SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_050656427.1 NCBI__GCF_002893965.1:WP_050656427.1 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 20 (the maximum) hits to proteins with known functional sites (download)

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, 92% coverage: 26:327/327 of query aligns to 41:350/367 of Q5SLR4

query
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Q5SLR4

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F66 (= F52) binding substrate
YYR 94:96 (≠ QGR 79:81) binding thiamine diphosphate
Y95 (≠ G80) binding substrate
MPEH 128:131 (≠ VP-H 115:117) binding substrate
S144 (≠ A130) binding substrate
SPI 144:146 (≠ ATL 130:132) binding thiamine diphosphate
174:180 (vs. 160:166, 43% identical) binding thiamine diphosphate
D175 (= D161) binding Mg(2+)
N204 (= N190) binding Mg(2+)
NFYAI 204:208 (≠ NGISV 190:194) binding thiamine diphosphate
Y206 (≠ I192) binding Mg(2+)
H273 (= H259) binding thiamine diphosphate

1umdA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methyl-2-oxopentanoate as an intermediate (see paper)
34% identity, 92% coverage: 26:327/327 of query aligns to 36:345/362 of 1umdA

query
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1umdA

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active site: I52 (= I42), S139 (≠ A130), R264 (= R255), H268 (= H259), S269 (≠ W260), Y277 (= Y267)
binding 2-oxo-4-methylpentanoic acid: F61 (= F52), Y90 (≠ G80), S139 (≠ A130)
binding magnesium ion: D170 (= D161), N199 (= N190), Y201 (≠ I192)
binding thiamine diphosphate: Y89 (≠ Q79), Y90 (≠ G80), R91 (= R81), P140 (≠ T131), I141 (≠ L132), G169 (= G160), D170 (= D161), G171 (= G162), N199 (= N190), Y201 (≠ I192), A202 (≠ S193), I203 (≠ V194), H268 (= H259)

1umcA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 with 4-methylpentanoate (see paper)
34% identity, 92% coverage: 26:327/327 of query aligns to 36:345/362 of 1umcA

query
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1umcA

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active site: I52 (= I42), S139 (≠ A130), R264 (= R255), H268 (= H259), S269 (≠ W260), Y277 (= Y267)
binding 4-methyl valeric acid: Y90 (≠ G80), H126 (= H117)
binding magnesium ion: D170 (= D161), N199 (= N190), Y201 (≠ I192)
binding thiamine diphosphate: Y89 (≠ Q79), Y90 (≠ G80), R91 (= R81), I141 (≠ L132), G169 (= G160), D170 (= D161), G171 (= G162), N199 (= N190), Y201 (≠ I192), I203 (≠ V194), H268 (= H259)

1umbA Branched-chain 2-oxo acid dehydrogenase (e1) from thermus thermophilus hb8 in holo-form (see paper)
34% identity, 92% coverage: 26:327/327 of query aligns to 36:345/362 of 1umbA

query
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V

E

E

A

L

V

R

V

V

T

Y

R
|
R

V

Y

G

G

G

P

H
|
H

W
x
S

E

S

G

A

-

D

D

D

A

D

Q

S

K

R

Y
|
Y

R

R

P

P

E

K

D

E

F

E

L

V

S

A

T

F

Y

W

R

R

-

K

D

D

P

P

L

I

D

P

I

R

M

F

R

R

S

R

R

F

L

L

D

E

A

A

-

R

-

G

-

L

-

W

-

N

-

E

L

E

L

W

A

E

D

E

Q

D

I

V

V

R

A

E

A

I

R

R

A

A

E

E

V

L

A

E

E

R

A

G

L

L

A

K

E

E

A

A

-

E

E

E

A

A

A

G

P

P

L

V

P

P

D

-

P

P

S

E

V

W

I

M

M

F

K

E

D

D

V

V

F

F

A

A

active site: I52 (= I42), S139 (≠ A130), R264 (= R255), H268 (= H259), S269 (≠ W260), Y277 (= Y267)
binding magnesium ion: D170 (= D161), N199 (= N190), Y201 (≠ I192)
binding thiamine diphosphate: Y89 (≠ Q79), Y90 (≠ G80), R91 (= R81), P140 (≠ T131), I141 (≠ L132), G169 (= G160), D170 (= D161), G171 (= G162), N199 (= N190), Y201 (≠ I192), A202 (≠ S193), I203 (≠ V194), H268 (= H259)

