SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_148219579.1 NCBI__GCF_000010725.1:WP_148219579.1 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)

P06959 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; E2; EC 2.3.1.12 from Escherichia coli (strain K12) (see 6 papers)
54% identity, 94% coverage: 14:252/254 of query aligns to 388:629/630 of P06959

query
sites
P06959

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K396 (≠ V22) modified: N6-acetyllysine
H603 (= H226) mutation to C: Abolishes catalytic activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
41 modified: N6-lipoyllysine
144 modified: N6-lipoyllysine
245 modified: N6-lipoyllysine

1eafA Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex (see paper)
56% identity, 92% coverage: 14:247/254 of query aligns to 3:237/243 of 1eafA

query
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1eafA

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active site: S164 (= S173), H216 (= H226)
binding sulfite ion: H216 (= H226), N220 (= N230), G221 (= G231)

P11961 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; E2; EC 2.3.1.12 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 2 papers)
43% identity, 83% coverage: 41:252/254 of query aligns to 213:425/428 of P11961

query
sites
P11961

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Sites not aligning to the query:

1 modified: Initiator methionine, Removed
43 modified: N6-lipoyllysine

P21883 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; E2; S complex, 48 kDa subunit; EC 2.3.1.12 from Bacillus subtilis (strain 168) (see paper)
43% identity, 83% coverage: 41:252/254 of query aligns to 227:439/442 of P21883

query
sites
P21883

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Sites not aligning to the query:

43 modified: N6-lipoyllysine

O00330 Pyruvate dehydrogenase protein X component, mitochondrial; Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex; E3-binding protein; E3BP; Lipoyl-containing pyruvate dehydrogenase complex component X; proX from Homo sapiens (Human) (see 5 papers)
36% identity, 90% coverage: 24:251/254 of query aligns to 273:500/501 of O00330

query
sites
O00330

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D370 (≠ P125) to V: in dbSNP:rs17850649

Sites not aligning to the query:

23 R → C: in dbSNP:rs1049306
97 modified: N6-lipoyllysine
183 R→A: Strongly decreased DLD binding.
185 S→A: Strongly decreased DLD binding.
186 P→A: Strongly decreased DLD binding.
187 A→M: Strongly decreased DLD binding.
189 R→A: Strongly decreased DLD binding.
190 N→A: Decreased DLD binding.; N→K: Moderately decreased interaction with DLD.
193 E→A: Strongly decreased DLD binding.
208 R→A: Strongly decreased DLD binding.; R→D: Decreased interaction with DLD.
210 I→A: Strongly decreased DLD binding.; I→R: Decreased interaction with DLD.; I→S: Decreased interaction with DLD.
213 K→A: Strongly decreased DLD binding.
214 E→A: Strongly decreased DLD binding.

2ii5A Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (e2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (bckdc), isobutyryl-coenzyme a-bound form (see paper)
34% identity, 81% coverage: 46:252/254 of query aligns to 22:230/234 of 2ii5A

query
sites
2ii5A

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A

A

S

A

L

V

G

L

L

K

L

A

Q

Y

F

P

P

R

I

F

L

N

N

A

A

S

S

L

V

D

D

P

E

S

N

G

C

K

Q

Q

N

L

I

I

T

L

Y

K

K

K

A

Y

S

I

H

N

N

I

I

G

G

I

I

A

A

I

M

D

D

T

T

P

E

N

Q

G

G

L

L

L

I

V

V

G

P

V

N

V

V

R

K

D

N

C

V

D

Q

R

I

K

R

G

S

W

I

R

F

E

E

L

I

A

A

A

T

E

E

V

L

A

N

T

R

L

L

S

Q

A

K

K

L

A

G

R

S

E

A

K

G

G

Q

L

L

P

S

L

T

A

N

E

D

M

L

S

I

G

G

C

T

F

F

T

T

I

L

S
|
S

S
x
N

L

I

G
|
G

G

S

L

I

G

G

T

T

G

Y

F

A

T

K

P

P

I

V

I

I

N

L

A

P

P

P

E

E

V

V

A

A

I

I

L

G

G

A

V

L

G

G

R

T

N
x
I

R

K

P

A

V

L

P

P

R

R

P

F

D

N

E

E

T

K

G

G

G

E

I

V

D

C

W

K

R

A

T

Q

M

I

L

M

P

N

L

V

S

S

L

W

S

S

Y

A

D

D

H
|
H

R

R

V

I

I

I

N

D

G

G

A

A

D

T

A

V

A

S

R

R

F

F

T

S

S

N

H

L

L

W

A

K

A

S

L

Y

L

L

A

E

D

N

P

P

A

A

T

F

L

M

I

L

active site: S151 (= S173), H204 (= H226)
binding isobutyryl-coenzyme a: S58 (≠ T80), N152 (≠ S174), G154 (= G176), I178 (≠ N200)

