:

410 H→Y: In ven6-1; reticulate leaf phenotype.

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
30% identity, 91% coverage: 14:191/195 of query aligns to 203:376/379 of 1ce8B

query
sites
1ce8B

N

N

I

I

V

L

Q

R

Y

M

L

L

A

V

Q

D

L

R

G

G

E

C

E

R

V

L

K

T

V

I

V

V

R

P

N

A

D

-

E

Q

I

T

S

S

V

A

A

E

D

D

I

V

A

L

G

K

L

M

R

N

P

P

D

D

R

G

I

I

V

F

V

L

S

S

P

N

G

G

P

P

C

G

S

D

P

P

E

A

E

P

A

C

G

D

I

Y

S

A

V

I

A

T

A

A

I

I

K

Q

E

K

Y

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

S

L

I

L

G

A

A

L

A

A

F

S

G

G

G

A

K

K

V

T

V

V

R

K

S

M

V

K

S

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

I

V

H

K

H

D

D

V

G

E

K

K

E

N

L

V

F

V

S

-

G

-

L

-

P

-

N

-

P

-

F

M

N

I

A

T

T

A

R

Q

Y

N

H

H

S

G

L

F

V

A

V

V

E

D

R

E

A

A

T

T

L

L

P

P

D

A

C

N

L

L

E

R

M

V

T

T

-

H

A

K

W

S

V

L

D

F

N

D

G

G

E

T

I

L

M

Q

G

G

L

I

R

H

H

R

R

T

D

D

L

K

P

P

V

A

W

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

-

A

S

S

I

P

L

G

T

P

E

H

G

D

G

A

M

A

E

P

L

L

L

F

D

D

N

H

F

F

L

I

K

E

L

L

S

I

R

E

Q

Q

Y

Y

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)
30% identity, 91% coverage: 14:191/195 of query aligns to 204:377/382 of P0A6F1

query
sites
P0A6F1

N

N

I

I

V

L

Q

R

Y

M

L

L

A

V

Q

D

L

R

G

G

E

C

E

R

V

L

K

T

V

I

V

V

R

P

N

A

D

-

E

Q

I

T

S

S

V

A

A

E

D

D

I

V

A

L

G

K

L

M

R

N

P

P

D

D

R

G

I

I

V

F

V

L

S

S

P

N

G
|
G

P

P

C
x
G

S

D

P

P

E

A

E

P

A

C

G

D

I

Y

S

A

V

I

A

T

A

A

I

I

K

Q

E

K

Y

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

S

L

I

L

G

A

A

L

A

A

F

S

G

G

G

A

K

K

V

T

V

V

R

K

S

M

V

K

S

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

I

V

H

K

H

D

D

V

G

E

K

K

E

N

L

V

F

V

S

-

G

-

L

-

P

-

N

-

P

-

F

M

N

I

A

T

T

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

V

A

V

V

E

D

R

E

A

A

T

T

L

L

P

P

D

A

C

N

L

L

E

R

M

V

T

T

-

H

A

K

W

S

V

L

D

F

N

D

G

G

E

T

I

L

M

Q

G

G

L

I

R

H

H

R

R

T

D

D

L

K

P

P

V

A

W

F

G

S

V

F

Q

Q

F

G

H

H

P

P

E

E

-

A

S

S

I

P

L

G

T

P

E

H

G

D

G

A

M

A

E

P

L

L

L

F

D

D

N

H

F

F

L

I

K

E

L

L

S

I

R

E

Q

Q

Y

Y

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

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
30% identity, 91% coverage: 14:191/195 of query aligns to 203:376/379 of 1c3oB

