SitesBLAST

P31023 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; Pyruvate dehydrogenase complex E3 subunit; E3; PDC-E3; EC 1.8.1.4 from Pisum sativum (Garden pea) (see 2 papers)
55% identity, 99% coverage: 5:463/464 of query aligns to 39:500/501 of P31023

query
sites
P31023

D

D

V

V

I

V

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I

G

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G

G

G

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P

G

G

Y

Y

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G

A

A

A

I

I

R

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C

A

A

A

Q

Q

L

L

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G

L

F

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K

T

T

A

T

C

C

V

I

E
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E

G
x
K

R
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R

D
x
G

T
x
A

L
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L

G
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G

T
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T

C
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C

L

L

N

N

V

V

G

G

C
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C

I

I

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P

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S

K

K

A

A

L

L

H

H

A

S

S

S

H

H

Q

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Y

H

H

E

E

A

A

E

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F

E

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N

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I

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T

A

M

M

L

M

A

G

Y

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D

D

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A

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N

N

L

T

T

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R

G

G

I

I

E

E

F

G

L

L

F

F

K

K

N

N

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Y

L

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G

G

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A
x
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E

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I

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V

-

D

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I

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G

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N

T

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-

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E

K

A

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H

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I

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G

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D

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G

A

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D

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K

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I

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D
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D

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M
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M

L
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H
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A

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D

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M

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H

H

67:76 (vs. 33:42, 70% identical) binding
C76 (= C42) modified: Disulfide link with 81, Redox-active
C81 (= C47) modified: Disulfide link with 76, Redox-active
G149 (≠ A115) binding
D348 (= D311) binding
MLAH 354:357 (= MLAH 317:320) binding

Sites not aligning to the query:

1:31 modified: transit peptide, Mitochondrion

1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
55% identity, 99% coverage: 5:463/464 of query aligns to 5:466/467 of 1dxlA

query
sites
1dxlA

D

D

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I

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x
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G

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Y

Y

V

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G

A

A

A

I

I

R

K

C

A

A

A

Q

Q

L

L

G

G

L

F

K

K

T

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C

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x
I

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E

G
x
K

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R

D

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T

A

L
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L

G

G

G
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G

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T

C
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C

L

L

N

N

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V

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G

C
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C

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K

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A

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L

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A

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R

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G

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I

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L

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N

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G

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x
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K

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x
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G

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I

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N

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M

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A

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H

active site: L38 (= L38), C42 (= C42), C47 (= C47), S50 (= S50), Y184 (≠ V181), E188 (= E185), H444 (= H441), H446 (= H443), E451 (= E448)
binding flavin-adenine dinucleotide: I9 (= I9), G11 (≠ S11), G12 (= G12), P13 (= P13), G14 (= G14), I32 (≠ V32), E33 (= E33), K34 (≠ G34), R35 (= R35), G40 (= G40), T41 (= T41), C42 (= C42), V45 (= V45), G46 (= G46), C47 (= C47), K51 (= K51), G113 (= G113), Y114 (≠ W114), G115 (≠ A115), A143 (= A138), T144 (≠ S139), G145 (= G140), S146 (= S141), S164 (= S161), Y184 (≠ V181), I185 (= I182), R274 (= R271), F277 (= F274), G313 (= G310), D314 (= D311), M320 (= M317), L321 (= L318), A322 (= A319), H323 (= H320), A325 (= A322), Y353 (= Y350)

1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
50% identity, 98% coverage: 5:460/464 of query aligns to 6:467/472 of 1zmdA

query
sites
1zmdA

D

D

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V

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T

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I

G
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G

S
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S

G
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P
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P

G
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G

G

G

Y

Y

V

V

G

A

A

A

I

I

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K

C

A

A

A

Q

Q

L

L

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G

L

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K

T

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A

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C

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x
I

E
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E

G
x
K

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x
N

D

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T

T

L
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L

G

G

G
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G

T
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T

C
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C

L

L

N

N

V
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V

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G

C
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C

I

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S

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K

A

A

L

L

H

N

A

N

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S

H

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V

Y

H

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M

A

A

E

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H

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A

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G

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M

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G

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L

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K

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N

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G

W
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A
x
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Q

-

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A

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S

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D

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E

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E

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M
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L