3dufA Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 92% coverage: 15:314/327 of query aligns to 36:333/365 of 3dufA

query
sites
3dufA

P

P

E

E

S

L

L

S

D

D

P

E

R

Q

L

L

A

K

I

-

D

E

I

L

F

M

T

R

V

R

M

M

A

V

R

Y

A

T

R

R

A

-

I

I

E

L

D

D

A

Q

V

R

Q

S

I

I

H
x
S

I

L

R

N

D

R

H

Q

G

G

F

R

A

L

G

G

F

F

W

Y

H

A

P

P

G

T

K

A

G

G

Q

Q

E

E

G

A

A

S

V

Q

A

I

G

A

A

S

V

H

A

F

A

A

M

L

R

E

D

K

D

E

D

D

Y

F

L

I

F

L

Y

P

Q

G

G
x
Y

R
|
R

G

D

A

V

T

P

W

Q

P

I

L

I

A

W

K

H

G

G

M

L

T

P

M

L

G

Y

P

Q

I

A

I

F

G

L

D

F

L

S

L

R

G

G

K

H

V

F

T

H

G

G

S

N

T

Q

G

I

G

P

K

E

G

G

A

V

G

N

V

V

P

-

H

-

W

-

A

-

D

-

P

-

A

-

L

-

G

-

I

-

M

L

G

P

E

P

G

Q

A
x
I

T

I

L
x
I

G

G

S

A

V

Q

Y

Y

P

I

V

Q

A

A

G

G

A

V

A

A

L

L

S

G

A

L

Q

K

M

M

R

R

G

G

T

K

G

K

Q

A

V

V

A

A

L

I

A

T

D

Y

F

T

G
|
G

D
|
D

G
|
G

T

G

A

T

A

S

R

Q

G

G

T

D

F

F

H

Y

E

E

T

G

L

I

L

N

E

F

A

A

S

G

R

A

W

F

K

K

L

A

P

P

L

A

V

I

Y

F

F

V

C

V

E

Q

N

N

N
|
N

G

R

I
x
F

S
x
A

V

I

T

S

T

T

P

P

F

V

E

E

S

K

V

Q

S

T

P

V

T

A

R

K

T

T

I

L

A

A

E

Q

R

K

A

A

T

V

A

A

Y

A

G

G

I

I

P

P

G

G

V

I

R

Q

V

V

D

D

G

G

H

M

D

D

A

P

V

L

A

A

V

V

Y

Y

H

A

A

A

T

V

K

K

A

A

I

R

D

E

R

R

A

A

R

I

D

N

G

G

Q

E

G

G

P

P

S

T

L

L

I

I

E

E

A

T

V

L

V

C

T

F

R
|
R

V

Y

G

G

G

P

H
|
H

W
x
T

E

M

G

S

-

G

-

D

D

D

A

P

Q

T

K

R

Y
|
Y

R

R

P

S

E

K

D

E

F

L

L

E

S

N

T

E

Y

W

-

A

-

K

R

K

D

D

P

P

L

L

D

V

I

R

M

F

R

R

S

K

R

F

L

L

D

E

A

A

L

K

-

G

-

L

-

W

-

S

-

E

L

E

A

E

D

N

Q

N

I

V

V

I

A

E

A

Q

A

A

R

K

A

E

E

E

V

I

A

K

E

E

A

A

L

I

A

K

E

K

A

A

E

D

A

E

A

T

P

P

active site: S62 (≠ H43), I139 (≠ A130), R264 (= R255), H268 (= H259), T269 (≠ W260), Y278 (= Y267)
binding magnesium ion: D170 (= D161), N199 (= N190), F201 (≠ I192)
binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: Y99 (≠ G80), R100 (= R81), I141 (≠ L132), G169 (= G160), D170 (= D161), G171 (= G162), N199 (= N190), F201 (≠ I192), A202 (≠ S193), H268 (= H259)

1w85A The crystal structure of pyruvate dehydrogenase e1 bound to the peripheral subunit binding domain of e2 (see paper)
31% identity, 92% coverage: 15:314/327 of query aligns to 36:327/358 of 1w85A

