SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Pf1N1B4_2547 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2547 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)
64% identity, 97% coverage: 1:192/197 of query aligns to 1:187/187 of P00903

query
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P00903

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C79 (= C79) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H173) mutation to Q: Loss of activity.
E170 (= E175) 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, 96% coverage: 2:191/197 of query aligns to 75:265/276 of Q42565

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Q42565

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G150 (= G77) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G102) 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)
41% identity, 97% coverage: 2:193/197 of query aligns to 4:186/193 of P00900

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P00900

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C84 (= C79) 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, 97% coverage: 2:193/197 of query aligns to 3:185/192 of 1i7qB

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1i7qB

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active site: G58 (≠ C54), C83 (= C79), L84 (= L80), H169 (= H173), E171 (= E175)
binding glutamic acid: P55 (= P51), G56 (= G52), P57 (= P53), G58 (≠ C54), C83 (= C79), L84 (= L80), Q87 (= Q83), Y131 (= Y127), H132 (= H128), S133 (= S129), L134 (= L130), H169 (= H173)

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)
32% identity, 83% coverage: 14:176/197 of query aligns to 254:405/430 of Q9LVW7

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Q9LVW7

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Sites not aligning to the query:

410 H→Y: In ven6-1; reticulate leaf phenotype.

7yc6A GMP synthase [glutamine-hydrolyzing] subunit A
33% identity, 98% coverage: 1:194/197 of query aligns to 1:179/183 of 7yc6A

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binding zinc ion: C76 (= C79), D101 (≠ G102), E123 (≠ I131), E123 (≠ I131), H136 (≠ W146), C140 (≠ D155), C140 (≠ D155), H158 (= H173)

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
27% identity, 100% coverage: 1:197/197 of query aligns to 1:188/475 of 2ywcA

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2ywcA

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I

V

L

R

P

N

G

D

D

E

A

L

-

T

P

I

L

A

E

E

E

I

V

E

L

A

K

L

H

N

R

P

P

E

Q

R

A

I

L

V

I

V

L

S

S

P

G

G
|
G

P

P

C
x
R

T

S

P

V

T

F

E

D

A

P

G

D

I

A

S

P

I

R

E

P

A

D

I

P

K

R

H

L

F

F

A

S

G

S

K

G

L

L

P

P

I

L

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

L

I

L

G

A

Q

Q

A

E

F

L

G

G

D

R

V

V

V

E

R

R

A

A

R

G

Q

R

V

A

M

E

H

Y

G

G

K

K

T

A

S

L

P

L

V

T

F

R

H

H

E

E

D

G

K

P

G

-

V

L

F

F

E

R

G

G

L

L

N

E

R

G

P

E

L

V

T

Q

V

V

T

W

R

M

Y

S

H

H

S

Q

L

D

I

A

V

V

K

-

R

-

E

-

T

T

L

A

P

P

D

P

C

-

L

-

E

-

L

-

T

P

A

G

W

W

T

R

Q

V

L

V

E

A

D

E

G

T

S

E

V

E

D

N

E

P

I

V

M

A

G

A

L

I

R

A

H

S

K

P

T

D

L

G

N

R

I

A

E

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

T

T

E

P

Q

K

G

G

H

M

E

Q

L

I

F

L

A

E

N

N

F

F

L

L

K

E

Q

L

T

A

G

G

G

V

T

K

R

R

active site: G51 (= G52), R53 (≠ C54), C78 (= C79), Y79 (≠ L80), H164 (= H173), E166 (= E175)

Sites not aligning to the query:

active site: 221, 343
binding xanthosine-5'-monophosphate: 288, 366, 367, 368, 408, 430, 467, 471, 472, 473

