SitesBLAST

R49 (= R51) mutation to A: Less than 1% of the wild-type enzyme activity.
K60 (= K62) mutation to A: Less than 1% of the wild-type enzyme activity.
D69 (≠ A71) mutation to A: No effect on the enzyme activity.
R72 (= R74) mutation to A: Less than 1% of the wild-type enzyme activity.
T105 (≠ S107) mutation to A: 20% of the wild-type enzyme activity.
E109 (≠ Q111) mutation to A: 10% of the wild-type enzyme activity.; mutation to Q: 40% of the wild-type enzyme activity at pH 7.5 and 27% of the wild-type enzyme activity at pH 4.
R134 (= R137) mutation to A: Less than 1% of the wild-type enzyme activity.

Sites not aligning to the query:

1:33 signal peptide
160 modified: Disulfide link with 193
193 modified: Disulfide link with 160

2fp2B Secreted chorismate mutase from mycobacterium tuberculosis (see paper)
33% identity, 52% coverage: 50:151/197 of query aligns to 12:112/163 of 2fp2B

query
sites
2fp2B

E

E

R
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R

L

L

D

E

V

V

A

A

P

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A

Q

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E

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D

A

A

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D

D

D

P

A

D

F

Y

A

V

R

T

R

R

F

V

F

F

D

D

K

D

Q

Q

F
x
I

E

R

A

A

S
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T

K
x
E

Q

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I

Q
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E

R

Y

R

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R

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F

H

S

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W

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Q

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N

G

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R

A

S

S

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A

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A

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D

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A

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R
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R

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active site: R13 (= R51), K24 (= K62), D33 (≠ A71), T69 (≠ S107), E70 (≠ K108), E73 (≠ Q111), R98 (= R137)
binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: R13 (= R51), K24 (= K62), I31 (= I69), E32 (= E70), D33 (≠ A71), R36 (= R74), Q40 (≠ I78), I66 (≠ F104), T69 (≠ S107), E70 (≠ K108), E73 (≠ Q111), R98 (= R137)

2ao2B The 2.07 angstrom crystal structure of mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions (see paper)
33% identity, 52% coverage: 50:151/197 of query aligns to 14:114/165 of 2ao2B

query
sites
2ao2B

E

E

R
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R

L

L

D

E

V

V

A

A

P

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A

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K

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W

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R

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A
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P

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I

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E

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R

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A

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active site: R15 (= R51), K26 (= K62), D35 (≠ A71), T71 (≠ S107), E72 (≠ K108), E75 (≠ Q111), R100 (= R137)
binding sulfate ion: K26 (= K62), R38 (= R74), Q42 (≠ I78)
binding tryptophan: L31 (≠ A67), P32 (= P68), I33 (= I69), E34 (= E70)

2ao2A The 2.07 angstrom crystal structure of mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions (see paper)
33% identity, 52% coverage: 50:151/197 of query aligns to 14:114/165 of 2ao2A

query
sites
2ao2A

E

E

R
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R

L

L

D

E

V

V

A

A

P

D

L

P

V

V

A

A

Q

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K

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W

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R

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G

Q

A

L

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P

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I

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E

A
x
D

P

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R

E

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Q

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E

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D

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D

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A

D

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A

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R

R

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F

F

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D

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D

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Q

F

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A

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E

R

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active site: R15 (= R51), K26 (= K62), D35 (≠ A71), T71 (≠ S107), E72 (≠ K108), E75 (≠ Q111), R100 (= R137)
binding sulfate ion: K26 (= K62), R38 (= R74), R100 (= R137)

Query Sequence

>WP_086511287.1 NCBI__GCF_002151265.1:WP_086511287.1
MSLHRALPIHSGRWLAIALVLLLAGCQTQPPEPPDEDKAAIDRMLVLIDERLDVAPLVAQ
SKWNSGAPIEAPEREAQILDQVAEDAEAAGVDDAFARRFFDKQFEASKQIQRRLHHQWLQ
EGRSPFADPPDLAEEVRPVLDRLTPQLIEALADMQRIAEVEGSGRYLEQRAAELIQDDFD
GEPRDVAIAPLRERFAP

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