SitesBLAST

S232 (= S209) modified: Phosphoserine; by PDK1
S293 (= S272) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
S300 (≠ K278) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
K336 (= K314) modified: N6-acetyllysine; mutation K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.

P26284 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; EC 1.2.4.1 from Rattus norvegicus (Rat) (see paper)
56% identity, 90% coverage: 31:342/348 of query aligns to 56:364/390 of P26284

query
sites
P26284

F

L

S

T

K

R

E

E

D

D

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

Q

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q

Q

L

L

Y

Y

G

K

M

Q

G

K

F

I

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

T

D

D

Q

H

V

L

I

I

T

T

G

A

Y

Y

R

R

D

A

H

H

G

G

H

F

M

T

L

F

A

N

C

R

G

G

M

H

S

A

A

V

R

R

G

A

V

I

M

L

A

A

E

E

L

L

T

T

G

G

R

R

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

A

K

K

E

-

K

-

H

N

F

F

Y

Y

G

G

H

N

G

G

I

I

V

V

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

N

G

G

N

K

D

D

N

E

V

V

S

C

L

L

A

T

Y

L

F

Y

G

G

D

D

G

G

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

F

E

E

S

A

F

Y

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

I

Y

F

I

I

V

C

E

E

N

N

R

R

Y

Y

A

G

M

M

G

G

T

T

S
|
S

V

V

S

E

R

R

A

A

S

A

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

-

S

D

F

F

G

-

I

I

P

P

G

G

Y

L

Q

R

V

V

D

D

G

G

M

M

D

D

V

I

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

K

E

F

A

A

V

A

E

A

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L

M

E

E

M

L

L

Q

T

T

Y

Y

R

R

Y

Y

R

H

G

G

H

H

S
|
S

M

M

S

S

D

D

P

P

-

G

A

V

K
x
S

Y

Y

R

R

S

T

K

R

D

E

E

E

V

I

Q

Q

K

E

M

V

R

R

S

S

E

K

H

S

D

D

P

P

I

I

E

M

Q

L

V

L

K

K

A

D

R

R

L

M

M

V

D

N

K

S

G

N

W

L

A

A

T

S

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

D

K

V

E

E

V

V

R

R

D

K

I

E

V

I

A

E

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

A

D

D

P

P

E

E

P

P

D

P

V

L

S

E

E

E

L

L

S232 (= S209) modified: Phosphoserine; by PDK1
S293 (= S272) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
S300 (≠ K278) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4

P29803 Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial; PDHE1-A type II; EC 1.2.4.1 from Homo sapiens (Human) (see 4 papers)
56% identity, 90% coverage: 31:342/348 of query aligns to 54:362/388 of P29803

query
sites
P29803

F

L

S

T

K

R

E

A

D

E

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

L

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q

Q

L

L

Y

Y

G

K

M

Q

G

K

F

F

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

S

D

D

Q

H

V

V

I

I

T

T

G

S

Y

Y

R

R

D

A

H

H

G

G

H

V

M

C

L

Y

A

T

C

R

G

G

M

L

S

S

A

V

R

R

G

S

V

I

M

L

A

A

E

E

L

L

T

T

G

G

R

R

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

T

K

K

E

-

K

-

H

N

F

F

Y

Y

G

G

H

N

G

G

I

I

V

V

G

G

A

A

Q

Q

V

G

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

K

G

G

N

N

D

D

N

E

V

I

S

C

L

L

A

T

Y

L

F

Y

G

G

D

D

G

G

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

A

E

E

S

A

F

F

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

V

Y

F

I

I

V

C

E

E

N

N

R

L

Y

Y

A

G

M
|
M

G

G

T

T

S
|
S

V

T

S

E

R

R

A

A

S

A

A

A

Q

S

T

P

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

-

S

N

F

F

G

-

I

I

P

P

G

G

Y

L

Q

K

V

V

D

D

G

G

M

M

D

D

V

V

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

K

E

F

A

A

V

A

E

N

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L

M

E

E

M

L

L

Q

T

T

Y

Y

R

R

Y

Y

R

H

G

G

H

H

S
|
S

M

M

S
|
S

D

D

P

P

-

G

A

V

K
x
S

Y

Y

R

R

S

T

K

R

D

E

E

E

V

I

Q

Q

K

E

M

V

R

R

S

S

E

K

H

R

D

D

P

P

I

I

E

I

Q

I

V

L

K

Q

A

D

R

R

L

M

M

V

D

N

K

S

G

K

W

L

A

A

T

T

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

G

K

A

E

E

V

V

R

R

D

K

I

E

V

I

A

D

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

T

D

D

P

P

E

E

P

P

D

H

V

L

S

E

E

E

L

L

M227 (= M206) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
S230 (= S209) mutation to A: Slightly reduces enzyme activity.
S291 (= S272) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Strongly reduces enzyme activity. Increases enzyme activity in stem cells.; mutation S->E,D: Abolishes enzyme activity. Increases neuronal cell death in response to glutamate excitotoxicity.
S293 (= S274) modified: Phosphoserine; mutation to A: Increases enzyme activity in stem cells.; mutation to D: Abolishes enzyme activity. Increases neuronal cell death in response to glutamate excitotoxicity.
S298 (≠ K278) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.

P08559 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; EC 1.2.4.1 from Homo sapiens (Human) (see 16 papers)
56% identity, 90% coverage: 31:342/348 of query aligns to 56:364/390 of P08559

query
sites
P08559

F

L

S

T

K

R

E

E

D

D

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

Q

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q

Q

L

L

Y

Y

G

K

M

Q

G

K

F

I

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

T

D

D

Q

H

V

L

I

I

T

T

G

A

Y
|
Y

R
|
R

D

A

H

H

G

G

H

F

M

T

L

F

A

T

C

R

G

G

M

L

S

S

A

V

R

R

G

E

V

I

M

L

A
|
A

E

E

L

L

T

T

G

G

R

R

R

K

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

A

K

K

E

-

K

-

H

N

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
|
V

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

N

G

G

N

K

D

D

N

E

V

V

S

C

L

L

A

T

Y

L

F

Y

G

G

D
|
D

G
|
G

A
|
A

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

F

E

E

S

A

F

Y

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

I

Y

F

I

I

V

C

E

E

N

N

N
|
N

R

R

Y
|
Y

A

G

M

M

G

G

T

T

S
|
S

V

V

S

E

R

R

A

A

S

A

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

D

S

F

F

-

G

-

I

I

P

P

G

G

Y

L

Q

R

V

V

D

D

G

G

M

M

D

D

V

I

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

R

E

F

A

A

V

A

E

A

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L
x
M

E

E

M

L

L

Q

T

T

Y

Y

R

R

Y

Y

R

H

G

G

H
|
H

S
|
S

M

M

S

S

D

D

P

P

-

G

A

V

K
x
S

Y

Y

R
|
R

S

T

K

R

D

E

E

E

V

I

Q

Q

K

E

M

V

R

R

S

S

E

K

H

S

D

D

P

P

I

I

E

M

Q

L

V

L

K

K

A

D

R

R

L

M

M

V

D

N

K

S

G

N

W

L

A

A

T

S

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

D

K

V

E

E

V

V

R

R

D

K

I

E

V

I

A

E

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

A

D

D

P

P

E

E

P

P

D

P

V

L

S

E

E

E

L

L

Y118 (= Y93) binding thiamine diphosphate
R119 (= R94) binding thiamine diphosphate
A136 (= A111) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
G165 (= G142) binding thiamine diphosphate
V167 (= V144) binding thiamine diphosphate; to M: in PDHAD; disrupts magnesium binding and results in deficient activity of the pyruvate dehydrogenase complex; dbSNP:rs2063174067
D196 (= D173) binding Mg(2+); binding thiamine diphosphate
G197 (= G174) binding thiamine diphosphate
A198 (= A175) binding thiamine diphosphate
N225 (= N202) binding Mg(2+); binding thiamine diphosphate
Y227 (= Y204) binding Mg(2+)
S232 (= S209) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
M282 (≠ L261) to L: in dbSNP:rs2229137
H292 (= H271) binding thiamine diphosphate
S293 (= S272) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300.; mutation to E: Interferes with substrate binding.
S300 (≠ K278) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
R302 (= R280) to C: in PDHAD; loss of activity; common mutation; dbSNP:rs137853252