1jdbF Carbamoyl phosphate synthetase from escherichia coli (see paper)
28% identity, 83% coverage: 14:176/197 of query aligns to 203:355/380 of 1jdbF

query
sites
1jdbF

N

N

V

I

V

L

Q

R

Y

M

L

L

G

V

E

D

L

R

G

G

S

C

E

R

V

L

K

T

V

I

V

V

R

P

N

A

D

-

E

Q

L

T

T

S

I

A

A

E

E

D

I

V

E

L

A

K

L

M

N

N

P

P

E

D

R

G

I

I

V

F

V

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

A

E

P

A

C

G

D

I

Y

S

A

I

I

E

T

A

A

I

I

K

Q

H

K

F

F

-

L

A

E

G

T

K

D

L

I

P

P

I

V

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

D

K

V

T

V

V

R

K

A

M

R

K

Q

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

V

V

F

K

H

D

E

V

D

E

K

K

G

N

V

V

F

V

E

-

G

-

L

-

N

-

R

-

P

-

L

M

T

I

V

T

T

A

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

K

D

R

E

E

A

T

T

L

L

P

P

D

A

C

N

L

L

E

R

L

V

T

T

A

-

W

H

T

K

Q

S

L

L

E

F

D

D

G

G

S

T

V

L

D

Q

E

G

I

I

M

H

G

R

L

T

R

D

H

K

K

P

T

A

L

F

N

S

I

F

E

Q

G

G

V

-

Q

-

F

-

H
|
H

P

P

E
|
E

S

A

active site: C268 (= C79), H352 (= H173), E354 (= E175)

Sites not aligning to the query:

binding glutamine: 119, 122

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
28% identity, 83% coverage: 14:176/197 of query aligns to 203:355/379 of 1ce8B

query
sites
1ce8B

N

N

V

I

V

L

Q

R

Y

M

L

L

G

V

E

D

L

R

G

G

S

C

E

R

V

L

K

T

V

I

V

V

R

P

N

A

D

-

E

Q

L

T

T

S

I

A

A

E

E

D

I

V

E

L

A

K

L

M

N

N

P

P

E

D

R

G

I

I

V

F

V

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

A

E

P

A

C

G

D

I

Y

S

A

I

I

E

T

A

A

I

I

K

Q

H

K

F

F

-

L

A

E

G

T

K

D

L

I

P

P

I

V

L

F

G

G

V

I

C
|
C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

S

G

G

G

A

D

K

V

T

V

V

R

K

A

M

R

K

Q

F

V

G

M

H

H

H

G

G

K

G

T

N

S

H

P

P

V

V

F

K

H

D

E

V

D

E

K

K

G

N

V

V

F

V

E

-

G

-

L

-

N

-

R

-

P

-

L

M

T

I

V

T

T

A

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

K

D

R

E

E

A

T

T

L

L

P

P

D

A

C

N

L

L

E

R

L

V

T

T

A

-

W

H

T

K

Q

S

L

L

E

F

D

D

G

G

S

T

V

L

D

Q

E

G

I

I

M

H

G

R

L

T

R

D

H

K

K

P

T

A

L

F

N

S

I

F

E

Q

G

G

V

-

Q

-

F

-

H
|
H

P

P

E
|
E

S

A

active site: C268 (= C79), H352 (= H173), E354 (= E175)

Sites not aligning to the query:

binding L-ornithine: 119, 122

P08955 CAD protein; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
26% identity, 93% coverage: 11:193/197 of query aligns to 185:356/2225 of P08955

