SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing PfGW456L13_2505 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2505 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)
75% identity, 99% coverage: 1:299/302 of query aligns to 1:299/304 of Q79AF6

query
sites
Q79AF6

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C131 (= C131) active site, Acyl-thioester intermediate; mutation C->A,S: Loss of catalytic activity. Still able to bind NAD(+), however with much lower affinity.
N170 (= N170) mutation N->A,D: Displays significant reduction in the level of allosteric activation of the aldol cleavage reaction by BphI.
I171 (= I171) 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 (= I195) 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 (= D208) 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)
56% identity, 96% coverage: 1:291/302 of query aligns to 1:295/303 of P9WQH3

query
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P9WQH3

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S41 (= S41) 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
57% identity, 95% coverage: 4:290/302 of query aligns to 4:294/295 of 4lrtB

query
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4lrtB

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Q

binding coenzyme a: V10 (≠ I10), G11 (= G11), P12 (= P12), G13 (= G13), N14 (= N14), I15 (= I15), V35 (= V35), G36 (= G36), V37 (= V37), S41 (= S41), A75 (= A77), T76 (= T78), S77 (= S79), A80 (≠ V82), L98 (= L100), T99 (= T101), P100 (= P102), C127 (= C131), G162 (= G166), T163 (= T167), N277 (= N273), L278 (= L274)

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
57% identity, 95% coverage: 4:290/302 of query aligns to 2:292/294 of 4lrsB

query
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4lrsB

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binding nicotinamide-adenine-dinucleotide: V8 (≠ I10), G9 (= G11), P10 (= P12), G11 (= G13), N12 (= N14), I13 (= I15), V33 (= V35), G34 (= G36), V35 (= V37), S39 (= S41), A73 (= A77), T74 (= T78), S75 (= S79), L96 (= L100), T97 (= T101), P98 (= P102), C125 (= C131), S156 (= S162), A157 (≠ V163), G158 (= G164), P159 (= P165), G160 (= G166), T161 (= T167), N164 (= N170), N275 (= N273), L276 (= L274), M279 (= M277)

1nvmB Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate (see paper)
56% identity, 96% coverage: 1:290/302 of query aligns to 1:307/312 of 1nvmB

query
sites
1nvmB

M

M

S

N

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Q

K

K

L

L

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K

A

V

A

A

I

I

I
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I

G
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G

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x
S

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G

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I

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D

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-

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I

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T

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S

A

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Y

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H

A

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N

N

S

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L

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A

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I

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G

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Y

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C

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N

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E

E

E

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-

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C

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x
A

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G

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G

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T

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A

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N

I

I

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E

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A

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G

G

A

A

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A

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A

A

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A

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E

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L

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R

D

D

T

T

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E

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-

N

D

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D

A

A

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L

A

E

E

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M

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E

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Y

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G

Y

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L

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K

-

Q

-

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Q

-

F

-

D

-

V

-

I

-

P

-

E

-

S

-

A

-

P

I

L

N

N

G

I

P

P

-

G

-

L

-

G

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F

F

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S

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L

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K

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S

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F

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E

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G

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A

G

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G

N
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N

L
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L

D

D

I

I

M
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M

T

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A

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G

A

L

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Q

binding nicotinamide-adenine-dinucleotide: I10 (= I10), G11 (= G11), S12 (≠ P12), G13 (= G13), N14 (= N14), I15 (= I15), V36 (= V35), G37 (= G36), I38 (≠ V37), A78 (= A77), T79 (= T78), S80 (= S79), L103 (= L100), T104 (= T101), P105 (= P102), C132 (= C131), S163 (= S162), A164 (≠ V163), G165 (= G164), P166 (= P165), G167 (= G166), T168 (= T167), N171 (= N170), N290 (= N273), L291 (= L274), M294 (= M277)

Q52060 Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.10 from Pseudomonas sp. (strain CF600) (see paper)
56% identity, 96% coverage: 1:290/302 of query aligns to 1:307/312 of Q52060

query
sites
Q52060

M

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I

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F

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A

A

T

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H

A

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N

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L

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A

I

I

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Y

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C

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V

N

N

L

L

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E

E

E

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H

A

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L

A

-

M

-

N

N

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N

M

M

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C

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G

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A

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A

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N

I

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-

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E

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-

A

-

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I

L

N

N

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I

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G

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-

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F

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F

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E

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G

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A

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G

N
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N

L

L

D

D

I

I

M

M

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T

A

S

A

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M

A

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Q

SGNI 12:15 (≠ PGNI 12:15) binding
163:171 (vs. 162:170, 78% identical) binding
N290 (= N273) binding

Query Sequence

>PfGW456L13_2505 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2505
MSKKLRAAIIGPGNIGTDLLMKMCRSQWIEPVWMVGVDPDSEGLKRAREMGIKTTAGGVD
GLLPHVLDDDIRIAFDATSAYVHAENSRKLNELGVIMIDLTPAAIGPYCVPPVNLKEHAS
SLAMNVNMVTCGGQATIPMVAAVSRVQPVSYGEIVATVSSGSVGPGTRQNIDEFTRTTAG
AVEKIGGARRGKAIIVINPAEPPLMMRDTIHCLTDDEPNQDAIRTSVLEMVREVQRYVPG
YKLINGPVFDGRKVSIFIEVEGLGDFLPKSAGNLDIMTAAGLRTAEMFAEEAHKGTLQLP
AR

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