query
sites
1w85A

P

P

E

E

S

L

L

S

D

D

P

E

R

Q

L

L

A

K

I

-

D

E

I

L

F

M

T

R

V

R

M

M

A

V

R

Y

A

T

R

R

A

-

I

I

E

L

D

D

A

Q

V

R

Q

S

I

I

H
x
S

I

L

R

N

D

R

H

Q

G

G

F

R

A

L

G

G

F

F

W

Y

H

A

P

P

G

T

K

A

G

G

Q

Q

E

E

G

A

A

S

V

Q

A

I

G

A

A

S

V

H

A

F

A

A

M

L

R

E

D

K

D

E

D

D

Y

F

L

I

F

L

Y

P

Q

G

G
x
Y

R
|
R

G

D

A

V

T

P

W

Q

P

I

L

I

A

W

K

H

G

G

M

L

T

P

M

L

G

Y

P

Q

I

A

I

F

G

L

D

F

L

S

L

R

G

G

K

H

V

F

T

H

G

G

S

N

T

Q

G

I

G

P

K

E

G

G

A

V

G

N

V

V

P

-

H

-

W

-

A

-

D

-

P

-

A

-

L

-

G

-

I

-

M

L

G

P

E

P

G

Q

A
x
I

T

I

L
x
I

G

G

S

A

V

Q

Y

Y

P

I

V

Q

A

A

G

G

A

V

A

A

L

L

S

G

A

L

Q

K

M

M

R

R

G

G

T

K

G

K

Q

A

V

V

A

A

L

I

A

T

D

Y

F

T

G
|
G

D
|
D

G
|
G

T
x
G

A

T

A

S

R

Q

G

G

T

D

F

F

H

Y

E

E

T

G

L

I

L

N

E

F

A

A

S

G

R

A

W

F

K

K

L

A

P

P

L

A

V

I

Y

F

F

V

C

V

E

Q

N

N

N
|
N

G

R

I
x
F

S
x
A

V
x
I

T

S

T

T

P

P

F

V

E

E

S

K

V

Q

S

T

P

V

T

A

R

K

T

T

I

L

A

A

E

Q

R

K

A

A

T

V

A

A

Y

A

G

G

I

I

P

P

G

G

V

I

R

Q

V

V

D

D

G

G

H

M

D

D

A

P

V

L

A

A

V

V

Y

Y

H

A

A

A

T

V

K

K

A

A

I

R

D

E

R

R

A

A

R

I

D

N

G

G

Q

E

G

G

P

P

S

T

L

L

I

I

E

E

A

T

V

L

V

C

T

F

R
|
R

V

Y

G

G

G

P

H
|
H

-
x
T

W

M

E

S

G

G

D

D

A

S

Q

K

K

E

Y

L

R

E

P

N

E

E

D

-

F

-

L

-

S

W

T

A

Y

K

R

K

D

D

P

P

L

L

D

V

I

R

M

F

R

R

S

K

R

F

L

L

D

E

A

A

L

K

-

G

-

L

-

W

-

S

-

E

L

E

A

E

D

N

Q

N

I

V

V

I

A

E

A

Q

A

A

R

K

A

E

E

E

V

I

A

K

E

E

A

A

L

I

A

K

E

K

A

A

E

D

A

E

A

T

P

P

active site: S62 (≠ H43), I139 (≠ A130), R264 (= R255), H268 (= H259), T269 (vs. gap)
binding magnesium ion: D170 (= D161), N199 (= N190), F201 (≠ I192)
binding thiamine diphosphate: Y99 (≠ G80), R100 (= R81), I139 (≠ A130), I141 (≠ L132), G169 (= G160), D170 (= D161), G171 (= G162), G172 (≠ T163), N199 (= N190), A202 (≠ S193), I203 (≠ V194), H268 (= H259)

1dtwA Human branched-chain alpha-keto acid dehydrogenase (see paper)
30% identity, 97% coverage: 11:326/327 of query aligns to 36:350/382 of 1dtwA