query
sites
P08955

F

L

T

K

Y

Y

N

N

V

Q

V

I

Q

R

Y

C

L

L

G

C

E

Q

L

L

G

G

S

A

E

E

V

V

K

T

V

V

R

P

N

W

D

N

E

H

L

-

T

-

I

-

A

-

E

E

I

L

E

D

A

S

L

Q

N

K

P

Y

E

D

R

G

I

L

V

F

V

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

A

E

S

-

Y

A

P

G

G

I

V

-

V

-

A

S

T

I

L

E

N

A

R

I

V

K

L

H

S

F

E

A

P

G

N

K

P

L

R

P

P

I

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

I

G

G

G

A

D

K

V

T

V

Y

R

K

A

M

R

R

Q

Y

V

G

M

N

H

R

G

G

K

H

T

N

S

Q

P

P

V

C

F

-

H

-

E

-

D

-

K

-

G

-

V

L

F

L

E

V

G

G

L

T

N

G

R

R

P

C

L

F

T

L

V

T

T

S

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

K

D

R

A

E

D

T

S

L

L

P

P

D

-

C

-

L

-

E

-

L

-

T

A

A

G

W

W

T

T

Q

P

L

L

E

F

D

T

G

N

S

A

V

N

D

D

-

C

E

S

I

N

M

E

G

G

L

I

R

V

H

H

K

D

T

S

L

L

N

P

I

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

R

L

A

T

G

E

P

Q

S

G

D

H

M

E

E

L

L

F

L

A

F

N

D

F

V

L

F

K

L

Q

E

T

T

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.

P27708 CAD protein; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
27% identity, 93% coverage: 11:193/197 of query aligns to 185:356/2225 of P27708

query
sites
P27708

F

L

T

K

Y

Y

N

N

V

Q

V

I

Q

R

Y

C

L

L

G

C

E

Q

L

R

G

G

S

A

E

E

V

V

K

T

V

V

R

P

N

W

D

D

E

H

L

-

T

-

I

-

A

-

E

A

I

L

E

D

A

S

L

Q

N

E

P

Y

E

E

R

G

I

L

V

F

V

L

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

A

E

S

A

Y

G

P

I

S

S

V

I

V

E

S

A

T

I

L

K

S

H

R

F

V

A

L

G

S

K

E

-

P

-

N

-

P

L

R

P

P

I

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

L

A

A

F

I

G

G

G

A

D

K

V

T

V

Y

R

K

A

M

R

R

Q

Y

V

G

M

N

H

R

G

G

K

H

T

N

S

Q

P

P

V

C

F

-

H

-

E

-

D

-

K

-

G

-

V

L

F

L

E

V

G

G

L

S

N

G

R

R

P

C

L

F

T

L

V

T

T

S

R

Q

Y

N

H

H

S

G

L

F

I

A

V

V

K

E

R

T

E

D

T

S

L

L

P

P

-

A

D

D

C

W

L

A

E

P

L

L

T

-

A

-

W

F

T

T

Q

N

L

A

E

N

D

D

G

G

S

S

V

N

D

E

E

-

I

-

M

-

G

G

L

I

R

V

H

H

K

N

T

S

L

L

N

P

I

F

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

Q

L

A

T

G

E

P

Q

S

G

D

H

M

E

E

L

L

F

L

A

F

N

D

F

I

L

F

K

L

Q

E

T

T

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
33 M → R: in DEE50; unknown pathological 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 ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
1473 binding ; H→A: No zinc-binding and no catalytic activity.
1475 binding
1505 binding
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 ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
1613 binding ; C→S: Reduces dihydroorotase activity.
1614 binding ; H→A: Abolishes dihydroorotase activity.
1637 binding ; E→T: Abolishes dihydroorotase activity.
1642 H→N: 11.5% of wild-type catalytic activity.
1661 binding
1686 binding ; binding ; D→N: Abolishes dihydroorotase activity.
1690 binding ; H→N: 3% of wild-type catalytic activity.
1789:2225 natural variant: Missing (in DEE50; unknown pathological 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

