SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_018123678.1 NCBI__GCF_000375485.1:WP_018123678.1 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)
51% identity, 98% coverage: 1:186/190 of query aligns to 1:186/187 of P00903

query
sites
P00903

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C79 (= C80) 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)
40% identity, 98% coverage: 2:187/190 of query aligns to 75:266/276 of Q42565

query
sites
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.

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)
39% identity, 97% coverage: 2:185/190 of query aligns to 4:187/193 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

1i7qB Anthranilate synthase from s. Marcescens (see paper)
39% identity, 97% coverage: 2:185/190 of query aligns to 3:186/192 of 1i7qB

query
sites
1i7qB

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active site: G58 (≠ S55), C83 (= C80), L84 (= L81), H169 (= H168), E171 (= E170)
binding glutamic acid: P55 (= P52), G56 (= G53), G58 (≠ S55), C83 (= C80), L84 (= L81), Q87 (= Q84), H132 (= H129), S133 (= S130), L134 (= L131)

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
40% identity, 98% coverage: 3:188/190 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

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 98% coverage: 3:188/190 of query aligns to 6:148/632 of 8hx9A

query
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8hx9A

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binding magnesium ion: S134 (≠ T174), D135 (≠ P175)

Sites not aligning to the query:

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

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
28% identity, 99% coverage: 1:189/190 of query aligns to 1:179/183 of 7yc6A

query
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7yc6A

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A

V

D

S

P

S

V

K

V

I

V

V

K

P

N

N

D

T

R

T

P

P

E

-

L

L

L

E

D

E

M

I

A

E

A

S

D

N

G

K

R

E

L

V

D

K

R

G

V

I

C

I

I

L

S

S

P

G

G

G

P

P

S

-

N

D

P

I

G

E

N

K

A

A

G

K

Y

N

C

C

L

I

E

D

F

I

L

-

N

-

R

A

L

L

P

N

H

A

V

K

V

L

P

P

V

I

L

L

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

C

L

L

I

G

A

H

L

H

A

A

Y

G

G

A

G

K

E

V

V

T

G

R

R

A

A

G

A

R

-

I

-

M

-

H

-

G

-

K

-

T

L

S

T

K

K

V

V

F

Y

H

V

E
x
D

N

K

E

E

G

N

-

P

L

L

F

F

E

K

G

N

L

V

P

P

S

R

G

E

M

F

E

N

V

A

C

W

R

A

Y

S

H

H

S

K

L

D

I
x
E

V

V

E

K

-

K

-

V

P

P

N

E

G

G

T

-

K

-

A

-

F

F

D

E

V

I

T

L

A

A

T
x
H

A

S

G

D

R

I

G
x
C

E

Q

I

V

M

E

G

A

L

M

K

K

Y

H

R

K

D

T

R

K

P

P

W

I

H

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

S

V

I

A

L

H

T

T

P

E

D

Y

G

G

P

N

K

E

L

I

L

L

K

K

N

N

F

F

L

C

N

K

I

V

S

C

G

G

binding zinc ion: C76 (= C80), D101 (≠ E111), E123 (≠ I132), E123 (≠ I132), H136 (≠ T146), C140 (≠ G150), C140 (≠ G150), H158 (= H168)

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
29% identity, 100% coverage: 1:190/190 of query aligns to 1:186/475 of 2ywcA

