SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_085637398.1 NCBI__GCF_002115805.1:WP_085637398.1 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)
56% identity, 97% coverage: 1:188/193 of query aligns to 1:187/187 of P00903

query
sites
P00903

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C79 (= C80) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H169) mutation to Q: Loss of activity.
E170 (= E171) 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: 2:187/193 of query aligns to 75:265/276 of Q42565

query
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Q42565

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G150 (= G78) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G103) 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)
48% identity, 96% coverage: 3:187/193 of query aligns to 7:189/673 of 8hx8A

query
sites
8hx8A

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binding magnesium ion: I175 (= I173), S177 (= S175)

Sites not aligning to the query:

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

1i7qB Anthranilate synthase from s. Marcescens (see paper)
41% identity, 95% coverage: 2:184/193 of query aligns to 3:184/192 of 1i7qB

query
sites
1i7qB

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active site: G58 (≠ C54), C83 (= C80), L84 (= L81), H169 (= H169), E171 (= E171)
binding glutamic acid: P55 (= P51), G56 (= G52), G58 (≠ C54), C83 (= C80), L84 (= L81), Q87 (= Q84), H132 (= H129), S133 (= S130), L134 (= L131)

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)
41% identity, 95% coverage: 2:184/193 of query aligns to 4:185/193 of P00900

query
sites
P00900

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C84 (= C80) active site, Nucleophile; for GATase activity

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
40% identity, 96% coverage: 3:187/193 of query aligns to 6:146/632 of 8hx9A

query
sites
8hx9A

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binding magnesium ion: S134 (= S175), D135 (≠ E176)

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
31% identity, 96% coverage: 1:185/193 of query aligns to 1:174/183 of 7yc6A

query
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7yc6A

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N

E

P

V

S

K

G

G

I

I

L

I

L

L

S

S

P

G

G

G

P

P

C

-

D

D

P

I

D

E

Q

K

A

A

G

K

I

N

C

C

L

I

P

D

L

I

T

A

L

L

A

N

A

A

A

K

E

-

T

-

G

-

M

L

P

P

L

I

M

L

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

T

L

L

I

G

A

Q

L

A

A

F

Y

G

G

S

E

V

V

V

G

R

R

H

A

S

A

E

-

I

-

V

-

H

-

G

-

K

L

M

T

G

K

L

V

M

Y

H

V

H
x
D

A

K

G

E

K

N

G

P

V

L

F

F

A

K

G

N

L

V

P

P

S

R

P

E

F

F

E

N

A

A

T

W

R

A

Y

S

H

H

S

K

L

D

V
x
E

V

V

D

K

K

K

D

-

T

-

I

V

P

P

N

E

C

G

L

F

E

E

V

I

T

L

A

A

W
x
H

L

S

E

D

D

I

G
x
C

T

Q

V

V

M

E

G

A

L

M

S

K

H

H

R

K

D

T

L

K

P

P

M

I

H

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

S

V

I

A

A

H

S

T

E

E

H

Y

G

G

H

N

A

E

L

I

L

L

K

K

N

N

F

F

binding zinc ion: C76 (= C80), D101 (≠ H110), E123 (≠ V132), E123 (≠ V132), H136 (≠ W147), C140 (≠ G151), C140 (≠ G151), H158 (= H169)

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
32% identity, 91% coverage: 14:189/193 of query aligns to 204:373/382 of P0A6F1

