SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_110205394.1 NCBI__GCF_003194585.1:WP_110205394.1 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 6 hits to proteins with known functional sites (download)

P9WQH3 Propanal dehydrogenase (CoA-propanoylating); Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.87; EC 1.2.1.10 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
73% identity, 98% coverage: 3:296/300 of query aligns to 4:297/303 of P9WQH3

query
sites
P9WQH3

K

K

A

A

T

K

A

V

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A

I

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G

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S

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L

S41 (= S40) mutation to D: 2200-fold decrease in catalytic efficiency with coenzyme A.; mutation to I: 6600-fold decrease in catalytic efficiency with coenzyme A.

4lrtB Crystal and solution structures of the bifunctional enzyme (aldolase/aldehyde dehydrogenase) from thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and coa accommodation whithin the shared cofactor-binding site
68% identity, 98% coverage: 1:294/300 of query aligns to 2:295/295 of 4lrtB

query
sites
4lrtB

M

M

R

G

K

K

A

A

T

V

A

A

I

I

V

V

G
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G

P
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P

G
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G

N
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N

I
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I

G

G

T

T

D

D

L

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M

L

Y

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K

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L

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S

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E

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A

L

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A

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D

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K

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C

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N

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D

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G

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N

G

G

D

D

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W

A

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G

G

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L

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D

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A

binding coenzyme a: G11 (= G10), P12 (= P11), G13 (= G12), N14 (= N13), I15 (= I14), G36 (= G35), V37 (= V36), S41 (= S40), A75 (= A74), T76 (= T75), C127 (= C126), T163 (= T162), N277 (= N276), L278 (= L277)

4lrsB Crystal and solution structures of the bifunctional enzyme (aldolase/aldehyde dehydrogenase) from thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and coa accommodation whithin the shared cofactor-binding site
68% identity, 97% coverage: 3:294/300 of query aligns to 2:293/294 of 4lrsB

query
sites
4lrsB

K

K

A

A

T

V

A

A

I

I

V

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G
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G

P
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P

G
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G

N
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N

I
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I

G

G

T

T

D

D

L

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M

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E

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G

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A

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D

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Q

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C

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N

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I

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D

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L

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G

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K

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F

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E

E

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V

E

R

G

G

A

N

G

G

D

D

F

Y

L

L

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P

Y

W

A

A

G

G

N
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N

L
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L

D

D

I

I

M
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M

T

T

A

A

R

R

V

V

G

G

D

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A

binding nicotinamide-adenine-dinucleotide: G9 (= G10), P10 (= P11), G11 (= G12), N12 (= N13), I13 (= I14), V35 (= V36), A73 (= A74), T74 (= T75), L96 (= L97), T97 (= T98), C125 (= C126), G158 (= G159), P159 (= P160), G160 (= G161), T161 (= T162), N164 (= N165), N275 (= N276), L276 (= L277), M279 (= M280)

Q79AF6 Acetaldehyde dehydrogenase 4; Acetaldehyde dehydrogenase [acetylating] 4; Propanal dehydrogenase (CoA-propanoylating); EC 1.2.1.10; EC 1.2.1.87 from Paraburkholderia xenovorans (strain LB400) (see 2 papers)
59% identity, 98% coverage: 2:296/300 of query aligns to 3:293/304 of Q79AF6