query
sites
2ywcA

M

M

F

V

L

L

L

V

I

L

D

D

N

F

Y

G

D

S

S

Q

F

Y

T

T

F

R

N

L

L

I

V

A

Q

R

A

R

F

L

Q

R

Q

E

L

L

G

R

A

A

D

F

P

S

V

L

V

I

V

L

K

P

N

G

D

D

R

A

P

P

E

-

L

-

L

L

D

E

M

E

A

V

A

L

D

K

G

H

R

R

L

P

D

Q

R

A

V

L

C

I

I

L

S

S

P

G

G
|
G

P

P

S
x
R

N

S

P

V

G

F

N

D

A

P

G

D

Y

A

C

P

L

R

E

P

F

D

L

P

N

R

R

L

L

F

P

S

H

S

V

G

V

L

P

P

V

L

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

C

L

L

L

G

A

H

Q

H

E

A

L

G

G

A

G

K

R

V

V

T

E

R

R

A

A

G

G

R

R

I

A

M

E

H

Y

G

G

K

K

T

A

S

L

K

L

V

T

F

R

H

H

E

E

N

G

E

P

G

-

L

L

F

F

E

R

G

G

L

L

P

E

S

G

G

E

M

V

E

Q

V

V

C

W

R

M

Y

S

H

H

-

Q

-

D

S

A

L

V

I

T

V

A

E

P

P

P

N

P

G

G

T

W

K

R

A

-

F

-

D

-

V

V

T

V

A

A

T

E

A

T

G

E

R

E

G

N

E

P

I

V

M

A

G

A

L

I

K

A

Y

S

R

P

D

D

R

G

P

R

W

A

H

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

T

T

P

P

D

K

G

G

P

M

K

Q

L

I

L

L

K

E

N

N

F

F

L

L

N

E

I

L

S

A

G

G

L

V

active site: G51 (= G53), R53 (≠ S55), C78 (= C80), Y79 (≠ L81), 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

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)
29% identity, 91% coverage: 14:186/190 of query aligns to 207:380/2225 of P20054

query
sites
P20054

N

N

L

Q

V

I

Q

R

A

C

F

L

Q

L

Q

N

L

R

G

G

A

V

D

D

P

L

V

K

V

V

K

-

N

-

D

-

R

-

P

P

E

W

L

D

L

Y

D

D

M

V

A

V

A

A

D

N

G

E

R

S

L

I

-

N

-

D

-

Y

D

D

R

G

V

V

C

F

I

I

S

S

P

N

G

G

P

P

S

G

N

D

P

P

G

S

N

L

A

C

G

G

Y

K

C

A

L

I

E

E

F

N

L

I

N

R

R

K

-

V

-

L

-

A

L

L

P

P

H

V

V

A

V

K

P

A

V

V

L

F

G

G

V

V

C

C

L

M

G

G

H

N

Q

Q

C

L

L

L

G

G

H

L

H

A

A

A

G

G

A

A

K

Q

V

-

T

-

R

-

A

-

G

-

R

-

I

-

M

-

H

-

G

-

K

-

T

T

S

H

K

K

V

M

F

A

H

F

E

G

N

N

E

R

G

G

L

L

F

N

E

Q

G

P

L

C

P

V

S

D

G

Q

M

I

E

S

-

G

-

R

-

C

-

H

-

I

V

T

C

S

R

Q

Y

N

H

H

S

G

L

F

I

V

V

I

E

D

P

S

N

N

-

S

-

L

-

P

-

A

-

G

-

S

G

G

T

W

K

K

A

T

F

Y

D

F

V

I

T

N

A

A

T

N

A

D

G

A

R

S

G

N

E

E

I

-

M

-

G

G

L

I

K

Y

Y

H

R

E

D

S

R

K

P

P

W

W

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

A

I

M

L

A

T

G

P

P

-

T

D

D

G

T

P

E

K

Y

L

L

L

F

K

D

N

N

F

F

L

V

N

D

Sites not aligning to the query:

1 modified: N-acetylmethionine

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)
27% identity, 92% coverage: 14:187/190 of query aligns to 254:422/430 of Q9LVW7