query
sites
P0A6F1

N

N

L

I

V

L

H

R

Y

M

L

L

G

V

E

D

L

R

G

G

T

C

D

R

V

L

K

T

V

I

V

V

R

P

N

A

D

Q

A

T

L

-

T

S

V

A

Q

E

D

D

A

V

M

L

G

K

L

M

N

N

P

P

S

D

G

G

I

I

L

F

L

L

S

S

P

N

G
|
G

P

P

C
x
G

D

D

P

P

D

A

Q

P

A

C

G

D

I

Y

C

A

L

I

P

T

L

A

T

I

L

Q

A

K

A

F

A

L

E

E

T

T

G

D

M

I

P

P

L

V

M

F

G

G

V

I

C

C

L
|
L

G

G

H

H

Q
|
Q

T

L

L

L

G

A

Q

L

A

A

F

S

G

G

G

A

S

K

V

T

V

V

R

-

H

-

S

-

E

-

I

-

V

-

H

-

G

-

K

K

M

M

G

K

L

F

M

G

H

H

A

G

G

G

K

N

G

H

V

P

F

V

A

K

G

D

L

V

P

E

S

K

P

N

F

V

E

V

-

M

-

I

A

T

T

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

V

A

V

V

D

D

K

E

D

A

T

T

I

L

P

P

N

A

C

N

L

L

E

R

V

V

T

T

-

H

A

K

W

S

L

L

E

F

D

D

G

G

T

T

V

L

M

Q

G

G

L

I

S

H

H

R

R

T

D

D

L

K

P

P

M

A

H

F

G

S

V

F

Q

Q

F

G

H

H

P

P

E

E

S

A

I

S

A

P

S

G

E

P

H

H

G

D

H

A

A

A

L

P

L

L

K

F

N

D

F

H

V

F

N

I

E

E

L

L

G241 (= G52) binding L-glutamine
G243 (≠ C54) binding L-glutamine
L270 (= L81) binding L-glutamine
Q273 (= Q84) binding L-glutamine
N311 (≠ Y128) binding L-glutamine
G313 (≠ S130) binding L-glutamine
F314 (≠ L131) 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)
32% identity, 91% coverage: 14:189/193 of query aligns to 203:372/379 of 1ce8B

query
sites
1ce8B

N

N

L

I

V

L

H

R

Y

M

L

L

G

V

E

D

L

R

G

G

T

C

D

R

V

L

K

T

V

I

V

V

R

P

N

A

D

Q

A

T

L

-

T

S

V

A

Q

E

D

D

A

V

M

L

G

K

L

M

N

N

P

P

S

D

G

G

I

I

L

F

L

L

S

S

P

N

G

G

P

P

C

G

D

D

P

P

D

A

Q

P

A

C

G

D

I

Y

C

A

L

I

P

T

L

A

T

I

L

Q

A

K

A

F

A

L

E

E

T

T

G

D

M

I

P

P

L

V

M

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

T

L

L

L

G

A

Q

L

A

A

F

S

G

G

G

A

S

K

V

T

V

V

R

-

H

-

S

-

E

-

I

-

V

-

H

-

G

-

K

K

M

M

G

K

L

F

M

G

H

H

A

G

G

G

K

N

G

H

V

P

F

V

A

K

G

D

L

V

P

E

S

K

P

N

-

V

F

M

E

I

A

T

T

A

R

Q

Y

N

H

H

S

G

L

F

V

A

V

V

D

D

K

E

D

A

T

T

I

L

P

P

N

A

C

N

L

L

E

R

V

V

T

T

-

H

A

K

W

S

L

L

E

F

D

D

G

G

T

T

V

L

M

Q

G

G

L

I

S

H

H

R

R

T

D

D

L

K

P

P

M

A

H

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

I

S

A

P

S

G

E

P

H

H

G

D

H

A

A

A

L

P

L

L

K

F

N

D

F

H

V

F

N

I

E

E

L

L

active site: C268 (= C80), H352 (= H169), E354 (= E171)