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K

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Q

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G

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K

F

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K

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G

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A

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L

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Q

R

I

I

A

P

T

V

D

N

G

T

S

R

Y

F

R

Q

T

T

N

K

V

I

P

P

G

N

V

I

Y

Y

A

A

I

I

G
|
G

D
|
D

V

V

I

V

E

A

G

G

P

P

M
|
M

L
|
L

A
|
A

H
|
H

K

K

A
|
A

E

E

D

D

E

E

G

G

M

I

A

I

V

C

A

V

E

E

M

G

I

M

A

A

G

G

Q

G

H

A

P

V

H

H

V

I

N

D

Y

Y

G

N

V

C

I

V

P

P

G

S

V
|
V

I

I

Y
|
Y

T

T

H

H

P

P

E

E

V

V

A

A

S

W

V

V

G

G

K

K

T

S

E

E

Q

Q

L

L

K

K

A

E

E

E

G

G

V

I

A

E

Y

Y

K

K

V

V

G

G

K

K

F

F

S

P

F

F

M

A

G

A

N

N

G

S

R

R

A

A

K

K

A

T

N

N

F

A

A

D

A

T

D

D

G

G

F

M

V

V

K

K

L

I

L

L

A

G

D

Q

K

K

A

S

T

T

D

D

R

R

I

V

L

L

G

G

A

A

H

H

V

I

I

L

G

G

P

P

M

G

A

A

G

G

D

E

L

M

I

V

H

N

E

E

V

A

C

A

V

L

A

A

M

L

E

E

F

Y

G

G

A

A

A

S

A

C

E

E

D

D

L

I

A

A

R

R

T

V

C

C

H
|
H

A

A

H
|
H

P
|
P

T

T

Y

L

S

S

E
|
E

A

A

M

F

R

R

E

E

A

A

A

N

L

L

A

A

C

A

G

S

D

F

G

G

active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V181), E190 (= E185), H448 (= H441), H450 (= H443), E455 (= E448)
binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), S12 (= S11), G13 (= G12), P14 (= P13), G15 (= G14), I33 (≠ V32), E34 (= E33), K35 (≠ G34), N36 (≠ R35), G41 (= G40), T42 (= T41), C43 (= C42), V46 (= V45), G47 (= G46), C48 (= C47), S51 (= S50), K52 (= K51), G115 (= G113), Y116 (≠ W114), G117 (≠ A115), A145 (= A138), T146 (≠ S139), G147 (= G140), S148 (= S141), S166 (= S161), I187 (= I182), R278 (= R271), F281 (= F274), G317 (= G310), D318 (= D311), M324 (= M317), L325 (= L318), A326 (= A319), H327 (= H320), A329 (= A322), Y357 (= Y350), H450 (= H443), P451 (= P444)
binding 1,4-dihydronicotinamide adenine dinucleotide: K52 (= K51), F153 (≠ I146), I182 (≠ V177), G183 (= G178), G185 (= G180), V186 (= V181), I187 (= I182), E190 (= E185), V205 (≠ I200), E206 (= E201), F207 (= F202), L208 (≠ M203), T239 (vs. gap), C275 (≠ S268), I276 (≠ T269), G277 (= G270), R278 (= R271), M324 (= M317), L325 (= L318), V355 (= V348), Y357 (= Y350)

1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
50% identity, 98% coverage: 5:460/464 of query aligns to 6:467/472 of 1zmcA