query
sites
Q9LVW7

N

N

L

I

V

L

Q

R

A

R

F

L

Q

S

L

Y

G

G

A

C

D

Q

P

I

V

T

V

V

K

P

N

S

D

T

R

F

P

P

-

A

E

E

L

A

L

L

D

K

M

M

A

N

A

P

D

D

G

G

R

-

L

-

D

-

R

-

V

I

C

L

I

F

S

S

P

N

G

G

P

P

S

G

N

D

P

P

G

S

N

A

A

V

G

P

Y

Y

C

A

L

V

E

E

F

T

L

V

N

K

R

E

L

L

P

L

H

G

V

K

V

V

P

P

V

V

L

Y

G

G

V

I

C

C

L

M

G

G

H

H

Q

Q

C

L

L

L

G

G

H

Q

H

A

A

L

G

G

A

G

K

K

V

T

T

F

R

K

A

M

G

K

R

F

I

G

M

H

H

H

G

G

K

G

T

N

S

H

K

P

V

V

F

R

H

N

E

N

N

R

E

T

G

G

L

Q

F

V

E

E

G

-

L

-

P

-

S

-

G

-

M

-

E

I

V

S

C

A

R

Q

Y

N

H

H

S

N

L

Y

I

A

V

V

E

D

P

P

N

A

G

S

T

L

K

P

-

G

A

G

F

V

D

E

V

V

T

T

-

H

A

V

T

N

A

L

G

N

R

D

G

G

E

S

I

C

M

A

G

G

L

L

K

S

Y

F

R

P

D

E

R

M

P

N

W

V

H

M

G

S

V

L

Q

Q

F

Y

H

H

P

P

E

E

S

A

I

S

L

P

T

G

P

P

-
x
H

D

D

G

S

P

D

K

N

L

A

L

F

K

R

N

E

F

F

L

I

N

E

I

L

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

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

query
sites
3r75B

L

L

L

I

I

V

D

D

N

A

Y

E

D

D

S

H

F

F

T

T

F

A

N

M

L

I

V

A

Q

Q

A

Q

F

L

Q

S

L

L

G

G

-

L

A

A

D

T

P

E

V

V

V

C

V

G

K

V

N

H

D

D

R

A

P

V

E

D

L

L

L

-

D

-

M

-

A

-

D

-

G

A

R

R

L

Y

D

D

R

V

V

V

C

V

I

M

S

G

P

P

G

G

P

P

S

G

N

D

P

P

G

S

N

D

A

A

G

G

-

D

-

P

Y

R

C

I

L

A

E

R

F

L

L

Y

N

A

R

W

L

L

P

R

H

H

V

L

V

I

-

D

-

E

-

G

-

K

P

P

V

F

L

M

G

A

V

V

C
|
C

L

L

G

S

H

H

Q

Q

C

I

L

L

G

N

H

A

H

I

A

L

G

G

A

I

K

P

V

L

T

V

R

R

-

R

-

E

-

V

-

P

-

N

-

Q

-

G

-

I

-

Q

A

V

G

E

R

I

I

D

M

L

H

F

G

G

K

Q

T

R

S

E

K

R

V

V

F

G

H

F

E
x
Y

N

N

E

T

G

Y

L

V

F

A

E

Q

G

T

L

V

P

R

S

D

G

E

M

M

E

D

V

V

C

-

R

-

Y

-

H

-

S

-

L

-

I

-

V

-

E

-

P

-

N

D

G

G

T

V

K

G

A

T

F

V

D

A

V

I

T

S

A

R

T

D

A

P

G

R

R

T

G

G

E

E

I

V

M

H

G

A

L

L

K

-

Y

-

R

R

D

G

R

P

P

T

W

F

H

S

G

S

V

M

Q

Q

F

F

H
|
H

P

A

E

E

S

S

I

V

L

L

T

T

P

V

D

D

G

G

P

P

K

R

L

I

L

L

binding zinc ion: C512 (= C80), Y552 (≠ E111), 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

Q09794 Multifunctional protein ura1; 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 Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 92% coverage: 13:187/190 of query aligns to 274:442/2244 of Q09794

query
sites
Q09794

F

Y

N

N

L

Q

V

I

Q

R

A

C

F

F

Q

L

Q

N

L

R

G

G

A

V

D

E

P

L

V

L

V

V

K

-

N

-

D

-

R

-

P

P

E

W

L

D

L

Y

D

D

M

F

A

T

A

K

D

E

G

-

R

T

L

Y

D

D

R

G

V

L

C

F

I

I

S

S

P

N

G

G

P

P

S

G

N

D

P

P

G

S

N

L

A

M

G

D

Y

L

C

V

L

V

E

D

F

R

L

V

N

K

R

R

L

V

-

L

-

E

P

S

H

K

V

T

V

V

P

P

V

V

L

F

G

G

V

I

C

C

L

F

G

G

H

H

Q

Q

C

I

L

M

G

A

H

R

H

A

A

A

G

G

A

A

K

S

V

T

T

T

R

K

A

M

-

K

-

F

G

G

R

N

I

R

M

G

H

H

G

N

K

I

T

P

S

C

K

T

V

C

F

M

H

I

E

S

N

G

E

R

G

C

L

Y

F

I

E

T

G

S

L

Q

P

N

S

H

G

G

M

Y

E

A

V

V

C

-

R

D

Y

A

H

S

S

S

L

L

I

-

V

-

E

-

P

S

N

N

G

G

T

W

K

K

A

E

F

L

D

F

V

V

T

N

A

A

T

N

A

D

G

G

R

S

G

N

E

E

I

-

M

-

G

G

L

I

K

Y

Y

N

R

T

D

E

R

Y

P

P

W

F

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

I

T

L

P

T

G

P

P

-

R

D

D

G

T

P

E

K

F

L

L

L

F

K

D

N

V

F

F

L

I

N

D

I

V

Sites not aligning to the query:

1119 modified: Phosphoserine
1881 modified: Phosphoserine
1885 modified: Phosphoserine

P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
29% identity, 90% coverage: 11:181/190 of query aligns to 185:349/2225 of P08955

query
sites
P08955

F

L

T

K

F

Y

N

N

L

Q

V

I

Q

R

A

C

F

L

Q

C

Q

Q

L

L

G

G

A

A

D

E

P

V

V

T

V

V

K

P

N

W

D

N

R

H

P

-

E

E

L

L

L

D

D

S

M

Q

A

K

A

Y

D

D

G

G

R

-

L

-

D

-

R

-

V

L

C

F

I

L

S

S

P

N

G

G

P

P

S

G

N

D

P

P

G

A

N

S

A

Y

G

P

Y

G

C

V

L

V

E

A

F

T

L

L

N

N

R

R

L

V

-

L

-

S

-

E

P

P

H

N

V

P

V

R

P

P

V

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

C

L

L

L

G

A

H

L

H

A

A

I

G

G

A

A

K

K

V

T

T

Y

R

-

A

-

G

-

R

K

I

M

M

R

H

Y

G

G

K

N

T

R

S

G

K

-

V

-

F

-

H

H

E

N

N

Q

E

P

G

C

L

L

F

L

E

V

G

G

L

T

P

G

S

R

G

C

M

F

E

L

V

T

C

S

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

E

D

-

A

-

D

-

S

-

L

P

P

N

A

G

G

T

W

K

T

A

P

F

L

D

F

V

T

T

N

A

A

T

N

A

D

G

C

R

S

G

N

E

E

I

-

M

-

G

G

L

I

K

V

Y

H

R

D

D

S

R

L

P

P

W

F

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

R

L

A

T

G

P

P

D

S

G

D

P

M

K

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.

5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
32% identity, 61% coverage: 74:189/190 of query aligns to 75:193/490 of 5tw7F

query
sites
5tw7F

V

I

P

P

V

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

C

F

L

M

G

A

H

H

A

L

G

G

A

G

K

E

V

V

T

Q

R

P

A

G

G

N

R

Q

I

R

M

E

H

F

G

G

K

-

T

Y

S

A

K

Q

V

V

F

K

H

T

E

I

N

D

E

S

G

G

L

L

F

T

E

R

G

G

L

I

-

Q

-

D

-

A

P

P

S

N

G

T

M

L

E

D

V

V

C

W

R

M

Y

S

H

H

S

G

L

D

I

K

V

V

E

S

-

K

-

L

P

P

N

D

G

G

T

-

K

-

A

-

F

F

D

A

V

V

T

I

A

G

T

D

A

T

G

P

R

S

G

C

E

P

I

I

M

A

G

M

L

M

K

E

Y

N

R

T

D

E

R

K

P

Q

W

F

H

Y

G

G

V

I

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

P

K

D

Q

G

G

P

R

K

A

L

L

K

N

N

R

F

F

-

V

L

L

N

D

I

I

S

C

G

G

active site: C81 (= C80), Y82 (≠ L81), H171 (= H168), E173 (= E170)

Sites not aligning to the query:

active site: 55, 229, 345
binding magnesium ion: 466, 469, 472

P05990 Multifunctional protein r; Protein rudimentary; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
27% identity, 74% coverage: 42:181/190 of query aligns to 229:366/2224 of P05990

query
sites
P05990

D

D

G

E

R

Q

L

F

D

D

R

A

V

L

C

F

I

L

S

S

P

N

G

G

P

P

S

G

N

N

P

P

G

E

N

S

A

-

G

-

Y

-

C

C

L

D

E

Q

F

I

L

V

N

Q

R

Q

L

V

P

R

H

K

V

V

V

I

-

E

-

G

-

Q

-

K

P

P

V

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

C

L

L

L

G

A

H

K

H

A

A

I

G

G

A

C

K

S

V

T

T

Y

R

K

A

M

G

K

R

Y

I

G

M

N

H

R

G

G

K

H

T

N

S

L

K

P

V

C

F

L

H

H

E

R

N

A

E

T

G

G

L

-

F

-

E

-

G

-

L

-

P

-

S

R

G

C

M

L

E

M

V

T

C

S

R

Q

Y

N

H

H

S

G

L

Y

I

A

V

V

E

D

-

L

-

E

-

Q

-

L

P

P

N

D

G

G

T

W

K

S

A

E

F

L

D

F

V

V

T

N

A

A

T

N

A

D

G

G

R

T

G

N

E

E

I

-

M

-

G

G

L

I

K

V

Y

H

R

A

D

S

R

K

P

P

W

Y

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

H

L

A

T

G

P

P

D

Q

G

D

P

T

K

E

L

F

L

L

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

2vxoB Human gmp synthetase in complex with xmp (see paper)
34% identity, 61% coverage: 75:189/190 of query aligns to 77:187/658 of 2vxoB