1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
28% identity, 96% coverage: 2:191/197 of query aligns to 8:197/501 of 1gpmA

query
sites
1gpmA

L

I

L

L

M

I

I

L

D

D

N

F

Y

G

D

S

S

Q

F

Y

T

T

Y

Q

N

L

V

V

V

A

Q

R

Y

R

L

V

G

R

E

E

L

L

G

G

S

V

E

Y

V

C

K

E

V

L

V

W

R

A

N

W

D

D

E

-

L

V

T

T

I

E

A

A

E

Q

I

I

E

R

A

D

L

F

N

N

P

P

E

S

R

G

I

I

V

I

V

L

S

S

P

G

G
|
G

P

P

C

E

T

S

P

T

T

T

E

E

A

E

G

N

I

S

S

P

I

R

E

A

A

P

I

Q

K

Y

H

V

F

F

A

E

G

A

K

G

L

V

P

P

I

V

L

F

G

G

V

V

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

T

I

M

G

A

Q

M

A

Q

F

L

G

G

D

H

V

V

V

E

R

A

A

S

R

N

Q

E

V

R

M

E

H

F

G

G

K

Y

T

A

S

Q

P

V

V

E

F

V

H

V

E

N

D

D

K

S

G

A

V

L

F

V

E

R

G

G

L

I

N

E

R

D

P

A

L

L

T

T

V

A

T

D

R

G

Y

K

H

P

S

L

L

L

I

D

V

V

-

W

-

M

-

S

-

H

-

G

-

D

K

K

R

V

E

T

T

A

L

I

P

P

D

S

C

D

L

F

E

I

L

T

T

V

A

A

W

S

T

T

Q

E

L

-

E

-

D

-

G

S

S

C

V

P

D

F

E

A

I

I

M

M

G

A

L

N

R

E

H

E

K

K

T

R

L

F

N

Y

I

-

E

-

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

E

R

Q

Q

G

G

H

M

E

R

L

M

F

L

A

E

N

R

F

F

L

V

K

R

active site: G57 (= G52), C84 (= C79), Y85 (≠ L80), H179 (= H173), E181 (= E175)

Sites not aligning to the query:

active site: 237, 357
binding adenosine monophosphate: 231, 232, 233, 238, 256, 257, 258, 313
binding pyrophosphate 2-: 233, 235, 236, 237, 238, 357

5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
28% identity, 84% coverage: 33:197/197 of query aligns to 36:195/490 of 5tw7F

query
sites
5tw7F

E

D

L

M

T

P

I

L

A

D

E

E

I

I

E

K

A

A

L

F

N

N

P

P

E

K

R

G

I

I

V

I

V

L

S

S

P

G

G
|
G

P

P

C

N

T

S

P

V

T

Y

E

E

A

S

G

D

I

Y

S

Q

I

A

E

D

A

T

I

-

K

G

H

I

F

F

A

D

G

L

K

G

L

I

P

P

I

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

F

I

M

G

A

Q

H

A

H

F

L

G

G

D

E

V

V

V

Q

R

P

A

G

R

N

Q

Q

V

R

M

E

H

F

G

G

K

-

T

Y

S

A

P

Q

V

V

F

K

H

T

E

I

D

D

K

S

G

G

V

L

F

T

E

R

G

G

L

I

-

Q

-

D

N

D

R

A

P

P

L

N

T

T

V

L

T

D

R

V

Y

W

H

M

S

S

L

H

I

G

V

D

K

K

R

V

E

S

T

K

L

L

P

P

D

D

C

G

L

F

E

A

L

V

T

I

A

G

W

-

T

-

Q

-

L

-

E

-

D

D

G

T

S

P

V

S

D

C

E

P

I

I

M

A

G

M

L

M

R

E

H

N

K

T

T

E

L

K

N

Q

I

F

E

Y

G

G

V

I

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

T

T

E

K

Q

Q

G

G

H

R

E

A

L

L

F

L

A

N

N

R

F

F

L

V

K

L

Q

D

T

I

G

C

G

G

T

A

R

Q

active site: G55 (= G52), C81 (= C79), Y82 (≠ L80), H171 (= H173), E173 (= E175)

Sites not aligning to the query:

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

P05990 CAD protein; Protein rudimentary; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
28% identity, 79% coverage: 37:191/197 of query aligns to 225:372/2224 of P05990

query
sites
P05990

A

A

E

R

I

L

E

E

A

D

L

E

N

Q

P

F

E

D

R

A

I

L

V

F

V

L

S

S

P

N

G

G

P

P

C

G

T

N

P

P

T

E

E

S

A

C

G

D

I

Q

S

I

I

V

E

Q

A

Q

I

V

K

R

H

K

F

V

-

I

-

E

A

E

G

G

K

Q

L

K

P

P

I

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

L

G

A

Q

K

A

A

F

I

G

G

G

C

D

S

V

T

V

Y

R

K

A

M

R

K

Q

Y

V

G

M

N

H

R

G

G

K

H

T

N

S

L

P

P

V

C

F

L

H

H

E

R

D

A

K

T

G

G

V

-

F

-

E

-

G

-

L

-

N

-

R

R

P

C

L

L

T

M

V

T

T

S

R

Q

Y

N

H

H

S

G

L

Y

I

A

V

V

K

D

R

L

E

E

T

Q

L

L

P

P

D

D

C

-

L

-

E

-

L

-

T

-

A

G

W

W

T

S

Q

E

L

L

-

F

-

V

-

N

-

A

E

N

D

D

G

G

S

T

V

N

D

E

E

-

I

-

M

-

G

G

L

I

R

V

H

H

K

A

T

S

L

K

N

P

I

Y

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

H

I

H

L

A

T

G

E

P

Q

Q

G

D

H

T

E

E

-

F

L

L

F

F

A

D

N

V

F

F

L

M

K

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

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
27% identity, 78% coverage: 36:189/197 of query aligns to 37:214/517 of 3uowA

query
sites
3uowA

I

L

A

K

E

D

I

I

E

K

A

D

L

M

N

N

P

I

E

K

R

G

I

V

V

I

V

L

S

S

P

G

G
|
G

P

P

C

Y

T

S

P

V

T

T

E

E

A

A

G

G

-

S

-

P

-

H

I

L

S

K

I

K

E

E

A

V

I

F

K

E

H

Y

F

F

-

L

A

E

G

K

K

K

L

I

P

P

I

I

L

F

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

E

I

I

G

A

Q

V

A

Q

F

M

G

N

G

G

D

E

V

V

V

K

R

K

A

S

R

K

Q

T

V

S

M

E

H

Y

G

G

K

C

T

T

S

-

P

-

V

-

F

-

H

-

E

-

D

D

K

V

G

N

V

I

F

L

E

R

G

N

L

D

N

N

-

I

R

N

P

N

L

I

T

T

V

Y

T

C

R

R

Y

N

H

F

S

S

-

S

-

A

-

M

-

D

L

L

I

Y

V

S

K

N

R

Y

E

K

T

L

L

M

P

N

D

C

C

C

L

L

E

F

-

E

-

N

-

I

-

K

-

S

-

D

-

I

L

T

T

T

A

V

W

W

T

M

Q

N

L

H

E

N

D

D

G

E

-

V

-

T

-

K

-

I

-

P

-

E

-

N

-

F

-

Y

-

L

-

V

S

S

V

S

D

S

E

E

-

N

-

C

-

L

I

I

M

C

G

S

L

I

R

Y

H

N

K

K

T

E

L

Y

N

N

I

I

E

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

S

V

I

Y

L

E

T

S

E

L

Q

D

G

G

H

E

E

L

L

M

F

F

A

Y

N

N

F

F

active site: G53 (= G52), C84 (= C79), Y85 (≠ L80), H198 (= H173), E200 (= E175)

Sites not aligning to the query:

