SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Pf6N2E2_1463 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1463 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 4 hits to proteins with known functional sites (download)

Q51507 Isochorismate pyruvate lyase; IPL; Chorismate mutase; CM; Salicylate biosynthesis protein; EC 4.2.99.21; EC 5.4.99.5 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 5 papers)
45% identity, 92% coverage: 1:85/92 of query aligns to 10:94/101 of Q51507

query
sites
Q51507

M

L

E

A

D

D

I

I

R
|
R

R

E

E

A

I

I

D

D

A

R

L

I

D

D

Q

L

A

D

V

I

I

V

T

Q

L

A

L

L

G

G

K

R

R
|
R

Y

M

Q

D

Y

Y

V

V

L

K

A
|
A

A

A

S

S

K

R

F

F

K
|
K

T
x
A

S

S

V

E

T

A

S

A

V

I

Q

P

A

A

P

P

E

E

R

R

L

V

K

A

A

A

M

M

L

L

A

P

T

E

R

R

R

A

E

R

W

W

A

A

E

E

A

E

E

N

G

G

L

L

S

D

P

A

D

P

A

F

I

V

E

E

K

G

L

L

Y

F

S

A

D

Q

L

I

V

I

H

H

H

W

F

Y

I
|
I

A

A

E

E

E
x
Q

M

I

K

K

R

Y

W

W

R14 (= R5) binding
R31 (= R22) binding
A37 (= A28) mutation to I: Increases the rate constant for the mutase activity by a factor of 1000, and also increases the lyase catalytic efficiency by a factor of 6.
K42 (= K33) binding ; mutation to A: Active across the entire pH range from 4 to 9. 11-fold reduction of the affinity for isochorismate and 7-fold reduction of the catalytic efficiency for lyase activity. 6-fold reduction of the affinity for chorismate and 15-fold reduction of the catalytic efficiency for mutase activity.; mutation to E: Loss of both lyase and mutase activity at any pH tested.; mutation to H: At pH 5, 15-fold reduction of the affinity for isochorismate, but only a slight reduction of the catalytic efficiency for lyase activity. At pH 7.5, 13-fold reduction of the affinity for isochorismate and 4-fold reduction of the catalytic efficiency for lyase activity. At pH 5, strong reduction of the affinity for chorismate, but only a 2-fold reduction of the catalytic efficiency for mutase activity. At pH 7.5, strong reduction of the affinity for chorismate, but only a slight reduction of the catalytic efficiency for mutase activity.; mutation to Q: Loss of mutase activity. 15-fold reduction of the affinity for isochorismate and 3-fold reduction of the catalytic efficiency for isochorismate-pyruvate lyase activity.
A43 (≠ T34) mutation to P: Slight reduction of the affinity for isochorismate and of the catalytic efficiency for isochorismate-pyruvate lyase activity. Slight reduction of the affinity for chorismate and of the catalytic efficiency for mutase activity.
I87 (= I78) mutation to T: 4-fold reduction of the affinity for isochorismate and 3-fold reduction of the catalytic efficiency for isochorismate-pyruvate lyase activity. 4-fold reduction of the affinity for chorismate and 15-fold reduction of the catalytic efficiency for mutase activity.
Q90 (≠ E81) binding

2h9dD Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
45% identity, 92% coverage: 1:85/92 of query aligns to 10:94/100 of 2h9dD

query
sites
2h9dD

M

L

E

A

D

D

I

I

R

R

R
x
E

E

A

I

I

D
|
D

A

R

L

I

D

D

Q

L

A

D

V

I

I

V

T

Q

L

A

L

L

G

G

K

R

R
|
R

Y

M

Q

D

Y

Y

V

V

L

K

A

A

S

S

K

R

F

F

K
|
K

T

A

S

S

V

E

T

A

S

A

V

I

Q

P

A

A

P

P

E

E

R

R

L

V

K

A

A

A

M
|
M

L

L

A

P

T

E

R

R

R

A

E

R

W

W

A

A

E

E

A

E

E

N

G

G

L

L

S

D

P

A

D

P

A

F

I

V

E

E

K

G

L

L

Y

F

S

A

D

Q

L

I

V

I

H

H

H

W

F

Y

I

I

A

A

E

E

E
x
Q

M

I

K

K

R

Y

W

W

binding calcium ion: E15 (≠ R6), D18 (= D9)
binding pyruvic acid: R31 (= R22), K42 (= K33), M57 (= M48), Q90 (≠ E81)

2h9cA Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa (see paper)
42% identity, 92% coverage: 1:85/92 of query aligns to 10:86/88 of 2h9cA

query
sites
2h9cA

M

L

E

A

D

D

I

I

R

R

R

E

E

A

I

I

D

D

A

R

L

I

D

D

Q

L

A

D

V

I

I

V

T
x
Q

L

A

L

L

G

G

K
x
R

R
|
R

Y

M

Q

D

Y

Y

V

V

L
x
K

A
|
A

A

A

S

S

K
x
R

F

F

K

-

T

-

S

-

V

-

T

-

S

-

V

-

Q

-

A

A

P

P

E

E

R
|
R

L

V

K

A

A

A

M
|
M

L

L

A

P

T

E

R

R

R

A

E

R

W

W

A

A

E

E

A

E

E

N

G

G

L

L

S

D

P

A

D

P

A

F

I

V

E

E

K

G

L

L

Y

F

S

A

D

Q

L

I

V
x
I

H

H

H

W

F
x
Y

I

I

A

A

E

E

E

Q

M

I

K

K

R

Y

W

W

binding nitrate ion: Q26 (≠ T17), R30 (≠ K21), R31 (= R22), K36 (≠ L27), A37 (= A28), R40 (≠ K31), R45 (= R44), M49 (= M48), I75 (≠ V74), Y78 (≠ F77)

2h9dA Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
40% identity, 92% coverage: 1:85/92 of query aligns to 10:84/84 of 2h9dA

query
sites
2h9dA

M

L

E

A

D

D

I

I

R

R

R

E

E

A

I

I

D

D

A

R

L

I

D

D

Q

L

A

D

V

I

I

V

T

Q

L

A

L

L

G

G

K

R

R
|
R

Y

M

Q

D

Y

Y

V

V

L

K

A

A

S

S

K

R

F

F

K

-

T

-

S

-

V

-

T

-

S

-

V

-

Q

-

A

-

P

-

E

E

R

R

L

V

K

A

A

A

M
|
M

L

L

A

P

T

E

R

R

R

A

E

R

W

W

A

A

E

E

A

E

E

N

G

G

L

L

S

D

P

A

D

P

A

F

I

V

E

E

K

G

L

L

Y

F

S

A

D

Q

L

I

V

I

H

H

H

W

F

Y

I

I

A

A

E

E

E

Q

M

I

K

K

R

Y

W

W

binding pyruvic acid: R31 (= R22), M47 (= M48)

Query Sequence

>Pf6N2E2_1463 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1463
MEDIRREIDALDQAVITLLGKRYQYVLAASKFKTSVTSVQAPERLKAMLATRREWAEAEG
LSPDAIEKLYSDLVHHFIAEEMKRWTANQTHN

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