query
sites
2vxoB

P

P

V

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

C

M

L

M

G

N

H

K

H

V

A

F

G

G

A

G

K

T

V

V

T

-

R

-

A

-

G

-

R

-

I

-

M

-

H

H

G

K

K

K

T

S

S

D

K

G

V

V

F

F

H

N

-

I

-

S

-

V

-

D

E

N

N

T

E

C

G

S

L

L

F

F

E

R

G

G

L

L

P

Q

S

K

G

E

M

E

E

V

V

V

C

L

R

L

Y

T

H

H

S

G

L

D

I

S

V

V

E

D

P

-

N

K

G

V

T

A

K

D

A

G

F

F

D

K

V

V

T

V

A

A

T

R

A

S

G

G

R

-

G

N

E

I

I

V

M

A

G

G

L

I

K

A

Y

N

R

E

D

S

R

K

P

K

W

L

H

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

T

T

P

E

D

N

G

G

P

K

K

V

L

I

L

L

K

K

N

N

F

F

L

L

-

Y

N

D

I

I

S

A

G

G

active site: C82 (= C80), Y83 (≠ L81), H165 (= H168), E167 (= E170)

Sites not aligning to the query:

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

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)
28% identity, 90% coverage: 11:181/190 of query aligns to 185:349/2225 of P27708

query
sites
P27708

F

L

T

K

F

Y

N

N

L

Q

V

I

Q

R

A

C

F

L

Q

C

Q

Q

L

R

G

G

A

A

D

E

P

V

V

T

V

V

K

P

N

-

D

-

R

-

P

-

E

-

L

-

L

W

D

D

M

H

A

A

A

L

D

D

G

S

R

Q

-

E

L

Y

D

E

R

G

V

L

C

F

I

L

S

S

P

N

G

G

P

P

S

G

N

D

P

P

G

A

N

S

A

Y

G

P

Y

S

C

V

L

V

E

S

F

T

L

L

N

S

R

R

L

V

-

L

-

S

-

E

P

P

H

N

V

P

V

R

P

P

V

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

C

L

L

L

G

A

H

L

H

A

A

I

G

G

A

A

K

K

V

T

T

Y

R

-

A

-

G

-

R

K

I

M

M

R

H

Y

G

G

K

N

T

R

S

G

K

-

V

-

F

-

H

H

E

N

N

Q

E

P

G

C

L

L

F

L

E

V

G

G

L

S

P

G

S

R

G

C

M

F

E

L

V

T

C

S

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

E

E

P

T

N

D

G

S

T

L

K

P

A

A

-

D

-

W

F

A

D

P

V

L

T

F

A

T

T

N

A

A

G

N

R

D

G

G

E

S

I

N

M

E

G

G

L

I

K

V

Y

H

R

N

D

S

R

L

P

P

W

F

H

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

Q

L

A

T

G

P

P

D

S

G

D

P

M

K

E

L

L

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

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
33% identity, 61% coverage: 75:189/190 of query aligns to 99:212/693 of P49915

query
sites
P49915

P

P

V

V

L

L

G

G

V

I

C
|
C

L

Y

G

G

H

M

Q

Q

C

M

L

M

G

N

H

K

H

V

A

F

G

G

A

G

K

T

V

V

T

H

R

K

A

K

G

S

R

V

I

R

M

E

H

D

G

G

K

V

T

F

S

N

K

I

V

S

F

V

H

D

E

N

N

T

E

C

G

S

L

L

F

F

E

R

G

G

L

L

P

Q

S

K

G

E

M

E

E

V

V

V

C

L

R

L

Y

T

H

H

S

G

L

D

I

S

V

V

E

D

P

-

N

K

G

V

T

A

K

D

A

G

F

F

D

K

V

V

T

V

A

A

T

R

A

S

G

G

R

-

G

N

E

I

I

V

M

A

G

G

L

I

K

A

Y

N

R

E

D

S

R

K

P

K

W

L

H

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

T

T

P

E

D

N

G

G

P

K

K

V

L

I

L

L

K

K

N

N

F

F

L

L

-

Y

N

D

I

I

S

A

G

G

C104 (= C80) active site, For GATase activity
H190 (= H168) active site, For GATase activity
E192 (= E170) active site, For GATase activity