query
sites
1zmcA

D

D

V

V

I

T

I

V

I
|
I

G
|
G

S
|
S

G
|
G

P
|
P

G
|
G

G

G

Y

Y

V

V

G

A

A

A

I

I

R

K

C

A

A

A

Q

Q

L

L

G

G

L

F

K

K

T

T

A

V

C

C

V
x
I

E
|
E

G
x
K

R
x
N

D

E

T

T

L
|
L

G

G

G
|
G

T
|
T

C
|
C

L

L

N

N

V
|
V

G
|
G

C
|
C

I

I

P

P

S
|
S

K
|
K

A

A

L

L

H

N

A

N

S

S

H

H

Q

Y

V

Y

H

H

E

M

A

A

E

H

-

G

H

T

N

D

F

F

E

A

K

S

M

R

G

G

I

I

K

E

V

M

P

S

A

E

P

V

K

R

I

L

D

N

W

L

K

D

T

K

M

M

L

M

A

E

Y

Q

K

K

D

S

D

T

V

A

I

V

G

K

Q

A

N

L

T

T

K

G

G

G

I

I

E

A

F

H

L

L

F

F

K

K

K

Q

N

N

K

K

V

V

D

V

W

H

L

V

K

N

G
|
G

W
x
Y

A
x
G

S

K

I

I

P

T

-

G

-

K

-

N

-

Q

-

V

E

T

A

A

G

T

K

K

V

A

K

D

V

G

G

G

D

T

E

Q

T

V

H

I

E

D

A

T

K

K

H

N

I

I

I

L

I

I

A
|
A

S
x
T

G
|
G

S
|
S

E

E

P

V

A

T

S

P

I

F

P

P

G

G

A

-

E

-

V

I

E

T

I

I

D

D

E

E

K

D

V

T

V

I

V

V

T

S

S
|
S

T

T

G

G

A

A

L

L

E

S

L

L

G

K

K

K

I

V

P

P

K

E

R

K

M

M

V

V

V
x
I

G
|
G

G

A

G
|
G

V
|
V

I
|
I

G

G

L

V

E
|
E

L

L

G

G

S

S

V

V

Y

W

A

Q

R

R

L

L

G

G

T

A

E

D

V

V

S

T

V

A

I
x
V

E
|
E

F
|
F

M
x
L

D

G

G

H

I

V

T

G

-

G

P
x
V

G

G

Q

I

D

D

L

M

E

E

V

I

A

S

R

K

Q

N

F

F

Q

Q

K

R

I

I

L

L

T

Q

K

K

Q

Q

G

G

L

F

K

K

F

F

-

K

-

L

-

N

-
x
T

-
x
K

I
x
V

T

T

G

G

A

A

A

T

V

K

Q

K

K

-

V

-

A

-

T

S

K

D

S

G

K

K

A

I

K

D

V

V

T

S

Y

I

K

E

M

A

R

A

K

S

D

G

S

K

E

A

D

E

S

V

L

I

E

T

A

C

D

D

I

V

V

L

L

L

V

V

S
x
C

T
x
I

G
|
G

R
|
R

K

R

P

P

F
|
F

T

T

E

K

G

N

L

L

G

G

L

L

D

E

A

E

L

L

G

G

V

I

K

E

M

L

T

D

E

P

R
|
R

G

G

Q

R

I

I

A

P

T

V

D

N

G

T

S

R

Y

F

R

Q

T

T

N

K

V

I

P

P

G

N

V

I

Y

Y

A

A

I

I

G
|
G

D
|
D

V

V

I

V

E

A

G

G

P

P

M
|
M

L
|
L

A
|
A

H
|
H

K

K

A
|
A

E

E

D

D

E

E

G

G

M

I

A

I

V

C

A

V

E

E

M

G

I

M

A

A

G

G

Q

G

H

A

P

V

H

H

V

I

N

D

Y

Y

G

N

V

C

I

V

P

P

G

S

V

V

I

I

Y
|
Y

T

T

H

H

P

P

E

E

V

V

A

A

S

W

V

V

G

G

K

K

T

S

E

E

Q

Q

L

L

K

K

A

E

E

E

G

G

V

I

A

E

Y

Y

K

K

V

V

G

G

K

K

F

F

S

P

F

F

M

A

G

A

N

N

G

S

R

R

A

A

K

K

A

T

N

N

F

A

A

D

A

T

D

D

G

G

F

M

V

V

K

K

L

I

L

L

A

G

D

Q

K

K

A

S

T

T

D

D

R

R

I

V

L

L

G

G

A

A

H

H

V

I

I

L

G

G

P

P

M

G

A

A

G

G

D

E

L

M

I

V

H

N

E

E

V

A

C

A

V

L

A

A

M

L

E

E

F

Y

G

G

A

A

A

S

A

C

E

E

D

D

L

I

A

A

R

R

T

V

C

C

H
|
H

A

A

H
|
H

P

P

T

T

Y

L

S

S

E
|
E

A

A

M

F

R

R

E

E

A

A

A

N

L

L

A

A

C

A

G

S

D

F

G

G

active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V181), E190 (= E185), H448 (= H441), H450 (= H443), E455 (= E448)
binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), S12 (= S11), G13 (= G12), P14 (= P13), G15 (= G14), I33 (≠ V32), E34 (= E33), K35 (≠ G34), N36 (≠ R35), G41 (= G40), T42 (= T41), C43 (= C42), V46 (= V45), G47 (= G46), C48 (= C47), K52 (= K51), G115 (= G113), Y116 (≠ W114), G117 (≠ A115), A145 (= A138), T146 (≠ S139), G147 (= G140), S148 (= S141), S166 (= S161), I187 (= I182), R278 (= R271), F281 (= F274), G317 (= G310), D318 (= D311), M324 (= M317), L325 (= L318), A326 (= A319), H327 (= H320), A329 (= A322), Y357 (= Y350)
binding nicotinamide-adenine-dinucleotide: I182 (≠ V177), G183 (= G178), G185 (= G180), V205 (≠ I200), E206 (= E201), F207 (= F202), L208 (≠ M203), V214 (≠ P208), T239 (vs. gap), K240 (vs. gap), V241 (≠ I230), C275 (≠ S268), I276 (≠ T269), G277 (= G270), R278 (= R271), R297 (= R290), M324 (= M317)

P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 13 papers)
50% identity, 98% coverage: 5:460/464 of query aligns to 43:504/509 of P09622