2ii4A Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (e2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (bckdc), coenzyme a-bound form (see paper)
34% identity, 81% coverage: 46:252/254 of query aligns to 22:230/234 of 2ii4A

query
sites
2ii4A

S

A

V

L

A

K

I

I

P

P

H

H

V

F

T

G

H

Y

H

C

D

D

D

E

A

V

D

D

I

L

T

T

E

E

L

L

E

V

A

K

L

L

R
|
R

R

E

L

L

A

K

E

P

D

I

D

A

S

F

A

A

-

R

-

G

V

I

K

K

I

L

T
x
S

P

F

L

M

I

P

F

F

L

F

I

L

K

K

G

A

V

A

A

S

A

L

V

G

L

L

K

L

A

Q

Y

F

P

P

R

I

F

L

N

N

A

A

S

S

L

V

D

D

P

E

S

N

G

C

K

Q

Q

N

L

I

I

T

L

Y

K

K

K

A

Y

S

I

H

N

N

I

I

G

G

I

I

A
|
A

I
x
M

D
|
D

T

T

P

E

N

Q

G

G

L

L

L

I

V

V

G

P

V

N

V

V

R

K

D

N

C

V

D

Q

R

I

K

R

G

S

W

I

R

F

E

E

L

I

A

A

A

T

E

E

V

L

A

N

T

R

L

L

S
x
Q

A

K

K

L

A

G

R

S

E

A

K

G

G

Q

L

L

P

S

L

T

A

N

E

D

M

L

S

I

G

G

C

T

F

F

T

T

I

L

S
|
S

S
x
N

L
x
I

G
|
G

G
x
S

L

I

G

G

T

T

G

Y

F

A

T

K

P

P

I

V

I

I

N

L

A

P

P

P

E

E

V

V

A

A

I

I

L

G

G

A

V

L

G

G

R
x
T

N
x
I

R

K

P

A

V

L

P

P

R

R

P

F

D

N

E

E

T

K

G

G

G

E

I

V

D

C

W

K

R

A

T

Q

M

I

L

M

P

N

L

V

S

S

L

W

S

S

Y

A

D

D

H
|
H

R

R

V

I

I

I

N

D

G
|
G

A

A

D

T

A

V

A

S

R

R

F

F

T

S

S

N

H

L

L

W

A

K

A

S

L

Y

L

L

A

E

D

N

P

P

A

A

T

F

L

M

I

L

active site: S151 (= S173), H204 (= H226)
binding coenzyme a: R43 (= R67), S58 (≠ T80), A99 (= A121), M100 (≠ I122), D101 (= D123), Q130 (≠ S152), S151 (= S173), N152 (≠ S174), I153 (≠ L175), G154 (= G176), S155 (≠ G177), T177 (≠ R199), I178 (≠ N200), H204 (= H226), G209 (= G231)

2ii3A Crystal structure of a cubic core of the dihydrolipoamide acyltransferase (e2b) component in the branched-chain alpha-ketoacid dehydrogenase complex (bckdc), oxidized coenzyme a-bound form (see paper)
34% identity, 81% coverage: 46:252/254 of query aligns to 22:230/234 of 2ii3A

query
sites
2ii3A

S

A

V

L

A

K

I

I

P

P

H

H

V

F

T

G

H

Y

H

C

D

D

D

E

A

V

D

D

I

L

T

T

E

E

L

L

E

V

A

K

L

L

R
|
R

R

E

L

L

A

K

E

P

D

I

D

A

S

F

A

A

-

R

-

G

V

I

K

K

I

L

T
x
S

P
x
F

L
x
M

I

P

F

F

L

F

I

L

K

K

G

A

V

A

A

S

A

L

V

G

L

L

K

L

A

Q

Y

F

P

P

R

I

F

L

N

N

A

A

S

S

L

V

D

D

P

E

S

N

G

C

K

Q

Q

N

L

I

I

T

L

Y

K

K

K

A

Y

S

I

H

N

N

I

I

G

G

I

I

A

A

I
x
M

D
|
D

T

T

P

E

N

Q

G

G

L

L

L

I

V

V

G

P

V

N

V

V

R

K

D

N

C

V

D

Q

R

I

K

R

G

S

W

I

R

F

E

E

L

I

A

A

A

T

E

E

V

L

A

N

T

R

L

L

S

Q

A

K

K

L

A

G

R

S

E

A

K

G

G

Q

L

L

P

S

L

T

A

N

E

D

M

L

S

I

G

G

C

T

F

F

T

T

I

L

S
|
S

S
x
N

L

I

G
|
G

G
x
S

L

I

G

G

T

T

G

Y

F

A

T

K

P

P

I

V

I

I

N

L

A

P

P

P

E

E

V

V

A

A

I

I

L

G

G

A

V

L

G
|
G

R
x
T

N
x
I

R

K

P

A

V

L

P

P

R

R

P

F

D

N

E

E

T

K

G

G

G

E

I

V

D

C

W

K

R

A

T

Q

M

I

L

M

P

N

L

V

S

S

L

W

S

S

Y

A

D

D

H
|
H

R

R

V

I

I

I

N

D

G

G

A

A

D

T

A

V

A

S

R

R

F

F

T

S

S

N

H

L

L

W

A

K

A

S

L

Y

L

L

A

E

D

N

P

P

A

A

T

F

L

M

I

L

active site: S151 (= S173), H204 (= H226)
binding oxidized coenzyme a: R43 (= R67), S58 (≠ T80), F59 (≠ P81), M60 (≠ L82), M100 (≠ I122), D101 (= D123), S151 (= S173), N152 (≠ S174), G154 (= G176), S155 (≠ G177), G176 (= G198), T177 (≠ R199), I178 (≠ N200)