query
sites
Q79AF6

R

K

K

K

A

I

T

K

A

C

A

A

I

L

V

I

G

G

P

P

G

G

N

N

I

I

G

G

T

T

D

D

L

L

M

L

Y

A

K

K

L

L

L

Q

R

R

S

S

E

P

V

V

I

L

E

E

P

P

R

I

W

W

M

M

I

V

G

G

V

I

D

D

P

P

S

E

S

S

E

D

G

G

L

L

K

K

L

R

A

A

R

R

D

E

K

M

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G

L

I

E

K

S

T

T

T

H

A

E

D

G

G

V

V

D

D

W

G

L

L

L

I

-

P

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H

K

M

Q

Q

D

A

E

D

L

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P

V

D

Q

L

I

I

V

F

F

E

D

A

A

T

T

S

S

A

A

Y

Y

V

V

H

H

R

A

D

D

Y

N

A

S

P

R

R

K

Y

V

Q

N

E

A

A

L

G

G

I

A

R

L

A

M

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D

D

L

L

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T

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P

A

A

V

I

G

G

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P

A

F

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C

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V

P

P

P

T

V

V

N

N

G

L

E

K

E

E

H

H

V

V

G

G

A

K

-

G

-

E

W

M

N

N

V

V

N

N

M

M

I

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T

T

C
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C

G

G

Q

Q

A

A

T

T

I

I

P

P

M

M

V

V

A

A

V

V

S

S

R

R

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P

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S

A

Y

Y

A

G

E

E

I

I

V

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A

A

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V

S

S

A

K

S

S

A

A

G

G

P

P

G

G

T

T

R

R

A

K

N
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N

I
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I

D

D

E

E

F

F

T

T

R

R

T

T

S

A

N

G

G

A

V

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M

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K

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G

G

A

A

E

K

R

K

G

G

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K

A

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I
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I

I

I

L

L

N

N

P

P

A

A

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E

P

P

M

L

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I

M

M

R

R

D
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D

T

T

I

V

F

H

C

C

A

L

V

L

E

E

P

S

D

E

A

P

D

D

R

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D

A

A

K

I

I

A

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E

E

S

S

V

I

H

H

R

A

M

M

E

I

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K

A

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Q

Q

E

K

Y

Y

V

V

P

P

G

G

Y

Y

R

K

L

L

L

V

Q

N

E

G

P

P

Q

V

F

F

D

D

D

G

A

-

S

-

E

-

A

-

T

-

L

-

G

-

K

-

V

L

K

R

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S

S

I

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F

Y

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L

E

E

V

V

E

E

G

G

A

L

G

G

D

D

F

Y

L

L

P

P

P

K

Y

Y

A

A

G

G

N

N

L

L

D

D

I

I

M

M

T

T

A

A

R

R

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T

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A

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E

H

M

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F

A

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E

S

E

L

I

L

L

C131 (= C126) active site, Acyl-thioester intermediate; mutation C->A,S: Loss of catalytic activity. Still able to bind NAD(+), however with much lower affinity.
N170 (= N165) mutation N->A,D: Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI.
I171 (= I166) mutation I->A,F: Exhibits preferences for aldehydes similar as wild-type. Exhibits about 80% of wild-type acetaldehyde channeling efficiency. Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI.
I195 (= I190) mutation to A: 5-fold decrease in affinity for acetaldehyde. Increase in affinity for butyraldehyde and pentaldehyde, leading to a 9- and 20-fold increase in catalytic efficiency with butyraldehyde and pentaldehyde as substrate, respectively. Exhibits 84% of wild-type acetaldehyde channeling efficiency.; mutation to F: 4- to 7-fold decrease in catalytic efficiency with aldehydes three to four carbons in length. Does not significantly reduce the channeling efficiency of the enzyme complex toward acetaldehyde or propanaldehyde.; mutation to L: Does not significantly reduce the channeling efficiency of the enzyme complex toward acetaldehyde or propanaldehyde.; mutation to W: 5- to 16-fold decrease in catalytic efficiency with aldehydes two to four carbons in length. Exhibits 59% of wild-type acetaldehyde channeling efficiency.
D208 (= D203) mutation to A: 2-fold decrease in catalytic efficiency.