query
sites
1c3oB

N

N

I

I

V

L

Q

R

Y

M

L

L

A

V

Q

D

L

R

G

G

E

C

E

R

V

L

K

T

V

I

V

V

R

P

N

A

D

-

E

Q

I

T

S

S

V

A

A

E

D

D

I

V

A

L

G

K

L

M

R

N

P

P

D

D

R

G

I

I

V

F

V

L

S

S

P
x
N

G
|
G

P

P

C
x
G

S

D

P

P

E

A

E

P

A

C

G

D

I

Y

S

A

V

I

A

T

A

A

I

I

K

Q

E

K

Y

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

S

L

I

L

G

A

A

L

A

A

F

S

G

G

G

A

K

K

V

T

V

V

R

K

S

M

V

K

S

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

I

V

H

K

H

D

D

V

G

E

K

K

E

N

L

V

F

V

S

-

G

-

L

-

P

-

N

-

P

-

F

M

N

I

A

T

T

A

R

Q

Y
x
N

H
|
H

S
x
G

L
x
F

V

A

V

V

E

D

R

E

A

A

T

T

L

L

P

P

D

A

C

N

L

L

E

R

M

V

T

T

-

H

A

K

W

S

V

L

D

F

N

D

G

G

E

T

I

L

M

Q

G

G

L

I

R

H

H

R

R

T

D

D

L

K

P

P

V

A

W

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

-

A

S

S

I

P

L

G

T

P

E

H

G

D

G

A

M

A

E

P

L

L

L

F

D

D

N

H

F

F

L

I

K

E

L

L

S

I

R

E

Q

Q

Y

Y

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

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
28% identity, 96% coverage: 1:188/195 of query aligns to 1:184/475 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

F

R

N

L

I

I

V

A

Q

R

Y

R

L

L

A

R

Q

E

L

L

G

-

E

R

E

A

V

F

K

S

V

L

V

I

R

L

N

P

D

G

E

D

I

A

S

P

V

L

A

E

D

E

I

V

A

L

G

K

L

H

R

R

P

P

D

Q

R

A

I

L

V

I

V

L

S

S

P

G

G
|
G

P

P

C
x
R

S

S

P

V

E

F

E

D

A

P

G

D

I

A

S

P

V

R

A

P

A

D

I

P

K

R

E

L

Y

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

S

L

I

L

G

A

A

Q

A

E

F

L

G

G

K

R

V

V

V

E

R

R

S

A

V

G

S

R

L

A

M

E

H

Y

G

G

K

K

T

A

S

L

P

L

I

T

H

R

H

H

D

E

G

G

K

P

E

-

L

L

F

F

S

R

G

G

L

L

P

E

N

G

P

E

F

V

N

Q

A

V

T

W

R

M

Y

S

H

H

S

Q

L

D

V

A

V

V

E

-

R

-

A

T

T

A

L

P

P

P

D

P

C

G

L

W

E

R

M

V

T

V

A

A

W

E

V

T

D

E

N

E

G

N

E

P

I

V

M

A

G

A

L

I

R

A

H

S

R

P

D

D

L

G

P

R

V

A

W

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

T

T

E

P

G

K

G

G

M

M

E

Q

L

I

L

L

D

E

N

N

F

F

L

L

K

E

L

L

S

A

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

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)
30% identity, 92% coverage: 11:190/195 of query aligns to 185:359/2225 of P27708

query
sites
P27708

F

L

T

K

F

Y

N

N

I

Q

V

I

Q

R

Y

C

L

L

A

C

Q

Q

L

R

G

G

E

A

E

E

V

V

K

T

V

V

R

P

N

W

D

D

E

H

-

A

I

L

S

D

V

S

A

Q

D

E

I

Y

A

E

G

G

L

L

R

-

P

-

D

-

R

-

I

-

V

F

V

L

S

S

P

N

G

G

P

P

C

G

S

D

P

P

E

A

E

S

A

Y

G

P

I

S

S

V

V

V

A

S

A

T

I

L

K

S

E

R

Y

V

A

L

G

S

K

E

-

P

-

N

-

P

I

R

P

P

L

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

A

L

A

A

F

I

G

G

G

A

K

K

V

T

V

Y

R

K

S

M

V

R

S

Y

L

G

M

N

H

R

G

G

K

H

T

N

S

Q

P

P

I

C

H

-

D

-

G

-

K

-

E

-

L

L

F

L

S

V

G

G

L

S

P

G

N

R

P

C

F

F

N

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

V

V

E

E

R

T

A

D

T

S

L

L

P

P

-

A

D

D

C

W

L

A

E

P

M

L

T

F

A

T

W

N

V

A

D

N

N

D

G

G

E

S

I

N

M

E

G

G

L

I

R

V

H

H

R

N

D

S

L

L

P

P

V

F

W

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

Q

L

A

T

G

E

P

G

S

G

D

M

M

E

E

L

L

-

F

D

D

N

I

F

F

L

L

K

E

L

T

S

V

R

K

Q

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)
30% identity, 92% coverage: 11:190/195 of query aligns to 185:359/2225 of P08955

