SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012674117.1 NCBI__GCF_000021545.1:WP_012674117.1 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)
60% identity, 94% coverage: 1:187/198 of query aligns to 1:186/187 of P00903

query
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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)
51% identity, 97% coverage: 2:194/198 of query aligns to 75:272/276 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)
47% identity, 94% coverage: 3:189/198 of query aligns to 7:191/673 of 8hx8A

query
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8hx8A

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binding magnesium ion: I175 (= I173), S177 (≠ T175)

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, 95% coverage: 2:189/198 of query aligns to 4:190/193 of P00900

query
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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)
41% identity, 95% coverage: 2:189/198 of query aligns to 3:189/192 of 1i7qB

query
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1i7qB

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active site: G58 (≠ C55), C83 (= C80), L84 (= L81), H169 (= H169), E171 (= E171)
binding glutamic acid: P55 (= P52), G56 (= G53), G58 (≠ C55), C83 (= C80), L84 (= L81), Q87 (= Q84), H132 (= H129), S133 (= S130), L134 (= L131)

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
38% identity, 94% coverage: 3:189/198 of query aligns to 6:148/632 of 8hx9A

query
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8hx9A

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binding magnesium ion: S134 (≠ T175), 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
36% identity, 93% coverage: 1:185/198 of query aligns to 1:174/183 of 7yc6A

query
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7yc6A

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M

I

I

L

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

Y

K

E

Y

L

I

G

G

Q

V

D

S

V

S

L

K

V

I

K

V

R

P

N

N

D

T

E

-

I

T

T

P

V

L

E

E

D

E

I

I

K

E

R

S

M

N

D

K

N

E

V

V

D

K

A

G

I

I

V

I

I

L

S

S

P

G

G

G

P

P

C

-

T

D

P

I

N

E

E

K

A

A

G

K

I

N

S

C

V

I

D

D

V

I

I

A

K

L

E

N

F

A

K

K

G

-

V

-

Y

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

Q

L

A

A

F

Y

G

G

A

G

K

E

I

V

V

G

K

R

A

A

K

A

C

-

L

-

M

-

H

-

G

-

K

-

T

L

S

T

K

K

I

V

Y

Y

-

V

H
x
D

N

K

E

E

K

N

G

P

L

L

F

F

E

K

G

N

I

V

P

P

N

R

P

E

F

F

N

N

A

A

V

W

R

A

Y

S

H

H

S

K

L

-

V

-

I

-

D

D

E
|
E

-

V

S

K

T

K

L

V

P

P

E

E

D

G

I

F

E

E

I

I

T

L

A

A

R
x
H

S

S

D

D

D

I

G
x
C

E

Q

I

V

M

E

A

A

I

M

Q

K

H

H

K

K

K

T

Y

K

P

P

I

I

W

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

S

V

I

A

L

H

T

T

E

E

Y

Y

G

G

L

N

K

E

L

I

L

L

E

K

N

N

F

F

binding zinc ion: C76 (= C80), D101 (≠ H110), E123 (= E135), E123 (= E135), H136 (≠ R147), C140 (≠ G151), C140 (≠ G151), H158 (= H169)

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, 96% coverage: 6:196/198 of query aligns to 235:430/430 of Q9LVW7