1nvmB Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate (see paper)
56% identity, 99% coverage: 2:297/300 of query aligns to 3:311/312 of 1nvmB

query
sites
1nvmB

R

Q

K

K

A

L

T

K

A

V

A

A

I

I

V
x
I

G
|
G

P
x
S

G
|
G

N
|
N

I
|
I

G

G

T

T

D

D

L

L

M

M

Y

I

K

K

L

V

L

L

R

R

-

N

S

A

E

K

V

Y

I

L

E

E

P

M

R

G

W

A

M

M

I

V

G
|
G

V
x
I

D

D

P

A

S

A

S

S

E

D

G

G

L

L

K

A

L

R

A

A

R

Q

D

R

K

M

G

G

L

V

E

T

S

T

T

T

H

Y

E

A

G

G

V

V

D

E

W

G

L

L

L

I

K

K

Q

L

D

P

E

E

L

F

P

A

D

D

L

I

-

D

-

F

I

V

F

F

E

D

A
|
A

T
|
T

S

S

A

A

-

S

-

A

Y

H

V

V

H

Q

R

N

D

E

Y

A

A

L

P

L

R

R

Y

Q

Q

A

E

K

A

P

G

G

I

I

R

R

A

L

V

I

D

D

L
|
L

T
|
T

P

P

A

A

V

I

G

G

P

P

A

Y

V

C

I

V

P

P

P

V

V

V

N

N

G

L

E

E

H

H

V

L

G

G

A

K

W

L

N

N

V

V

N

N

M

M

I

V

T

T

C
|
C

G

G

Q

Q

A

A

T

T

I

I

P

P

M

M

V

V

A

A

V

V

S

S

R

R

V

V

T

A

P

K

V

V

S

H

Y

Y

A

A

E

E

I

I

V

V

A

A

S

S

V

I

S

S

A

K

S

S

A

A

G
|
G

P
|
P

G
|
G

T
|
T

R

R

A

A

N
|
N

I

I

D

D

E

E

F

F

T

T

R

E

T

T

S

S

N

K

G

A

V

I

M

E

T

V

I

I

G

G

A

A

E

A

R

K

G

G

K

K

A

A

I

I

L

M

N

N

P

P

A

A

E

E

P

P

M

L

I

I

M

M

R

R

D

D

T

T

I

V

F

Y

C

V

A

-

V

L

E

S

P

A

D

A

A

A

D

D

R

Q

D

A

A

A

I

V

A

A

E

A

S

S

V

V

H

A

R

E

M

M

E

V

R

Q

A

A

V

V

Q

Q

E

A

Y

Y

V

V

P

P

G

G

Y

Y

R

R

L

L

L

K

Q

Q

E

Q

P

V

Q

Q

F

F

D

D

D

V

A

I

S

P

E

E

A

S

T

A

-

P

-

L

-

N

-

I

-

P

-

G

L

L

G

G

K

R

-

F

-

S

-

G

V

L

K

K

V

T

S

S

I

V

F

F

V

L

E

E

V

V

E

E

G

G

A

A

G

A

D

H

F

Y

L

L

P

P

P

A

Y

Y

A

A

G

G

N
|
N

L
|
L

D

D

I

I

M
|
M

T

T

A

S

A

A

A

L

R

A

V

T

G

A

D

E

H

R

I

M

A

A

R

Q

S

S

L

M

L

L

T

N

binding nicotinamide-adenine-dinucleotide: I10 (≠ V9), G11 (= G10), S12 (≠ P11), G13 (= G12), N14 (= N13), I15 (= I14), G37 (= G35), I38 (≠ V36), A78 (= A74), T79 (= T75), L103 (= L97), T104 (= T98), C132 (= C126), G165 (= G159), P166 (= P160), G167 (= G161), T168 (= T162), N171 (= N165), N290 (= N276), L291 (= L277), M294 (= M280)

