SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_004044227.1 NCBI__GCF_000337315.1:WP_004044227.1 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 19 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)
43% identity, 92% coverage: 4:222/239 of query aligns to 2:185/187 of P00903

query
sites
P00903

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C79 (= C97) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H205) mutation to Q: Loss of activity.
E170 (= E207) 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, 93% coverage: 4:225/239 of query aligns to 75:267/276 of Q42565

query
sites
Q42565

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G150 (= G95) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G120) 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)
42% identity, 98% coverage: 3:236/239 of query aligns to 5:202/673 of 8hx8A

query
sites
8hx8A

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binding magnesium ion: I175 (= I209), S177 (≠ T211)

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)
34% identity, 95% coverage: 1:228/239 of query aligns to 1:193/193 of P00900

query
sites
P00900

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M1 (= M1) modified: Initiator methionine, Removed
C84 (= C97) active site, Nucleophile; for GATase activity

1i7qB Anthranilate synthase from s. Marcescens (see paper)
34% identity, 94% coverage: 4:228/239 of query aligns to 3:192/192 of 1i7qB

query
sites
1i7qB

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K

active site: G58 (= G74), C83 (= C97), L84 (= L98), H169 (= H205), E171 (= E207)
binding glutamic acid: P55 (= P71), G56 (= G72), G58 (= G74), C83 (= C97), L84 (= L98), Q87 (= Q101), H132 (= H146), S133 (= S147), L134 (= L148)

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 94% coverage: 3:227/239 of query aligns to 4:150/632 of 8hx9A

query
sites
8hx9A

R

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R

E

D

D

I

F

D

D

P

-

D

-

G

A

I

I

V

V

S

S

P

P

G

R

P

A

G

I

T

T

P

-

A

-

E

-

A

-

G

-

V

-

S

-

V

-

S

-

V

-

F

-

R

-

D

D

L

S

D

G

Y

L

P

P

T

V

L

L

G

G

V

V

C

C

L

L

G

-

H

-

Q

-

S

-

L

-

C

-

A

-

L

-

G

-

S

-

R

-

V

-

G

-

H

-

A

-

P

-

H

-

V

-

V

M

H

H

G

G

K

R

P

V

S

S

L

E

V

V

E

R

H

H

D

T

G

G

A

E

G

D

V

V

F

F

S

R

G

G

L

L

P

P

D

S

R

P

I

F

E

T

V

A

G

V

R

R

Y

Y

H

H

S

D

L

-

A

-

V

-

E

-

H

-

E

-

D

-

V

-

P

-

E

E

L

L

A

E

V

P

T

L

A

A

Y

W

T

S

V

-

A

-

E

-

G

-

S

-

E

-

A

-

E

-

N

-

S

D

D

D

G

G

D

-

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

V

M

M

G

G

V

L

R

R

H

H

R

R

E

E

K

K

P

P

H

L

V

W

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

I

I

L

G

T
x
S

D
|
D

S

F

G

G

K

R

D

E

I

I

V

M

R

A

N

N

F

F

V

R

A

D

L

L

A

A

V

L

G

A

binding magnesium ion: S134 (≠ T211), D135 (= D212)

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

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
29% identity, 64% coverage: 55:208/239 of query aligns to 224:356/382 of P0A6F1