query
sites
P09622

D

D

V

V

I

T

I

V

I

I

G

G

S

S

G

G

P

P

G

G

Y

Y

V

V

G

A

A

A

I

I

R

K

C

A

A

A

Q

Q

L

L

G

G

L

F

K

K

T

T

A

V

C

C

V

I

E
|
E

G
x
K

R
x
N

D
x
E

T
|
T

L
|
L

G
|
G

T
|
T

C
|
C

L

L

N

N

V

V

G

G

C

C

I

I

P

P

S

S

K
|
K

A

A

L

L

H

N

A

N

S

S

H

H

Q

Y

V

Y

H

H

E

M

A

A

E

H

-

G

H
x
K

N

D

F

F

E

A

K

S

M

R

G

G

I

I

K

E

V

M

P

S

A

E

P

V

K

R

I

L

D

N

W

L

K

D

T

K

M

M

L

M

A

E

Y

Q

K

K

D

S

D

T

V

A

I

V

G

K

Q

A

N

L

T

T

K

G

G

G

I

I

E

A

F

H

L

L

F

F

K

K

K

Q

N

N

K

K

V

V

D

V

W

H

L

V

K

N

G

G

W

Y

A
x
G

S

K

I

I

P

T

-

G

-

K

-

N

-

Q

-

V

E

T

A

A

G

T

K

K

V

A

K

D

V

G

G

G

D

T

E

Q

T

V

H

I

E

D

A

T

K

K

H

N

I

I

I

L

I

I

A

A

S
x
T

G
|
G

S
|
S

E

E

P

V

A

T

S

P

I

F

P

P

G

G

A

-

E

-

V

I

E

T

I

I

D

D

E

E

K

D

V

T

V

I

V

V

T

S

S

S

T

T

G

G

A

A

L

L

E

S

L

L

G

K

K

K

I

V

P

P

K

E

R

K

M

M

V

V

V

I

G
|
G

G
x
A

G
|
G

V
|
V

I
|
I

G
|
G

L
x
V

E
|
E

L

L

G

G

S

S

V

V

Y

W

A

Q

R

R

L

L

G

G

T

A

E

D

V

V

S

T

V

A

I

V

E
|
E

F

F

M

L

D

G

G

H

I

V

T

G

-

G

P

V

G

G

Q

I

D

D

L

M

E

E

V

I

A

S

R

K

Q

N

F

F

Q

Q

K

R

I

I

L

L

T

Q

K

K

Q

Q

G

G

L

F

K

K

F

F

-

K

-

L

-

N

-

T

-

K

I
x
V

T

T

G

G

A

A

A

T

V

K

Q

K

K

-

V

-

A

-

T

S

K

D

S

G

K

K

A

I

K

D

V

V

T

S

Y

I

K

E

M

A

R

A

K

S

D

G

S

K

E

A

D

E

S

V

L

I

E

T

A

C

D

D

I

V

V

L

L

L

V

V

S

C

T

I

G
|
G

R

R

K

R

P

P

F

F

T

T

E

K

G

N

L

L

G

G

L

L

D

E

A

E

L

L

G

G

V

I

K

E

M

L

T

D

E

P

R

R

G

G

Q

R

I

I

A

P

T

V

D

N

G

T

S

R

Y

F

R

Q

T

T

N

K

V

I

P

P

G

N

V

I

Y

Y

A

A

I

I

G

G

D
|
D

V

V

I

V

E

A

G

G

P

P

M
|
M

L
|
L

A
|
A

H
|
H

K

K

A

A

E

E

D

D

E

E

G

G

M

I

A

I

V

C

A

V

E
|
E

M

G

I

M

A

A

G

G

Q

G

H

A

P

V

H
|
H

V

I

N

D

Y

Y

G

N

V

C

I

V

P

P

G

S

V

V

I

I

Y

Y

T

T

H

H

P

P

E

E

V

V

A

A

S

W

V

V

G

G

K

K

T

S

E

E

Q

Q

L

L

K

K

A

E

E

E

G

G

V

I

A

E

Y

Y

K

K

V

V

G

G

K

K

F

F

S

P

F

F

M

A

G

A

N

N

G

S

R

R

A

A

K

K

A

T

N

N

F

A

A

D

A

T

D

D

G

G

F

M

V

V

K

K

L

I

L

L

A

G

D

Q

K

K

A

S

T

T

D
|
D

R

R

I

V

L

L

G

G

A

A

H

H

V

I

I

L

G

G

P

P

M

G

A

A

G

G

D

E

L

M

I

V

H

N

E
|
E

V

A

C

A

V

L

A

A

M

L

E

E

F
x
Y

G

G

A

A

A

S

A

C

E

E

D
|
D

L

I

A

A

R
|
R

T

V

C

C

H
|
H

A

A

H

H

P
|
P

T

T

Y

L

S
|
S

E
|
E

A

A

M

F

R
|
R

E

E

A

A

A

N

L

L

A

A

C

A

G

S

D

F

G

G

71:80 (vs. 33:42, 70% identical) binding
K72 (≠ G34) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
K89 (= K51) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
K104 (≠ H65) to T: in dbSNP:rs1130477
G154 (≠ A115) binding
TGS 183:185 (≠ SGS 139:141) binding
220:227 (vs. 178:185, 75% identical) binding
E243 (= E201) binding
V278 (≠ I230) binding
G314 (= G270) binding
D355 (= D311) binding
MLAH 361:364 (= MLAH 317:320) binding
E375 (= E331) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
H383 (= H339) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
D448 (= D404) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to N: Does not affect dihydrolipoyl dehydrogenase activity.
E466 (= E422) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
Y473 (≠ F429) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to F: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to H: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.
D479 (= D435) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
R482 (= R438) mutation to A: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to M: Does not affect interaction with PDHX.
H485 (= H441) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
P488 (= P444) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
S491 (= S447) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
E492 (= E448) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
R495 (= R451) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989

Sites not aligning to the query:

505 K→M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.

P09624 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine decarboxylase complex subunit L; Lipoamide dehydrogenase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex E3 component; EC 1.8.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
51% identity, 99% coverage: 3:463/464 of query aligns to 26:498/499 of P09624

query
sites
P09624

S

S

Y

H

D

D

V

V

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I

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E
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E

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x
K

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D
x
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K

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L

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T

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C

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L

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N

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C
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C

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K

A

A

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L

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N

A

N

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F

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E

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M

E

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E

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D

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-

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M

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F

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A

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H

56:65 (vs. 33:42, 70% identical) binding
C65 (= C42) modified: Disulfide link with 70, Redox-active
C70 (= C47) modified: Disulfide link with 65, Redox-active
K74 (= K51) binding
G139 (≠ A115) binding
D346 (= D311) binding
MLAH 352:355 (= MLAH 317:320) binding
H478 (= H443) active site, Proton acceptor

Sites not aligning to the query:

1:21 modified: transit peptide, Mitochondrion

1v59A Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+
51% identity, 99% coverage: 3:463/464 of query aligns to 5:477/478 of 1v59A

query
sites
1v59A

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N

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|
G

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N

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x
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G

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E

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G

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Y

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E

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F

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x
Q

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x
A

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E

E

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A

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K

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A

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Q

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K

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F

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L

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K

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K

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Q

G

G

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L

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F

F

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G

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A

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A
x
K

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V

-

I

-

S

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A

K

K

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R

A

N

A

D

T

D

K

K

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K

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V