SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_084236418.1 NCBI__GCF_001592305.1:WP_084236418.1 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)
59% identity, 96% coverage: 7:196/197 of query aligns to 2:187/187 of P00903

query
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P00903

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C79 (= C88) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H177) mutation to Q: Loss of activity.
E170 (= E179) 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)
48% identity, 96% coverage: 7:195/197 of query aligns to 75:265/276 of Q42565

query
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Q42565

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G150 (= G86) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G111) 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)
45% identity, 99% coverage: 3:197/197 of query aligns to 2:191/673 of 8hx8A

query
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8hx8A

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binding magnesium ion: I175 (= I181), S177 (≠ T183)

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: 7:197/197 of query aligns to 4:190/193 of P00900

query
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P00900

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C84 (= C88) 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: 7:197/197 of query aligns to 3:189/192 of 1i7qB

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1i7qB

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active site: G58 (≠ C63), C83 (= C88), L84 (= L89), H169 (= H177), E171 (= E179)
binding glutamic acid: P55 (= P60), G56 (= G61), G58 (≠ C63), C83 (= C88), L84 (= L89), Q87 (= Q92), H132 (= H137), S133 (= S138), L134 (= L139)

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
35% identity, 99% coverage: 3:197/197 of query aligns to 1:148/632 of 8hx9A

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8hx9A

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binding magnesium ion: S134 (≠ T183), D135 (≠ E184)

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
32% identity, 95% coverage: 7:193/197 of query aligns to 2:174/183 of 7yc6A

query
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7yc6A

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D

D

N

N

Y

G

D

G

S

Q

F

Y

T

V

Y

H

N

R

I

I

V

H

Q

R

Y

S

F

L

G

K

E

Y

L

I

G

G

A

V

D

S

V

S

T

K

V

I

V

V

R

P

N

N

D

T

E

-

I

T

T

P

V

L

D

E

E

E

I

I

Q

E

R

S

R

N

V

-

D

-

A

-

G

K

Q

E

I

V

D

K

R

G

L

I

V

I

I

L

S

S

P

G

G

G

P

P

-

D

C

I

S

E

P

K

A

A

E

K

A

N

G

C

I

I

S

D

V

I

P

A

A

-

I

-

Q

-

H

-

F

L

A

N

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

A

L

A

A

F

Y

G

G

K

E

I

V

I

G

R

R

A

A

Q

-

E

-

L

-

M

-

H

-

G

A

K

L

T

T

S

K

V

V

I

Y

T

V

T
x
D

T

K

Q

E

E

N

G

P

V

L

F

F

A

K

G

N

L

V

P

P

K

R

Q

E

F

F

T

-

V

-

N

N

R

A

Y

W

H

A

S

S

L

H

A

K

I

D

E
|
E

R

V

E

K

T

K

C

V

P

P

D

E

C

G

L

F

K

E

V

I

T

L

A

A

W
x
H

T

S

D

D

D

I

G
x
C

E

Q

I

V

M

E

G

A

V

M

K

K

H

H

K

K

T

T

L

K

P

P

I

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

E

E

H

Y

G

G

H

N

A

E

M

I

L

L

K

K

N

N

F

F

binding zinc ion: C76 (= C88), D101 (≠ T118), E123 (= E142), E123 (= E142), H136 (≠ W155), C140 (≠ G159), C140 (≠ G159), H158 (= H177)

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
29% identity, 97% coverage: 7:197/197 of query aligns to 2:184/475 of 2ywcA