query
sites
Q9LVW7

D

N

N

S

Y

R

D

D

S

G

F

K

T

S

Y

Y

N

K

I

V

V

I

Q

A

Y

Y

F

D

Y

F

E

G

L

I

G

K

Q

Q

D

N

V

I

L

L

V

R

K

R

R

L

N

S

D

S

-

Y

-

G

-

C

E

Q

I

I

T

T

V

V

-

V

-

P

-

S

-

T

-

F

-

P

-

A

E

E

D

A

I

L

K

K

R

M

M

-

D

-

N

N

V

P

D

D

A

G

I

I

V

L

I

F

S

S

P

N

G

G

P

P

C

G

T

D

P

P

N

S

E

A

A

V

G

P

I

Y

S

A

V

V

D

E

V

T

I

V

K

K

E

E

F

L

K

L

G

G

V

K

Y

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

Q

Q

A

A

F

L

G

G

A

G

K

K

I

T

V

F

K

K

A

M

K

K

C

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

K

P

I

V

Y

R

H

N

N

N

E

R

K

T

G

G

L

Q

F

V

E

E

G

-

I

-

P

-

N

-

P

-

F

-

N

I

A

S

V

A

R

Q

Y

N

H

H

S

N

L

Y

V

A

I

V

D

D

E

P

S

A

T

S

L

L

P

P

E

G

D

G

I

V

E

E

I

V

T

T

-

H

A

V

R

N

S

L

D

N

D

D

G

G

E

S

I

C

M

A

A

G

I

L

Q

S

H

F

K

P

K

E

Y

M

P

N

I

V

W

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

Y
x
H

G

D

L

S

-

D

K

N

L

A

L

F

E

R

N

E

F

F

I

I

H

E

L

L

A

M

E

K

K

R

A

S

K

K

T

Q

T

S

S

S

H410 (≠ Y177) mutation to Y: In ven6-1; reticulate leaf phenotype.

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
30% identity, 95% coverage: 9:197/198 of query aligns to 188:382/382 of P0A6F1

query
sites
P0A6F1

D

D

S

E

F

L

T

P

Y

F

N

H

I

V

V

V

Q

A

Y

Y

F

D

Y

F

E

G

L

A

G

K

Q

R

D

N

V

I

L

L

-

R

-

M

-

L

V

V

K

D

R

R

N

G

D

C

E

R

I

L

T

T

V

I

-

V

-

P

-

A

-

Q

-

T

-

S

-

A

E

E

D

D

I

V

K

L

R

K

M

M

D

-

N

N

V

P

D

D

A

G

I

I

V

F

I

L

S

S

P

N

G
|
G

P

P

C
x
G

T

D

P

P

N

A

E

P

A

C

G

D

I

Y

S

A

V

I

D

T

V

A

I

I

K

Q

E

K

F

F

-

L

K

E

G

T

V

D

Y

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

Q

L

A

A

F

S

G

G

A

A

K

K

I

T

V

V

K

K

A

M

K

K

C

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

K

P

I

V

Y

K

H

D

N

V

E

E

K

K

G

N

L

V

F

V

E

-

G

-

I

-

P

-

N

-

P

-

F

M

N

I

A

T

V

A

R

Q

Y
x
N

H

H

S
x
G

L
x
F

V

A

I

V

D

D

E

E

S

A

T

T

L

L

P

P

E

A

D

N

I

L

E

R

I

V

T

T

A

H

R

K

S

S

-

L

D

F

D

D

G

G

E

T

I

L

M

Q

A

G

I

I

Q

H

H

R

K

T

K

D

Y

K

P

P

I

A

W

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

Y

H

-

D

G

A

L

A

K

P

L

L

L

F

E

D

N

H

F

F

I

I

H

E

L

L

A

I

E

E

K

Q

A

Y

K

R

T

K

T

T

S

A

K

K

G241 (= G53) binding L-glutamine
G243 (≠ C55) 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)
30% identity, 94% coverage: 9:195/198 of query aligns to 187:379/379 of 1ce8B