P11181 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168 from Bos taurus (Bovine) (see 2 papers)
34% identity, 81% coverage: 46:252/254 of query aligns to 270:478/482 of P11181

query
sites
P11181

S

A

V

L

A

K

I

I

P

P

H

H

V

F

T

G

H

Y

H

C

D

D

D

E

A

V

D

D

I

L

T

T

E

E

L

L

E

V

A

K

L

L

R
|
R

R

E

L

L

A

K

E

P

D

I

D

A

S

F

A

A

-

R

-

G

V

I

K

K

I

L

T
x
S

P

F

L

M

I

P

F

F

L

F

I

L

K

K

G

A

V

A

A

S

A

L

V

G

L

L

K

L

A

Q

Y

F

P

P

R

I

F

L

N

N

A

A

S

S

L

V

D

D

P

E

S

N

G

C

K

Q

Q

N

L

I

I

T

L

Y

K

K

K

A

Y

S

I

H

N

N

I

I

G

G

I

I

A

A

I

M

D
|
D

T

T

P

E

N

Q

G

G

L

L

L

I

V

V

G

P

V

N

V

V

R

K

D

N

C

V

D

Q

R

I

K

R

G

S

W

I

R

F

E

E

L

I

A

A

A

T

E

E

V

L

A

N

T

R

L

L

S
x
Q

A

K

K

L

A

G

R

S

E

A

K

G

G

Q

L

L

P

S

L

T

A

N

E

D

M

L

S

I

G

G

C

T

F

F

T

T

I

L

S
|
S

S
x
N

L

I

G

G

G
x
S

L

I

G

G

T

T

G

Y

F

A

T

K

P

P

I

V

I

I

N

L

A

P

P

P

E

E

V

V

A

A

I

I

L

G

G

A

V

L

G
|
G

R

T

N
x
I

R

K

P

A

V

L

P

P

R

R

P

F

D

N

E

E

T

K

G

G

G

E

I

V

D

C

W

K

R

A

T

Q

M

I

L

M

P

N

L

V

S

S

L

W

S

S

Y

A

D

D

H

H

R

R

V

I

I

I

N

D

G

G

A

A

D

T

A

V

A

S

R

R

F

F

T

S

S

N

H

L

L

W

A

K

A

S

L

Y

L

L

A

E

D

N

P

P

A

A

T

F

L

M

I

L

R291 (= R67) binding CoA
S306 (≠ T80) binding CoA
D349 (= D123) binding CoA
Q378 (≠ S152) binding CoA
S399 (= S173) binding CoA
N400 (≠ S174) binding CoA
S403 (≠ G177) binding CoA
G424 (= G198) binding CoA
I426 (≠ N200) binding CoA

Sites not aligning to the query:

105 modified: N6-lipoyllysine

P0AFG6 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; EC 2.3.1.61 from Escherichia coli (strain K12) (see 3 papers)
33% identity, 88% coverage: 29:252/254 of query aligns to 179:402/405 of P0AFG6

query
sites
P0AFG6

V

V

P

P

L

M

T

T

R

R

L

L

Q

R

I

K

L

R

A

V

G

A

A

E

A

R

L

L

-

L

-

E

T

A

R

K

N

N

S

S

V

T

A

A

I

M

P

-

H

-

V

L

T

T

H

T

H

F

D

N

D

E

A

V

D

N

I

M

T

K

E

P

L

I

E

M

A

D

L

L

R

R

R

K

R

Q

L

Y

A

G

E

E

-

A

-

F

-

E

D

K

D

R

S

H

A

G

V

I

K

R

I

L

T

G

P

F

L

M

I

S

F

F

L

Y

I

V

K

K

G

A

V

V

A

V

A

E

V

A

L

L

K

K

A

R

Y

Y

P

P

R

E

F

V

N

N

A

A

S

S

L

I

D

D

P

-

S

-

G

G

K

D

Q

D

L

V

I

V

L

Y

K

H

K

N

Y

Y

I

F

N

D

I

V

G

S

I

M

A

A

I

V

D

S

T

T

P

P

N

R

G

G

L

L

L

V

V

T

G

P

V

V

V

L

R

R

D

D

C

V

D

D

R

T

K

L

G

G

W

M

R

A

E

D

L

I

A

E

A

K

E

K

V

I

A

K

T

E

L

L

S

A

A

V

K

K

A

G

R

R

E

D

K

G

G

K

L

L

P

T

L

V

A

E

E

D

M

L

S

T

G

G

C

N

F

F

T

T

I

I

S

T

S

N

L

G

G

G

G

V

L

F

G

G

G

S

T

L

G

M

F

S

T

T

P

P

I

I

N

N

A

P

P

P

E

Q

V

S

A

A

I

I

L

L

G

G

V

M

G

H

-

A

-

I

R

K

N

D

R

R

P

P

V

M

P

A

R

V

P

-

D

-

E

-

T

N

G

G

G

Q

I

V

D

E

W

I

R

L

T

P

M

M

L

M

P

Y

L

L

S

A

L

L

S

S

Y

Y

D

D

H

H

R

R

V

L

I

I

N

D

G

G

A

R

D

E

A

S

A

V

R

G

F

F

T

L

S

V

H

T

L

I

A

K

A

E

L

L

A

E

D

D

P

P

A

T

T

R

L

L

I

L

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
44 modified: N6-lipoyllysine
148 modified: N6-acetyllysine

P11182 Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; 52 kDa mitochondrial autoantigen of primary biliary cirrhosis; Branched chain 2-oxo-acid dehydrogenase complex component E2; BCOADC-E2; Branched-chain alpha-keto acid dehydrogenase complex component E2; BCKAD-E2; BCKADE2; BCKDH-E2; Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; Dihydrolipoamide branched chain transacylase; Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; EC 2.3.1.168 from Homo sapiens (Human) (see 7 papers)
33% identity, 90% coverage: 24:252/254 of query aligns to 249:478/482 of P11182