Sites not aligning to the query:

1:29 modified: transit peptide, Mitochondrion
10 R → P: in PDHAD; affects mitochondrial import of precursor protein; dbSNP:rs137853257

6cfoA Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
56% identity, 90% coverage: 31:342/348 of query aligns to 28:336/362 of 6cfoA

query
sites
6cfoA

F

L

S

T

K

R

E

E

D

D

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

Q

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q
|
Q

L

L

Y

Y

G

K

M

Q

G

K

F

I

I

I

G

R

G

G

F
|
F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

T

D

D

Q

H

V

L

I

I

T

T

G

A

Y
|
Y

R
|
R

D

A

H

H

G

G

H

F

M

T

L

F

A

T

C

R

G

G

M

L

S

S

A

V

R

R

G

E

V

I

M

L

A

A

E

E

L

L

T

T

G

G

R

R

R

K

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

A

K

K

E

-

K

-

H

N

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
|
V

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

N

G

G

N

K

D

D

N

E

V

V

S

C

L

L

A

T

Y

L

F

Y

G
|
G

D
|
D

G
|
G

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

F

E

E

S

A

F

Y

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

I

Y

F

I

I

V

C

E

E

N

N

N
|
N

R

R

Y
|
Y

A
x
G

M

M

G

G

T

T

S

S

V

V

S

E

R

R

A

A

S

A

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

D

S

F

F

-

G

-

I

I

P

P

G

G

Y

L

Q

R

V

V

D

D

G

G

M

M

D

D

V

I

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

R

E

F

A

A

V

A

E

A

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L

M

E

E

M

L

L

Q

T

T

Y

Y

R
|
R

Y

Y

R

H

G

G

H
|
H

S
|
S

M

M

S

S

D

D

P

P

-

G

A

V

K

S

Y
|
Y

R

R

S

T

K

R

D

E

E

E

V

I

Q

Q

K

E

M

V

R

R

S

S

E

K

H

S

D

D

P

P

I

I

E

M

Q

L

V

L

K

K

A

D

R

R

L

M

M

V

D

N

K

S

G

N

W

L

A

A

T

S

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

D

K

V

E

E

V

V

R

R

D

K

I

E

V

I

A

E

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

A

D

D

P

P

E

E

P

P

D

P

V

L

S

E

E

E

L

L

active site: Q52 (= Q55), G137 (= G142), R260 (= R267), H264 (= H271), S265 (= S272), Y273 (= Y279)
binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1S)-1-hydroxy-1-[(R)-hydroxy(oxo)-lambda~5~-phosphanyl]ethyl}-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: F62 (= F65), Y90 (= Y93), R91 (= R94), G137 (= G142), V139 (= V144), G167 (= G172), D168 (= D173), G169 (= G174), N197 (= N202), Y199 (= Y204), G200 (≠ A205), H264 (= H271)
binding magnesium ion: D168 (= D173), N197 (= N202), Y199 (= Y204)

1ni4A Human pyruvate dehydrogenase (see paper)
56% identity, 90% coverage: 31:342/348 of query aligns to 28:336/362 of 1ni4A

query
sites
1ni4A

F

L

S

T

K

R

E

E

D

D

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

Q

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q
|
Q

L

L

Y

Y

G

K

M

Q

G

K

F

I

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

T

D

D

Q

H

V

L

I

I

T

T

G

A

Y
|
Y

R
|
R

D

A

H

H

G

G

H

F

M

T

L

F

A

T

C

R

G

G

M

L

S

S

A

V

R

R

G

E

V

I

M

L

A

A

E

E

L

L

T

T

G

G

R

R

R

K

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

A

K

K

E

-

K

-

H

N

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
|
V

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

N

G

G

N

K

D

D

N

E

V

V

S

C

L

L

A

T

Y

L

F

Y

G
|
G

D
|
D

G
|
G

A
|
A

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

F

E

E

S

A

F

Y

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

I

Y

F

I

I

V

C

E

E

N

N

N
|
N

R

R

Y
|
Y

A
x
G

M

M

G

G

T

T

S

S

V

V

S

E

R

R

A

A

S

A

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

D

S

F

F

-

G

-

I

I

P

P

G

G

Y

L

Q

R

V

V

D

D

G

G

M

M

D

D

V

I

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

R

E

F

A

A

V

A

E

A

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L

M

E

E

M

L

L

Q

T

T

Y

Y

R
|
R

Y

Y

R

H

G

G

H
|
H

S
|
S

M

M

S

S

D

D

P

P

-

G

A

V

K

S

Y
|
Y

R

R

S

T

K

R

D

E

E

E

V

I

Q

Q

K

E

M

V

R

R

S

S

E

K

H

S

D

D

P

P

I

I

E

M

Q

L

V

L

K

K

A

D

R

R

L

M

M

V

D

N

K

S

G

N

W

L

A

A

T

S

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

D

K

V

E

E

V

V

R

R

D

K

I

E

V

I

A

E

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

A

D

D

P

P

E

E

P

P

D

P

V

L

S

E

E

E

L

L

active site: Q52 (= Q55), G137 (= G142), R260 (= R267), H264 (= H271), S265 (= S272), Y273 (= Y279)
binding magnesium ion: D168 (= D173), N197 (= N202), Y199 (= Y204)
binding thiamine diphosphate: Y90 (= Y93), R91 (= R94), V139 (= V144), G167 (= G172), D168 (= D173), G169 (= G174), A170 (= A175), N197 (= N202), G200 (≠ A205), H264 (= H271)

3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
56% identity, 90% coverage: 31:342/348 of query aligns to 29:337/363 of 3exeA

query
sites
3exeA

F

L

S

T

K

R

E

E

D

D

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

Q

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q
|
Q

L

L

Y

Y

G

K

M

Q

G

K

F

I

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

T

D

D

Q

H

V

L

I

I

T

T

G

A

Y
|
Y

R
|
R

D

A

H

H

G

G

H

F

M

T

L

F

A

T

C

R

G

G

M

L

S

S

A

V

R

R

G

E

V

I

M

L

A

A

E

E

L

L

T

T

G

G

R

R

R

K

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

A

K

K

E

-

K

-

H

N

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
|
V

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

N

G

G

N

K

D

D

N

E

V

V

S

C

L

L

A

T

Y

L

F

Y

G
|
G

D
|
D

G
|
G

A
|
A

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

F

E

E

S

A

F

Y

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

I

Y

F

I

I

V

C

E

E

N

N

N
|
N

R

R

Y
|
Y

A
x
G

M

M

G

G

T

T

S

S

V

V

S

E

R

R

A

A

S

A

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

D

S

F

F

-

G

-

I

I

P

P

G

G

Y

L

Q

R

V

V

D

D

G

G

M

M

D

D

V

I

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

R

E

F

A

A

V

A

E

A

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L

M

E

E

M

L

L

Q

T

T

Y

Y

R
|
R

Y

Y

R

H

G

G

H
|
H

S
|
S

M

M

S

S

D

D

P

P

-

G

A

V

K

S

Y
|
Y

R

R

S

T

K

R

D

E

E

E

V

I

Q

Q

K

E

M

V

R

R

S

S

E

K

H

S

D

D

P

P

I

I

E

M

Q

L

V

L

K

K

A

D

R

R

L

M

M

V

D

N

K

S

G

N

W

L

A

A

T

S

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

D

K

V

E

E

V

V

R

R

D

K

I

E

V

I

A

E

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

A

D

D

P

P

E

E

P

P

D

P

V

L

S

E

E

E

L

L

active site: Q53 (= Q55), G138 (= G142), R261 (= R267), H265 (= H271), S266 (= S272), Y274 (= Y279)
binding manganese (ii) ion: D169 (= D173), N198 (= N202), Y200 (= Y204)
binding thiamine diphosphate: Y91 (= Y93), R92 (= R94), V140 (= V144), G168 (= G172), D169 (= D173), G170 (= G174), A171 (= A175), N198 (= N202), Y200 (= Y204), G201 (≠ A205), H265 (= H271)