query
sites
1ce8B

D

D

S

E

F

L

T

P

Y

F

N

H

I

V

V

V

Q

A

Y

Y

F

D

Y

F

E

G

L

A

G

K

Q

R

D

N

V

I

L

L

-

R

-

M

-

L

V

V

K

D

R

R

N

G

D

C

E

R

I

L

T

T

V

I

-

V

-

P

-

A

-

Q

-

T

-

S

-

A

E

E

D

D

I

V

K

L

R

K

M

M

D

-

N

N

V

P

D

D

A

G

I

I

V

F

I

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

N

A

E

P

A

C

G

D

I

Y

S

A

V

I

D

T

V

A

I

I

K

Q

E

K

F

F

-

L

K

E

G

T

V

D

Y

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

Q

L

A

A

F

S

G

G

A

A

K

K

I

T

V

V

K

K

A

M

K

K

C

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

K

P

I

V

Y

K

H

D

N

V

E

E

K

K

G

N

L

V

F

V

E

-

G

-

I

-

P

-

N

-

P

-

F

M

N

I

A

T

V

A

R

Q

Y

N

H

H

S

G

L

F

V

A

I

V

D

D

E

E

S

A

T

T

L

L

P

P

E

A

D

N

I

L

E

R

I

V

T

T

A

H

R

K

S

S

-

L

D

F

D

D

G

G

E

T

I

L

M

Q

A

G

I

I

Q

H

H

R

K

T

K

D

Y

K

P

P

I

A

W

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

Y

H

-

D

G

A

L

A

K

P

L

L

L

F

E

D

N

H

F

F

I

I

H

E

L

L

A

I

E

E

K

Q

A

Y

K

R

T

K

T

T

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

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)
29% identity, 94% coverage: 9:195/198 of query aligns to 187:379/379 of 1c3oB

query
sites
1c3oB

D

D

S

E

F

L

T

P

Y

F

N

H

I

V

V

V

Q

A

Y

Y

F

D

Y

F

E

G

L

A

G
x
K

Q

R

D

N

V

I

L

L

-

R

-

M

-

L

V

V

K

D

R

R

N

G

D

C

E

R

I

L

T

T

V

I

-

V

-

P

-

A

-

Q

-

T

-

S

-

A

E

E

D

D

I

V

K

L

R

K

M

M

D

-

N

N

V

P

D

D

A

G

I

I

V

F

I

L

S

S

P
x
N

G
|
G

P

P

C
x
G

T

D

P

P

N

A

E

P

A

C

G

D

I

Y

S

A

V

I

D

T

V

A

I

I

K

Q

E

K

F

F

-

L

K

E

G

T

V

D

Y

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

Q

L

A

A

F

S

G

G

A

A

K

K

I

T

V

V

K

K

A

M

K

K

C

F

L

G

M

H

H

H

G

G

K

G

T

N

S

H

K

P

I

V

Y

K

H

D

N

V

E

E

K

K

G

N

L

V

F

V

E

-

G

-

I

-

P

-

N

-

P

-

F

M

N

I

A

T

V

A

R

Q

Y
x
N

H
|
H

S
x
G

L
x
F

V

A

I

V

D

D

E

E

S

A

T

T

L

L

P

P

E

A

D

N

I

L

E

R

I

V

T

T

A

H

R

K

S

S

-

L

D

F

D

D

G

G

E

T

I

L

M

Q

A

G

I

I

Q

H

H

R

K

T

K

D

Y

K

P

P

I

A

W

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

Y

H

-

D

G

A

L

A

K

P

L

L

L

F

E

D

N

H

F

F

I

I

H

E

L

L

A

I

E

E

K

Q

A

Y

K

R

T

K

T

T

active site: K201 (≠ G23), S268 (≠ C80), H352 (= H169), E354 (= E171)
binding glutamine: N239 (≠ P52), G240 (= G53), G242 (≠ C55), S268 (≠ C80), L269 (= L81), N310 (≠ Y128), H311 (= H129), G312 (≠ S130), F313 (≠ L131)