query
sites
P11182

G

G

E

K

V

D

E

K

T

T

V

E

P

P

L

I

T

K

R

G

L

F

Q

Q

I

-

L

K

A

A

G

M

A

V

A

K

L

T

T

M

R

S

N

A

S

A

V

L

A

K

I

I

P

P

H

H

V

F

T

G

H

Y

H

C

D

D

D

E

A

I

D

D

I

L

T

T

E

E

L

L

E

V

A

K

L

L

R

R

R

E

L

L

A

K

E

P

D

I

D

A

S

F

A

A

-

R

-

G

V

I

K

K

I

L

T

S

P

F

L

M

I

P

F

F

L

F

I

L

K

K

G

A

V

A

A

S

A

L

V

G

L

L

K

L

A

Q

Y

F

P

P

R

I

F

L

N

N

A

A

S

S

L

V

D

D

P

E

S

N

G

C

K

Q

Q

N

L

I

I

T

L

Y

K

K

K

A

Y

S

I

H

N

N

I

I

G

G

I

I

A

A

I

M

D

D

T

T

P

E

N

Q

G

G

L

L

L

I

V

V

G

P

V

N

V

V

R

K

D

N

C

V

D

Q

R

I

K

C

G

S

W

I

R

F

E

D

L

I

A

A

A

T

E

E

V

L

A

N

T

R

L

L

S

Q

A

K

K

L

A

G

R

S

E

V

K
x
S

G

Q

L

L

P

S

L

T

A

T

E

D

M

L

S

T

G

G

C

T

F

F

T

T

I

L

S

S

S

N

L

I

G

G

G

S

L

I

G

G

T

T

G

F

F

A

T

K

P

P

I

V

I

I

N

M

A

P

P

P

E

E

V

V

A

A

I

I

L

G

G

A

V

L

G

G

R

S

N

I

R

K

P

A

V

I

P

P

R

R

P

F

D

N

E

Q

T

K

G

G

G

E

I

V

D

Y

W

K

R

A

T

Q

M

I

L

M

P

N

L

V

S

S

L

W

S

S

Y

A

D

D

H

H

R

R

V

V

I

I

N

D

G

G

A

A

D

T

A

M

A

S

R

R

F

F

T

S

S

N

H

L

L

W

A

K

A

S

L

Y

L

L

A

E

D

N

P

P

A

A

T

F

L

M

I

L

S384 (≠ K158) to G: in dbSNP:rs12021720

Sites not aligning to the query:

105 K→A: Abolishes lipoylation but retains normal interaction with PPM1K.
145:160 Critical for association with PPM1K
147 E→A: Has no effect on the interaction with PPM1K.
148 E→A: Completely abolishes the interaction with PPM1K.
149 D→A: Completely abolishes the interaction with PPM1K.
152 E→A: Has no effect on the interaction with PPM1K.
159 D→A: Has no effect on the interaction with PPM1K.

Q9N0F1 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K; E2o; PE2o; EC 2.3.1.61 from Sus scrofa (Pig) (see paper)
32% identity, 89% coverage: 27:252/254 of query aligns to 227:452/455 of Q9N0F1

query
sites
Q9N0F1

E

E

T

K

V

M

P

N

L

R

T

M

R

R

L

Q

Q

R

I

I

L

A

A

Q

G

R

A

L

A

K

L

E

T

A

R

Q

N

N

S

T

V

C

A

A

I

M

P

-

H

-

V

L

T

T

H

T

H

F

D

N

D

E

A

I

D

D

I

M

T

S

E

N

L

I

E

Q

A

D

L

M

R

R

R

A

R

R

L

H

A

K

E

E

-

A

-

F

-

L

D

K

S

H

A

N

V

L

K

K

I

L

T

G

P

F

L

M

I

S

F

A

L

F

I

V

K

K

G

A

V

S

A

A

A

F

V

A

L

L

K

Q

A

E

Y

Q

P

P

R

V

F

V

N

N

A

A

S

V

L

I

D

D

P

D

S

T

G

T

K

K

Q

E

L

V

I

V

L

Y

K

R

K

D

Y

Y

I

I

N

D

I

I

G

S

I

V

A

A

I

V

D

A

T

T

P

P

N

R

G

G

L

L

L

V

V

V

G

P

V

V

V

I

R

R

D

N

C

V

D

E

R

T

K

M

G

N

W

Y

R

A

E

D

L

I

A

E

A

R

E

T

V

I

A

S

T

E

L

L

S

G

A

E

K

K

A

A

R

R

E

K

K

N

G

E

L

L

P

A

L

I

A

E

E

D

M

M

S

D

G

G

C

T

F

F

T

T

I

I

S
|
S

S

N

L

G

G

G

G

V

L

F

G

G

G

S

T

L

G

F

F

G

T

T

P

P

I

I

N

N

A

P

P

P

E

Q

V

S

A

A

I

I

L

L

G

G

V

M

G

-

R

-

N

H

R

A

P

I

V

V

P

D

R

R

P

P

D

V

E

A

T

V

G

G

-

K

I

V

D

E

W

I

R

R

T

P

M

M

L

M

P

Y

L

V

S

A

L

L

S

T

Y

Y

D

D

H
|
H

R

R

V

L

I

I

N
x
D

G

G

A

R

D

E

A

A

A

V

R

T

F

F

T

L

S

R

H

K

L

I

A

K

A

A

L

A

L

V

A

E

D

D

P

P

A

R

T

V

L
|
L

I
x
L

S374 (= S173) mutation to A: Loss of activity.
H426 (= H226) active site; mutation to C: 16% of activity.
D430 (≠ N230) active site; mutation D->A,E,N: Loss of activity.

Sites not aligning to the query:

451:453 mutation LLL->AAA,DDD: Loss of activity.