P16387 Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial; Pyruvate dehydrogenase complex component E1 alpha; PDHE1-A; EC 1.2.4.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
51% identity, 92% coverage: 30:348/348 of query aligns to 75:392/420 of P16387

query
sites
P16387

E

E

F

T

S

S

K

K

E

A

D

T

D

L

L

L

K

Q

A

M

Y

Y

R

K

E

D

M

M

L

V

L

I

I

I

R

R

F

M

E

E

E

M

K

A

A

C

G

D

Q

A

L

L

Y

Y

G

K

M

A

G

K

F

K

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

S

I

V

G

G

Q

Q

E

E

A

A

V

I

V

A

V

V

G

G

M

I

Q

E

L

N

A

A

L

I

K

T

E

K

G

L

D

D

Q

S

V

I

I

I

T

T

G

S

Y

Y

R

R

D

C

H

H

G

G

H

F

M

T

L

F

A

M

C

R

G

G

M

A

S

S

A

V

R

K

G

A

V

V

M

L

A

A

E

E

L

L

T

M

G

G

R

R

G

A

G

G

L

V

S

S

K

Y

G

G

K

K

G

G

S

S

M

M

H

H

M

L

F

Y

S

A

K

P

E

-

K

-

H

G

F

F

Y

Y

G

G

H

N

G

G

I

I

V

V

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

L

A

A

F

F

A

A

N

H

R

Q

Y

Y

R

K

G

N

N

E

D

D

N

A

V

C

S

S

L

F

A

T

Y

L

F

Y

G

G

D

D

G

G

A

A

A

S

N

N

Q

Q

G

G

Q

Q

V

V

Y

F

E

E

S

S

F

F

N

N

M

M

A

A

A

K

L

L

W

W

K

N

L

L

P

P

V

V

I

V

Y

F

I

C

V

C

E

E

N

N

R

K

Y

Y

A

G

M

M

G

G

T

T

S

A

V

A

S

S

R

R

A

S

S

S

A

A

Q

M

T

T

D

E

F

Y

S

F

Q

K

R

R

G

G

A

Q

S

Y

F

-

G

-

I

I

P

P

G

G

Y

L

Q

K

V

V

D

N

G

G

M

M

D

D

V

I

R

L

A

A

V

V

K

Y

A

Q

A

A

A

S

D

K

E

F

A

A

V

K

E

D

H

W

C

C

R

L

S

S

G

G

K

K

G

G

P

P

I

L

I

V

L

L

E

E

M

Y

L

E

T

T

Y

Y

R

R

Y

Y

R

G

G

G

H

H

S
|
S

M

M

S

S

D

D

P

P

-

G

A

T

K

T

Y

Y

R

R

S

T

K

R

D

D

E

E

V

I

Q

Q

K

H

M

M

R

R

S

S

E

K

H

N

D

D

P

P

I

I

E

A

Q

G

V

L

K

K

A

M

R

H

L

L

M

I

D

D

K

L

G

G

W

I

A

A

T

T

E

E

D

A

E

E

L

V

K

K

Q

A

I

Y

D

D

K

K

E

S

V

A

R

R

D

K

I

Y

V

V

A

D

D

E

S

Q

A

V

D

E

F

L

A

A

Q

D

S

A

D

A

P

P

E

P

P

P

D

E

-

A

-

K

V

L

S

S

E

I

L

L

Y

F

T

E

D

D

I

V

L

Y

L

V

S313 (= S272) modified: Phosphoserine; by PDK1 and PDK2

Sites not aligning to the query:

1:33 modified: transit peptide, Mitochondrion

P26267 Pyruvate dehydrogenase E1 component subunit alpha type I, mitochondrial; PDHA1; PDHE1-A; EC 1.2.4.1 from Ascaris suum (Pig roundworm) (Ascaris lumbricoides) (see paper)
52% identity, 91% coverage: 32:346/348 of query aligns to 53:364/396 of P26267

query
sites
P26267

S

T

K

K

E

E

D

D

D

A

L

V

K

H

A

Y

Y

Y

R

T

E

Q

M

M

L

L

L

T

I

I

R

R

F

M

E

E

E

S

K

A

A

A

G

G

Q

N

L

L

Y

Y

G

K

M

E

G

K

F

K

I

V

G

R

G

G

F

F

C

C

H

H

L

L

Y

Y

I

S

G

G

Q

Q

E

E

A

A

V

C

V

A

V

V

G

G

M

T

Q

K

L

A

A

A

L

M

K

D

E

A

G

G

D

D

Q

A

V

A

I

V

T

T

G

A

Y

Y

R

R

D

C

H

H

G

G

H

W

M

T

L

Y

A

L

C

S

G

G

M

S

S

S

A

V

R

A

G

K

V

V

M

L

A

C

E

E

L

L

T

T

G

G

R

R

R

I

G

T

G

G

L

N

S

V

K

Y

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

G

K

E

E

-

K

-

H

N

F

F

Y

Y

G

G

H

N

G

G

I

I

V

V

G

G

A

A

Q

Q

V

Q

S

P

L

L

G

G

T

T

G

G

L

I

A

A

F

F

A

A

N

M

R

K

Y

Y

R

R

G

K

N

E

D

K

N

N

V

V

S

C

L

I

A

T

Y

M

F

F

G

G

D

D

G

G

A

A

A

T

N

N

Q

Q

G

G

Q

Q

V

L

Y

F

E

E

S

S

F

M

N

N

M

M

A

A

A

K

L

L

W

W

K

D

L

L

P

P

V

V

I

L

Y

Y

I

V

V

C

E

E

N

N

R

G

Y

Y

A

G

M

M

G

G

T

T

S

A

V

A

S

A

R

R

A

S

S

S

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

T

R

R

G

G

A

D

S

Y

F

-

G

-

I

V

P

P

G

G

Y

I

Q

W

V

V

D

D

G

G

M

M

D

D

V

V

R

L

A

A

V

V

K

R

A

Q

A

A

A

V

D

R

E

W

A

A

V

K

E

E

H

W

C

C

R

N

S

A

G

G

K

K

G

G

P

P

I

L

I

M

L

I

E

E

M

M

L

A

T

T

Y

Y

R

R

Y

Y

R

S

G

G

H

H

S
|
S

M

M

S

S

D

D

P

P

-

G

A

T

K
x
S

Y

Y

R

R

S

T

K

R

D

E

E

E

V

V

Q

Q

K

E

M

V

R

R

S

K

E

T

H

R

D

D

P

P

I

I

E

T

Q

G

V

F

K

K

A

D

R

K

L

I

M

V

D

T

K

A

G

G

W

L

A

V

T

T

E

E

D

D

E

E

L

I

K

K

Q

E

I

I

D

D

K

K

E

Q

V

V

R

R

D

K

I

E

V

I

A

D

D

A

S

A

A

V

D

K

F

Q

A

A

Q

H

S

T

D

D

P

K

E

E

P

S

D

P

V

V

S

E

E

L

L

M

Y

L

T

T

D

D

I

I

S289 (= S272) modified: Phosphoserine
S296 (≠ K278) modified: Phosphoserine

Q8H1Y0 Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial; PDHE1-A; Protein IAA-CONJUGATE-RESISTANT 4; EC 1.2.4.1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
50% identity, 92% coverage: 30:348/348 of query aligns to 57:373/393 of Q8H1Y0