query
sites
2ywcA

L

V

L

L

M

V

V

L

D

D

N

F

Y

G

D

S

S

Q

F

Y

T

T

Y

R

N

L

I

I

V

A

Q

R

Y

R

F

L

G

R

E

E

L

L

G

R

A

A

D

F

V

S

T

L

V

I

V

L

R

P

N

G

D

D

E

A

I

P

T

L

V

E

D

E

E

V

I

L

Q

K

R

H

R

R

V

P

D

Q

A

A

G

-

Q

-

I

-

D

-

R

-

L

L

V

I

I

L

S

S

P

G

G
|
G

P

P

C
x
R

S

S

P

V

A

F

E

D

A

P

G

D

I

A

S

P

V

R

P

P

A

D

I

P

Q

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

A

Q

A

E

F

L

G

G

K

R

I

V

I

E

R

R

A

A

Q

G

E

R

L

A

M

E

H

Y

G

G

K

K

T

-

S

A

V

L

I

L

T

T

T

R

T

H

Q

E

E

G

G

P

V

L

F

F

A

R

G

G

L

L

P

E

K

G

Q

E

F

V

T

Q

V

V

N

W

R

M

Y

S

H

H

S

Q

L

D

A

A

I

V

E

-

R

-

E

T

T

A

C

P

P

P

D

P

C

G

L

W

K

R

V

V

T

V

A

A

W

E

T

T

D

E

G

N

E

P

I

V

M

A

G

A

V

I

K

A

H

S

K

P

T

D

L

G

P

R

I

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

E

P

H

K

G

G

H

M

A

Q

M

I

L

L

K

E

N

N

F

F

L

L

E

E

Q

L

A

A

active site: G51 (= G61), R53 (≠ C63), C78 (= C88), Y79 (≠ L89), H164 (= H177), E166 (= E179)

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)
29% identity, 83% coverage: 16:179/197 of query aligns to 185:338/2225 of P27708

query
sites
P27708

F

L

T

K

Y

Y

N

N

I

Q

V

I

Q

R

Y

C

F

L

G

C

E

Q

L

R

G

G

A

A

D

E

V

V

T

T

V

V

R

P

N

W

D

D

E

H

I

A

T

-

V

-

D

-

E

-

I

-

Q

-

R

-

V

L

D

D

A

S

G

Q

Q

E

I

Y

D

E

R

G

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

S

D

P

P

A

A

E

S

A

Y

G

P

I

S

S

V

V

V

P

S

A

T

I

L

Q

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

A

L

A

A

F

I

G

G

G

A

K

K

I

T

I

Y

R

K

A

M

Q

R

E

Y

L

G

M

N

H

R

G

G

K

H

T

N

S

-

V

-

I

-

T

-

Q

Q

E

P

G

C

V

L

F

L

A

V

G

G

L

S

P

G

K

R

Q

C

F

F

T

L

V

T

N

S

R

Q

Y

N

H

H

S

G

L

F

A

A

I

V

E

E

R

T

E

D

T

S

C

L

P

P

-

A

D

D

C

W

L

A

K

P

V

L

T

F

A

T

W

N

T

A

D

N

D

D

G

G

E

S

I

N

M

E

G

G

V

I

K

V

H

H

K

N

T

S

L

L

P

P

I

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

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)
24% identity, 90% coverage: 19:195/197 of query aligns to 254:421/430 of Q9LVW7

query
sites
Q9LVW7

N

N

I

I

V

L

Q

R

Y

R

F

L

G

S

E

S

L

Y

G

G

A

C

D

Q

V

I

T

T

V

V

R

P

N

S

D

T

E

F

I

P

T

A

V

A

D

E

E

A

I

L

Q

K

R

M

R

N

V

P

D

D

A

G

G

-

Q

-

I

-

D

-

R

-

L

I

V

L

I

F

S

S

P

N

G

G

P

P

C

G

S

D

P

P

A

S

E

A

A

V

G

P

I

Y

S

A

V

V

P

E

A

T

I

V

Q

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

A

Q

A

A

F

L

G

G

K

K

I

T

I

F

R

K

A

M

Q

K

E

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

V

P

I

V

T

R

T

N

Q

R

E

T

G

G

V

-

F

-

A

-

G

-

L

-

P

-

K

-

Q

Q

F

V

T

E

V

I

N

S

-

A

R

Q

Y

N

H

H

S

N

L

Y

A

A

I

V

E

D

R

P

E

A

T

S

C

L

P

P

D

G

C

G

L

V

K

E

V

V

T

T

A

H

W

V

T

N

-

L

D

N

D

D

G

G

E

S

I

C

M

A

G

G

V

L

K

S

H

F

K

P

T

E

L

M

P

N

I

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

E

P

H
|
H

-

D

G

S

H

D

A

N

M

A

L

F

K

R

N

E

F

F

L

I

E

E

H410 (= H185) mutation to Y: In ven6-1; reticulate leaf phenotype.

