SitesBLAST

Comparing 3606921 Dshi_0349 chorismate mutase (RefSeq) 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)
30% identity, 89% coverage: 12:98/98 of query aligns to 10:99/101 of Q51507

query
sites
Q51507

L

L

A

A

E

D

H

I

R
|
R

D

E

S

A

I

I

D

D

R

R

L

I

D

D

A

L

I

D

L

I

V

V

F

Q

T

A

L

L

A

G

E

R

R
|
R

F

M

K

D

H

Y

T

V

Q

K

A
|
A

V

A

G

S

R

R

L

F

K
|
K

A
|
A

E

S

H

E

A

A

L

A

P

I

P

P

S

A

D

-

P

P

T

E

R

R

E

V

E

A

S

A

Q

M

I

L

K

P

R

E

L

R

S

A

E

R

L

W

A

A

E

E

M

E

A

N

D

G

L

L

D

D

P

A

D

P

F

F

A

V

K

E

-

G

-

L

-

F

-

A

K

Q

F

I

L

I

N

H

F

W

I

Y

I
|
I

Q

A

E

E

V
x
Q

I

I

Q

K

H

Y

H

W

K

R

Q

Q

H

T

Q

R

S

G

R14 (= R16) binding

R31 (= R33) binding

A37 (= A39) 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 (= K44) 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 (= A45) 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 (= I86) 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 (≠ V89) binding

query
sites
2h9dD

L

L

A

A

E

D

H

I

R

R

D
x
E

S

A

I

I

D
|
D

R

R

L

I

D

D

A

L

I

D

L

I

V

V

F

Q

T

A

L

L

A

G

E

R

R
|
R

F

M

K

D

H

Y

T

V

Q

K

A

A

V

A

G

S

R

R

L

F

K
|
K

A

A

E

S

H

E

A

A

L

A

P

I

P

P

S

A

D

-

P

P

T

E

R

R

E

V

E

A

S

A

Q
x
M

I

L

K

P

R

E

L

R

S

A

E

R

L

W

A

A

E

E

M

E

A

N

D

G

L

L

D

D

P

A

D

P

F

F

A

V

K

E

-

G

-

L

-

F

-

A

K

Q

F

I

L

I

N

H

F

W

I

Y

I

I

Q

A

E

E

V
x
Q

I

I

Q

K

H

Y

H

W

K

R

Q

Q

H

T

Q

R

S

G

Query Sequence

>3606921 Dshi_0349 chorismate mutase (RefSeq)
MTDAVSRAAQVLAEHRDSIDRLDAILVFTLAERFKHTQAVGRLKAEHALPPSDPTREESQ
IKRLSELAEMADLDPDFAKKFLNFIIQEVIQHHKQHQS

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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Query Sequence

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