SitesBLAST

Q73 (= Q73) mutation to A: It has very broad nucleophile scope and excellent regio- and diastereoselectivity in the amination reaction. This mutation strongly moves the specificity of MAL away from ammonia and towards methylamine. It is highly enantioselective.
H194 (= H194) mutation to A: Strong (160-fold) decrease of the catalytic efficiency for deamination and slight (1.8-fold) decrease of affinity binding for L-threo-beta-methylaspartate. 7-fold decrease of the catalytic efficiency for amination and 20-fold decrease of affinity binding for mesaconate. It does not show any major conformational changes.; mutation to R: It abolishes deaminase and aminase activities and does not show any major conformational changes.
D238 (= D238) binding
E273 (= E273) binding
D307 (= D307) binding
Q329 (= Q329) mutation to A: Very strong decrease of the catalytic efficiency for deamination, whereas the affinity binding for L-threo-beta-methylaspartate is not affected. Strong (240-fold) decrease of the catalytic efficiency for amination and slight (2.4-fold) decrease of affinity binding for mesaconate. It does not show any major conformational changes.; mutation to R: It abolishes deaminase and aminase activities and does not show any major conformational changes.
K331 (= K331) active site, Proton acceptor; mutation to A: It abolishes deaminase and aminase activities and does not show any major conformational changes.; mutation to G: It abolishes deaminase and aminase activities and does not show any major conformational changes.; mutation to H: It abolishes deaminase and aminase activities and does not show any major conformational changes.; mutation to Q: It abolishes deaminase and aminase activities and does not show any major conformational changes.; mutation to R: It abolishes deaminase and aminase activities and does not show any major conformational changes.
L384 (= L384) mutation to A: It has very broad electrophile scope and excellent regio- and enantioselectivity in the amination reaction.

3zvhA Methylaspartate ammonia lyase from clostridium tetanomorphum mutant q73a (see paper)
57% identity, 99% coverage: 1:409/413 of query aligns to 1:409/415 of 3zvhA

query
sites
3zvhA

M

M

K

K

I

I

K

V

Q

D

A

V

L

L

F

C

T

T

A

P

G

G

Y

L

S

T

S

G

F

F

Y

Y

F

F

D

D

Q

Q

Q

R

A

A

I

I

K

K

N

K

G

G

A

A

G

G

H

H

D

D

G

G

F

F

I

T

Y

Y

T

T

G

G

A

S

P

T

V

V

T

T

P

E

G

G

F

F

T

T

S

Q

V

V

R

R

Q

Q

A

K

G

G

E

E

C

S

V

I

S

S

V

V

Q

L

L

L

I

V

L

L

E

E

N

D

G

G

A

Q

V

V

A

A

V

H

G

G

D

D

C

C

A

A

V

V

Q

A

Y

Y

S

S

G

G

A

A

G

G

R

R

D

D

P

P

L

L

F

F

L

L

A

A

E

K

N

D

F

F

I

I

P

P

F

V

L

I

N

E

D

K

H

E

I

I

K

A

P

P

L

K

L

L

E

I

G

G

R

R

D

E

V

I

D

T

T

N

F

F

L

K

P

P

N

M

A

A

R

E

F

E

F

F

D

D

K

K

L

M

R

T

I

V

D

N

G

G

H

N

L

R

L

L

H

H

T

T

A

A

V

I

R

R

Y

Y

G

G

L

I

S

T

Q

Q

A

A

L

I

L

L

D

D

A

A

T

V

A

A

L

K

A

T

S

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G

K

R

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L

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K

M

A

A

E

E

V

V

V

I

C

R

D

D

E

E

W

Y

Q

N

L

P

P

G

C

A

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P

I

E

N

A

A

I

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P

P

L

V

F

F

G

A

Q
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Q

S

S

G

G

D

D

R

R

Y

Y

I

D

A

N

V

V

D

D

K

K

M

M

I

I

L

I

K

K

G

E

V

A

D

D

V

V

L

L

P

P

H
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H

A

A

L

L

I

I

N

N

V

V

E

E

K

K

L

L

G

G

L

L

K

K

G

G

E

E

K

K

L

L

R

L

E

E

Y

Y

V

V

R

K

W

W

L

L

S

R

D

D

R

R

I

I

L

I

S

K

L

L

R

R

A

V

S

R

P

E

R

D

Y

Y

R

A

P

P

T

I

L

F

H

H

I

I

D
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D

V

V

Y

Y

G

G

T

T

I

I

G

G

L

A

I

A

F

F

D

D

M

V

D

D

P

I

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K

R

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C

M

A

A

D

D

Y

Y

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A

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A

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E

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A

A

A

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K

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L

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E
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E

G

G

P

P

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M

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D

A

V

G

E

N

D

K

R

P

Q

D

K

Q

Q

I

M

R

E

M

A

L

M

T

R

A

D

I

L

T

R

K

A

E

E

L

L

T

D

R

G

L

R

G

G

S

V

G

D

V

A

K

E

I

L

V

V

A

A

D
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D

E

E

W

W

C

C

N

N

T

T

Y

V

Q

E

D

D

I

V

I

K

D

F

F

F

T

T

D

D

A

N

G

K

S

A

C

G

H

H

M

M

V

V

Q
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Q

I

I

K
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K

T

T

P

P

D

D

L

L

G

G

I

V

H

N

N

N

I

I

V

A

D

D

A

A

V

I

L

M

Y

Y

C

C

N

K

K

A

H

N

A

G

M

M

E

G

A

A

Y

Y

Q

C

G

G

T

T

C

C

N

N

E

E

T

T

E

N

I

R

S

S

A

A

R

E

T

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C

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H

N

V

I

A

G

L

M

A

A

A

C

R

G

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A

M

R

R

Q

M

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L

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A

K

K

P

P

G

G

M

M

G

G

F

V

D

D

E

E

G

G

L

M

N

M

I

I

V

V

F

K

N

N

E

E

M

M

N

N

R

R

T

V

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L

A

A

L

L

L

V

active site: Q172 (= Q172), H194 (= H194), D238 (= D238), E273 (= E273), D307 (= D307), Q329 (= Q329), K331 (= K331)
binding magnesium ion: D238 (= D238), E273 (= E273), D307 (= D307)

Query Sequence

>BWI76_RS08475 FitnessBrowser__Koxy:BWI76_RS08475
MKIKQALFTAGYSSFYFDDQQAIKNGAGHDGFIYTGAPVTPGFTSVRQAGECVSVQLILE
NGAVAVGDCAAVQYSGAGGRDPLFLAENFIPFLNDHIKPLLEGRDVDTFLPNARFFDKLR
IDGHLLHTAVRYGLSQALLDATALASGRLKAEVVCDEWQLPCIPEAIPLFGQSGDDRYIA
VDKMILKGVDVLPHALINNVEEKLGLKGEKLREYVRWLSDRILSLRASPRYRPTLHIDVY
GTIGLIFDMDPVRCADYIASLEKEAQGLPLYIEGPVDAGNKPDQIRMLTAITKELTRLGS
GVKIVADEWCNTYQDIIDFTDAGSCHMVQIKTPDLGGIHNIVDAVLYCNKHAMEAYQGGT
CNETEISARTCVHVALAARPMRMLIKPGMGFDEGLNIVFNEMNRTIALLQAKD

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