Sites not aligning to the query:

binding glutamine: 46

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
28% identity, 95% coverage: 1:189/198 of query aligns to 1:184/475 of 2ywcA

query
sites
2ywcA

M

M

I

V

L

L

M

V

I

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

Y

R

E

E

L

L

G

R

Q

A

D

F

V

S

L

L

V

I

K

L

R

P

N

G

D

D

E

A

I

P

T

L

V

E

E

E

D

V

I

L

K

K

R

H

M

R

D

P

N

Q

V

-

D

-

A

A

I

L

V

I

I

L

S

S

P

G

G
|
G

P

P

C
x
R

T

S

P

V

N

F

E

D

A

P

G

D

I

A

S

P

V

R

D

P

V

D

I

P

K

R

E

L

F

F

K

S

G

S

V

G

Y

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

Q

Q

A

E

F

L

G

G

A

G

K

R

I

V

V

E

K

R

A

A

K

G

C

R

L

A

M

E

H

Y

G

G

K

K

T

A

S

L

K

L

I

T

Y

R

H

H

N

-

E

E

K

G

G

P

L

L

F

F

E

R

G

G

I

L

P

E

N

G

P

E

F

V

N

Q

A

V

V

W

R

M

Y

S

H

H

S

Q

L

D

V

A

I

V

D

-

E

-

S

T

T

A

L

P

P

P

E

P

D

G

I

W

E

R

I

V

T

V

A

A

R

E

S

T

D

E

G

N

E

P

I

V

M

A

A

A

I

I

Q

A

H

S

K

P

K

D

Y

G

P

R

I

A

W

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

T

T

E

P

Y

K

G

G

L

M

K

Q

L

I

L

L

E

E

N

N

F

F

I

L

H

E

L

L

A

A

active site: G51 (= G53), R53 (≠ C55), 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

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)
30% identity, 86% coverage: 2:172/198 of query aligns to 265:425/2244 of Q09794

query
sites
Q09794

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Sites not aligning to the query:

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

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)
31% identity, 64% coverage: 46:171/198 of query aligns to 219:341/2198 of Q18990

query
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Q18990

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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.

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, 73% coverage: 27:171/198 of query aligns to 193:338/2225 of P27708

query
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P27708

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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)
30% identity, 65% coverage: 43:171/198 of query aligns to 230:355/2224 of P05990

query
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P05990

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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, 80% coverage: 13:171/198 of query aligns to 187:338/2225 of P08955

query
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P08955

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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.

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
28% identity, 81% coverage: 34:193/198 of query aligns to 35:222/517 of 3uowA

query
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active site: G53 (= G53), C84 (= C80), Y85 (≠ L81), H198 (= H169), E200 (= E171)

Sites not aligning to the query:

active site: 255, 381
binding xanthosine-5'-monophosphate: 325, 404, 405, 406, 446, 509, 513, 514, 515

P07258 Carbamoyl phosphate synthase arginine-specific small chain; CPS; CPSase; CPSase-arg; Arginine-specific carbamoyl phosphate synthetase, glutamine chain; Carbamoyl phosphate synthase A; CPS-A; Glutamine-dependent carbamoyl phosphate synthetase; EC 6.3.5.5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
31% identity, 74% coverage: 27:172/198 of query aligns to 201:352/411 of P07258

query
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P07258

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-

K

-

P

-

Y

-

F

I

V

E

N

I

L

T

N

A

D

R

K

S

S

D

N

D

E

G

G

E

M

I

I

M

-

A

-

I

-

Q

-

H

H

K

L

K

Q

Y

R

P

P

I

I

W

F

G

S

V

T

Q

Q

F

F

H
|
H

P

P

E

E

S

A

C264 (= C80) mutation to D: Abolishes glutamine-dependent CPSase activity.
H307 (= H129) mutation to D: Abolishes glutamine-dependent CPSase activity.
H349 (= H169) mutation to D: Abolishes glutamine-dependent CPSase activity.

Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
28% identity, 81% coverage: 34:193/198 of query aligns to 40:232/555 of Q8IJR9

query
sites
Q8IJR9

I

V

T

E

V

L

E

K

D

D

I

I

K

K

R

D

M

M

D

-

N

N

V

I

D

K

A

G

I

V

V

I

I

L

S

S

P

G

G

G

P

P

C

Y

T

S

P

V

N

T

E

E

A

A

G

G

-

S

-

P

-

H

I

L

S

K

V

K

D

E

V

V

I

F

K

E

E

Y

F

F

-

L

K

E

G

K

V

K

Y

I

P

P

I

I

L

F

G

G

V

I

C
|
C

L

Y

G

G

H

M

Q
|
Q

S

E

I

I

G

A

Q

V

A

Q

F

M

G

N

A

G

K

E

I

V

V

K

K

K

A

S

K

K

-

T

-

S

-

E

-

Y

-

G

-
x
C

-

T

-

D

-

V

-

N

-

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

C

C

L

R

M

N

H

F

G

G

K

D

T

S

S

S

K

S

-

A

-

M

-

D

I

L

Y

Y

H

S

N

N

E

Y

K

K

-

L

-

M

-

N

-

E

-

T

-

C

G

C

L

L

F

F

E

E

G

N

I

I

P
x
K

N

S

P

D

F

I

N

T

A

T

V

V

R
x
W

Y

M

H
x
N

S

H

L

-

V

-

I

N

D
|
D

E

E

S

V

T

T

-

K

L

I

P

P

E

E

D

N

I

F

E

Y

I

L

T

V

A

S

R

S

S

S

D

E

D

N

G

C

E

L

I

I

M

C

A

S

I

I

Q

Y

H

N

K

K

K

E

Y

Y

P

N

I

I

W

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E

E

S

V

I
x
Y

L
x
E

T

S

E

L

Y

D

G

G

L

E

K

L

L

M

L

F

E

Y

N

N

F

F

I

A

H

Y

L

N

A

I

E

C

K

K

A

C

K

K

C89 (= C80) mutation to A: Loss of glutaminase activity, however, glutamine binding is not affected. In presence of exogenous ammonia, the amination of XMP to produce GMP is normal. 2.3-fold decrease in affinity for ATP and 1.8-fold decrease in affinity for XMP. 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-113.
Q93 (= Q84) binding L-glutamine
C113 (vs. gap) mutation to A: 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-89.
K160 (≠ P120) mutation to L: No effect on glutaminase activity. 1.2-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
W167 (≠ R127) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ H129) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D134) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H169) binding L-glutamine
Y212 (≠ I173) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ L174) mutation to A: 40 percent decrease in glutaminase activity. 1.4-fold decrease in affinity for glutamine. 1.3-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.

Sites not aligning to the query:

18 Y→F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
20 H→A: Slight decrease in affinity for glutamine. 1.8-fold increase in affinity for ATP. Slight increase in affinity for XMP. Moderate reduction in glutaminase activity.
24 K→L: 50 percent decrease in glutaminase activity. 5.3-fold decrease in affinity for glutamine. 1.7-fold increase in affinity for ATP. 2.8-fold decrease in affinity for XMP.
25 R→L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
336 binding XMP
371 Important for ATPPase activity; D→A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
374 E→L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
376 K→L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
386 K→L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
387 T→A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
388 Important for ATPPase activity; H→A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
389 Important for ATPPase activity; H→A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
390 N→A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
411 K→L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
412 D→A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
413 D→A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
415 K→L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
476 binding XMP
539 R→L: 85 percent decrease in glutaminase activity.
547 binding XMP; K→L: 85 percent decrease in glutaminase activity.
552 binding XMP
553 binding XMP; E→L: 85 percent decrease in glutaminase activity.
555 E→L: 20 percent decrease in glutaminase activity. No effect on GMP formation.

Query Sequence

>WP_012674117.1 NCBI__GCF_000021545.1:WP_012674117.1
MILMIDNYDSFTYNIVQYFYELGQDVLVKRNDEITVEDIKRMDNVDAIVISPGPCTPNEA
GISVDVIKEFKGVYPILGVCLGHQSIGQAFGAKIVKAKCLMHGKTSKIYHNEKGLFEGIP
NPFNAVRYHSLVIDESTLPEDIEITARSDDGEIMAIQHKKYPIWGVQFHPESILTEYGLK
LLENFIHLAEKAKTTSKQ

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