SitesBLAST

Comparing BWI76_RS10615 FitnessBrowser__Koxy:BWI76_RS10615 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 2 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)
31% identity, 91% coverage: 4:92/98 of query aligns to 8:96/101 of Q51507

query
sites
Q51507

S

T

S

G

L

L

A

A

D

D

V

I

R
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R

S

E

Q

A

I

I

D

D

S

R

I

I

D

D

S

L

E

D

L

I

V

V

S

Q

L

A

I

L

A

G

Q

R

R
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R

A

M

T

D

C

Y

V

V

Q

K

A
|
A

A

A

A

S

A

R

F

F

K
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K

T
x
A

D

S

H

E

S

A

A

A

V

I

R

P

A

A

P

P

E

E

R

R

V

V

Q

A

V

M

I

L

D

P

R

E

V

R

R

A

E

R

K

W

A

A

A

E

A

N

G

G

L

L

P

D

E

A

V

P

I

F

I

V

E

E

K

G

V

L

Y

F

R

A

S

Q

M

I

I

I

D

H

A

W

F

Y

I
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I

E

A

Y

E

E
x
Q

L

I

E

K

Q

Y

H

W

N

R

Q

Q

R14 (= R10) binding substrate

R31 (= R27) binding substrate

A37 (= A33) 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 (= K38) binding substrate; 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 (≠ T39) 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 (= I83) 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 (≠ E86) binding substrate

query
sites
2h9dD

S

T

S

G

L

L

A

A

D

D

V

I

R

R

S
x
E

Q

A

I

I

D
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D

S

R

I

I

D

D

S

L

E

D

L

I

V

V

S

Q

L

A

I

L

A

G

Q

R

R
|
R

A

M

T

D

C

Y

V

V

Q

K

A

A

A

S

A

R

F

F

K
|
K

T

A

D

S

H

E

S

A

A

A

V

I

R

P

A

A

P

P

E

E

R

R

V

V

Q

A

V
x
M

I

L

D

P

R

E

V

R

R

A

E

R

K

W

A

A

A

E

A

N

G

G

L

L

P

D

E

A

V

P

I

F

I

V

E

E

K

G

V

L

Y

F

R

A

S

Q

M

I

I

I

D

H

A

W

F

Y

I

I

E

A

Y

E

E
x
Q

L

I

E

K

Q

Y

H

W

N

R

Q

Q

Query Sequence

>BWI76_RS10615 FitnessBrowser__Koxy:BWI76_RS10615
MTFSSLADVRSQIDSIDSELVSLIAQRATCVQAAAAFKTDHSAVRAPERVQQVIDRVREK
AAAAGLPEVIIEKVYRSMIDAFIEYELEQHNQRQRQKR

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

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