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)
28% identity, 83% coverage: 16:179/197 of query aligns to 185:338/2225 of P08955

query
sites
P08955

F

L

T

K

Y

Y

N

N

I

Q

V

I

Q

R

Y

C

F

L

G

C

E

Q

L

L

G

G

A

A

D

E

V

V

T

T

V

V

R

-

N

-

D

-

E

-

I

-

T

-

V

-

D

-

E

P

I

W

Q

N

R

H

R

E

V

L

D

D

A

S

G

Q

Q

K

I

Y

D

D

R

G

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

S

D

P

P

A

A

E

S

A

Y

G

P

I

G

S

V

V

V

P

A

A

T

I

L

Q

N

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

A

L

A

A

F

I

G

G

G

A

K

K

I

T

I

Y

R

K

A

M

Q

R

E

Y

L

G

M

N

H

R

G

G

K

H

T

-

S

-

V

-

I

-

T

-

T

N

Q

Q

E

P

G

C

V

L

F

L

A

V

G

G

L

T

P

G

K

R

Q

C

F

F

T

L

V

T

N

S

R

Q

Y

N

H

H

S

G

L

F

A

A

I

V

E

D

R

A

E

D

T

S

C

L

P

P

D

-

C

-

L

-

K

-

V

-

T

A

A

G

W

W

T

T

-

P

-

L

-

F

-

T

-

N

-

A

D

N

D

D

G

C

E

S

I

N

M

E

G

G

V

I

K

V

H

H

K

D

T

S

L

L

P

P

I

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.

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
27% identity, 90% coverage: 19:195/197 of query aligns to 203:371/379 of 1ce8B

query
sites
1ce8B

N

N

I

I

V

L

Q

R

Y

M

F

L

G

V

E

D

L

R

G

G

A

C

D

R

V

L

T

T

V

I

V

V

R

P

N

A

D

Q

E

T

I

S

T

A

V

E

D

D

E

V

I

L

Q

K

R

M

R

N

V

P

D

D

A

G

G

-

Q

-

I

-

D

-

R

-

L

I

V

F

I

L

S

S

P

N

G

G

P

P

C

G

S

D

P

P

A

A

E

P

A

C

G

D

I

Y

S

A

V

I

P

T

A

A

I

I

Q

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

A

L

A

A

F

S

G

G

G

A

K

K

I

T

I

V

R

K

A

M

Q

K

E

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

V

P

I

V

T

K

T

D

T

V

Q

E

E

K

G

N

V

V

F

V

A

-

G

-

L

-

P

-

K

-

Q

-

F

M

T

I

V

T

N

A

R

Q

Y

N

H

H

S

G

L

F

A

A

I

V

E

D

R

E

E

A

T

T

C

L

P

P

D

A

C

N

L

L

K

R

V

V

T

T

A

H

W

K

T

S

-

L

D

F

D

D

G

G

E

T

I

L

M

Q

G

G

V

I

K

H

H

R

K

T

T

D

L

K

P

P

I

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

I

S

L

P

T

G

E

P

H

H

G

D

H

A

A

A

-

P

M

L

L

F

K

D

N

H

F

F

L

I

E

E

active site: C268 (= C88), H352 (= H177), E354 (= E179)

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)
27% identity, 90% coverage: 19:195/197 of query aligns to 204:372/382 of P0A6F1