query
sites
Q8H1Y0

E

E

F

T

S

S

K

S

E

E

D

E

D

I

L

L

K

A

A

F

Y

F

R

R

E

D

M

M

L

A

L

R

I

M

R

R

F

M

E

E

E

I

K

A

A

A

G

D

Q

S

L

L

Y

Y

G

K

M

A

G

K

F

L

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

Y

I

D

G

G

Q

Q

E

E

A

A

V

L

V

A

V

V

G

G

M

M

Q

E

L

A

A

A

L

I

K

T

E

K

G

K

D

D

Q

A

V

I

I

I

T

T

G

S

Y

Y

R
|
R

D

D

H

H

G

C

H

T

M

F

L

I

A

G

C

R

G

G

M

G

S

K

A

L

R

V

G

D

V

A

M

F

A

S

E

E

L

L

T

M

G

G

R

R

R

K

G

T

G

G

L

C

S

S

K

H

G

G

K

K

G

G

S

S

M

M

H

H

M

F

F

Y

S

K

K

K

E

D

K

A

H

S

F

F

Y

Y

G

G

H

H

G

G

I

I

V

V

G

G

A

A

Q

Q

V

I

S

P

L

L

G

G

T

C

G

G

L

L

A

A

F

F

A

A

N

Q

R

K

Y

Y

R

N

G

K

N

D

D

E

N

A

V

V

S

T

L

F

A

A

Y

L

F

Y

G

G

D

D

G

G

A

A

N

N

Q

Q

G

G

Q

Q

V

L

Y

F

E

E

S

A

F

L

N

N

M

I

A

S

A

A

L

L

W

W

K

D

L

L

P

P

V

A

I

I

Y

L

I

V

V

C

E

E

N

N

R

H

Y

Y

A

G

M

M

G

G

T

T

S

A

V

T

S

W

R

R

A

S

S

A

A

K

Q

S

T

P

D

A

F

Y

S

F

Q

K

R

R

G

G

A

D

S

Y

F

-

G

-

I

V

P

P

G

G

Y

L

Q

K

V

V

D

D

G

G

M

M

D

D

V

A

R

L

A

A

V

V

K

K

A

Q

A

A

A

C

D

K

E

F

A

A

V

K

E

E

H

H

C

A

R

L

S

K

G

N

K

-

G

G

P

P

I

I

L

L

E

E

M

M

L

D

T

T

Y

Y

R

R

Y

Y

R

H

G

G

H

H

S

S

M

M

S

S

D

D

P

P

-

G

A

S

K

T

Y

Y

R

R

S

T

K

R

D

D

E

E

V

I

Q

S

K

G

M

V

R

R

S

Q

E

V

H

R

D

D

P

P

I

I

E

E

Q

R

V

V

K

R

A

K

R

L

L

L

M

L

D

T

K

H

G

D

W

I

A

A

T

T

E

E

D

K

E

E

L

L

K

K

Q

D

I

M

D

E

K

K

E

E

V

I

R

R

D

K

I

E

V

V

A

D

D

D

S

A

A

V

D

A

F

Q

A

A

Q

K

S

E

D

S

P

P

E

I

P

P

D

D

V

A

S

S

E

E

L

L

Y

F

T

T

D

N

I

M

L

Y

L

V

R121 (= R94) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.

Q10489 Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial; PDHE1-A; EC 1.2.4.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
48% identity, 95% coverage: 18:348/348 of query aligns to 51:389/409 of Q10489

query
sites
Q10489

P

P

V

V

K

K

K

L

D

D

-

D

-

S

-

V

F

F

A

E

G

G

-

Y

-

K

-

I

-

D

-

V

-

P

G

S

T

T

I

E

A

I

E

E

F

V

S

T

K

K

E

G

D

E

D

L

L

L

K

G

A

L

Y

Y

R

E

E

K

M

M

L

V

L

T

I

I

R

R

F

L

E

E

E

L

K

A

A

C

G

D

Q

A

L

L

Y

Y

G

K

M

A

G

K

F

K

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

S

I

I

G

G

Q

Q

E

E

A

A

V

V

V

A

G

G

M

I

Q

E

L

G

A

A

L

I

K

T

E

L

G

D

D

D

Q

S

V

I

I

I

T

T

G

S

Y

Y

R

R

D

C

H

H

G

G

H

F

M

A

L

Y

A

T

C

R

G

G

M

L

S

S

A

I

R

R

G

S

V

I

M

I

A

G

E

E

L

L

T

M

G

G

R

R

R

Q

G

C

G

G

L

A

S

S

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

I

F

F

S

A

K

K

E

-

K

-

H

N

F

F

Y

Y

G

G

H

N

G

G

I

I

V

V

G

G

A

A

Q

Q

V

I

S

P

L

L

G

G

T

A

G

G

L

I

A

G

F

F

A

A

N

Q

R

K

Y

Y

R

L

G

E

N

K

D

P

N

T

V

T

S

T

L

F

A

A

Y

L

F

Y

G

G

D

D

G

G

A

A

A

S

N

N

Q

Q

G

G

Q

Q

V

A

Y

F

E

E

S

A

F

F

N

N

M

M

A

A

A

K

L

L

W

W

K

G

L

L

P

P

V

V

I

I

Y

F

I

A

V

C

E

E

N

N

R

K

Y

Y

A

G

M

M

G

G

T

T

S

S

V

A

S

E

R

R

A

S

S

S

A

A

Q

M

T

T

D

E

F

F

S

Y

Q

K

R

R

G

G

A

Q

S

Y

F

-

G

-

I

I

P

P

G

G

Y

L

Q

L

V

V

D

N

G

G

M

M

D

D

V

V

R

L

A

A

V

V

K

L

A

Q

A

A

A

S

D

K

E

F

A

A

V

K

E

K

H

Y

C

T

R

V

S

E

G

N

K

S

G

Q

P

P

I

L

L

M

E

E

M

F

L

V

T

T

Y

Y

R

R

Y
|
Y

R

G

G

G

H

H

S
|
S

M

M

S
|
S

D

D

P

P

-

G

A

T

K

T

Y

Y

R

R

S

S

K

R

D

E

E

E

V

V

Q

Q

K

K

M

V

R

R

S

A

E

A

H

R

D

D

P

P

I

I

E

E

Q

G

V

L

K

K

A

K

R

H

L

I

M

M

D

E

K

W

G

G

W

V

A

A

T

N

E

A

D

N

E

E

L

L

K

K

Q

N

I

I

D

E

K

K

E

R

V

I

R

R

D

G

I

M

V

V

A

D

D

E

S

E

A

V

D

R

F

I

A

A

Q

E

S

E

D

S

P

P

E

F

P

P

D

D

V

P

S

I

E

E

-

E

-

S

L

L

Y

F

T

S

D

D

I

V

L

Y

L

V

Y306 (= Y268) modified: Phosphotyrosine
S310 (= S272) modified: Phosphoserine
S312 (= S274) modified: Phosphoserine

Sites not aligning to the query:

6 modified: Phosphothreonine

6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
51% identity, 90% coverage: 31:342/348 of query aligns to 28:314/340 of 6cerE

query
sites
6cerE

F

L

S

T

K

R

E

E

D

D

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

Q

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q
|
Q

L

L

Y

Y

G

K

M

Q

G

K

F

I

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

T

D

D

Q

H

V

L

I

I

T

T

G

A

Y
|
Y

R
|
R

D

A

H

H

G

G

H

F

M

T

L

F

A

T

C

R

G

G

M

L

S

S

A

V

R

R

G

E

V

I

M

L

A

A

E

E

L

L

T

T

G

G

R

R

R

K

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

A

K

-

E

-

K

K

H

N

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
x
M

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

N

G

G

N

K

D

D

N

E

V

V

S

C

L

L

A

T

Y

L

F

Y

G

G

D

D

G

G

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

F

E

E

S

A

F

Y

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

I

Y

F

I

I

V

C

E

E

N

N

R

R

Y

-

A

-

M

-

G

-

T

-

S

-

V

-

S

-

R

R

A

A

S

A

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

D

S

F

F

-

G

-

I

I

P

P

G

G

Y

L

Q

R

V

V

D

D

G

G

M

M

D

D

V

I

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

R

E

F

A

A

V

A

E

A

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L

M

E

E

M

L

L

Q

T

T

Y

Y

R
|
R

Y

Y

R
x
H

G

-

H

-

S

-

M

-

S

-

D

-

P

-

A

-

K

-

Y

-

R

-

S

-

K

-

D

E

E

E

V

I

Q

Q

K

E

M

V

R

R

S

S

E

K

H

S

D

D

P

P

I

I

E

M

Q

L

V

L

K

K

A

D

R

R

L

M

M

V

D

N

K

S

G

N

W

L

A

A

T

S

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

D

K

V

E

E

V

V

R

R

D

K

I

E

V

I

A

E

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

A

D

D

P

P

E

E

P

P

D

P

V

L

S

E

E

E

L

L

active site: Q52 (= Q55), G137 (= G142), R252 (= R267)
binding magnesium ion: R252 (= R267), H254 (≠ R269)
binding thiamine diphosphate: Y90 (= Y93), R91 (= R94), M139 (≠ V144), R252 (= R267)