Sites not aligning to the query:

binding L-ornithine: 119, 122

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, 92% coverage: 14:190/193 of query aligns to 254:424/430 of Q9LVW7

query
sites
Q9LVW7

N

N

L

I

V

L

H

R

Y

R

L

L

G

S

E

S

L

Y

G

G

T

C

D

Q

V

I

K

T

V

V

R

P

N

S

D

-

A

T

L

F

T

P

V

A

Q

A

D

E

A

A

M

L

G

K

L

M

N

N

P

P

S

D

G

G

I

I

L

L

L

F

S

S

P

N

G

G

P

P

C

G

D

D

P

P

D

S

Q

A

A

V

G

P

I

Y

C

A

L

V

P

E

L

-

T

T

L

V

A

K

A

E

A

L

E

L

T

G

G

K

M

V

P

P

L

V

M

Y

G

G

V

I

C

C

L

M

G

G

H

H

Q

Q

T

L

L

L

G

G

Q

Q

A

A

F

L

G

G

S

K

V

T

V

F

R

-

H

-

S

-

E

-

I

-

V

-

H

-

G

-

K

K

M

M

G

K

L

F

M

G

H

H

A

G

G

G

K

N

-

H

G

P

V

V

F

R

A

N

G

N

L

R

P

T

S

G

P

Q

F

V

E

E

-

I

A

S

T

A

R

Q

Y

N

H

H

S

N

L

Y

V

A

V

V

D

D

K

P

D

A

T

S

I

L

P

P

N

G

C

G

L

V

E

E

V

V

T

T

-

H

A

V

W

N

L

L

E

N

D

D

G

G

T

S

V

C

M

A

G

G

L

L

S

S

H

F

R

P

D

E

L

M

P

N

M

V

H

M

G

S

V

L

Q

Q

F

Y

H

H

P

P

E

E

S

A

I

S

A

P

S

G

E

P

H
|
H

-

D

G

S

H

D

A

N

L

A

L

F

K

R

N

E

F

F

V

I

N

E

E

L

L

M

K

K

H410 (= H177) mutation to Y: In ven6-1; reticulate leaf phenotype.

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
31% identity, 97% coverage: 1:187/193 of query aligns to 1:182/475 of 2ywcA

query
sites
2ywcA

M

M

L

V

L

L

L

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

H

R

Y

R

L

L

G

R

E

E

L

L

G

R

T

A

D

F

V

S

K

L

V

I

V

L

R

P

N

G

D

D

A

A

L

-

T

P

V

L

Q

E

D

E

A

V

M

L

G

K

L

H

N

R

P

P

S

Q

G

A

I

L

L

I

L

L

S

S

P

G

G
|
G

P

P

-
x
R

-

S

-

V

C

F

D

D

P

P

D

D

Q

-

A

A

G

P

I

R

C

P

L

D

P

P

L

R

T

L

L

F

A

S

A

-

E

-

T

S

G

G

M

L

P

P

L

L

M

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

T

L

L

L

G

A

Q

Q

A

E

F

L

G

G

S

R

V

V

V

E

R

R

H

A

S

G

E

R

I

A

V

E

H

Y

G

G

K

K

M

A

G

L

L

L

M

T

H

R

H

H

A

E

G

G

K

P

G

-

V

L

F

F

A

R

G

G

L

L

P

E

S

G

P

E

F

V

E

Q

A

V

T

W

R

M

Y

S

H

H

S

Q

L

D

V

A

V

V

D

T

K

A

D

P

T

-

I

-

P

P

N

P

C

G

L

W

E

R

V

V

T

V

A

A

W

E

L

T

E

E

D

E

G

N

T

P

V

V

M

A

G

A

L

I

S

A

H

S

R

P

D

D

L

G

P

R

M

A

H

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

A

H

S

T

E

P

H

K

G

G

H

M

A

Q

L

I

L

L

K

E

N

N

F

F

V

L

N

E

active site: G51 (= G52), R53 (vs. gap), C78 (= C80), Y79 (≠ L81), H164 (= H169), E166 (= E171)

Sites not aligning to the query:

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

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
31% identity, 91% coverage: 14:189/193 of query aligns to 203:372/379 of 1c3oB

query
sites
1c3oB

N

N

L

I

V

L

H

R

Y

M

L

L

G

V

E

D

L

R

G

G

T

C

D

R

V

L

K

T

V

I

V

V

R

P

N

A

D

Q

A

T

L

-

T

S

V

A

Q

E

D

D

A

V

M

L

G

K

L

M

N

N

P

P

S

D

G

G

I

I

L

F

L

L

S

S

P
x
N

G
|
G

P

P

C
x
G

D

D

P

P

D

A

Q

P

A

C

G

D

I

Y

C

A

L

I

P

T

L

A

T

I

L

Q

A

K

A

F

A

L

E

E

T

T

G

D

M

I

P

P

L

V

M

F

G

G

V

I

C
x
S

L
|
L

G

G

H

H

Q

Q

T

L

L

L

G

A

Q

L

A

A

F

S

G

G

G

A

S

K

V

T

V

V

R

-

H

-

S

-

E

-

I

-

V

-

H

-

G

-

K

K

M

M

G

K

L

F

M

G

H

H

A

G

G

G

K

N

G

H

V

P

F

V

A

K

G

D

L

V

P

E

S

K

P

N

F

V

E

V

-

M

-

I

A

T

T

A

R

Q

Y
x
N

H
|
H

S
x
G

L
x
F

V

A

V

V

D

D

K

E

D

A

T

T

I

L

P

P

N

A

C

N

L

L

E

R

V

V

T

T

-

H

A

K

W

S

L

L

E

F

D

D

G

G

T

T

V

L

M

Q

G

G

L

I

S

H

H

R

R

T

D

D

L

K

P

P

M

A

H

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

I

S

A

P

S

G

E

P

H

H

G

D

H

A

A

A

L

P

L

L

K

F

N

D

F

H

V

F

N

I

E

E

L

L

active site: S268 (≠ C80), H352 (= H169), E354 (= E171)
binding glutamine: N239 (≠ P51), G240 (= G52), G242 (≠ C54), S268 (≠ C80), L269 (= L81), N310 (≠ Y128), H311 (= H129), G312 (≠ S130), F313 (≠ L131)

Sites not aligning to the query:

active site: 201
binding glutamine: 46

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)
31% identity, 92% coverage: 11:188/193 of query aligns to 185:355/2225 of P27708

query
sites
P27708

F

L

T

K

Y

Y

N

N

L

Q

V

I

H

R

Y

C

L

L

G

C

E

Q

L

R

G

G

T

A

D

E

V

V

K

T

V

V

R

P

N

W

D

D

-

H

A

A

L

L

T

D

V

S

Q

Q

D

E

A

Y

M

E

G

G

L

L

N

-

P

-

S

-

G

-

I

-

L

F

L

L

S

S

P

N

G

G

P

P

C

G

D

D

P

P

-

A

D

S

Q

Y

A

P

G

S

I

V

C

V

L

S

P

T

L

L

T

S

L

R

A

V

A

L

A

S

E

E

T

P

G

N

-

P

M

R

P

P

L

V

M

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

T

L

L

L

G

A

Q

L

A

A

F

I

G

G

G

A

S

K

V

T

V

Y

R

K

H

-

S

-

E

-

I

M

V

R

H

Y

G

G

K

N

M

R

G

G

L

-

M

-

H

-

H

H

A

N

G

Q

K

P

G

C

V

L

F

L

A

V

G

G

L

S

P

G

S

R

P

C

F

F

E

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

V

V

D

E

K

T

D

D

T

S

I

L

P

P

-

A

N

D

C

W

L

A

E

P

V

L

T

F

A

T

W

N

L

A

E

N

D

D

G

G

T

S

V

N

M

E

G

G

L

I

S

V

H

H

R

N

D

S

L

L

P

P

M

F

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

Q

A

A

S

G

E

P

H

S

G

D

H

M

A

E

L

L

K

F

N

D

F

I

V

F

N

L

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)
31% identity, 89% coverage: 11:182/193 of query aligns to 185:349/2225 of P08955