query
sites
P0A6F1

S

S

T

A

D

E

D

D

V

V

R

L

D

K

I

M

D

N

P

P

D

D

G

G

I

I

V

F

V

L

S

S

P

N

G
|
G

P

P

G
|
G

T

D

P

P

A

A

E

P

-

C

-

D

-

Y

A

A

G

I

V

T

S

A

V

I

S

Q

V

K

F

F

R

L

D

E

L

T

D

D

Y

I

P

P

T

V

L

F

G

G

V

I

C

C

L
|
L

G

G

H

H

Q
|
Q

S

L

L

L

C

A

A

L

A

A

L

S

G

G

S

A

R

K

V

T

G

V

H

K

A

M

P

K

H

F

V

G

V

H

H

H

G

G

K

G

P

N

S

H

L

P

V

V

E

K

H

D

D

V

G

E

A

K

G

N

V

V

F

V

S

-

G

-

L

-

P

-

D

-

R

-

I

M

E

I

V

T

G

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

A

A

V

V

E

D

H

E

E

A

D

T

V

L

P

P

P

A

E

N

L

L

A

R

V

V

T

T

A

H

Y

K

T

S

V

L

A

F

E

D

G

G

S

T

E

-

A

-

E

-

N

-

S

-

D

-

G

-

D

-

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

-

V

L

M

Q

G

G

V

I

R

H

H

R

R

T

E

D

K

K

P

P

H

A

V

F

G

S

V

F

Q

Q

F

G

H

H

P

P

E

E

S

A

G241 (= G72) binding L-glutamine
G243 (= G74) binding L-glutamine
L270 (= L98) binding L-glutamine
Q273 (= Q101) binding L-glutamine
N311 (≠ Y145) binding L-glutamine
G313 (≠ S147) binding L-glutamine
F314 (≠ L148) 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)
29% identity, 64% coverage: 55:208/239 of query aligns to 223:355/379 of 1ce8B

query
sites
1ce8B

S

S

T

A

D

E

D

D

V

V

R

L

D

K

I

M

D

N

P

P

D

D

G

G

I

I

V

F

V

L

S

S

P

N

G

G

P

P

G

G

T

D

P

P

A

A

E

P

-

C

-

D

-

Y

A

A

G

I

V

T

S

A

V

I

S

Q

V

K

F

F

R

L

D

E

L

T

D

D

Y

I

P

P

T

V

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

L

L

L

C

A

A

L

A

A

L

S

G

G

S

A

R

K

V

T

G

V

H

K

A

M

P

K

H

F

V

G

V

H

H

H

G

G

K

G

P

N

S

H

L

P

V

V

E

K

H

D

D

V

G

E

A

K

G

N

V

V

F

V

S

-

G

-

L

-

P

-

D

-

R

-

I

M

E

I

V

T

G

A

R

Q

Y

N

H

H

S

G

L

F

A

A

V

V

E

D

H

E

E

A

D

T

V

L

P

P

P

A

E

N

L

L

A

R

V

V

T

T

A

H

Y

K

T

S

V

L

A

F

E

D

G

G

S

T

E

-

A

-

E

-

N

-

S

-

D

-

G

-

D

-

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

-

V

L

M

Q

G

G

V

I

R

H

H

R

R

T

E

D

K

K

P

P

H

A

V

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

active site: C268 (= C97), H352 (= H205), E354 (= E207)

Sites not aligning to the query:

binding L-ornithine: 119, 122

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
28% identity, 64% coverage: 55:208/239 of query aligns to 223:355/379 of 1c3oB

query
sites
1c3oB

S

S

T

A

D

E

D

D

V

V

R

L

D

K

I

M

D

N

P

P

D

D

G

G

I

I

V

F

V

L

S

S

P
x
N

G
|
G

P

P

G
|
G

T

D

P

P

A

A

E

P

-

C

-

D

-

Y

A

A

G

I

V

T

S

A

V

I

S

Q

V

K

F

F

R

L

D

E

L

T

D

D

Y

I

P

P

T

V

L

F

G

G

V

I

C
x
S

L
|
L

G

G

H

H

Q

Q

S

L

L

L

C

A

A

L

A

A

L

S

G

G

S

A

R

K

V

T

G

V

H

K

A

M

P

K

H

F

V

G

V

H

H

H

G

G

K

G

P

N

S

H

L

P

V

V

E

K

H

D

D

V

G

E

A

K

G

N

V

V

F

V

S

-

G

-

L

-

P

-

D

-

R

-

I

M

E

I

V

T

G

A

R

Q

Y
x
N

H
|
H

S
x
G

L
x
F

A

A

V

V

E

D

H

E

E

A

D

T

V

L

P

P

P

A

E

N

L

L

A

R

V

V

T

T

A

H

Y

K

T

S

V

L

A

F

E

D

G

G

S

T

E

-

A

-

E

-

N

-

S

-

D

-

G

-

D

-

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

-

V

L

M

Q

G

G

V

I

R

H

H

R

R

T

E

D

K

K

P

P

H

A

V

F

G

S

V

F

Q

Q

F

G

H
|
H

P

P

E
|
E

S

A

active site: S268 (≠ C97), H352 (= H205), E354 (= E207)
binding glutamine: N239 (≠ P71), G240 (= G72), G242 (= G74), S268 (≠ C97), L269 (= L98), N310 (≠ Y145), H311 (= H146), G312 (≠ S147), F313 (≠ L148)