Q52060 Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.10 from Pseudomonas sp. (strain CF600) (see paper)
56% identity, 99% coverage: 2:297/300 of query aligns to 3:311/312 of Q52060

query
sites
Q52060

R

Q

K

K

A

L

T

K

A

V

A

A

I

I

V

I

G

G

P
x
S

G
|
G

N
|
N

I
|
I

G

G

T

T

D

D

L

L

M

M

Y

I

K

K

L

V

L

L

R

R

-

N

S

A

E

K

V

Y

I

L

E

E

P

M

R

G

W

A

M

M

I

V

G

G

V

I

D

D

P

A

S

A

S

S

E

D

G

G

L

L

K

A

L

R

A

A

R

Q

D

R

K

M

G

G

L

V

E

T

S

T

T

T

H

Y

E

A

G

G

V

V

D

E

W

G

L

L

L

I

K

K

Q

L

D

P

E

E

L

F

P

A

D

D

L

I

-

D

-

F

I

V

F

F

E

D

A

A

T

T

S

S

A

A

-

S

-

A

Y

H

V

V

H

Q

R

N

D

E

Y

A

A

L

P

L

R

R

Y

Q

Q

A

E

K

A

P

G

G

I

I

R

R

A

L

V

I

D

D

L

L

T

T

P

P

A

A

V

I

G

G

P

P

A

Y

V

C

I

V

P

P

P

V

V

V

N

N

G

L

E

E

H

H

V

L

G

G

A

K

W

L

N

N

V

V

N

N

M

M

I

V

T

T

C

C

G

G

Q

Q

A

A

T

T

I

I

P

P

M

M

V

V

A

A

V

V

S

S

R

R

V

V

T

A

P

K

V

V

S

H

Y

Y

A

A

E

E

I

I

V

V

A

A

S

S

V

I

S

S

A

K

S
|
S

A
|
A

G
|
G

P
|
P

G
|
G

T
|
T

R
|
R

A
|
A

N
|
N

I

I

D

D

E

E

F

F

T

T

R

E

T

T

S

S

N

K

G

A

V

I

M

E

T

V

I

I

G

G

A

A

E

A

R

K

G

G

K

K

A

A

I

I

L

M

N

N

P

P

A

A

E

E

P

P

M

L

I

I

M

M

R

R

D

D

T

T

I

V

F

Y

C

V

A

-

V

L

E

S

P

A

D

A

A

A

D

D

R

Q

D

A

A

A

I

V

A

A

E

A

S

S

V

V

H

A

R

E

M

M

E

V

R

Q

A

A

V

V

Q

Q

E

A

Y

Y

V

V

P

P

G

G

Y

Y

R

R

L

L

L

K

Q

Q

E

Q

P

V

Q

Q

F

F

D

D

D

V

A

I

S

P

E

E

A

S

T

A

-

P

-

L

-

N

-

I

-

P

-

G

L

L

G

G

K

R

-

F

-

S

-

G

V

L

K

K

V

T

S

S

I

V

F

F

V

L

E

E

V

V

E

E

G

G

A

A

G

A

D

H

F

Y

L

L

P

P

P

A

Y

Y

A

A

G

G

N
|
N

L

L

D

D

I

I

M

M

T

T

A

S

A

A

A

L

R

A

V

T

G

A

D

E

H

R

I

M

A

A

R

Q

S

S

L

M

L

L

T

N

SGNI 12:15 (≠ PGNI 11:14) binding NAD(+)
163:171 (vs. 157:165, 100% identical) binding NAD(+)
N290 (= N276) binding NAD(+)

Query Sequence

>WP_110205394.1 NCBI__GCF_003194585.1:WP_110205394.1
MRKATAAIVGPGNIGTDLMYKLLRSEVIEPRWMIGVDPSSEGLKLARDKGLESTHEGVDW
LLKQDELPDLIFEATSAYVHRDYAPRYQEAGIRAVDLTPAAVGPAVIPPVNGEEHVGAWN
VNMITCGGQATIPMVAAVSRVTPVSYAEIVASVSSASAGPGTRANIDEFTRTTSNGVMTI
GGAERGKAIIILNPAEPPMIMRDTIFCAVEPDADRDAIAESVHRMERAVQEYVPGYRLLQ
EPQFDDASEATLGKVKVSIFVEVEGAGDFLPPYAGNLDIMTAAAARVGDHIARSLLTQEK

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