P11179 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K; EC 2.3.1.61 from Bos taurus (Bovine) (see paper)
32% identity, 89% coverage: 27:252/254 of query aligns to 227:452/455 of P11179

query
sites
P11179

E

E

T

K

V

M

P

N

L

R

T

M

R

R

L

Q

Q

R

I

I

L

A

A

Q

G

R

A

L

A

K

L

E

T

A

R

Q

N

N

S

T

V

C

A

A

I

M

P

-

H

-

V

L

T

T

H

T

H

F

D

N

D

E

A

I

D

D

I

M

T

S

E

N

L

I

E

Q

A

E

L

M

R

R

R

A

R

R

L

H

A

K

E

D

-

A

-

F

-

L

D

K

S

H

A

N

V

L

K

K

I

L

T

G

P

F

L

M

I

S

F

A

L

F

I

V

K

K

G

A

V

S

A

A

A

F

V

A

L

L

K

Q

A

E

Y

Q

P

P

R

V

F

V

N

N

A

A

S

V

L

I

D

D

P

D

S

A

G

T

K

K

Q

E

L

V

I

V

L

Y

K

R

K

D

Y

Y

I

I

N

D

I

I

G

S

I

V

A

A

I

V

D

A

T

T

P

P

N

R

G

G

L

L

L

V

V

V

G

P

V

V

V

I

R

R

D

N

C

V

D

E

R

T

K

M

G

N

W

Y

R

A

E

D

L

I

A

E

A

R

E

T

V

I

A

S

T

E

L

L

S

G

A

E

K

K

A

A

R

R

E

K

K

N

G

E

L

L

P

A

L

I

A

E

E

D

M

M

S

D

G

G

C

T

F

F

T

T

I

I

S

S

S

N

L

G

G

G

G

V

L

F

G

G

G

S

T

L

G

F

F

G

T

T

P

P

I

I

N

N

A

P

P

P

E

Q

V

S

A

A

I

I

L

L

G

G

V

M

G

-

R

-

N

H

R

A

P

I

V

V

P

D

R

R

P

P

D

V

E

V

T

I

G

G

-

K

I

V

D

E

W

V

R

R

T

P

M

M

L

M

P

Y

L

V

S

A

L

L

S

T

Y

Y

D

D

H

H

R

R

V

L

I

I

N

D

G

G

A

R

D

E

A

A

A

V

R

T

F

F

T

L

S

R

H

K

L

I

A

K

A

A

L

A

L

V

A

E

D

D

P

P

A

R

T

V

L

L

I

L

Sites not aligning to the query:

111 modified: N6-lipoyllysine

P36957 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K; EC 2.3.1.61 from Homo sapiens (Human) (see 5 papers)
32% identity, 89% coverage: 27:252/254 of query aligns to 225:450/453 of P36957

query
sites
P36957

E
|
E

T
x
K

V

M

P

N

L

R

T

M

R
|
R

L

Q

Q

R

I

I

L

A

A

Q

G

R

A

L

A

K

L

E

T

A

R

Q

N

N

S

T

V

C

A

A

I

M

P

-

H

-

V

L

T

T

H

T

H

F

D

N

D

E

A

I

D

D

I

M

T

S

E

N

L

I

E

Q

A

E

L

M

R

R

R

A

R

R

L

H

A

K

E

E

-

A

-

F

-

L

D

K

S

H

A

N

V

L

K

K

I

L

T

G

P

F

L

M

I

S

F

A

L

F

I

V

K

K

G

A

V

S

A

A

A

F

V

A

L

L

K

Q

A

E

Y

Q

P

P

R

V

F

V

N

N

A

A

S

V

L

I

D

D

P
x
D

S

T

G

T

K

K

Q

E

L

V

I

V

L

Y

K

R

K

D

Y

Y

I

I

N

D

I

I

G

S

I

V

A

A

I

V

D

A

T

T

P

P

N

R

G

G

L

L

L

V

V

V

G

P

V

V

V

I

R

R

D

N

C

V

D

E

R

A

K

M

G

N

W

F

R

A

E

D

L

I

A

E

A

R

E

T

V

I

A

T

T

E

L

L

S

G

A

E

K

K

A

A

R

R

E

K

K

N

G

E

L

L

P

A

L

I

A

E

E

D

M

M

S

D

G

G

C

T

F

F

T

T

I

I

S

S

S

N

L
x
G

G

G

G

V

L

F

G

G

G

S

T

L

G

F

F

G

T

T

P

P

I

I

N

N

A

P

P

P

E

Q

V

S

A

A

I

I

L

L

G

G

V

M

G

-

R

-

N

H

R

G

P

I

V

F

P

D

R

R

P

P

D

V

E

A

T

I

G

G

-

K

I

V

D

E

W

V

R

R

T

P

M

M

L

M

P

Y

L

V

S

A

L

L

S

T

Y
|
Y

D

D

H
|
H

R

R

V

L

I

I

N

D

G

G

A

R

D

E

A

A

A

V

R

T

F

F

T

L

S

R

H

K

L

I

A

K

A

A

L

A

L

V

A

E

D

D

P

P

A

R

T

V

L

L

I

L

R231 (= R33) to Q: in PPGL7; uncertain significance; not changed dihydrolipoyllysine-residue succinyltransferase activity; dbSNP:rs771616810
D304 (≠ P105) to N: not changed dihydrolipoyllysine-residue succinyltransferase activity; dbSNP:rs373295097
G374 (≠ L175) to E: in PPGL7; decreased dihydrolipoyllysine-residue succinyltransferase activity; dbSNP:rs1270341616
Y422 (= Y224) to C: in PPGL7; uncertain significance; not changed dihydrolipoyllysine-residue succinyltransferase activity; dbSNP:rs778239022
H424 (= H226) active site; mutation to A: Loss of dihydrolipoyllysine-residue succinyltransferase activity.

Sites not aligning to the query:

1:67 modified: transit peptide, Mitochondrion
213 natural variant: P -> A
224:226 REK→AEA: Reduced nuclear localization of the 2-oxoglutarate dehydrogenase complex. Reduced histone succinylation.