query
sites
P08955

F

L

T

K

F

Y

N

N

I

Q

V

I

Q

R

Y

C

L

L

A

C

Q

Q

L

L

G

G

E

A

E

E

V

V

K

T

V

V

R

P

-

W

N

N

D

H

E

E

I

L

S

D

V

S

A

Q

D

K

I

Y

A

D

G

G

L

L

R

-

P

-

D

-

R

-

I

-

V

F

V

L

S

S

P

N

G

G

P

P

C

G

S

D

P

P

E

A

E

S

A

Y

G

P

I

G

S

V

V

V

A

A

A

T

I

L

K

N

E

R

Y

V

A

L

G

S

K

E

-

P

-

N

-

P

I

R

P

P

L

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

A

L

A

A

F

I

G

G

G

A

K

K

V

T

V

Y

R

K

S

M

V

R

S

Y

L

G

M

N

H

R

G

G

K

H

T

N

S

Q

P

P

I

C

H

-

D

-

G

-

K

-

E

-

L

L

F

L

S

V

G

G

L

T

P

G

N

R

P

C

F

F

N

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

V

V

E

D

R

A

A

D

T

S

L

L

P

P

D

-

C

-

L

-

E

-

M

-

T

A

A

G

W

W

V

T

-

P

-

L

-

F

-

T

-

N

-

A

D

N

N

D

G

C

E

S

I

N

M

E

G

G

L

I

R

V

H

H

R

D

D

S

L

L

P

P

V

F

W

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

R

L

A

T

G

E

P

G

S

G

D

M

M

E

E

L

L

-

F

D

D

N

V

F

F

L

L

K

E

L

T

S

V

R

R

Q

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.

1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
24% identity, 95% coverage: 2:186/195 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

F

Q

N

L

I

V

V

A

Q

R

Y

R

L

V

A

R

Q

E

L

L

G

G

E

V

E

Y

V

C

K

E

V

L

V

W

R

A

N

W

D

D

E

-

I

V

S

T

V

E

A

A

D

Q

I

I

A

R

G

D

L

F

R

N

P

P

D

S

R

G

I

I

V

I

V

L

S

S

P

G

G
|
G

P

P

C

E

S

S

P

T

E

T

E

E

A

E

G

N

I

S

S

P

V

R

A

A

A

P

I

Q

K

Y

E

V

Y

F

A

E

G

A

K

G

I

V

P

P

L

V

L

F

G

G

V

V

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

T

I

M

G

A

A

M

A

Q

F

L

G

G

K

H

V

V

V

E

R

A

S

S

V

N

S

E

L

R

M

E

H

F

G

G

K

Y

T

A

S

Q

P

V

I

E

H

V

D

N

G

D

K

S

E

A

L

L

F

V

S

R

G

G

L

I

P

E

N

D

P

A

F

L

N

T

A

A

T

D

R

G

Y

K

H

P

S

L

L

L

V

D

V

V

-

W

-

M

-

S

-

H

-

G

-

D

E

K

R

V

A

T

T

A

L

I

P

P

D

S

C

D

L

F

E

I

M

T

T

V

A

A

W

S

V

T

D

E

N

S

G

C

E

P

I

F

M

A

G

I

L

M

R

A

H

N

R

E

D

E

L

K

P

R

V

F

W

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

E

R

G

Q

G

G

M

M

E

R

L

M

L

L

D

E

N

R

F

F

L

V

K

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

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)
29% identity, 65% coverage: 45:170/195 of query aligns to 233:355/2224 of P05990