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

P20054 Protein PYR1-3; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Dictyostelium discoideum (Social amoeba)
26% identity, 92% coverage: 14:195/197 of query aligns to 207:384/2225 of P20054

query
sites
P20054

N

N

V

Q

V

I

Q

R

Y

C

L

L

G

L

E

N

L

R

G

G

S

V

E

D

V

L

K

K

V

V

R

P

N

W

D

D

E

Y

L

D

T

V

I

V

A

A

E

N

I

E

E

S

A

I

L

N

N

D

P

Y

E

D

R

G

I

V

V

F

V

I

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

S

E

L

A

C

G

G

I

K

S

A

I

I

E

E

A

N

I

I

K

R

H

K

F

V

A

L

G

A

K

-

L

L

P

P

-

V

-

A

-

K

-

A

I

V

L

F

G

G

V

V

C

C

L

M

G

G

H

N

Q

Q

S

L

I

L

G

G

Q

L

A

A

F

A

G

G

G

A

D

Q

V

T

V

H

R

K

A

M

R

A

Q

F

V

G

M

N

H

R

G

G

K

L

T

N

S

Q

P

P

V

C

F

V

H

D

E

Q

D

I

K

S

G

G

V

-

F

-

E

-

G

-

L

-

N

-

R

R

P

C

L

H

T

I

V

T

T

S

R

Q

Y

N

H

H

S

G

L

F

I

V

V

I

K

D

R

S

E

N

T

S

L

L

P

P

D

A

C

G

L

-

E

-

L

-

T

S

A

G

W

W

-

K

T

T

Q

Y

L

F

E

I

D

N

G

A

S

N

V

D

D

A

E

S

I

N

M

E

G

G

L

I

R

Y

H

H

K

E

T

S

L

K

N

P

I

W

E

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

S

A

I

M

L

A

T

G

E

P

Q

T

G

D

H

T

E

E

-

Y

L

L

F

F

A

D

N

N

F

F

L

V

K

D

Q

N

T

V

G

C

G

G

Sites not aligning to the query:

1 modified: N-acetylmethionine

Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
25% identity, 78% coverage: 36:189/197 of query aligns to 42:224/555 of Q8IJR9

query
sites
Q8IJR9

I

L

A

K

E

D

I

I

E

K

A

D

L

M

N

N

P

I

E

K

R

G

I

V

V

I

V

L

S

S

P

G

G

G

P

P

C

Y

T

S

P

V

T

T

E

E

A

A

G

G

-

S

-

P

-

H

I

L

S

K

I

K

E

E

A

V

I

F

K

E

H

Y

F

F

-

L

A

E

G

K

K

K

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P

P

I

I

L

F

G

G

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I

C
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C

L

Y

G

G

H

M

Q
|
Q

S

E

I

I

G

A

Q

V

A

Q

F

M

G

N

G

G

D

E

V

V

V

K

R

K

A

S

R

K

Q

T

V

S

M

E

H

Y

G

G

K
x
C

T

T

S

D

P

V

V

N

F

I

H

L

E

R

D

N

K

D

G

N

V

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

F

F

E

G

G

D

L

S

N

S

R

S

P

A

L

M

T

D

V

L

T

Y

R

S

Y

N

H

Y

S

K

L

L

I

M

V

N

K

E

R

T

E

C

T

C

L

L

P

F

D

E

C

N

L

I

E
x
K

-

S

-

D

-

I

L

T

T

T

A

V

W
|
W

T

M

Q
x
N

L

H

E

N

D
|
D

G

E

-

V

-

T

-

K

-

I

-

P

-

E

-

N

-

F

-

Y

-

L

-

V

S

S

V

S

D

S

E

E

-

N

-

C

-

L

I

I

M

C

G

S

L

I

R

Y

H

N

K

K

T

E

L

Y

N

N

I

I

E

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

Q

D

G

G

H

E

E

L

L

M

F

F

A

Y

N

N

F

F

C89 (= C79) 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 (= Q83) binding
C113 (≠ K103) 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 (≠ E142) 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 (= W146) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ Q148) binding ; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D151) binding ; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H173) binding
Y212 (≠ I177) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ L178) 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
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
539 R→L: 85 percent decrease in glutaminase activity.
547 binding ; K→L: 85 percent decrease in glutaminase activity.
552 binding
553 binding ; E→L: 85 percent decrease in glutaminase activity.
555 E→L: 20 percent decrease in glutaminase activity. No effect on GMP formation.