query
sites
P08955

F

L

T

K

Y

Y

N

N

L

Q

V

I

H

R

Y

C

L

L

G

C

E

Q

L

L

G

G

T

A

D

E

V

V

K

T

V

V

-

P

R

W

N

N

D

H

A

E

L

L

T

D

V

S

Q

Q

D

K

A

Y

M

-

G

-

L

-

N

-

P

-

S

D

G

G

I

L

L

F

L

L

S

S

P

N

G

G

P

P

C

G

D

D

P

P

-

A

D

S

Q

Y

A

P

G

G

I

V

C

V

L

A

P

T

L

L

T

N

L

R

A

V

A

L

A

S

E

E

T

P

G

N

-

P

M

R

P

P

L

V

M

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

T

L

L

L

G

A

Q

L

A

A

F

I

G

G

G

A

S

K

V

T

V

Y

R

K

H

-

S

-

E

-

I

M

V

R

H

Y

G

G

K

N

M

R

G

G

L

-

M

-

H

-

H

H

A

N

G

Q

K

P

G

C

V

L

F

L

A

V

G

G

L

T

P

G

S

R

P

C

F

F

E

L

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

V

V

D

D

K

A

D

D

T

S

I

L

P

P

N

-

C

-

L

-

E

-

V

-

T

A

A

G

W

W

L

T

-

P

-

L

-

F

-

T

-

N

-

A

E

N

D

D

G

C

T

S

V

N

M

E

G

G

L

I

S

V

H

H

R

D

D

S

L

L

P

P

M

F

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

R

A

A

S

G

E

P

H

S

G

D

H

M

A

E

L

L

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)
32% identity, 83% coverage: 14:174/193 of query aligns to 191:344/2198 of Q18990

query
sites
Q18990

N

N

L

Q

V

I

H

R

Y

C

L

L

G

A

E

K

L

R

G

G

T

F

D

R

V

V

K

K

V

V

-

P

R

W

N

N

D

H

A

P

L

I

T

D

V

T

Q

E

D

S

A

-

M

-

G

-

L

-

N

D

P

Y

S

D

G

G

I

L

L

F

L

L

S

S

P

N

G

G

P

P

C

G

D

D

P

P

D

E

Q

-

A

-

G

-

I

I

C

C

L

A

P

P

L

L

T

V

-

D

-

R

L

L

A

A

A

K

-

V

-

I

A

A

E

R

T

G

G

D

M

K

P

P

L

I

M

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

T

I

L

L

G

S

Q

R

A

A

F

I

G

G

G

A

S

K

V

T

V

Y

R

K

H

-

S

-

E

-

I

L

V

K

H

Y

G

G

K

N

M

R

G

G

L

-

M

-

H

-

H

H

A

N

G

Q

K

P

G

C

V

T

F

H

A

Y

G

A

L

T

P

G

S

R

P

C

F

Y

E

I

A

T

T

S

R

Q

Y

N

H

H

S

G

L

Y

V

A

V

V

D

D

K

P

D

D

T

S

I

L

P

P

N

A

C

D

L

W

E

K

V

A

T

L

A

F

W

T

L

N

E

E

-

N

D

D

G

K

T

T

V

N

M

E

G

G

L

I

S

V

H

H

R

S

D

S

L

K

P

P

M

F

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

T

A

A

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.

1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
28% identity, 97% coverage: 2:189/193 of query aligns to 8:199/501 of 1gpmA