query
sites
P05990

D

D

R

A

I

L

V

F

V

L

S

S

P

N

G

G

P

P

C

G

S

N

P

P

E

E

E

S

A

C

G

D

I

Q

S

I

V

V

A

Q

I

V

K

R

E

K

Y

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

S

L

I

L

G

A

A

K

A

A

F

I

G

G

G

C

K

S

V

T

V

Y

R

K

S

M

V

K

S

Y

L

G

M

N

H

R

G

G

K

H

T

N

S

L

P

P

I

C

H

L

H

H

-

R

-

A

D

T

G

G

K

R

E

C

L

L

F

M

S

T

G

-

L

-

P

-

N

-

P

-

F

-

N

-

A

-

T

S

R

Q

Y

N

H

H

S

G

L

Y

V

A

V

V

E

D

R

L

A

E

T

Q

L

L

P

P

D

D

C

G

L

W

-

S

E

E

M

L

T

F

A

V

W

N

V

A

D

N

N

D

G

G

E

T

I

N

M

E

G

G

L

I

R

V

H

H

R

A

D

S

L

K

P

P

V

Y

W

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

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)
29% identity, 92% coverage: 13:191/195 of query aligns to 238:410/2214 of P07259

query
sites
P07259

F

Y

N

N

I

Q

V

I

Q

R

Y

C

L

F

A

I

Q

K

L

R

G

G

E

V

E

E

V

L

K

K

V

V

R

P

-

W

N

N

D

Y

E

D

I

F

S

T

V

K

A

E

D

D

I

Y

A

D

G

G

L

L

R

-

P

-

D

-

R

-

I

-

V

F

V

I

S

S

P

N

G

G

P

P

C

G

S

D

P

P

-

S

-

V

-

L

E

D

A

L

G

S

I

Q

S

R

V

L

A

S

A

N

I

V

K

L

E

E

Y

-

A

A

G

K

K

K

I

T

P

P

L

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

I

G

A

A

R

A

A

F

A

G

G

G

A

K

S

V

T

V

L

R

K

S

L

V

K

S

F

L

G

M

N

H

R

G

G

K

H

T

N

S

I

P

P

I

C

H

-

D

-

G

-

K

T

E

S

L

T

F

I

S

S

G

G

L

-

P

-

N

R

P

C

F

Y

N

I

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

V

V

E

D

R

V

A

D

T

T

L

L

P

T

D

S

C

G

-

W

-

K

-

P

L

L

E

F

M

V

T

N

A

A

W

N

V

D

D

D

N

S

G

N

E

E

I

-

M

-

G

G

L

I

R

Y

H

H

R

S

D

E

L

L

P

P

V

Y

W

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

I

T

L

P

T

G

E

P

G

R

G

D

M

T

E

E

-

F

L

L

L

F

D

D

N

V

F

F

L

I

K

Q

L

A

S

V

R

K

Q

E

Y

F

Sites not aligning to the query:

1857 modified: Phosphoserine; by PKA

P07258 Carbamoyl phosphate synthase arginine-specific small chain; CPS; CPSase; CPSase-arg; Arginine-specific carbamoyl phosphate synthetase, glutamine chain; Carbamoyl phosphate synthase A; CPS-A; Glutamine-dependent carbamoyl phosphate synthetase; EC 6.3.5.5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 93% coverage: 14:194/195 of query aligns to 196:376/411 of P07258