2vxoB Human gmp synthetase in complex with xmp (see paper)
30% identity, 62% coverage: 74:195/197 of query aligns to 77:187/658 of 2vxoB

query
sites
2vxoB

P

P

I

V

L

L

G

G

V

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

S

M

I

M

G

N

Q

K

A

V

F

F

G

G

D

T

V

V

V

-

R

-

A

-

R

-

Q

-

V

-

M

-

H

H

G

K

K

K

T

S

S

D

P

G

V

V

F

F

H

N

-

I

-

S

-

V

-

D

E

N

D

T

K

C

G

S

V

L

F

F

E

R

G

G

L

L

N

Q

R

K

P

E

L

E

T

V

V

V

T

L

R

L

Y

T

H

H

S

G

L

D

I

S

V

V

K

D

R

K

E

-

T

-

L

V

P

A

D

D

C

G

L

F

E

K

L

V

T

V

A

A

W

R

T

S

Q

-

L

-

E

-

D

-

G

G

S

N

V

I

D

-

E

-

I

V

M

A

G

G

L

I

R

A

H

N

K

E

T

S

L

K

N

K

I

L

E

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

T

T

E

E

Q

N

G

G

H

K

E

V

L

I

F

L

A

K

N

N

F

F

L

L

K

Y

Q

D

T

I

G

A

G

G

active site: C82 (= C79), Y83 (≠ L80), H165 (= H173), E167 (= E175)

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

P07259 Protein URA2; EC 6.3.5.5; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 83% coverage: 13:176/197 of query aligns to 238:389/2214 of P07259

query
sites
P07259

Y

Y

N

N

V

Q

V

I

Q

R

Y

C

L

F

G

I

E

K

L

R

G

G

S

V

E

E

V

L

K

K

V

V

-

P

R

W

N

N

D

Y

E

D

L

F

T

T

I

K

A

E

E

D

I

Y

E

D

A

G

L

L

N

-

P

-

E

-

R

-

I

-

V

F

V

I

S

S

P

N

G

G

P

P

C

G

T

D

P

P

T

S

E

V

A

L

G

D

I

D

S

L

I

S

E

Q

A

R

I

L

K

S

H

N

F

V

-

L

-

E

A

A

G

K

K

K

L

T

P

P

I

V

L

F

G

G

V

I

C

C

L

L

G

G

H

H

Q

Q

S

L

I

I

G

A

Q

R

A

A

F

A

G

G

G

A

D

S

V

T

V

L

R

K

A

L

R

K

Q

F

V

G

M

N

H

R

G

G

K

H

T

N

S

I

P

P

V

C

F

T

H

S

E

T

D

I

K

S

G

G

V

-

F

-

E

-

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D

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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)
29% identity, 62% coverage: 74:195/197 of query aligns to 99:212/693 of P49915

query
sites
P49915

P

P

I

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G

G

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C
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C

L

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G

G

H

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F

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G

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V

V

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K

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H

D

G

G

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P

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E

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D

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H

H

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A

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-

L

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D

-

G

G

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A

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H
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H

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T

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E

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N

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F

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Y

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G

G

C104 (= C79) active site, For GATase activity
H190 (= H173) active site, For GATase activity
E192 (= E175) active site, For GATase activity

Sites not aligning to the query:

337 binding
522 binding
610 binding
685 binding
691 binding

Query Sequence

>Pf1N1B4_2547 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2547
MLLMIDNYDSFTYNVVQYLGELGSEVKVVRNDELTIAEIEALNPERIVVSPGPCTPTEAG
ISIEAIKHFAGKLPILGVCLGHQSIGQAFGGDVVRARQVMHGKTSPVFHEDKGVFEGLNR
PLTVTRYHSLIVKRETLPDCLELTAWTQLEDGSVDEIMGLRHKTLNIEGVQFHPESILTE
QGHELFANFLKQTGGTR

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