query
sites
1gpmA

L

I

L

L

L

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

H

R

Y

R

L

V

G

R

E

E

L

L

G

G

T

V

D

Y

V

C

K

E

V

L

V

W

R

A

N

W

D

D

A

V

L

T

T

E

V

A

Q

Q

D

-

A

I

M

R

G

D

L

F

N

N

P

P

S

S

G

G

I

I

L

I

L

L

S

S

P

G

G
|
G

P

P

-

E

C

S

D

T

P

T

D

E

Q

E

A

N

G

S

I

P

C

R

L

A

P

P

L

Q

T

Y

L

V

A

F

A

-

E

E

T

A

G

G

M

V

P

P

L

V

M

F

G

G

V

V

C
|
C

L
x
Y

G

G

H

M

Q

Q

T

T

L

M

G

A

Q

M

A

Q

F

L

G

G

S

H

V

V

V

E

R

A

H

S

S

N

E

E

I

R

V

E

H

F

G

G

K

Y

M

A

G

Q

L

V

M

E

H

V

A

N

G

D

K

S

G

A

V

L

F

V

A

R

G

G

L

I

P

E

S

D

P

A

F

L

E

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

D

K

K

D

V

T

T

-

A

I

I

P

P

N

S

C

D

L

F

E

I

V

T

T

V

A

A

W

S

L

T

E

E

D

S

G

C

T

P

V

F

M

A

G

I

L

M

S

A

H

N

R

E

D

E

L

K

P

R

M

F

H

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

A

H

S

T

E

R

H

Q

G

G

H

M

A

R

L

M

L

L

K

E

N

R

F

F

V

V

N

R

E

D

L

I

active site: G57 (= G52), C84 (= C80), Y85 (≠ L81), H179 (= H169), E181 (= E171)

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

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)
32% identity, 83% coverage: 13:172/193 of query aligns to 238:389/2214 of P07259

query
sites
P07259

Y

Y

N

N

L

Q

V

I

H

R

Y

C

L

F

G

I

E

K

L

R

G

G

T

V

D

E

V

L

K

K

V

V

R

P

-

W

N

N

D

Y

A

D

L

F

T

T

V

K

Q

E

D

D

A

Y

M

-

G

-

L

-

N

-

P

-

S

D

G

G

I

L

L

F

L

I

S

S

P

N

G

G

P

P

C

G

D

D

P

P

-

S

-

V

-

L

D

D

Q

D

A

L

G

S

I

Q

C

R

L

L

P

S

L

N

T

V

L

L

A

E

A

A

A

K

E

K

T

T

G

-

M

-

P

P

L

V

M

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

T

L

L

I

G

A

Q

R

A

A

F

A

G

G

G

A

S

S

V

T

V

L

R

K

H

L

S

-

E

-

I

-

V

-

H

-

G

-

K

K

M

F

G

G

L

N

M

R

H

G

H

H

A

N

G

I

K

P

G

C

V

T

F

S

A

T

G

I

L

S

P

G

S

R

P

C

F

Y

E

I

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

A

V

V

D

D

K

V

D

D

T

T

I

L

P

T

N

S

C

G

-

W

-

K

-

P

L

L

E

F

V

V

T

N

A

A

W

-

L

-

E

N

D

D

G

D

T

S

V

N

M

E

G

G

L

I

S

Y

H

H

R

S

D

E

L

L

P

P

M

Y

H

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

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
30% identity, 61% coverage: 73:189/193 of query aligns to 97:210/693 of P49915

query
sites
P49915

G

G

M

K

P

P

L

V

M

L

G

G

V

I

C
|
C

L

Y

G

G

H

M

Q

Q

T

M

L

M

G

N

Q

K

A

V

F

F

G

G

S

T

V

V

V

H

R

K

H

K

S

S

E

V

I

R

V

E

H

D

G

G

K

V

M

F

G

N

L

I

M

S

H

V

H

D

A

N

G

T

K

C

G

S

V

L

F

F

A

R

G

G

L

L

P

Q

S

K

P

E

F

E

E

V

A

V

T

L

R

L

Y

T

H

H

S

G

L

D

V

S

V

V

D

D

K

K

D

-

T

-

I

V

P

A

N

D

C

G

L

F

E

K

V

V

T

V

A

A

W

-

L

R

E

S

D

G

G

N

T

I

V

V

M

A

G

G

L

I

S

A

H

N

R

E

D

S

L

K

P

K

M

L

H

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

A

L

S

T

E

E

H

N

G

G

H

K

A

V

L

I

L

L

K

K

N

N

F

F

V

L

N

Y

E

D

L

I

C104 (= C80) active site, For GATase activity
H190 (= H169) active site, For GATase activity
E192 (= E171) 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)
30% identity, 61% coverage: 73:189/193 of query aligns to 75:185/658 of 2vxoB