6zzkA Crystal structure of the catalytic domain of c. Glutamicum acef (e2p) in ternary complex with coa and dihydrolipoamide. (see paper)
35% identity, 74% coverage: 51:237/254 of query aligns to 29:221/240 of 6zzkA

query
sites
6zzkA

H

Q

V

L

T

T

H

Q

H

L

D

H

D

E

A

V

D

D

I

M

T

T

E

R

L

V

E

A

A

E

L

L

R
|
R

R

K

L

N

A
x
K

E

P

-

A

-

F

-

I

D

E

D

K

S

H

A

G

V

V

K

N

I

L

T
|
T

P

Y

L
|
L

I

P

F

F

L

F

I

V

K

K

G

A

V

V

A

V

A

E

V

A

L

L

K

V

A

S

Y

H

P

P

R

N

F

V

N

N

A

A

S

S

L

F

D

N

P

A

S

K

G

T

K

K

Q

E

L

M

I

T

L

Y

K

H

K

S

Y

S

I

V

N

N

I

L

G

S

I

I

A
|
A

I

V

D
|
D

T

T

P

P

N

A

G

G

L
|
L

L

L

V

T

G

P

V

V

V

I

R

H

D

D

C

A

D

Q

R

D

K

L

G

S

W

I

R

P

E

E

L

I

A

A

A

K

E

A

V

I

A

V

T

D

L

L

S

A

A

D

K

R

A

S

R
|
R

E

N

K

N

G

K

L

L

P

K

L

P

A

N

E

D

M

L

S

S

G

G

C

T

F

F

T

T

I

I

S
x
T

S
x
N

L
x
I

G

G

G
x
S

L

E

G

G

G

A

T

L

G

S

F

D

T

T

P
|
P

I
|
I

I

L

N

V

A

P

P

P

E

Q

V

A

A

G

I
|
I

L

L

G

G

V

T

G
|
G

R

A

-
x
I

-

V

N

K

R

R

P

P

V

V

P

V

-

I

R

T

P

E

D

D

E

G

T

I

G

D

G

S

I

I

D

A

W

I

R

R

T

Q

M

M

L

V

P

F

L

L

S

P

L

L

S

T

Y

Y

D

D

H

H

R

Q

V

V

I

V

N

D

G

G

A

A

D

D

A

A

A

G

R

R

F

F

binding coenzyme a: R45 (= R67), K49 (≠ A71), T61 (= T80), L63 (= L82), A102 (= A121), D104 (= D123), R137 (= R156), T154 (≠ S173), N155 (≠ S174), I156 (≠ L175), S158 (≠ G177), G179 (= G198), I181 (vs. gap)
binding 6,8-dimercapto-octanoic acid amide: L109 (= L128), P166 (= P185), I167 (= I186), I175 (= I194)

Sites not aligning to the query:

binding 6,8-dimercapto-octanoic acid amide: 16, 20

6zzjA Crystal structure of the catalytic domain of corynebacterium glutamicum acetyltransferase acef (e2p) in complex with oxidized coa. (see paper)
35% identity, 74% coverage: 51:237/254 of query aligns to 29:221/240 of 6zzjA

query
sites
6zzjA

H

Q

V

L

T

T

H

Q

H

L

D

H

D

E

A

V

D

D

I

M

T

T

E

R

L

V

E

A

A

E

L

L

R
|
R

R

K

L

N

A
x
K

E

P

-

A

-

F

-

I

D

E

D

K

S

H

A

G

V

V

K

N

I

L

T
|
T

P

Y

L
|
L

I

P

F

F

L

F

I

V

K

K

G

A

V

V

A

V

A

E

V

A

L

L

K

V

A

S

Y

H

P

P

R

N

F

V

N

N

A

A

S

S

L

F

D

N

P

A

S

K

G

T

K

K

Q

E

L

M

I

T

L

Y

K

H

K

S

Y

S

I

V

N

N

I

L

G

S

I

I

A
|
A

I
x
V

D
|
D

T

T

P

P

N

A

G

G

L

L

V

T

G

P

V

V

V

I

R

H

D

D

C

A

D

Q

R

D

K

L

G

S

W

I

R

P

E

E

L

I

A

A

A

K

E

A

V

I

A

V

T

D

L

L

S

A

A

D

K

R

A

S

R
|
R

E

N

K

N

G

K

L

L

P

K

L

P

A

N

E

D

M

L

S

S

G

G

C

T

F

F

T

T

I

I

S
x
T

S
x
N

L
x
I

G

G

G
x
S

L

E

G

G

G

A

T

L

G

S

F

D

T

T

P

P

I

I

I

L

N

V

A

P

P

P

E

Q

V

A

A

G

I

I

L

L

G

G

V

T

G
|
G

R

A

-
x
I

-

V

N

K

R

R

P

P

V

V

P

V

-

I

R

T

P

E

D

D

E

G

T

I

G

D

G

S

I

I

D

A

W

I

R

R

T

Q

M

M

L

V

P

F

L

L

S

P

L

L

S

T

Y

Y

D

D

H

H

R

Q

V

V

I

V

N

D

G

G

A

A

D

D

A

A

A

G

R

R

F

F

binding oxidized coenzyme a: R45 (= R67), K49 (≠ A71), T61 (= T80), L63 (= L82), A102 (= A121), V103 (≠ I122), D104 (= D123), R137 (= R156), T154 (≠ S173), N155 (≠ S174), I156 (≠ L175), S158 (≠ G177), G179 (= G198), I181 (vs. gap)