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
34% identity, 56% coverage: 92:225/239 of query aligns to 73:184/475 of 2ywcA

query
sites
2ywcA

P

P

T

L

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

L

L

L

C

A

A

Q

A

E

L

L

G

G

S

G

R

R

V

V

G

E

H

R

A

A

P

G

H

R

V

A

V

E

H

Y

G

G

K

K

P

A

S

L

L

L

V

T

E

R

H

H

D

E

G

G

A

P

G

-

V

L

F

F

S

R

G

G

L

L

P

E

D

G

R

E

I

V

E

Q

V

V

G

W

R

M

Y

S

H

H

S

Q

L

D

A

A

V

V

E

T

H

A

E

P

D

-

V

-

P

P

E

G

L

W

A

R

V

V

T

V

A

A

Y

E

T

T

V

-

A

-

E

-

G

-

S

-

E

-

A

E

E

E

N

N

S

P

D

-

G

-

D

-

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

-

V

V

M

A

G

A

V

I

R

A

H

S

R

P

E

D

K

G

P

R

H

A

V

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

T

T

D

P

S

K

G

G

K

M

D

Q

I

I

V

L

R

E

N

N

F

F

V

L

A

E

L

L

A

A

active site: C78 (= C97), Y79 (≠ L98), H164 (= H205), E166 (= E207)

Sites not aligning to the query:

active site: 51, 53, 221, 343
binding xanthosine-5'-monophosphate: 288, 366, 367, 368, 408, 467, 471, 472, 473

5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
26% identity, 74% coverage: 54:230/239 of query aligns to 37:196/490 of 5tw7F

query
sites
5tw7F

L

M

S

P

T

L

D

D

D

E

V

I

R

K

D

A

I

F

D

N

P

P

D

K

G

G

I

I

V

I

V

L

S

S

P

G

G
|
G

P

P

G

N

T

S

P

V

A

Y

E

E

A

S

G

D

V

Y

S

Q

V

A

S

D

V

T

-

G

F

I

R

F

D

D

L

L

D

G

Y

I

P

P

T

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

F

L

M

C

A

A

H

L

L

G

G

S

G

R

E

V

V

G

Q

H

P

A

G

P

N

H

Q

V

R

V

E

H

F

G

G

K

Y

P

A

S

Q

L

V

V

K

E

T

H

I

D

D

G

-

A

S

G

G

V

L

F

T

S

R

G

G

L

I

P

Q

D

D

R

-

I

-

E

-

V

-

G

-

R

-

Y

-

H

-

S

-

L

-

A

-

V

-

E

-

H

-

E

-

D

D

V

A

P

P

P

N

E

T

L

L

A

D

V

V

T

W

A

-

Y

-

T

-

V

M

A

S

E

H

G

G

S

D

E

K

A

V

E

S

N

K

S

L

D

P

G

D

D

G

T

F

G

A

T

V

E

I

G

G

D

D

E

T

P

P

A

S

V

C

-

P

V

I

M

A

G

M

V

M

R

E

H

N

R

T

E

E

K

K

P

Q

H

F

V

Y

G

G

V

I

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

D

K

S

Q

G

G

K

R

D

A

I

L

V

L

R

N

N

R

F

F

V

V

A

L

L

D

A

I

V

C

G

G

D

A

G

Q

P

P

active site: G55 (= G72), C81 (= C97), Y82 (≠ L98), H171 (= H205), E173 (= E207)

Sites not aligning to the query:

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

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, 62% coverage: 62:208/239 of query aligns to 281:405/430 of Q9LVW7