query
sites
1dtwA

E

Q

V

I

E

N

P

P

E

-

S

S

L

E

D

D

P

P

R

H

L

L

-

P

-

K

-

E

-

K

A

V

I

L

D

K

I

L

F

Y

T

K

V

S

M

M

A

T

R

L

A

L

R

N

A

T

I

M

E

-

D

D

A

R

V

I

Q

L

I

Y

H
x
E

I

S

R

Q

D

R

H

Q

G

G

F

R

A

I

G

S

F

F

W

Y

H

M

P

T

G

N

K

Y

G

G

Q

E

E

E

G

G

A

T

V

H

A

V

G

G

A

S

V

A

A

A

M

L

R

D

D

N

D

T

D

D

Y

L

L

V

F

F

Y

G

Q
|
Q

G
x
Y

R
|
R

G

E

A

A

T

G

W

V

P

L

L

M

A

Y

K

R

G

D

M

Y

T

P

M

L

G

E

P

L

I

F

I

M

G

A

D

Q

L

C

L

Y

G

G

K

N

V

I

T

-

G

-

S

S

T

D

G

L

G

G

K

K

G

G

A

R

G

Q

V

M

P

P

-

V

H

H

W

Y

A

G

D

C

P

K

A

E

L

R

G

H

I

F

M

V

G

T

E

I

G
x
S

A
x
S

T
x
P

L
|
L

G

A

S
x
T

V
x
Q

Y

I

P

P

V

Q

A

A

A

V

G

G

A

A

L

Y

S

A

A

A

Q

K

M

R

R

A

G

N

T

A

G

N

Q

R

V

V

A

V

L

I

A

C

D

Y

F

F

G
|
G

D
x
E

G
|
G

T
x
A

A

A

A

S

R

E

G

G

T

D

F

A

H

H

E

A

T

G

L

F

L

N

E

F

A

A

S

A

R

T

W

L

K

E

L

C

P

P

L

I

V

I

Y

F

F

F

C

C

E
x
R

N

N

N
|
N

G

G

I
x
Y

S
x
A

V
x
I

T

S

T

T

P

P

F

T

E

S

S

E

V

Q

S

Y

P

R

T

G

R

D

T

G

I

I

A

A

E

A

R

R

A

G

T

P

A

G

Y

Y

G

G

I

I

P

M

G

S

V

I

R

R

V

V

D

D

G

G

H

N

D

D

A

V

V

F

A

A

V

V

Y

Y

H

N

A

A

T

T

K

K

A

E

A

A

I

R

D

R

R

R

A

A

R

V

D

A

G

E

Q

N

G

Q

P

P

S

F

L

L

I

I

E

E

A

A

V

M

V

T

T

Y

R
|
R

V

I

G

G

G

H

H
|
H

W
x
S

E

T

G

S

D

D

A

D

Q

S

K

-

Y

-

R

-

P

-

E

-

D

-

F

-

L

-

S

S

T

A

Y
|
Y

R

R

D

H

P

P

L

I

D

S

I

R

M

L

R

R

S

H

R

Y

L

L

-

L

-

S

-

Q

-

G

-

W

D

D

A

E

L

E

L

Q

A

E

D

K

Q

A

I

W

V

R

A

K

A

Q

A

S

R

R

A

R

E

K

V

V

A

M

E

E

A

A

L

F

A

E

E

Q

A

A

E

E

A

R

A

K

P

P

L

K

P

P

D

N

P

P

S

N

V

L

I

L

M

F

K

S

D

D

V

V

F

Y

active site: E70 (≠ H43), S156 (≠ A130), R281 (= R255), H285 (= H259), S286 (≠ W260), Y294 (= Y276)
binding potassium ion: S155 (≠ G129), S156 (≠ A130), P157 (≠ T131), T160 (≠ S134), Q161 (≠ V135)
binding magnesium ion: E187 (≠ D161), N216 (= N190), Y218 (≠ I192)
binding thiamine diphosphate: Q106 (= Q79), Y107 (≠ G80), R108 (= R81), L158 (= L132), G186 (= G160), E187 (≠ D161), G188 (= G162), A189 (≠ T163), R214 (≠ E188), N216 (= N190), Y218 (≠ I192), A219 (≠ S193), I220 (≠ V194), H285 (= H259)

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, 97% coverage: 11:326/327 of query aligns to 83:409/441 of P11960

query
sites
P11960

E

Q

V

I

E

N

P

P

E

-

S

S

L

E

D

D

P

P

R

H

L

L

A

P

I

Q

D

E

I

E

F

V

T

L

V

K

M

L

A

Y

R

R

A

S

R

M

A

T

I

L

-

L

-

N

-

T

E

M

D

D

A

R

V

I

Q

L

I

Y

H

E

I

S

R

Q

D

R

H

Q

G

G

F

R

A

I

G

S

F

F

W

Y

H

M

P

T

G

N

K

Y

G

G

Q

E

E

E

G

G

A

T

V

H

A

V

G

G

A

S

V

A

A

A

M

L

R

E

D

R

D

T

D

D

Y

L

L

V

F

F

Y

G

Q

Q

G

Y

R

R

G

E

A

A

T

G

W

V

P

L

L

M

A

Y

K

R

G

D

M

Y

T

P

M

L

G

E

P

L

I

F

I

M

G

A

D

Q

L

C

L

Y

G

G

K

N

V

V

T

-

G

-

S

S

T

D

G

P

G

G

K

K

G

G

A

R

G

Q

V

M

P

P

-

V

H

H

W

Y

A

G

D

C

P

K

A

E

L

R

G

H

I

F

M

V

G

T

E

I

G

S

A

S

T

P

L

L

G

A

S

T

V

Q

Y

I

P

P

V

Q

A

A

A

V

G

G

A

A

L

Y

S

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Y

S333 (≠ W260) modified: Phosphoserine; by BCKDK

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)
30% identity, 97% coverage: 11:326/327 of query aligns to 87:413/445 of P12694

query
sites
P12694

E

Q

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Y

Y158 (≠ G80) binding thiamine diphosphate
R159 (= R81) binding thiamine diphosphate; to W: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs769688327
Q190 (≠ G114) to K: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
S206 (≠ G129) binding K(+)
S207 (≠ A130) binding thiamine diphosphate
P208 (≠ T131) binding K(+)
T211 (≠ S134) binding K(+); to M: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123503
Q212 (≠ V135) binding K(+)
E238 (≠ D161) binding Mg(2+)
G239 (= G162) binding thiamine diphosphate
A240 (≠ T163) binding thiamine diphosphate
G249 (≠ T172) 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 (= A176) to T: in MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs199599175
A254 (≠ S177) to D: in MSUD1A; uncertain significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs373713279
R265 (≠ E188) 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 (= N190) 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 (≠ I192) binding Mg(2+)
A285 (= A208) 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 (≠ A213) 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 (= R220) to H: in MSUD1A; uncertain significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs200137189
T310 (= T233) to R: in MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852875
I326 (= I249) to T: in MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity
H336 (= H259) binding thiamine diphosphate
S337 (≠ W260) modified: Phosphoserine; by BCKDK; mutation to A: Substantially decreases the stability of the BCKD complex.
S347 (≠ P269) mutation to A: Does not affect the stability of the BCKD complex.
F409 (≠ M322) to C: in MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs137852872
Y413 (≠ F326) to C: in MSUD1A; uncertain significance; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity; dbSNP:rs398123508

Sites not aligning to the query:

1:45 modified: transit peptide, Mitochondrion
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