query
sites
P07258

N

N

I

I

V

I

Q

R

Y

C

L

L

A

V

Q

K

L

R

G

G

E

A

E

N

V

V

K

T

V

V

V

F

R

P

N

Y

D

D

E

-

I

Y

S

R

V

I

A

Q

D

D

I

V

A

A

G

S

L

-

R

E

P

F

D

D

R

G

I

I

V

F

V

L

S

S

P

N

G

G

P

P

C

G

S

N

P

P

E

E

E

L

A

C

G

Q

I

A

S

T

V

I

A

S

A

N

I

V

K

R

E

E

Y

L

A

L

G

N

K

N

-

P

-

V

-

Y

-

D

-

C

I

I

P

P

L

I

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

A

L

A

A

F

S

G

G

G

A

K

S

V

T

V

H

R

K

S

-

V

-

S

-

L

L

M

K

H

Y

G

G

K

N

T

R

S

A

P

-

I

-

H

-

H

H

D

N

G

I

K

P

E

A

L

M

F

D

S

L

G

T

L

T

P

G

N

Q

P

C

F

H

N

I

A

T

T

S

R

Q

Y

N

H
|
H

S

G

L

Y

V

A

V

V

E

D

R

P

A

E

T

T

L

L

P

P

D

K

C

D

L

Q

E

W

M

K

T

P

A

Y

W

F

V

V

-

N

-

L

D

N

N

D

G

K

E

S

I

N

M

E

G

G

L

M

R

I

H

H

R

L

D

Q

L

R

P

P

V

I

W

F

G

S

V

T

Q

Q

F

F

H
|
H

P

P

E

E

S

A

I

-

L

-

T

-

E

K

G

G

-

P

-

L

-

D

-

T

M

A

E

I

L

L

L

F

D

D

N

K

F

F

L

F

K

D

L

N

S

I

R

E

Q

K

Y

Y

P

Q

V

L

Q

Q

C264 (= C79) mutation to D: Abolishes glutamine-dependent CPSase activity.
H307 (= H128) mutation to D: Abolishes glutamine-dependent CPSase activity.
H349 (= H168) mutation to D: Abolishes glutamine-dependent CPSase activity.

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)
29% identity, 91% coverage: 14:190/195 of query aligns to 191:362/2198 of Q18990

query
sites
Q18990

N

N

I

Q

V

I

Q

R

Y

C

L

L

A

A

Q

K

L

R

G

G

E

F

E

R

V

V

K

K

V

V

-

P

R

W

N

N

D

H

E

P

I

I

S

D

V

T

-

E

A

S

D

D

I

Y

A

D

G

G

L

L

R

-

P

-

D

-

R

-

I

-

V

F

V

L

S

S

P

N

G

G

P

P

C

G

S

D

P

P

E

E

E

I

A

C

G

A

I

P

S

L

V

V

A

D

A

R

I

L

K

A

E

K

Y

V

-

I

-

A

A

R

G

G

K

D

I

K

P

P

L

I

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

I

I

L

G

S

A

R

A

A

F

I

G

G

G

A

K

K

V

T

V

Y

R

K

S

L

V

K

S

Y

L

G

M

N

H

R

G

G

K

H

T

N

S

Q

P

P

I

C

H

T

H

H

D

-

G

-

K

-

E

-

L

-

F

-

S

Y

G

A

L

T

P

G

N

R

P

C

F

Y

N

I

A

T

T

S

R

Q

Y

N

H

H

S

G

L

Y

V

A

V

V

E

D

R

P

A

D

T

S

L

L

P

P

-

A

D

D

C

W

L

K

E

A

M

L

T

F

A

T

W

N

V

E

D

N

N

D

G

K

E

T

I

N

M

E

G

G

L

I

R

V

H

H

R

S

D

S

L

K

P

P

V

F

W

F

G

S

V

V

Q

Q

F

F

H

H

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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.

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)
31% identity, 92% coverage: 3:181/195 of query aligns to 434:610/622 of 3r75B

query
sites
3r75B

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C

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binding zinc ion: C512 (= C79), Y552 (≠ P119), 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_012470589.1 NCBI__GCF_000020385.1:WP_012470589.1
MLLMIDNYDSFTFNIVQYLAQLGEEVKVVRNDEISVADIAGLRPDRIVVSPGPCSPEEAG
ISVAAIKEYAGKIPLLGVCLGHQSIGAAFGGKVVRSVSLMHGKTSPIHHDGKELFSGLPN
PFNATRYHSLVVERATLPDCLEMTAWVDNGEIMGLRHRDLPVWGVQFHPESILTEGGMEL
LDNFLKLSRQYPVQL

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