Sites not aligning to the query:

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

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
27% identity, 85% coverage: 27:187/190 of query aligns to 218:372/379 of 1ce8B

query
sites
1ce8B

V

V

V

P

V

A

K

Q

N

T

D

S

R

A

P

E

E

D

L

V

L

L

D

K

M

M

A

N

A

P

D

D

G

G

R

-

L

-

D

-

R

-

V

I

C

F

I

L

S

S

P

N

G

G

P

P

S

G

N

D

P

P

G

A

N

P

A

C

G

D

Y

Y

C

A

L

I

E

T

F

A

L

I

N

Q

R

K

-

F

L

L

P

E

H

T

V

D

V

I

P

P

V

V

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

C

L

L

L

G

A

H

L

H

A

A

S

G

G

A

A

K

K

V

T

T

V

R

K

A

M

G

K

R

F

I

G

M

H

H

H

G

G

K

G

T

N

S

H

K

P

V

V

F

K

H

D

E

V

N

E

E

K

G

N

L

V

F

V

E

-

G

-

L

-

P

-

S

-

G

-

M

M

E

I

V

T

C

A

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

E

D

P

E

N

A

G

T

T

L

K

P

A

A

-

N

F

L

D

R

V

V

T

T

-

H

A

K

T

S

A

L

G

F

R

D

G

G

E

T

I

L

M

Q

G

G

L

I

K

H

Y

R

R

T

D

D

R

K

P

P

W

A

H

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

I

S

L

P

T

G

P

P

-

H

D

D

G

A

P

A

K

P

L

L

L

F

K

D

N

H

F

F

L

I

N

E

I

L

active site: C268 (= C80), 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)
27% identity, 85% coverage: 27:187/190 of query aligns to 219:373/382 of P0A6F1

query
sites
P0A6F1

V

V

V

P

V

A

K

Q

N

T

D

S

R

A

P

E

E

D

L

V

L

L

D

K

M

M

A

N

A

P

D

D

G

G

R

-

L

-

D

-

R

-

V

I

C

F

I

L

S

S

P

N

G
|
G

P

P

S
x
G

N

D

P

P

G

A

N

P

A

C

G

D

Y

Y

C

A

L

I

E

T

F

A

L

I

N

Q

R

K

-

F

L

L

P

E

H

T

V

D

V

I

P

P

V

V

L

F

G

G

V

I

C

C

L
|
L

G

G

H

H

Q
|
Q

C

L

L

L

G

A

H

L

H

A

A

S

G

G

A

A

K

K

V

T

T

V

R

K

A

M

G

K

R

F

I

G

M

H

H

H

G

G

K

G

T

N

S

H

K

P

V

V

F

K

H

D

E

V

N

E

E

K

G

N

L

V

F

V

E

-

G

-

L

-

P

-

S

-

G

-

M

M

E

I

V

T

C

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

I

A

V

V

E

D

P

E

N

A

G

T

T

L

K

P

A

A

-

N

F

L

D

R

V

V

T

T

-

H

A

K

T

S

A

L

G

F

R

D

G

G

E

T

I

L

M

Q

G

G

L

I

K

H

Y

R

R

T

D

D

R

K

P

P

W

A

H

F

G

S

V

F

Q

Q

F

G

H

H

P

P

E

E

S

A

I

S

L

P

T

G

P

P

-

H

D

D

G

A

P

A

K

P

L

L

L

F

K

D

N

H

F

F

L

I

N

E

I

L

G241 (= G53) binding L-glutamine
G243 (≠ S55) 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

Query Sequence

>WP_018123678.1 NCBI__GCF_000375485.1:WP_018123678.1
MFLLIDNYDSFTFNLVQAFQQLGADPVVVKNDRPELLDMAADGRLDRVCISPGPSNPGNA
GYCLEFLNRLPHVVPVLGVCLGHQCLGHHAGAKVTRAGRIMHGKTSKVFHENEGLFEGLP
SGMEVCRYHSLIVEPNGTKAFDVTATAGRGEIMGLKYRDRPWHGVQFHPESILTPDGPKL
LKNFLNISGL

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