3dv0A Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
31% identity, 92% coverage: 15:314/327 of query aligns to 36:318/349 of 3dv0A

query
sites
3dv0A

P

P

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P

active site: S62 (≠ H43), I139 (≠ A130), R264 (= R255), H268 (= H259)
binding magnesium ion: D170 (= D161), N199 (= N190), F201 (≠ I192)
binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (≠ G80), R100 (= R81), I141 (≠ L132), G169 (= G160), D170 (= D161), G171 (= G162), N199 (= N190), F201 (≠ I192), A202 (≠ S193), I203 (≠ V194), R264 (= R255)

2bffA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
29% identity, 97% coverage: 11:326/327 of query aligns to 37:360/392 of 2bffA

query
sites
2bffA

E

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R

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S

E

T

G

S

-

D

D

D

A

S

Q

S

K

A

Y
|
Y

R

R

P

E

E

V

D

G

F

Y

L

W

S

D

T

K

Y

Q

R

D

D

H

P

P

L

I

D

S

I

R

M

L

R

R

S

H

R

Y

L

L

-

L

-

S

-

Q

-

G

-

W

D

D

A

E

L

E

L

Q

A

E

D

K

Q

A

I

W

V

R

A

K

A

Q

A

S

R

R

A

R

E

K

V

V

A

M

E

E

A

A

L

F

A

E

E

Q

A

A

E

E

A

R

A

K

P

P

L

K

P

P

D

N

P

P

S

N

V

L

I

L

M

F

K

S

D

D

V

V

F

Y

active site: E71 (≠ H43), S157 (≠ A130), R282 (= R255), H286 (= H259), S287 (≠ W260), Y295 (= Y267)
binding manganese (ii) ion: E188 (≠ D161), N217 (= N190), Y219 (≠ I192)
binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: Q107 (= Q79), Y108 (≠ G80), R109 (= R81), L159 (= L132), G187 (= G160), E188 (≠ D161), G189 (= G162), A190 (≠ T163), R215 (≠ E188), N217 (= N190), Y219 (≠ I192), A220 (≠ S193), I221 (≠ V194), H286 (= H259)

2bewA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 97% coverage: 11:326/327 of query aligns to 37:358/390 of 2bewA