6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
51% identity, 90% coverage: 31:342/348 of query aligns to 29:316/342 of 6cerA

query
sites
6cerA

F

L

S

T

K

R

E

E

D

D

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

Q

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q
|
Q

L

L

Y

Y

G

K

M

Q

G

K

F

I

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

T

D

D

Q

H

V

L

I

I

T

T

G

A

Y
|
Y

R
|
R

D

A

H

H

G

G

H

F

M

T

L

F

A

T

C

R

G

G

M

L

S

S

A

V

R

R

G

E

V

I

M

L

A

A

E

E

L

L

T

T

G

G

R

R

R

K

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

A

K

-

E

-

K

K

H

N

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
x
M

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

N

G

G

N

K

D

D

N

E

V

V

S

C

L

L

A

T

Y

L

F

Y

G

G

D

D

G

G

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

F

E

E

S

A

F

Y

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

I

Y

F

I

I

V

C

E

E

N

N

R

-

Y

-

A

-

M

-

G

-

T

-

S

-

V

-

S

-

R

R

A

A

S

A

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

D

S

F

F

-

G

-

I

I

P

P

G

G

Y

L

Q

R

V

V

D

D

G

G

M

M

D

D

V

I

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

R

E

F

A

A

V

A

E

A

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L

M

E

E

M

L

L

Q

T

T

Y

Y

R
|
R

Y

-

R

-

G

-

H

-

S

-

M

-

S

-

D

-

P

-

A

-

K

-

Y

Y

R

H

S

T

K

R

D

E

E

E

V

I

Q

Q

K

E

M

V

R

R

S

S

E

K

H

S

D

D

P

P

I

I

E

M

Q

L

V

L

K

K

A

D

R

R

L

M

M

V

D

N

K

S

G

N

W

L

A

A

T

S

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

D

K

V

E

E

V

V

R

R

D

K

I

E

V

I

A

E

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

A

D

D

P

P

E

E

P

P

D

P

V

L

S

E

E

E

L

L

active site: Q53 (= Q55), G138 (= G142), R252 (= R267)
binding thiamine diphosphate: Y91 (= Y93), R92 (= R94), M140 (≠ V144), R252 (= R267)

3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
50% identity, 90% coverage: 31:342/348 of query aligns to 28:305/331 of 3exhE

query
sites
3exhE

F

L

S

T

K

R

E

E

D

D

D

G

L

L

K

K

A

Y

Y

Y

R

R

E

M

M

M

L

Q

L

T

I

V

R

R

F

M

E

E

E

L

K

K

A

A

G

D

Q
|
Q

L

L

Y

Y

G

K

M

Q

G

K

F

I

I

I

G

R

G

G

F

F

C

C

H

H

L

L

Y

C

I

D

G

G

Q

Q

E

E

A

A

V

C

V

V

G

G

M

L

Q

E

L

A

A

G

L

I

K

N

E

P

G

T

D

D

Q

H

V

L

I

I

T

T

G

A

Y
|
Y

R
|
R

D

A

H

H

G

G

H

F

M

T

L

F

A

T

C

R

G

G

M

L

S

S

A

V

R

R

G

E

V

I

M

L

A

A

E

E

L

L

T

T

G

G

R

R

R

K

G

G

L

C

S

A

K

K

G

G

K

K

G

G

S

S

M

M

H

H

M

M

F

Y

S

A

K

-

E

-

K

K

H

N

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
|
V

G

G

A

A

Q

Q

V

V

S

P

L

L

G

G

T

A

G

G

L

I

A

A

F

L

A

A

N

C

R

K

Y

Y

R

N

G

G

N

K

D

D

N

E

V

V

S

C

L

L

A

T

Y

L

F

Y

G
|
G

D
|
D

G
|
G

A

A

N

N

Q

Q

G

G

Q

Q

V

I

Y

F

E

E

S

A

F

Y

N

N

M

M

A

A

L

L

W

W

K

K

L

L

P

P

V

C

I

I

Y

F

I

I

V

C

E

E

N

N

N
|
N

R

R

Y

-

A

-

M

-

G

-

T

-

S

-

V

-

S

E

R

R

A

A

S

A

A

A

Q

S

T

T

D

D

F

Y

S

Y

Q

K

R

R

G

G

A

D

S

F

F

-

G

-

I

I

P

P

G

G

Y

L

Q

R

V

V

D

D

G

G

M

M

D

D

V

I

R

L

A

C

V

V

K

R

A

E

A

A

A

T

D

R

E

F

A

A

V

A

E

A

H

Y

C

C

R

R

S

S

G

G

K

K

G

G

P

P

I

I

I

L

L

M

E

E

M

L

L

Q

T

T

Y

Y

R

-

Y

-

R

-

G

-

H

-

S

-

M

-

S

-

D

-

P

-

A

-

K

-

Y

-

R

-

S

-

K

-

D

-

E

-

V

-

Q

-

K

-

M

-

R

-

S

S

E

K

H

S

D

D

P

P

I

I

E

M

Q

L

V

L

K

K

A

D

R

R

L

M

M

V

D

N

K

S

G

N

W

L

A

A

T

S

E

V

D

E

E

E

L

L

K

K

Q

E

I

I

D

D

K

V

E

E

V

V

R

R

D

K

I

E

V

I

A

E

D

D

S

A

A

A

D

Q

F

F

A

A

Q

T

S

A

D

D

P

P

E

E

P

P

D

P

V

L

S

E

E

E

L

L

active site: Q52 (= Q55), G137 (= G142)
binding manganese (ii) ion: D168 (= D173), N197 (= N202)
binding thiamine diphosphate: Y90 (= Y93), R91 (= R94), V139 (= V144), G167 (= G172), D168 (= D173), G169 (= G174), N197 (= N202)

