SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_041950033.1 NCBI__GCF_000015565.1:WP_041950033.1 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)

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)
88% identity, 98% coverage: 8:309/309 of query aligns to 3:304/304 of Q79AF6

query
sites
Q79AF6

K

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C131 (= C136) active site, Acyl-thioester intermediate; mutation C->A,S: Loss of catalytic activity. Still able to bind NAD(+), however with much lower affinity.
N170 (= N175) mutation N->A,D: Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI.
I171 (= I176) 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 (= I200) 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 (= D213) mutation to A: 2-fold decrease in catalytic efficiency.

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)
59% identity, 94% coverage: 8:298/309 of query aligns to 3:297/303 of P9WQH3

query
sites
P9WQH3

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S41 (= S46) 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
58% identity, 94% coverage: 7:295/309 of query aligns to 2:294/295 of 4lrtB

query
sites
4lrtB

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binding coenzyme a: G11 (= G16), P12 (= P17), G13 (= G18), N14 (= N19), I15 (= I20), G36 (= G41), V37 (≠ I42), S41 (= S46), A75 (= A82), T76 (= T83), C127 (= C136), T163 (= T172), N277 (= N278), L278 (= L279)

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
58% identity, 93% coverage: 9:295/309 of query aligns to 2:292/294 of 4lrsB

query
sites
4lrsB

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binding nicotinamide-adenine-dinucleotide: G9 (= G16), P10 (= P17), G11 (= G18), N12 (= N19), I13 (= I20), V35 (≠ I42), A73 (= A82), T74 (= T83), L96 (= L105), T97 (= T106), C125 (= C136), G158 (= G169), P159 (= P170), G160 (= G171), T161 (= T172), N164 (= N175), N275 (= N278), L276 (= L279), M279 (= M282)

1nvmB Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate (see paper)
57% identity, 94% coverage: 8:299/309 of query aligns to 3:311/312 of 1nvmB

query
sites
1nvmB

K

Q

K

K

I

L

K

K

C

V

A

A

L

I

I
|
I

G
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G

P
x
S

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

L

L

M

A

I

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-

V

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N

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A

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Y

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A

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A
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A

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H

H

A

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Q

N

N

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A

A

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I

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Y

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C

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P

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V

N

N

L

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E

Q

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K

R

-

E

-

M

L

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N

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N

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C
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C

G

G

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A

G
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G

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A

N
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N

I

I

D

D

E

E

F

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A

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A

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G

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K

A

A

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N

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L

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M

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A

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S

I

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A

Y

Y

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G

Y

Y

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L

-

K

-

Q

-

V

-

Q

-

F

-

D

-

V

-

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-

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-

E

-

S

-

A

-

P

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L

N

N

G

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-

G

-

L

-

G

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F

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G

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A

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Y

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A

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G

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N

L
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L

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M
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M

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T

A

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A

A

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N

binding nicotinamide-adenine-dinucleotide: I10 (= I15), G11 (= G16), S12 (≠ P17), G13 (= G18), N14 (= N19), I15 (= I20), G37 (= G41), I38 (= I42), A78 (= A82), T79 (= T83), L103 (= L105), T104 (= T106), C132 (= C136), G165 (= G169), P166 (= P170), G167 (= G171), T168 (= T172), N171 (= N175), N290 (= N278), L291 (= L279), M294 (= M282)

Q52060 Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.10 from Pseudomonas sp. (strain CF600) (see paper)
57% identity, 94% coverage: 8:299/309 of query aligns to 3:311/312 of Q52060

query
sites
Q52060

K

Q

K

K

I

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K

K

C

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A

A

L

I

I

I

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G

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x
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G

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I

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T

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D

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L

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A

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F

D

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A

A

T

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N

N

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A

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-

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A

A

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I

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G

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Y

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N

N

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E

Q

E

H

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V

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R

-

E

-

M

L

N

N

V

V

N

N

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M

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T

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C

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G

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A

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E

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S

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x
A

G
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G

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P

G
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G

T
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T

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R

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x
A

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N

I

I

D

D

E

E

F

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T

T

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E

T

T

A

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K

A

A

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E

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I

G

G

A

A

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A

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K

A

A

I

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N

N

P

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A

A

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E

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M

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T

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A

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A

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I

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-

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-

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-

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-

F

-

D

-

V

-

I

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P

-

E

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S

-

A

-

P

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L

N

N

G

I

P

P

-

G

-

L

-

G

V

R

F

F

D

S

G

G

Q

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R

K

V

T

S

S

V

V

F

F

M

L

E

E

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V

E

E

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G

L

A

G

A

D

H

Y

Y

L

L

P

P

K

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

T

T

A

A

E

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M

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F

M

A

A

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E

S

I

M

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L

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N

SGNI 12:15 (≠ PGNI 17:20) binding NAD(+)
163:171 (vs. 167:175, 78% identical) binding NAD(+)
N290 (= N278) binding NAD(+)

Query Sequence

>WP_041950033.1 NCBI__GCF_000015565.1:WP_041950033.1
MNEGIPMKKIKCALIGPGNIGTDLLAKLQRSPVLEPVWMVGIDPASDGLKRASEMGIKTT
AEGVDGLIPHMKADGVQIVFDATSAYVHAENSAKVNAQGAMMIDLTPAAIGPYCVPPVNL
KQHVGRREMNVNMVTCGGQATIPMVYAVSRVQPVAYGEIVATVSSRSVGPGTRKNIDEFT
RTTAGAVEKVGGARQGKAIIIINPAEPPLIMRDTVHCLVEGKPDEAAITQSIHDMIREVQ
KYVPGYKLVNGPVFDGQRVSVFMEVEGLGDYLPKYAGNLDIMTAAAARTAEMFAEEILKG
ELVLEPVAA

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