query
sites
2bewA

E

Q

V

I

E

N

P

P

E

-

S

S

L

E

D

D

P

P

R

H

L

L

-

P

-

K

-

E

-

K

A

V

I

L

D

K

I

L

F

Y

T

K

V

S

M

M

A

T

R

L

A

L

R

N

A

T

I

M

E

-

D

D

A

R

V

I

Q

L

I

Y

H
x
E

I

S

R

Q

D

R

H

Q

G

G

F

R

A

I

G

S

F

F

W

Y

H
x
M

P

T

G

N

K

Y

G

G

Q

E

E

E

G

G

A

T

V

H

A

V

G

G

A

S

V

A

A

A

M

L

R

D

D

N

D

T

D

D

Y

L

L

V

F

F

Y

G

Q
|
Q

G
x
Y

R
|
R

G

E

A

A

T

G

W

V

P

L

L

M

A

Y

K

R

G

D

M

Y

T

P

M

L

G

E

P

L

I

F

I

M

G

A

D

Q

L

C

L

Y

G

G

K

N

V

I

T

-

G

-

S

S

T

D

G

L

G

G

K

K

G

G

A

R

G

Q

V

M

P

P

-

V

H

H

W

Y

A

G

D

C

P

K

A

E

L

R

G

H

I

F

M

V

G

T

E

I

G

S

A
x
S

T

P

L
|
L

G

A

S

T

V

Q

Y

I

P

P

V

Q

A

A

A

V

G

G

A

A

L

Y

S

A

A

A

Q

K

M

R

R

A

G

N

T

A

G

N

Q

R

V

V

A

V

L

I

A

C

D

Y

F

F

G
|
G

D
x
E

G
|
G

T
x
A

A

A

A

S

R

E

G

G

T

D

F

A

H

H

E

A

T

G

L

F

L

N

E

F

A

A

S

A

R

T

W

L

K

E

L

C

P

P

L

I

V

I

Y

F

F

F

C

C

E
x
R

N

N

N
|
N

G

G

I
x
Y

S
x
A

V
x
I

T

S

T

T

P

P

F

T

E

S

S

E

V

Q

S

Y

P

R

T

G

R

D

T

G

I

I

A

A

E

A

R

R

A

G

T

P

A

G

Y

Y

G

G

I

I

P

M

G

S

V

I

R

R

V

V

D

D

G

G

H

N

D

D

A

V

V

F

A

A

V

V

Y

Y

H

N

A

A

T

T

K

K

A

E

A

A

I

R

D

R

R

R

A

A

R

V

D

A

G

E

Q

N

G

Q

P

P

S

F

L

L

I

I

E

E

A

A

V

M

V

T

T

Y

R
|
R

V

I

G

G

G

H

H
|
H

W
x
S

E

T

G

S

-

D

D

D

A

S

Q

S

K

A

Y
|
Y

R

R

P

-

E

-

D

-

F

-

L

-

S

-

T

N

Y

Y

R

W

D

D

P

K

L

Q

D

D

I

H

M

P

R

I

S

S

R

R

L

L

D

R

A

H

L

Y

L

L

A

L

D

S

Q

Q

-

G

-

W

-

D

-

E

-

Q

-

E

-

K

-

A

I

W

V

R

A

K

A

Q

A

S

R

R

A

R

E

K

V

V

A

M

E

E

A

A

L

F

A

E

E

Q

A

A

E

E

A

R

A

K

P

P

L

K

P

P

D

N

P

P

S

N

V

L

I

L

M

F

K

S

D

D

V

V

F

Y

active site: E71 (≠ H43), S157 (≠ A130), R282 (= R255), H286 (= H259), S287 (≠ W260), Y295 (= Y267)
binding manganese (ii) ion: E188 (≠ D161), N217 (= N190), Y219 (≠ I192), A220 (≠ S193)
binding c2-1-hydroxyphenyl-thiamin diphosphate: M82 (≠ H54), Q107 (= Q79), Y108 (≠ G80), R109 (= R81), L159 (= L132), G187 (= G160), E188 (≠ D161), G189 (= G162), A190 (≠ T163), R215 (≠ E188), N217 (= N190), Y219 (≠ I192), A220 (≠ S193), I221 (≠ V194), H286 (= H259)

2bevA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 97% coverage: 11:326/327 of query aligns to 37:358/390 of 2bevA

query
sites
2bevA

E

Q

V

I

E

N

P

P

E

-

S

S

L

E

D

D

P

P

R

H

L

L

-

P

-

K

-

E

-

K

A

V

I

L

D

K

I

L

F

Y

T

K

V

S

M

M

A

T

R

L

A

L

R

N

A

T

I

M

E

-

D

D

A

R

V

I

Q

L

I

Y

H
x
E

I

S

R

Q

D

R

H

Q

G

G

F

R

A

I

G

S

F
|
F

W

Y

H

M

P

T

G

N

K

Y

G

G

Q

E

E

E

G

G

A

T

V

H

A

V

G

G

A

S

V

A

A

A

M

L

R

D

D

N

D

T

D

D

Y

L

L

V

F

F

Y

G

Q
|
Q

G
x
Y

R
|
R

G

E

A

A

T

G

W

V

P

L

L

M

A

Y

K

R

G

D

M

Y

T

P

M

L

G

E

P

L

I

F

I

M

G

A

D

Q

L

C

L

Y

G

G

K

N

V

I

T

-

G

-

S

S

T

D

G

L

G

G

K

K

G

G

A

R

G

Q

V

M

P

P

-

V

H

H

W

Y

A

G

D

C

P

K

A

E

L

R

G

H

I

F

M

V

G

T

E

I

G

S

A
x
S

T

P

L
|
L

G

A

S

T

V

Q

Y

I

P

P

V

Q

A

A

A

V

G

G

A

A

L

Y

S

A

A

A

Q

K

M

R

R

A

G

N

T

A

G

N

Q

R

V

V

A

V

L

I

A

C

D

Y

F

F

G
|
G

D
x
E

G
|
G

T
x
A

A

A

A

S

R

E

G

G

T

D

F

A

H

H

E

A

T

G

L

F

L

N

E

F

A

A

S

A

R

T

W

L

K

E

L

C

P

P

L

I

V

I

Y

F

F

F

C

C

E
x
R

N

N

N
|
N

G

G

I
x
Y

S
x
A

V
x
I

T

S

T

T

P

P

F

T

E

S

S

E

V

Q

S

Y

P

R

T

G

R

D

T

G

I

I

A

A

E

A

R

R

A

G

T

P

A

G

Y

Y

G

G

I

I

P

M

G

S

V

I

R

R

V

V

D

D

G

G

H

N

D

D

A

V

V

F

A

A

V

V

Y

Y

H

N

A

A

T

T

K

K

A

E

A

A

I

R

D

R

R

R

A

A

R

V

D

A

G

E

Q

N

G

Q

P

P

S

F

L

L

I

I

E

E

A

A

V

M

V

T

T

Y

R
|
R

V

I

G

G

G

H

H
|
H

W
x
S

E

T

G

S

-

D

D

D

A

S

Q

S

K

A

Y
|
Y

R

R

P

-

E

-

D

-

F

-

L

-

S

-

T

N

Y

Y

R

W

D

D

P

K

L

Q

D

D

I

H

M

P

R

I

S

S

R

R

L

L

D

R

A

H

L

Y

L

L

A

L

D

S

Q

Q

-

G

-

W

-

D

-

E

-

Q

-

E

-

K

-

A

I

W

V

R

A

K

A

Q

A

S

R

R

A

R

E

K

V

V

A

M

E

E

A

A

L

F

A

E

E

Q

A

A

E

E

A

R

A

K

P

P

L

K

P

P

D

N

P

P

S

N

V

L

I

L

M

F

K

S

D

D

V

V

F

Y

active site: E71 (≠ H43), S157 (≠ A130), R282 (= R255), H286 (= H259), S287 (≠ W260), Y295 (= Y267)
binding manganese (ii) ion: E188 (≠ D161), N217 (= N190), Y219 (≠ I192), A220 (≠ S193)
binding c2-1-hydroxy-2-methyl-butyl-thiamin diphosphate: F80 (= F52), Q107 (= Q79), Y108 (≠ G80), R109 (= R81), S157 (≠ A130), L159 (= L132), G187 (= G160), E188 (≠ D161), G189 (= G162), A190 (≠ T163), R215 (≠ E188), N217 (= N190), Y219 (≠ I192), A220 (≠ S193), I221 (≠ V194), H286 (= H259)