3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 91% coverage: 28:344/348 of query aligns to 35:342/365 of 3dufA

query
sites
3dufA

I

M

A

P

E

E

F

L

S

S

K

D

E

E

D

Q

D

L

L

K

K

E

A

L

Y

M

R

R

E

R

M

M

L

V

L

Y

I

T

R

R

R

I

F

L

E

D

E

Q

K

R

A

S

G

I

Q
x
S

L

L

Y

N

G

R

M

Q

G

G

F

R

I

L

G

G

G

-

F

F

C

Y

H

A

L

P

Y

T

I

A

G

G

Q

Q

E

E

A

A

V

S

V

Q

V

I

G

A

M

S

Q

H

L

F

A

A

L

L

K

E

E

K

G

E

D

D

Q

F

V

I

I

L

T

P

G

G

Y
|
Y

R
|
R

D

D

H

V

G

P

H

Q

M

I

L

I

A

W

C

H

G

G

M

L

S

P

A

L

R

Y

G

Q

V

A

M

F

A

L

E

F

L

S

T

R

G

G

R

H

R

F

G

H

G

G

L

N

S

Q

K

I

G

P

K

E

G

G

G

V

S

N

M

V

H

-

M

-

F

-

S

-

K

-

E

-

K

-

H

-

F

-

Y

L

G

P

H

Q

G
x
I

I

I

V
x
I

G

G

A

A

Q

Q

V

Y

S

I

L

Q

G

A

T

A

G

G

L

V

A

A

F

L

A

G

N

L

R

K

Y

M

R

R

G

G

N

K

D

K

N

A

V

V

S

A

L

I

A

T

Y

Y

F

T

G
|
G

D
|
D

G
|
G

A

G

A

T

N

S

Q

Q

G

G

Q

D

V

F

Y

Y

E

E

S

G

F

I

N

N

M

F

A

A

A

G

L

A

W

F

K

K

L

A

P

P

V

A

I

I

Y

F

I

V

V

V

E

Q

N

N

N
|
N

R

R

Y
x
F

A
|
A

M

I

G

S

T

T

S

P

V

V

S

E

R

K

A

Q

S

T

A

V

Q

A

T

K

D

T

F

L

S

A

Q

Q

R

K

G

A

A

V

S

A

F

A

G

G

I

I

P

P

G

G

Y

I

Q

Q

V

V

D

D

G

G

M

M

D

D

V

P

R

L

A

A

V

V

K

Y

A

A

A

V

D

K

E

A

A

A

V

R

E

E

H

R

C

A

R

I

S

N

G

G

K

E

G

G

P

P

I

T

I

L

L

I

E

E

M

T

L

L

T

C

Y

F

R
|
R

Y

Y

R

G

G

P

H
|
H

S
x
T

M

M

S

S

-

G

-

D

D

D

P

P

A

T

K

R

Y
|
Y

R

R

S

S

K

K

D

-

E

E

V

L

Q

E

K

N

M

E

R

W

S

A

E

K

H

K

D

D

P

P

I

L

E

V

Q

R

V

F

K

R

A

K

R

F

L

L

M

E

D

A

K

K

G

G

W

L

A

W

T

S

E

E

D

E

E

E

L

E

K

N

Q

N

I

V

D

I

K

E

E

Q

V

A

R

K

D

E

I

E

V

I

A

K

D

E

S

A

A

I

D

K

F

K

A

A

Q

D

S

E

D

T

P

P

E

K

P

Q

D

K

V

V

S

T

E

D

L

L

Y

I

T

S

active site: S62 (≠ Q55), I139 (≠ G142), R264 (= R267), H268 (= H271), T269 (≠ S272), Y278 (= Y279)
binding magnesium ion: D170 (= D173), N199 (= N202), F201 (≠ Y204)
binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (= Y93), R100 (= R94), I141 (≠ V144), G169 (= G172), D170 (= D173), G171 (= G174), N199 (= N202), F201 (≠ Y204), A202 (= A205), H268 (= H271)

P12694 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha; EC 1.2.4.4 from Homo sapiens (Human) (see 14 papers)
32% identity, 91% coverage: 31:346/348 of query aligns to 97:412/445 of P12694

query
sites
P12694

F

L

S

P

K

K

E

E

D

K

D

V

L

L

K

K

A

L

Y

Y

R

K

E

S

M

M

L

T

L

L

I

L

R

N

R

T

F

M

E

D

E

R

K

I

A

L

G

Y

Q

E

L

S

Y

Q

G

R

M

Q

G

G

F

R

I

I

G

S

G

F

F

Y

C

M

H

T

L

N

Y

Y

I

-

G

G

Q

E

E

E

A

G

V

T

V

H

V

V

G

G

M

S

Q

A

L

A

A

A

L

L

K

D

E

N

G

T

D

D

Q

L

V

V

I

F

T

G

G

Q

Y
|
Y

R
|
R

D

E

H

A

G

G

H

V

M

L

L

M

A

Y

C

R

G

D

M

Y

S

P

A

L

R

E

G

L

V

F

M

M

A

A

E

Q

L

C

T

Y

G

G

R

N

R

I

G

S

G

D

L

L

S

G

K

K

G

G

K

R

G
x
Q

G

M

S

P

M

V

H

H

M

Y

F

G

S

C

K

K

E

E

K

R

H

H

F

F

Y

V

G

T

G

I

H
x
S

G
x
S

I
x
P

V

L

G

A

A
x
T

Q
|
Q

V

I

S

P

L

Q

G

A

T

V

G

G

L

A

A

A

F

Y

A

A

N

A

R

K

Y

R

R

A

G

N

N

A

D

N

N

R

V

V

S

V

L

I

A

C

Y

Y

F

F

G

G

D
x
E

G
|
G

A
|
A

A

A

N

S

Q

E

G

G

Q

D

V

A

Y

H

E

A

S
x
G

F

F

N

N

M

F

A
|
A

L

T

W

L

K

E

L

C

P

P

V

I

I

I

Y

F

I

F

V

C

E
x
R

N

N

N
|
N

R

G

Y
|
Y

A

A

M

I

G

S

T

T

S

P

V

T

S

S

R

E

A

Q

S

Y

A

R

Q

G

T

D

D

G

F

I

S
x
A

Q

A

R

R

G

G

A

P

S
x
G

F

Y

G

G

I

I

P

M

G

S

Y

I

Q
x
R

V

V

D

D

G

G

M

N

D

D

V

V

R

F

A

A

V

V

K

Y

A

N

A

A

A
x
T

D

K

E

E

A

A

V

R

E

R

H

R

C

A

R

V

S

A

G

E

K

N

G

Q

P

P

I

F

I

L

L
x
I

E

E

M

A

L

M

T

T

Y

Y

R

R

Y

I

R

G

G

H

H
|
H

S
|
S

M

T

S

S

-

D

D

D

P

S

A

S

K

A

Y

Y

R

R

S
|
S

K

V

D

D

E

E

V

V

Q

N

K

Y

M

W

R

D

S

K

E

Q

H

D

D

H

P

P

I

I

E

S

Q

R

V

L

K

R

A

H

R

Y

L

L

M

L

D

S

K

Q

G

G

W

W

A

W

T

D

E

E

D

E

E

Q

L

E

K

K

Q

A

I

W

D

R

K

K

E

Q

V

S

R

R

D

R

I

K

V

V

A

M

D

E

S

A

A

F

D

E

F

Q

A

A

Q

E

S

R

D

K

P

P

E

K

P

P

D

N

V

P

S

N

E

L

L

L

Y
x
F

T

S

D

D

I

V

Y158 (= Y93) binding thiamine diphosphate
R159 (= R94) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
Q190 (≠ G125) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
S206 (≠ H141) binding K(+)
S207 (≠ G142) binding thiamine diphosphate
P208 (≠ I143) binding K(+)
T211 (≠ A146) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
Q212 (= Q147) binding K(+)
E238 (≠ D173) binding Mg(2+)
G239 (= G174) binding thiamine diphosphate
A240 (= A175) binding thiamine diphosphate
G249 (≠ S184) to S: in MSUD1A; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852874
A253 (= A188) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
A254 (= A189) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
R265 (≠ E200) binding thiamine diphosphate; to W: in MSUD1A; uncertain significance; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852873
N267 (= N202) binding Mg(2+); to S: in MSUD1A; uncertain significance; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs1568508047
Y269 (= Y204) binding Mg(2+)
A285 (≠ S220) to P: in MSUD1A; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123508
G290 (≠ S225) to R: in MSUD1A; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852871
R297 (≠ Q232) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
T310 (≠ A245) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
I326 (≠ L261) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
H336 (= H271) binding thiamine diphosphate
S337 (= S272) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
S347 (= S281) mutation to A: Does not affect the stability of the BCKD complex.
F409 (≠ Y343) to C: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852872

Sites not aligning to the query:

1:45 modified: transit peptide, Mitochondrion
413 Y → C: in MSUD1A; uncertain significance; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123508
438 Y → N: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852870