query
sites
P0A6F1

N

N

I

I

V

L

Q

R

Y

M

F

L

G

V

E

D

L

R

G

G

A

C

D

R

V

L

T

T

V

I

V

V

R

P

N

A

D

Q

E

T

I

S

T

A

V

E

D

D

E

V

I

L

Q

K

R

M

R

N

V

P

D

D

A

G

G

-

Q

-

I

-

D

-

R

-

L

I

V

F

I

L

S

S

P

N

G
|
G

P

P

C
x
G

S

D

P

P

A

A

E

P

A

C

G

D

I

Y

S

A

V

I

P

T

A

A

I

I

Q

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

A

L

A

A

F

S

G

G

G

A

K

K

I

T

I

V

R

K

A

M

Q

K

E

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

V

P

I

V

T

K

T

D

T

V

Q

E

E

K

G

N

V

V

F

V

A

-

G

-

L

-

P

-

K

-

Q

-

F

M

T

I

V

T

N

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

A

A

I

V

E

D

R

E

E

A

T

T

C

L

P

P

D

A

C

N

L

L

K

R

V

V

T

T

A

H

W

K

T

S

-

L

D

F

D

D

G

G

E

T

I

L

M

Q

G

G

V

I

K

H

H

R

K

T

T

D

L

K

P

P

I

A

E

F

G

S

V

F

Q

Q

F

G

H

H

P

P

E

E

S

A

I

S

L

P

T

G

E

P

H

H

G

D

H

A

A

A

-

P

M

L

L

F

K

D

N

H

F

F

L

I

E

E

G241 (= G61) binding L-glutamine
G243 (≠ C63) binding L-glutamine
L270 (= L89) binding L-glutamine
Q273 (= Q92) binding L-glutamine
N311 (≠ Y136) binding L-glutamine
G313 (≠ S138) binding L-glutamine
F314 (≠ L139) binding L-glutamine

Sites not aligning to the query:

47 binding L-glutamine

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
33% identity, 71% coverage: 56:194/197 of query aligns to 72:207/693 of P49915

query
sites
P49915

L

I

V

I

I

I

S

S

P

G

G

G

P

P

C

N

S

S

-

V

-

Y

P

A

A

E

E

D

A

A

G

P

I

W

S

F

V

D

P

P

A

A

I

I

Q

-

H

-

F

F

A

T

G

I

K

G

L

K

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

A

K

A

V

F

F

G

G

K

T

I

V

I

H

R

K

A

K

Q

S

E

V

L

R

M

E

H

D

G

G

K

V

T

F

S

N

V

I

I

S

T

V

T

D

T

N

Q

T

E

C

G

S

V

L

F

F

A

R

G

G

L

L

P

Q

K

K

Q

E

F

E

T

V

V

V

N

L

R

L

Y

T

H

H

S

G

L

D

A

S

I

V

E

D

R

K

E

-

T

-

C

V

P

A

D

D

C

G

L

F

K

K

V

V

T

V

A

A

W

R

T

S

D

G

D

N

G

-

E

I

I

V

M

A

G

G

V

I

K

A

H

N

K

E

T

S

L

K

P

K

I

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

E

E

H

N

G

G

H

K

A

V

M

I

L

L

K

K

N

N

F

F

L

L

C104 (= C88) active site, For GATase activity
H190 (= H177) active site, For GATase activity
E192 (= E179) 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

2vxoB Human gmp synthetase in complex with xmp (see paper)
33% identity, 71% coverage: 56:194/197 of query aligns to 50:182/658 of 2vxoB

query
sites
2vxoB

L

I

V

I

I

I

S

S

P

G

G
|
G

P

P

C

N

S

S

-

V

-

Y

P

A

A

E

E

D

A

A

G

P

I

W

S

F

V

D

P

P

A

A

I

I

Q

-

H

-

F

F

A

T

G

I

K

G

L

K

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

A

K

A

V

F

F

G

G

K

T

I

V

I

H

R

K

A

K

Q

S

E

D

L

-

M

-

H

-

G

G

K

V

T

F

S

N

V

I

I

S

T

V

T

D

T

N

Q

T

E

C

G

S

V

L

F

F

A

R

G

G

L

L

P

Q

K

K

Q

E

F

E

T

V

V

V

N

L

R

L

Y

T

H

H

S

G

L

D

A

S

I

V

E

D

R

K

E

-

T

-

C

V

P

A

D

D

C

G

L

F

K

K

V

V

T

V

A

A

W

R

T

S

D

G

D

N

G

-

E

I

I

V

M

A

G

G

V

I

K

A

H

N

K

E

T

S

L

K

P

K

I

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

E

E

H

N

G

G

H

K

A

V

M

I

L

L

K

K

N

N

F

F

L

L

active site: G55 (= G61), C82 (= C88), Y83 (≠ L89), H165 (= H177), E167 (= E179)