2beuA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 97% coverage: 11:326/327 of query aligns to 37:358/390 of 2beuA

query
sites
2beuA

E

Q

V

I

E

N

P

P

E

-

S

S

L

E

D

D

P

P

R

H

L

L

-

P

-

K

-

E

-

K

A

V

I

L

D

K

I

L

F

Y

T

K

V

S

M

M

A

T

R

L

A

L

R

N

A

T

I

M

E

-

D

D

A

R

V

I

Q

L

I

Y

H
x
E

I

S

R

Q

D

R

H

Q

G

G

F

R

A

I

G

S

F

F

W

Y

H

M

P

T

G

N

K

Y

G

G

Q

E

E

E

G

G

A

T

V

H

A

V

G

G

A

S

V

A

A

A

M

L

R

D

D

N

D

T

D

D

Y

L

L

V

F

F

Y

G

Q
|
Q

G
x
Y

R
|
R

G

E

A

A

T

G

W

V

P

L

L

M

A

Y

K

R

G

D

M

Y

T

P

M

L

G

E

P

L

I

F

I

M

G

A

D

Q

L

C

L

Y

G

G

K

N

V

I

T

-

G

-

S

S

T

D

G

L

G

G

K

K

G

G

A

R

G

Q

V

M

P

P

-

V

H

H

W

Y

A

G

D

C

P

K

A

E

L

R

G

H

I

F

M

V

G

T

E

I

G

S

A
x
S

T

P

L
|
L

G

A

S

T

V

Q

Y

I

P

P

V

Q

A

A

A

V

G

G

A

A

L

Y

S

A

A

A

Q

K

M

R

R

A

G

N

T

A

G

N

Q

R

V

V

A

V

L

I

A

C

D

Y

F

F

G
|
G

D
x
E

G
|
G

T
x
A

A

A

A

S

R

E

G

G

T

D

F

A

H

H

E

A

T

G

L

F

L

N

E

F

A

A

S

A

R

T

W

L

K

E

L

C

P

P

L

I

V

I

Y

F

F

F

C

C

E
x
R

N

N

N
|
N

G

G

I
x
Y

S
x
A

V
x
I

T

S

T

T

P

P

F

T

E

S

S

E

V

Q

S

Y

P

R

T

G

R

D

T

G

I

I

A

A

E

A

R

R

A

G

T

P

A

G

Y

Y

G

G

I

I

P

M

G

S

V

I

R

R

V

V

D

D

G

G

H

N

D

D

A

V

V

F

A

A

V

V

Y

Y

H

N

A

A

T

T

K

K

A

E

A

A

I

R

D

R

R

R

A

A

R

V

D

A

G

E

Q

N

G

Q

P

P

S

F

L

L

I

I

E

E

A

A

V

M

V

T

T

Y

R
|
R

V

I

G

G

G

H

H
|
H

W
x
S

E

T

G

S

-

D

D

D

A

S

Q

S

K

A

Y
|
Y

R

R

P

-

E

-

D

-

F

-

L

-

S

-

T

N

Y

Y

R

W

D

D

P

K

L

Q

D

D

I

H

M

P

R

I

S

S

R

R

L

L

D

R

A

H

L

Y

L

L

A

L

D

S

Q

Q

-

G

-

W

-

D

-

E

-

Q

-

E

-

K

-

A

I

W

V

R

A

K

A

Q

A

S

R

R

A

R

E

K

V

V

A

M

E

E

A

A

L

F

A

E

E

Q

A

A

E

E

A

R

A

K

P

P

L

K

P

P

D

N

P

P

S

N

V

L

I

L

M

F

K

S

D

D

V

V

F

Y

active site: E71 (≠ H43), S157 (≠ A130), R282 (= R255), H286 (= H259), S287 (≠ W260), Y295 (= Y267)
binding manganese (ii) ion: E188 (≠ D161), N217 (= N190), Y219 (≠ I192), A220 (≠ S193)
binding c2-1-hydroxy-3-methyl-propyl-thiamin diphosphate: Q107 (= Q79), Y108 (≠ G80), R109 (= R81), S157 (≠ A130), L159 (= L132), G187 (= G160), E188 (≠ D161), G189 (= G162), A190 (≠ T163), R215 (≠ E188), N217 (= N190), Y219 (≠ I192), A220 (≠ S193), I221 (≠ V194), H286 (= H259)