P11960 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha; EC 1.2.4.4 from Rattus norvegicus (Rat) (see paper)
31% identity, 91% coverage: 31:346/348 of query aligns to 93:408/441 of P11960

query
sites
P11960

F

L

S

P

K

Q

E

E

D

E

D

V

L

L

K

K

A

L

Y

Y

R

R

E

S

M

M

L

T

L

L

I

L

R

N

R

T

F

M

E

D

E

R

K

I

A

L

G

Y

Q

E

L

S

Y

Q

G

R

M

Q

G

G

F

R

I

I

G

S

G

F

F

Y

C

M

H

T

L

N

Y

Y

I

-

G

G

Q

E

E

E

A

G

V

T

V

H

V

V

G

G

M

S

Q

A

L

A

A

A

L

L

K

E

E

R

G

T

D

D

Q

L

V

V

I

F

T

G

G

Q

Y

Y

R

R

D

E

H

A

G

G

H

V

M

L

L

M

A

Y

C

R

G

D

M

Y

S

P

A

L

R

E

G

L

V

F

M

M

A

A

E

Q

L

C

T

Y

G

G

R

N

R

V

G

S

G

D

L

P

S

G

K

K

G

G

K

R

G

Q

G

M

S

P

M

V

H

H

M

Y

F

G

S

C

K

K

E

E

K

R

H

H

F

F

Y

V

G

T

G

I

H

S

G

S

I

P

V

L

G

A

A

T

Q

Q

V

I

S

P

L

Q

G

A

T

V

G

G

L

A

A

A

F

Y

A

A

N

A

R

K

Y

R

R

A

G

N

N

A

D

N

N

Q

V

I

S

V

L

I

A

C

Y

Y

F

F

G

G

D

E

G

G

A

A

N

S

Q

E

G

G

Q

D

V

A

Y

H

E

A

S

G

F

F

N

N

M

F

A

A

L

T

W

L

K

E

L

C

P

P

V

I

I

I

Y

F

I

F

V

C

E

R

N

N

R

G

Y

Y

A

A

M

I

G

S

T

T

S

P

V

T

S

S

R

E

A

Q

S

Y

A

R

Q

G

T

D

D

G

F

I

S

A

Q

A

R

R

G

G

A

P

S

G

F

Y

G

G

I

I

P

M

G

S

Y

I

Q

R

V

V

D

D

G

G

M

N

D

D

V

V

R

F

A

A

V

V

K

Y

A

N

A

A

A

T

D

K

E

E

A

A

V

R

E

R

H

R

C

A

R

V

S

A

G

E

K

N

G

Q

P

P

I

F

I

L

L

I

E

E

M

A

L

M

T

T

Y

Y

R

R

Y

I

R

G

G

H

H

H

S
|
S

M

T

S

S

-

D

D

D

P

S

A

S

K

A

Y

Y

R

R

S

S

K

V

D

D

E

E

V

V

Q

N

K

Y

M

W

R

D

S

K

E

Q

H

D

D

H

P

P

I

I

E

S

Q

R

V

L

K

R

A

Q

R

Y

L

L

M

L

D

N

K

Q

G

G

W

W

A

W

T

D

E

E

D

E

E

Q

L

E

K

K

Q

A

I

W

D

R

K

K

E

Q

V

S

R

R

D

K

I

K

V

V

A

M

D

E

S

A

A

F

D

E

F

Q

A

A

Q

E

S

R

D

K

P

L

E

K

P

P

D

N

V

P

S

S

E

L

L

L

Y

F

T

S

D

D

I

V

S333 (= S272) modified: Phosphoserine; by BCKDK

Q5SLR4 2-oxoisovalerate dehydrogenase subunit alpha; Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDH E1-alpha; EC 1.2.4.4 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
34% identity, 77% coverage: 38:306/348 of query aligns to 40:308/367 of Q5SLR4

query
sites
Q5SLR4

K

R

A

L

Y

Y

R

R

E

D

M

M

L

L

L

A

I

A

R

R

R

M

F

L

E

D

E

E

K

R

A

Y

G

T

Q

I

L

L

Y

I

G

R

M

T

G

G

F

-

I

K

G

T

G

S

F
|
F

C

I

H

A

L

P

Y

A

I

A

G

G

Q

H

E

E

A

A

V

A

V

Q

V

V

G

A

M

I

Q

A

L

H

A

A

L

I

K

R

E

P

G

G

-

F

D

D

Q

W

V

V

I

F

T

P

G
x
Y

Y
|
Y

R
|
R

D

D

H

H

G

G

H

L

M

A

L

L

A

A

C

L

G

G

M

I

S

P

A

L

R

K

G

E

V

L

M

L

A

G

E

Q

L

M

T

L

G

A

R

T

R

K

G

A

G

D

L

P

S

N

K

K

G

G

K

R

G

Q

G
x
M

S
x
P

M
x
E

H
|
H

M

P

F

G

S

S

K

K

E

A

K

L

H

N

F

F

Y

F

G

T

G

V

H

A

G
x
S

I
x
P

V
x
I

G

A

A

S

Q

H

V

V

S

P

L

P

G

A

T

A

G

G

L

A

A

A

F

I

A

S

N

M

R

K

Y

L

R

L

G

R

N

T

D

G

N

Q

V

V

S

A

L

V

A

C

Y

T

F

F

G
|
G

D
|
D

G
|
G

A
|
A

A
x
T

N
x
S

Q
x
E

G

G

Q

D

V

W

Y

Y

E

A

S

G

F

I

N

N

M

F

A

A

L

V

W

Q

K

G

L

A

P

P

V

A

I

V

Y

F

I

I

V

A

E

E

N

N

N
|
N

R
x
F

Y
|
Y

A
|
A

M
x
I

G

S

T

V

S

D

V

Y

S

R

R

H

A

Q

S

T

A

H

Q

S

T

P

D

T

F

I

S

A

Q

D

R

K

G

A

A

H

S

A

F

F

G

G

I

I

P

P

G

G

Y

Y

Q

L

V

V

D

D

G

G

M

M

D

D

V

V

R

L

A

A

V

S

K

Y

A

Y

A

V

D

K

E

E

A

A

V

V

E

E

H

R

C

A

R

R

S

R

G

G

K

E

G

G

P

P

I

S

I

L

L

V

E

E

M

L

L

R

T

V

Y

Y

R

R

Y

Y

R

G

G

P

H
|
H

S

S

M

S

S

A

-

D

D

D

P

D

A

S

K

R

Y

Y

R

R

S

P

K

K

D

E

E

E

V

V

Q

A

K

F

M

W

R

R

S

K

E

K

H

-

D

D

P

P

I

I

E

P

Q

R

V

F

K

R

A

R

R

F

L

L

M

E

D

A

K

R

G

G

F66 (= F65) binding substrate
YYR 94:96 (≠ GYR 92:94) binding thiamine diphosphate
Y95 (= Y93) binding substrate
MPEH 128:131 (≠ GSMH 126:129) binding substrate
S144 (≠ G142) binding substrate
SPI 144:146 (≠ GIV 142:144) binding thiamine diphosphate
174:180 (vs. 172:178, 57% identical) binding thiamine diphosphate
D175 (= D173) binding Mg(2+)
N204 (= N202) binding Mg(2+)
NFYAI 204:208 (≠ NRYAM 202:206) binding thiamine diphosphate
Y206 (= Y204) binding Mg(2+)
H273 (= H271) binding thiamine diphosphate