query
sites
2vxoB

G

G

M

K

P

P

L

V

M

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

T

M

L

M

G

N

Q

K

A

V

F

F

G

G

S

T

V

V

V

H

R

K

H

K

S

S

E

D

I

-

V

-

H

-

G

G

K

V

M

F

G

N

L

I

M

S

H

V

H

D

A

N

G

T

K

C

G

S

V

L

F

F

A

R

G

G

L

L

P

Q

S

K

P

E

F

E

E

V

A

V

T

L

R

L

Y

T

H

H

S

G

L

D

V

S

V

V

D

D

K

K

D

-

T

-

I

V

P

A

N

D

C

G

L

F

E

K

V

V

T

V

A

A

W

-

L

R

E

S

D

G

G

N

T

I

V

V

M

A

G

G

L

I

S

A

H

N

R

E

D

S

L

K

P

K

M

L

H

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

A

L

S

T

E

E

H

N

G

G

H

K

A

V

L

I

L

L

K

K

N

N

F

F

V

L

N

Y

E

D

L

I

active site: C82 (= C80), Y83 (≠ L81), H165 (= H169), E167 (= E171)

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

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)
26% identity, 91% coverage: 14:189/193 of query aligns to 207:382/2225 of P20054

query
sites
P20054

N

N

L

Q

V

I

H

R

Y

C

L

L

G

L

E

N

L

R

G

G

T

V

D

D

V

L

K

K

V

V

R

P

N

W

D

D

A

Y

L

D

T

V

V

V

Q

A

D

N

A

E

M

S

G

I

L

N

N

D

P

Y

S

D

G

G

I

V

L

F

L

I

S

S

P

N

G

G

P

P

C

G

D

D

P

P

D

S

Q

L

A

C

G

G

I

K

C

A

L

I

P

E

-

N

-

I

L

R

T

K

L

V

A

L

A

A

A

L

E

P

T

V

G

A

M

K

P

A

L

V

M

F

G

G

V

V

C

C

L

M

G

G

H

N

Q

Q

T

L

L

L

G

G

Q

L

A

A

F

A

G

G

G

A

S

Q

V

T

V

-

R

-

H

-

S

H

E

K

I

M

V

A

H

F

G

G

K

N

M

R

G

G

L

L

M

N

H

Q

H

P

A

C

G

V

K

D

G

Q

V

I

F

S

A

G

G

R

L

C

P

-

S

-

P

-

F

H

E

I

A

T

T

S

R

Q

Y

N

H

H

S

G

L

F

V

V

V

I

D

D

K

S

D

N

T

S

I

L

P

P

N

A

C

G

L

-

E

-

V

-

T

S

A

G

W

W

-

K

-

T

-

Y

-

F

-

I

-

N

L

A

E

N

D

D

G

A

T

S

V

N

M

E

G

G

L

I

S

Y

H

H

R

E

D

S

L

K

P

P

M

W

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

A

I

M

A

A

S

G

-

P

E

T

H

D

G

T

H

E

A

Y

L

L

L

F

K

D

N

N

F

F

V

V

N

D

E

N

L

V

Sites not aligning to the query:

1 modified: N-acetylmethionine

Query Sequence

>WP_085637398.1 NCBI__GCF_002115805.1:WP_085637398.1
MLLLIDNYDSFTYNLVHYLGELGTDVKVVRNDALTVQDAMGLNPSGILLSPGPCDPDQAG
ICLPLTLAAAETGMPLMGVCLGHQTLGQAFGGSVVRHSEIVHGKMGLMHHAGKGVFAGLP
SPFEATRYHSLVVDKDTIPNCLEVTAWLEDGTVMGLSHRDLPMHGVQFHPESIASEHGHA
LLKNFVNELKVPA

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