P35486 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial; PDHE1-A type I; EC 1.2.4.1 from Mus musculus (Mouse) (see 2 papers)
30% identity, 90% coverage: 24:316/327 of query aligns to 62:359/390 of P35486

query
sites
P35486

I

L

D

K

I

Y

F

Y

T

R

V

M

M

M

A

Q

R

T

A

V

R

R

A

R

I

M

E

E

D

L

A

K

V

A

Q

D

I

Q

H

L

I

Y

R

K

D

Q

H

K

G

I

F

I

A

R

G

G

F

F

W

C

H

H

P

L

G

C

K

D

G

G

Q

Q

E

E

G

A

A

C

V

C

A

V

G

G

A

L

V

E

A

A

A

G

M

I

R

N

D

P

D

T

D

D

Y

H

L

L

F

I

Y

T

Q

A

G

Y

R

R

G

A

A

H

T

G

W

F

P

T

L

F

A

T

K

R

G

G

M

L

T

P

M

V

G

R

P

A

I

I

I

L

G

A

D

E

L

L

L

T

G

G

K

R

V

R

T

G

G

G

S

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S232 (≠ P197) modified: Phosphoserine; by PDK1
S293 (≠ W260) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
S300 (≠ K266) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
K336 (≠ D293) modified: N6-acetyllysine; mutation K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.

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)
29% identity, 90% coverage: 24:316/327 of query aligns to 60:357/388 of P29803

query
sites
P29803

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M227 (≠ V194) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
S230 (≠ P197) mutation to A: Slightly reduces enzyme activity.
S291 (≠ W260) 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 (≠ G262) 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 (≠ K266) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.

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)
30% identity, 90% coverage: 24:316/327 of query aligns to 62:359/390 of P26284

query
sites
P26284

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S232 (≠ P197) modified: Phosphoserine; by PDK1
S293 (≠ W260) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
S300 (≠ K266) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4

1wciA Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch (see paper)
30% identity, 97% coverage: 11:326/327 of query aligns to 37:356/388 of 1wciA

query
sites
1wciA

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active site: E71 (≠ H43), S157 (≠ A130), R282 (= R255), H286 (= H259), S287 (≠ W260), Y295 (= Y276)
binding manganese (ii) ion: E188 (≠ D161), N217 (= N190), Y219 (≠ I192), A220 (≠ S193)
binding c2-1-hydroxy-3-methyl-butyl-thiamin: Q107 (= Q79), Y108 (≠ G80), R109 (= R81), L159 (= L132), G187 (= G160), E188 (≠ D161), G189 (= G162), A190 (≠ T163), R215 (≠ E188), N217 (= N190), Y219 (≠ I192), A220 (≠ S193), I221 (≠ V194), H286 (= H259)

3dv0E Snapshots of catalysis in the e1 subunit of the pyruvate dehydrogenase multi-enzyme complex (see paper)
30% identity, 92% coverage: 15:314/327 of query aligns to 36:313/344 of 3dv0E

query
sites
3dv0E

P

P

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x
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active site: S62 (≠ H43), I139 (≠ A130), R264 (= R255)
binding magnesium ion: G169 (= G160), D170 (= D161), Q197 (≠ E188), N199 (= N190)
binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: Y99 (≠ G80), R100 (= R81), I139 (≠ A130), I141 (≠ L132), G169 (= G160), D170 (= D161), G171 (= G162), N199 (= N190), F201 (≠ I192), A202 (≠ S193), I203 (≠ V194)

1w88A The crystal structure of pyruvate dehydrogenase e1(d180n,e183q) bound to the peripheral subunit binding domain of e2 (see paper)
29% identity, 92% coverage: 15:314/327 of query aligns to 35:309/340 of 1w88A

query
sites
1w88A

P

P

E

E

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D

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active site: S61 (≠ H43), I138 (≠ A130), R263 (= R255)
binding magnesium ion: D169 (= D161), N198 (= N190), F200 (≠ I192)
binding thiamine diphosphate: Y98 (≠ G80), R99 (= R81), I140 (≠ L132), G168 (= G160), D169 (= D161), G170 (= G162), A201 (≠ S193), I202 (≠ V194)

Query Sequence

>WP_050656427.1 NCBI__GCF_002893965.1:WP_050656427.1
MATHTSEQLTEVVEPESLDPRLAIDIFTVMARARAIEDAVQIHIRDHGFAGFWHPGKGQE
GAVAGAVAAMRDDDYLFYQGRGATWPLAKGMTMGPIIGDLLGKVTGSTGGKGAGVPHWAD
PALGIMGEGATLGSVYPVAAGAALSAQMRGTGQVALADFGDGTAARGTFHETLLEASRWK
LPLVYFCENNGISVTTPFESVSPTRTIAERATAYGIPGVRVDGHDAVAVYHATKAAIDRA
RDGQGPSLIEAVVTRVGGHWEGDAQKYRPEDFLSTYRDPLDIMRSRLDALLADQIVAAAR
AEVAEALAEAEAAPLPDPSVIMKDVFA

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