query
sites
Q9LVW7

I

M

D

N

P

P

D

D

G

G

I

I

V

L

V

F

S

S

P

N

G

G

P

P

G

G

T

D

P

P

A

S

E

A

A

V

G

P

V

Y

S

A

V

V

S

E

V

T

F

V

R

K

D

E

L

L

-

L

-

G

D

K

Y

V

P

P

T

V

L

Y

G

G

V

I

C

C

L

M

G

G

H

H

Q

Q

S

L

L

L

C

G

A

Q

A

A

L

L

G

G

S

G

R

K

V

T

G

F

H

K

A

M

P

K

H

F

V

G

V

H

H

H

G

G

K

G

P

N

S

H

L

P

V

V

E

R

H

N

D

N

G

R

A

T

G

G

V

-

F

-

S

-

G

-

L

-

P

-

D

-

R

Q

I

V

E

E

V

I

-

S

G

A

R

Q

Y

N

H

H

S

N

L

Y

A

A

V

V

E

D

H

P

E

A

D

S

V

L

P

P

P

G

E

G

L

V

A

E

V

V

T

T

A

H

Y

V

T

N

V

L

A

N

E

D

G

G

S

S

E

C

A

A

E

-

N

-

S

-

D

-

G

-

D

-

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

-

M

-

G

G

V

L

R

S

H

F

R

P

E

E

K

M

P

N

H

V

V

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.

Q18990 Multifunctional protein pyr-1; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Caenorhabditis elegans (see 3 papers)
28% identity, 61% coverage: 63:207/239 of query aligns to 217:341/2198 of Q18990

query
sites
Q18990

D

D

P

Y

D

D

G

G

I

L

V

F

V

L

S

S

P

N

G

G

P

P

G

G

T

D

P

P

A

E

E

I

A

C

G

A

V

P

S

L

V

V

-

D

-

R

-

L

-

A

S

K

V

V

F

I

R

A

D

R

L

G

D

D

Y

K

P

P

T

I

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

I

L

L

C

S

A

R

A

A

L

I

G

G

S

A

R

K

V

T

G

Y

H

K

A

L

P

K

H

Y

V

G

V

N

H

R

G

G

K

H

P

N

S

Q

L

P

V

C

E

T

H

H

D

Y

G

A

A

T

G

G

V

-

F

-

S

-

G

-

L

-

P

-

D

-

R

R

I

C

E

Y

V

I

-

T

G

S

R

Q

Y

N

H

H

S

G

L

Y

A

A

V

V

E

D

H

P

E

D

D

S

V

L

P

P

P

-

E

-

L

-

A

-

V

-

T

-

A

-

Y

-

T

-

V

-

A

A

E

D

G

W

S

K

E

A

A

L

E

F

N

T

S

N

D

E

G

N

D

D

T

K

G

T

T

N

E

E

G

-

D

-

E

-

P

-

A

-

V

-

M

-

G

G

V

I

R

V

H

H

R

S

E

S

K

K

P

P

H

F

V

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

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

P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
27% identity, 60% coverage: 65:207/239 of query aligns to 215:338/2225 of P27708

query
sites
P27708

D

E

G

G

I

L

V

F

V

L

S

S

P

N

G

G

P

P

G

G

T

D

P

P

A

A

E

S

A

Y

G

P

V

S

S

V

V

V

S

S

V

T

F

L

R

S

D

R

L

V

-

L

-

S

-

E

-

P

-

N

D

P

Y

R

P

P

T

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

L

L

C

A

A

L

A

A

L

I

G

G

S

A

R

K

V

T

G

Y

H

K

A

M

P

R

H

Y

-

G

-

N

V

R

V

G

H

H

G

N

K

Q

P

P

S

C

L

L

V

L

E

V

H

G

D

S

G

G

A

R

G

C

V

F

F

L

S

T

G

-

L

-

P

-

D

-

R

-

I

-

E

-

V

-

G

S

R

Q

Y

N

H

H

S

G

L

F

A

A

V

V

E

E

H

T

E

D

D

S

V

L

P

P

P

A

E

D

L

W

A

A

V

P

T

L

A

F

Y

T

T

N

V

A

A

N

E

D

G

G

S

S

E

N

A

E

E

-

N

-

S

-

D

-

G

-

D

-

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

-

M

-

G

G

V

I

R

V

H

H

R

N

E

S

K

L

P

P

H

F

V

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

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)
28% identity, 60% coverage: 65:207/239 of query aligns to 233:355/2224 of P05990