6zzkB Crystal structure of the catalytic domain of c. Glutamicum acef (e2p) in ternary complex with coa and dihydrolipoamide. (see paper)
35% identity, 74% coverage: 51:237/254 of query aligns to 30:222/241 of 6zzkB

query
sites
6zzkB

H

Q

V

L

T

T

H

Q

H

L

D

H

D

E

A

V

D

D

I

M

T

T

E

R

L

V

E

A

A

E

L

L

R
|
R

R

K

L

N

A
x
K

E

P

-

A

-

F

-

I

D

E

D

K

S

H

A

G

V

V

K

N

I

L

T
|
T

P

Y

L
|
L

I

P

F

F

L

F

I

V

K

K

G

A

V

V

A

V

A

E

V

A

L

L

K

V

A

S

Y

H

P

P

R

N

F

V

N

N

A

A

S

S

L

F

D

N

P

A

S

K

G

T

K

K

Q

E

L

M

I

T

L

Y

K

H

K

S

Y

S

I

V

N

N

I

L

G

S

I

I

A
|
A

I
x
V

D
|
D

T

T

P

P

N

A

G

G

L

L

V

T

G

P

V

V

V

I

R

H

D

D

C

A

D

Q

R

D

K

L

G

S

W

I

R

P

E

E

L

I

A

A

A

K

E

A

V

I

A

V

T

D

L

L

S

A

A

D

K

R

A

S

R
|
R

E

N

K

N

G

K

L

L

P

K

L

P

A

N

E

D

M

L

S

S

G

G

C

T

F

F

T

T

I

I

S
x
T

S
x
N

L
x
I

G

G

G
x
S

L

E

G

G

G

A

T

L

G

S

F

D

T

T

P

P

I

I

I

L

N

V

A

P

P

P

E

Q

V

A

A

G

I

I

L

L

G

G

V

T

G
|
G

R

A

-
x
I

-

V

N

K

R

R

P

P

V

V

P

V

-

I

R

T

P

E

D

D

E

G

T

I

G

D

G

S

I

I

D

A

W

I

R

R

T

Q

M

M

L

V

P

F

L

L

S

P

L

L

S

T

Y

Y

D

D

H

H

R

Q

V

V

I

V

N

D

G

G

A

A

D

D

A

A

A

G

R

R

F

F

binding coenzyme a: R46 (= R67), K50 (≠ A71), T62 (= T80), L64 (= L82), A103 (= A121), V104 (≠ I122), D105 (= D123), R138 (= R156), T155 (≠ S173), N156 (≠ S174), I157 (≠ L175), S159 (≠ G177), G180 (= G198), I182 (vs. gap)

Q8NNJ2 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex component E2; PDH component E2; EC 2.3.1.12 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
35% identity, 74% coverage: 51:237/254 of query aligns to 464:656/675 of Q8NNJ2

query
sites
Q8NNJ2

H

Q

V

L

T

T

H

Q

H

L

D

H

D

E

A

V

D

D

I

M

T

T

E

R

L

V

E

A

A

E

L

L

R

R

R

K

L

N

A

K

E

P

-

A

-

F

-

I

D

E

D

K

S

H

A

G

V

V

K

N

I

L

T

T

P

Y

L

L

I

P

F

F

L

F

I

V

K

K

G

A

V

V

A

V

A

E

V

A

L

L

K

V

A

S

Y

H

P

P

R

N

F

V

N

N

A

A

S

S

L

F

D

N

P

A

S

K

G

T

K

K

Q

E

L

M

I

T

L

Y

K

H

K

S

Y

S

I

V

N

N

I

L

G

S

I

I

A

A

I

V

D

D

T

T

P

P

N

A

G

G

L

L

V

T

G

P

V

V

V

I

R

H

D

D

C

A

D

Q

R

D

K

L

G

S

W

I

R

P

E

E

L

I

A

A

A

K

E

A

V

I

A

V

T

D

L

L

S

A

A

D

K

R

A

S

R

R

E

N

K

N

G

K

L

L

P

K

L

P

A

N

E

D

M

L

S

S

G

G

C

T

F

F

T

T

I

I

S

T

S

N

L

I

G

G

G

S

L

E

G

G

G

A

T

L

G

S

F

D

T

T

P

P

I

I

I

L

N

V

A

P

P

P

E

Q

V

A

A

G

I

I

L

L

G

G

V

T

G

G

R

A

-

I

-

V

N

K

R

R

P

P

V

V

P

V

R

I

P

T

D

E

E

D

T

-

G

-

G

G

I

I

D

D

-

S

-

I

-

A

W

I

R

R

T

Q

M

M

L

V

P

F

L

L

S

P

L

L

S

T

Y

Y

D

D

H

H

R

Q

V

V

I

V

N

D

G

G

A

A

D

D

A

A

A

G

R

R

F

F

Sites not aligning to the query:

43 K→Q: No effect on ODH and PDH activity; when associated with Q-162.
162 K→Q: No effect on ODH and PDH activity; when associated with Q-43. Strong reduction in the catalytic efficiency of ODH and slight reduction in that of PDH; when associated with Q-278.
278 K→Q: Strong reduction in the catalytic efficiency of ODH and slight reduction in that of PDH; when associated with Q-162.