1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
30% identity, 91% coverage: 28:344/348 of query aligns to 35:336/358 of 1w85A

query
sites
1w85A

I

M

A

P

E

E

F

L

S

S

K

D

E

E

D

Q

D

L

L

K

K

E

A

L

Y

M

R

R

E

R

M

M

L

V

L

Y

I

T

R

R

R

I

F

L

E

D

E

Q

K

R

A

S

G

I

Q
x
S

L

L

Y

N

G

R

M

Q

G

G

F

R

I

L

G

G

G

-

F

F

C

Y

H

A

L

P

Y

T

I

A

G

G

Q

Q

E

E

A

A

V

S

V

Q

V

I

G

A

M

S

Q

H

L

F

A

A

L

L

K

E

E

K

G

E

D

D

Q

F

V

I

I

L

T

P

G

G

Y
|
Y

R
|
R

D

D

H

V

G

P

H

Q

M

I

L

I

A

W

C

H

G

G

M

L

S

P

A

L

R

Y

G

Q

V

A

M

F

A

L

E

F

L

S

T

R

G

G

R

H

R

F

G

H

G

G

L

N

S

Q

K

I

G

P

K

E

G

G

G

V

S

N

M

V

H

-

M

-

F

-

S

-

K

-

E

-

K

-

H

-

F

-

Y

L

G

P

H

Q

G
x
I

I

I

V
x
I

G

G

A

A

Q

Q

V

Y

S

I

L

Q

G

A

T

A

G

G

L

V

A

A

F

L

A

G

N

L

R

K

Y

M

R

R

G

G

N

K

D

K

N

A

V

V

S

A

L

I

A

T

Y

Y

F

T

G
|
G

D
|
D

G
|
G

A
x
G

A

T

N

S

Q

Q

G

G

Q

D

V

F

Y

Y

E

E

S

G

F

I

N

N

M

F

A

A

A

G

L

A

W

F

K

K

L

A

P

P

V

A

I

I

Y

F

I

V

V

V

E

Q

N

N

N
|
N

R

R

Y
x
F

A
|
A

M
x
I

G

S

T

T

S

P

V

V

S

E

R

K

A

Q

S

T

A

V

Q

A

T

K

D

T

F

L

S

A

Q

Q

R

K

G

A

A

V

S

A

F

A

G

G

I

I

P

P

G

G

Y

I

Q

Q

V

V

D

D

G

G

M

M

D

D

V

P

R

L

A

A

V

V

K

Y

A

A

A

V

D

K

E

A

A

A

V

R

E

E

H

R

C

A

R

I

S

N

G

G

K

E

G

G

P

P

I

T

I

L

L

I

E

E

M

T

L

L

T

C

Y

F

R
|
R

Y

Y

R

G

G

P

H
|
H

S
x
T

M

M

S

S

D

G

P

D

A

S

K

K

Y

-

R

-

S

-

K

-

D

-

E

E

V

L

Q

E

K

N

M

E

R

W

S

A

E

K

H

K

D

D

P

P

I

L

E

V

Q

R

V

F

K

R

A

K

R

F

L

L

M

E

D

A

K

K

G

G

W

L

A

W

T

S

E

E

D

E

E

E

L

E

K

N

Q

N

I

V

D

I

K

E

E

Q

V

A

R

K

D

E

I

E

V

I

A

K

D

E

S

A

A

I

D

K

F

K

A

A

Q

D

S

E

D

T

P

P

E

K

P

Q

D

K

V

V

S

T

E

D

L

L

Y

I

T

S

active site: S62 (≠ Q55), I139 (≠ G142), R264 (= R267), H268 (= H271), T269 (≠ S272)
binding magnesium ion: D170 (= D173), N199 (= N202), F201 (≠ Y204)
binding thiamine diphosphate: Y99 (= Y93), R100 (= R94), I139 (≠ G142), I141 (≠ V144), G169 (= G172), D170 (= D173), G171 (= G174), G172 (≠ A175), N199 (= N202), A202 (= A205), I203 (≠ M206), H268 (= H271)

1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
34% identity, 77% coverage: 38:306/348 of query aligns to 35:303/362 of 1umdA

query
sites
1umdA

K

R

A

L

Y

Y

R

R

E

D

M

M

L

L

L

A

I

A

R

R

R

M

F

L

E

D

E

E

K

R

A

Y

G

T

Q
x
I

L

L

Y

I

G

R

M

T

G

G

F

-

I

K

G

T

G

S

F
|
F

C

I

H

A

L

P

Y

A

I

A

G

G

Q

H

E

E

A

A

V

A

V

Q

V

V

G

A

M

I

Q

A

L

H

A

A

L

I

K

R

E

P

G

G

-

F

D

D

Q

W

V

V

I

F

T

P

G
x
Y

Y
|
Y

R
|
R

D

D

H

H

G

G

H

L

M

A

L

L

A

A

C

L

G

G

M

I

S

P

A

L

R

K

G

E

V

L

M

L

A

G

E

Q

L

M

T

L

G

A

R

T

R

K

G

A

G

D

L

P

S

N

K

K

G

G

K

R

G

Q

G

M

S

P

M

E

H

H

M

P

F

G

S

S

K

K

E

A

K

L

H

N

F

F

Y

F

G

T

G

V

H

A

G
x
S

I
x
P

V
x
I

G

A

A

S

Q

H

V

V

S

P

L

P

G

A

T

A

G

G

L

A

A

A

F

I

A

S

N

M

R

K

Y

L

R

L

G

R

N

T

D

G

N

Q

V

V

S

A

L

V

A

C

Y

T

F

F

G
|
G

D
|
D

G
|
G

A

A

A

T

N

S

Q

E

G

G

Q

D

V

W

Y

Y

E

A

S

G

F

I

N

N

M

F

A

A

L

V

W

Q

K

G

L

A

P

P

V

A

I

V

Y

F

I

I

V

A

E

E

N

N

N
|
N

R

F

Y
|
Y

A
|
A

M
x
I

G

S

T

V

S

D

V

Y

S

R

R

H

A

Q

S

T

A

H

Q

S

T

P

D

T

F

I

S

A

Q

D

R

K

G

A

A

H

S

A

F

F

G

G

I

I

P

P

G

G

Y

Y

Q

L

V

V

D

D

G

G

M

M

D

D

V

V

R

L

A

A

V

S

K

Y

A

Y

A

V

D

K

E

E

A

A

V

V

E

E

H

R

C

A

R

R

S

R

G

G

K

E

G

G

P

P

I

S

I

L

L

V

E

E

M

L

L

R

T

V

Y

Y

R
|
R

Y

Y

R

G

G

P

H
|
H

S
|
S

M

S

S

A

-

D

D

D

P

D

A

S

K

R

Y
|
Y

R

R

S

P

K

K

D

E

E

E

V

V

Q

A

K

F

M

W

R

R

S

K

E

K

H

-

D

D

P

P

I

I

E

P

Q

R

V

F

K

R

A

R

R

F

L

L

M

E

D

A

K

R

G

G

active site: I52 (≠ Q55), S139 (≠ G142), R264 (= R267), H268 (= H271), S269 (= S272), Y277 (= Y279)
binding 2-oxo-4-methylpentanoic acid: F61 (= F65), Y90 (= Y93), S139 (≠ G142)
binding magnesium ion: D170 (= D173), N199 (= N202), Y201 (= Y204)
binding thiamine diphosphate: Y89 (≠ G92), Y90 (= Y93), R91 (= R94), P140 (≠ I143), I141 (≠ V144), G169 (= G172), D170 (= D173), G171 (= G174), N199 (= N202), Y201 (= Y204), A202 (= A205), I203 (≠ M206), H268 (= H271)

Query Sequence

>WP_011975252.1 NCBI__GCF_000017145.1:WP_011975252.1
MAPRKTASVSSRKTAAKPVKKDFAGGTIAEFSKEDDLKAYREMLLIRRFEEKAGQLYGMG
FIGGFCHLYIGQEAVVVGMQLALKEGDQVITGYRDHGHMLACGMSARGVMAELTGRRGGL
SKGKGGSMHMFSKEKHFYGGHGIVGAQVSLGTGLAFANRYRGNDNVSLAYFGDGAANQGQ
VYESFNMAALWKLPVIYIVENNRYAMGTSVSRASAQTDFSQRGASFGIPGYQVDGMDVRA
VKAAADEAVEHCRSGKGPIILEMLTYRYRGHSMSDPAKYRSKDEVQKMRSEHDPIEQVKA
RLMDKGWATEDELKQIDKEVRDIVADSADFAQSDPEPDVSELYTDILL

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