query
sites
P05990

D

D

G

A

I

L

V

F

V

L

S

S

P

N

G

G

P

P

G

G

T

N

P

P

A

E

E

S

A

C

G

D

V

Q

S

I

V

V

S

Q

V

Q

F

V

R

R

D

K

L

V

-

I

-

E

-

G

D

Q

Y

K

P

P

T

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

L

L

C

A

A

K

A

A

L

I

G

G

S

C

R

S

V

T

G

Y

H

K

A

M

P

K

H

Y

-

G

-

N

V

R

V

G

H

H

G

N

K

L

P

P

S

C

L

L

V

H

E

R

H

A

D

T

G

G

A

R

G

C

V

L

F

M

S

T

G

-

L

-

P

-

D

-

R

-

I

-

E

-

V

-

G

S

R

Q

Y

N

H

H

S

G

L

Y

A

A

V

V

E

D

H

L

E

E

D

Q

V

L

P

P

-

D

-

G

-

W

P

S

E

E

L

L

A

F

V

V

T

N

A

A

Y

-

T

-

V

-

A

-

E

-

G

-

S

-

E

-

A

-

E

-

N

-

S

N

D

D

G

G

D

T

T

N

G

E

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

-

M

-

G

G

V

I

R

V

H

H

R

A

E

S

K

K

P

P

H

Y

V

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

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, 67% coverage: 65:223/239 of query aligns to 215:362/2225 of P08955

query
sites
P08955

D

D

G

G

I

L

V

F

V

L

S

S

P

N

G

G

P

P

G

G

T

D

P

P

A

A

E

S

-

Y

A

P

G

G

V

V

S

V

V

A

S

T

V

L

F

N

R

R

D

V

L

L

D

S

-

E

-

P

-

N

-

P

Y

R

P

P

T

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

L

L

C

A

A

L

A

A

L

I

G

G

S

A

R

K

V

T

G

Y

H

K

A

M

P

R

H

Y

-

G

-

N

V

R

V

G

H

H

G

N

K

Q

P

P

S

C

L

L

V

L

E

V

H

G

D

T

G

G

A

R

G

C

V

F

F

L

S

T

G

-

L

-

P

-

D

-

R

-

I

-

E

-

V

-

G

S

R

Q

Y

N

H

H

S

G

L

F

A

A

V

V

E

D

H

A

E

D

D

S

V

L

P

P

P

-

E

-

L

-

A

-

V

-

T

-

A

-

Y

-

T

-

V

-

A

A

E

G

G

W

S

T

E

P

A

L

E

F

N

T

S

N

D

A

G

N

D

D

T

C

G

S

T

N

E

E

G

-

D

-

E

-

P

-

A

-

V

-

M

-

G

G

V

I

R

V

H

H

R

D

E

S

K

L

P

P

H

F

V

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

-

H

-

R

-

A

-

G

-

P

-

S

-

D

-

M

S

E

I

L

L

L

T

F

D

D

S

V

G

F

K

L

D

E

I

T

V

V

R

R

N

E

F

A

V

V

A

A

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)
26% identity, 69% coverage: 58:222/239 of query aligns to 43:196/501 of 1gpmA

query
sites
1gpmA

D

Q

V

I

R

R

D

D

I

F

D

N

P

P

D

S

G

G

I

I

V

I

V

L

S

S

P

G

G
|
G

P

P

G

E

T

S

P

T

A

T

E

E

A

E

G

N

V

S

S

P

V

R

S

A

-

P

-

Q

-

Y

V

V

F

F

R

-

D

E

L

A

D

G

Y

V

P

P

T

V

L

F

G

G

V

V

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

T

L

M

C

A

A

M

A

Q

L

L

G

G

S

G

R

H

V

V

G

E

H

A

A

S

P

N

H

E

V

R

V

E

H

F

G

G

K

Y

P

A

S

Q

L

V

V

E

E

V

H

V

D

N

G

D

A

S

G

A

V

L

F

V

S

R

G

G

L

I

P

E

D

D

R

A

I

L

E

T

V

A

-

D

G

G

R

K

-

P

Y

L

H

L

S

D

L

V

A

W

V

M

E

S

H

H

E

G

D

D

V

K

P

V

P

T

E

A

L

I

A

P

V

S

T

D

A

F

Y

I

T

T

V

V

A

A

E

S

G

T

S

E

E

S

A

C

E

-

N

-

S

-

D

-

G

-

D

-

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

P

A

F

V

A

V

I

M

M

G

A

V

-

R

-

H

N

R

E

E

E

K

K

P

R

H

F

V

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

D

R

S

Q

G

G

K

M

D

R

I

M

V

L

R

E

N

R

F

F

V

V

active site: G57 (= G72), C84 (= C97), Y85 (≠ L98), H179 (= H205), E181 (= E207)