6zzmB Crystal structure of the catalytic domain of corynebacterium mustelae predicted acetyltransferase acef (e2p). (see paper)
30% identity, 83% coverage: 28:239/254 of query aligns to 4:221/238 of 6zzmB

query
sites
6zzmB

T

T

V

A

P

K

L

V

T

N

R

R

L

I

Q

R

I

E

L

I

A

T

G

A

A

A

A

K

L

M

T

V

R

E

N

A

S

L

V

Q

A

I

I

S

P

A

H

Q

V

L

T

T

H

H

H

L

D

Q

D

E

A

V

D

D

I

M

T

T

E

K

L

I

E

A

A

E

L

L

R
|
R

R

K

R

E

L

S

A
x
K

-

P

-

A

-

F

E

Q

D

Q

D

K

S

Y

A

G

V

V

K
x
N

I

L

T
|
T

P
x
Y

L
|
L

I

P

F

F

L

F

I

V

K

K

G

A

V

A

A

V

A

E

V

A

L

L

K

V

A

S

Y

H

P

P

R

N

F

V

N

N

A

A

S

S

L

Y

D

N

P

A

S

E

G

T

K

K

Q

E

L

M

I

T

L

Y

K

H

K

A

Y

D

I

V

N

N

I

V

G

A

I

I

A
|
A

I

V

D
|
D

T

T

P

P

N

R

G

G

L

L

V

T

G

P

V

V

V

I

R

H

D

K

C

A

D

Q

R

E

K

L

G

T

W

F

R

P

E

E

L

I

A

A

A

Q

E

A

V

I

A

V

T

D

L

L

S

A

A

D

K

R

A

A

R

R

E

N

K

N

G

K

L

L

P

K

L

P

A

Q

E

D

M

L

S

M

G

G

G

A

C

T

F

F

T

T

I

I

S
x
T

S
x
N

L
x
I

G
|
G

G
x
S

L

E

G

G

G

A

T

L

G

S

F

D

T

T

P

P

I

I

I

L

N

V

A

P

P

P

E

Q

V

A

A

G

I

I

L

L

G

G

-

T

-
x
A

-

A

V
x
I

G

Q

R

K

N

R

R

A

P

V

V

V

P

V

R

T

P

E

D

D

E

G

T

V

G

D

G

A

I

I

D

A

W

I

R

R

T

Q

M

M

L

C

P

Y

L

M

S

P

L

F

S

T

Y

Y

D

D

H

H

R

Q

V

V

I

V

N

D

G

G

A

A

D

D

A

A

A

G

R

R

F

F

T

T

S

T

binding coenzyme a: R43 (= R67), K47 (≠ A71), N57 (≠ K78), T59 (= T80), Y60 (≠ P81), L61 (= L82), A100 (= A121), D102 (= D123), T152 (≠ S173), N153 (≠ S174), I154 (≠ L175), G155 (= G176), S156 (≠ G177), A177 (vs. gap), I179 (≠ V197)

P11180 Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex component E2; PDC-E2; PDCE2; EC 2.3.1.12 from Bos taurus (Bovine) (see paper)
32% identity, 88% coverage: 29:252/254 of query aligns to 423:646/647 of P11180

query
sites
P11180

V

I

P

P

L

I

T

S

R

N

L

I

Q

R

I

R

L

V

A

I

G

A

A

Q

A

R

L

L

T

M

R

Q

N

S

S

K

V

Q

A

T

I

I

P

P

H

H

V

Y

T

Y

H

L

H

S

D

I

D

D

A

V

D

N

I

M

T

G

E

E

L

V

E

L

A

L

L

V

R

R

R

K

R

E

L

L

A

N

E

K

D

M

-

L

D

E

S

G

A

K

V

S

K

K

I

I

T

S

P

V

L

N

I

D

F

F

L

I

I

I

K

K

G

A

V

S

A

A

A

L

V

A

L

C

K

L

A

K

Y

V

P

P

R

E

F

A

N

N

A

S

S

S

-

W

L

M

D

D

P

T

S

V

G

I

K

R

Q

Q

L

-

I

-

L

-

K

N

K

H

Y

V

I

V

N

D

I

I

G

S

I

V

A

A

I

V

D

S

T

T

P

P

N

A

G

G

L

L

L

I

V

T

G

P

V

I

V

V

R

F

D

N

C

A

D

H

R

I

K

K

G

G

W

L

R

E

E

T

L

I

A

A

A

N

E

D

V

V

A

V

T

S

L

L

S

A

A

T

K

K

A

A

R

R

E

E

K

G

G

K

L

L

P

Q

L

P

A

H

E

E

M

F

S

Q

G

G

C

T

F

F

T

T

I

I

S

S

S

N

L

L

G

G

G

M

L

F

G

G

G

I

T

K

G

N

F

F

T

S

P

A

I

I

N

N

A

P

P

P

E

Q

V

A

A

C

I

I

L

L

G

A

V

I

G

G

-

A

-

S

R

E

N

D

R

R

P

L

V

V

P

P

R

A

P

D

D

N

E

E

T

K

G

-

G

G

I

F

D

D

W

V

R

A

T

S

M

M

L

M

P

S

L

V

S

T

L

L

S

S

Y

C

D

D

H

H

R

R

V

V

I

V

N

D

G

G

A

A

D

V

A

G

A

A

R

Q

F

W

T

L

S

A

H

E

L

F

A

R

A

K

L

Y

L

L

A

E

D

K

P

P

A

I

T

T

L

M

I

L

Sites not aligning to the query:

132 modified: N6-lipoyllysine

Query Sequence

>WP_148219579.1 NCBI__GCF_000010725.1:WP_148219579.1
MTATDPTKSSAAAPTPQFDFSVYGEVETVPLTRLQILAGAALTRNSVAIPHVTHHDDADI
TELEALRRRLAEDDSAVKITPLIFLIKGVAAVLKAYPRFNASLDPSGKQLILKKYINIGI
AIDTPNGLLVGVVRDCDRKGWRELAAEVATLSAKAREKGLPLAEMSGGCFTISSLGGLGG
TGFTPIINAPEVAILGVGRNRPVPRPDETGGIDWRTMLPLSLSYDHRVINGADAARFTSH
LAALLADPATLIDV

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