Sites not aligning to the query:

active site: 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)
26% identity, 90% coverage: 19:195/197 of query aligns to 203:371/379 of 1c3oB

query
sites
1c3oB

N

N

I

I

V

L

Q

R

Y

M

F

L

G

V

E

D

L

R

G

G

A

C

D

R

V

L

T

T

V

I

V

V

R

P

N

A

D

Q

E

T

I

S

T

A

V

E

D

D

E

V

I

L

Q

K

R

M

R

N

V

P

D

D

A

G

G

-

Q

-

I

-

D

-

R

-

L

I

V

F

I

L

S

S

P
x
N

G
|
G

P

P

C
x
G

S

D

P

P

A

A

E

P

A

C

G

D

I

Y

S

A

V

I

P

T

A

A

I

I

Q

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

A

L

A

A

F

S

G

G

G

A

K

K

I

T

I

V

R

K

A

M

Q

K

E

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

V

P

I

V

T

K

T

D

T

V

Q

E

E

K

G

N

V

V

F

V

A

-

G

-

L

-

P

-

K

-

Q

-

F

M

T

I

V

T

N

A

R

Q

Y
x
N

H
|
H

S
x
G

L
x
F

A

A

I

V

E

D

R

E

E

A

T

T

C

L

P

P

D

A

C

N

L

L

K

R

V

V

T

T

A

H

W

K

T

S

-

L

D

F

D

D

G

G

E

T

I

L

M

Q

G

G

V

I

K

H

H

R

K

T

T

D

L

K

P

P

I

A

E

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

I

S

L

P

T

G

E

P

H

H

G

D

H

A

A

A

-

P

M

L

L

F

K

D

N

H

F

F

L

I

E

E

active site: S268 (≠ C88), H352 (= H177), E354 (= E179)
binding glutamine: N239 (≠ P60), G240 (= G61), G242 (≠ C63), S268 (≠ C88), L269 (= L89), N310 (≠ Y136), H311 (= H137), G312 (≠ S138), F313 (≠ L139)

Sites not aligning to the query:

active site: 201
binding glutamine: 46

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, 90% coverage: 3:180/197 of query aligns to 225:389/2214 of P07259

query
sites
P07259

K

K

K

V

I

L

Q

R

L

I

L

L

M

A

V

I

D

D

N

V

Y

-

D

-

S

G

F

M

T

K

Y

Y

N

N

I

Q

V

I

Q

R

Y

C

F

F

G

I

E

K

L

R

G

G

A

V

D

E

V

L

T

K

V

V

-

P

R

W

N

N

D

Y

E

D

I

F

T

T

V

K

D

E

E

D

I

Y

Q

-

R

-

V

-

D

-

A

-

G

-

Q

-

I

-

D

D

R

G

L

L

V

F

I

I

S

S

P

N

G

G

P

P

C

G

S

D

P

P

A

S

E

V

A

L

G

D

I

D

S

L

V

S

P

Q

A

R

I

L

Q

S

H

N

F

V

-

L

-

E

A

A

G

K

K

K

L

T

P

P

I

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

I

T

I

L

R

K

A

L

Q

K

E

F

L

G

M

N

H

R

G

G

K

H

T

N

S

I

V

P

I

C

T

T

T

S

T

T

Q

I

E

S

G

G

V

-

F

-

A

-

G

-

L

-

P

-

K

R

Q

C

F

Y

T

I

V

T

N

S

R

Q

Y

N

H

H

S

G

L

F

A

A

I

V

E

D

R

V

E

D

T

T

C

L

P

T

D

S

C

G

L

W

K

K

-

P

-

L

-

F

V

V

T

N

A

A

W

N

T

D

D

D

D

S

G

N

E

E

I

-

M

-

G

G

V

I

K

Y

H

H

K

S

T

E

L

L

P

P

I

Y

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

Sites not aligning to the query:

1857 modified: Phosphoserine; by PKA

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)
26% identity, 74% coverage: 35:179/197 of query aligns to 214:355/2224 of P05990

query
sites
P05990

R

R

N

G

D

A

E

S

I

V

T

T

V

L

D

L

E

P

I

W

Q

S

R

A

R

R

V

L

D

E

A

D

G

E

Q

Q

I

F

D

D

R

A

L

L

V

F

I

L

S

S

P

N

G

G

P

P

C

G

S

N

P

P

A

E

E

S

A

C

G

D

I

Q

S

I

V

V

P

Q

A

Q

I

V

Q

R

H

K

F

V

-

I

-

E

A

E

G

G

K

Q

L

K

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

A

K

A

A

F

I

G

G

G

C

K

S

I

T

I

Y

R

K

A

M

Q

K

E

Y

L

G

M

N

H

R

G

G

K

H

T

N

S

L

V

P

I

C

T

L

T

H

T

R

Q

A

E

T

G

G

V

-

F

-

A

-

G

-

L

-

P

-

K

R

Q

C

F

L

T

M

V

T

N

S

R

Q

Y

N

H

H

S

G

L

Y

A

A

I

V

E

D

R

L

E

E

T

Q

C

L

P

P

D

D

C

-

L

-

K

-

V

-

T

-

A

G

W

W

T

S

-

E

-

L

-

F

-

V

-

N

-

A

D

N

D

D

G

G

E

T

I

N

M

E

G

G

V

I

K

V

H

H

K

A

T

S

L

K

P

P

I

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, 97% coverage: 6:197/197 of query aligns to 432:617/622 of 3r75B

query
sites
3r75B

Q

R

L

A

L

L

M

I

V

V

D

D

N

A

Y

E

D

D

S

H

F

F

T

T

Y

A

N

M

I

I

V

A

Q

Q

Y

Q

F

L

G

S

E

S

L

L

G

G

A

L

D

A

V

T

T

E

V

V

V

C

R

-

N

-

D

-

E

-

I

-

T

-

V

-

D

-

E

G

I

V

Q

H

R

D

R

A

V

V

D

D

A

L

G

A

Q

R

I

Y

D

D

R

V

L

V

V

V

I

M

S

G

P

P

G

G

P

P

C

G

S

D

P

P

A

S

E

D

A

A

G

G

I

D

S

-

V

-

P

P

A

R

I

I

Q

A

H

R

F

L

A

Y

G

A

K

W

L

L

-

R

-

H

-

L

-

I

-

D

-

E

-

G

-

K

P

P

I

F

L

M

G

A

V

V

C
|
C

L

L

G

S

H

H

Q

Q

S

I

I

L

G

N

A

A

A

I

F

L

G

G

G

I

K

P

I

L

I

V

R

R

A

R

Q

E

E

V

L

P

M

N

H

Q

G

G

K

I

T

Q

S

V

V

E

I

I

T

D

T

-

Q

-

E

-

G

-

V

L

F

F

A

G

G

Q

L

R

P

E

K

R

Q

V

F

G

T

F

V
x
Y

N

N

R

T

Y

Y

H

V

S

A

L

Q

A

T

I

V

E

R

R

D

E

E

T

M

C

D

P

V

D

D

C

G

L

V

K

G

V

T

T

V

A

A

W

I

T

S

D

R

D

D

-

P

-

R

-

T

G

G

E

E

I

V

M

H

G

A

V

L

K

R

H

G

K

P

T

T

L

F

P

-

I

-

E

S

G

S

V

M

Q

Q

F

F

H
|
H

P

A

E

E

S

S

I

V

L

L

T

T

E

V

H

D

G

G

H

P

A

R

M

I

L

L

K

G

N

E

F

A

L

I

E

T

Q

H

A

A

binding zinc ion: C512 (= C88), Y552 (≠ V133), H597 (= H177)

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

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, 64% coverage: 54:179/197 of query aligns to 219:341/2198 of Q18990

query
sites
Q18990

D

D

R

G

L

L

V

F

I

L

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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.

Query Sequence

>WP_084236418.1 NCBI__GCF_001592305.1:WP_084236418.1
MTKKIQLLMVDNYDSFTYNIVQYFGELGADVTVVRNDEITVDEIQRRVDAGQIDRLVISP
GPCSPAEAGISVPAIQHFAGKLPILGVCLGHQSIGAAFGGKIIRAQELMHGKTSVITTTQ
EGVFAGLPKQFTVNRYHSLAIERETCPDCLKVTAWTDDGEIMGVKHKTLPIEGVQFHPES
ILTEHGHAMLKNFLEQA

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