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

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)
25% identity, 77% coverage: 46:228/239 of query aligns to 221:385/2225 of P20054

query
sites
P20054

V

V

L

V

V

P

Y

W

R

D

N

Y

D

D

A

V

L

V

S

A

T

N

D

E

D

S

V

I

R

N

D

D

I

Y

D

D

P

-

D

-

G

G

I

V

V

F

V

I

S

S

P

N

G

G

P

P

G

G

T

D

P

P

A

S

E

L

A

C

G

G

V

K

S

A

V

I

S

E

V

N

F

I

R

R

D

K

-

V

L

L

D

A

Y

L

P

P

T

V

-

A

-

K

-

A

-

V

L

F

G

G

V

V

C

C

L

M

G

G

H

N

Q

Q

S

L

L

L

C

G

A

L

A

A

L

A

G

G

S

A

R

Q

V

T

G

H

H

K

A

-

P

-

H

-

V

-

H

-

G

-

K

-

P

-

S

-

L

-

V

M

E

A

H

F

D

G

G

N

A

R

G

G

V

L

F

N

S

Q

G

P

L

C

P

V

D

D

R

Q

I

I

E

S

V

-

G

G

R

R

Y

C

H

H

S

I

L

T

A

S

V

Q

E

N

H

H

E

-

D

-

V

-

P

-

E

-

L

-

A

-

V

-

T

-

A

G

Y

F

T

V

V

I

A

D

E

S

G

N

S

S

E

L

A

P

E

A

N

G

S

S

D

G

G

W

D

K

T

T

G

Y

T

F

E

I

G

N

D

A

E

N

P

D

A

A

V

S

V

N

M

E

G

G

V

I

R

Y

H

H

R

E

E

S

K

K

P

P

H

W

V

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

A

I

M

L

A

T

G

D

P

S

T

G

D

K

T

D

E

-

Y

I

L

V

F

R

D

N

N

F

F

V

V

A

D

L

N

A

V

V

C

G

G

D

E

Sites not aligning to the query:

1 modified: N-acetylmethionine

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
27% identity, 55% coverage: 92:222/239 of query aligns to 99:207/693 of P49915

query
sites
P49915

P

P

T

V

L

L

G

G

V

I

C
|
C

L

Y

G

G

H

M

Q

Q

S

M

L

M

C

N

A

K

A

V

L

F

G

G

S

G

R

T

V

V

G

H

H

K

A

K

P

S

H

V

V

R

V

E

H

D

G

G

K

V

P

F

S

N

L

I

V

S

E

V

H

D

D

N

G

T

A

C

G

S

V

L

F

F

S

R

G

G

L

L

P

Q

D

K

R

E

I

E

E

V

V

V

G

L

R

L

Y

T

H

H

S

G

L

D

A

S

V

V

E

D

H

K

E

-

D

-

V

-

P

-

E

-

L

-

A

-

V

-

T

-

A

-

Y

-

T

-

V

V

A

A

E

D

G

G

S

F

E

K

A

V

E

V

N

A

S

R

D

S

G

G

D

N

T

-

G

-

T

-

E

-

G

-

D

-

E

-

P

-

A

-

V

I

V

V

M

A

G

G

V

I

R

A

H

N

R

E

E

S

K

K

P

K

H

L

V

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

T

T

D

E

S

N

G

G

K

K

D

V

I

I

V

L

R

K

N

N

F

F

V

L

C104 (= C97) active site, For GATase activity
H190 (= H205) active site, For GATase activity
E192 (= E207) 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

Query Sequence

>WP_004044227.1 NCBI__GCF_000337315.1:WP_004044227.1
MTRILVVDNYDSFAYNLVQYVGEAVSEARGGDESADGSSSDGSDDVLVYRNDALSTDDVR
DIDPDGIVVSPGPGTPAEAGVSVSVFRDLDYPTLGVCLGHQSLCAALGSRVGHAPHVVHG
KPSLVEHDGAGVFSGLPDRIEVGRYHSLAVEHEDVPPELAVTAYTVAEGSEAENSDGDTG
TEGDEPAVVMGVRHREKPHVGVQFHPESILTDSGKDIVRNFVALAVGDGPAAAAWEGER

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