SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_009779126.1 NCBI__GCF_000152985.1:WP_009779126.1 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)

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)
45% identity, 97% coverage: 4:327/333 of query aligns to 56:375/390 of P26284

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P26284

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S232 (= S183) modified: Phosphoserine; by PDK1
S293 (= S246) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
S300 (≠ K252) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4

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)
45% identity, 97% coverage: 4:327/333 of query aligns to 56:375/390 of P35486

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P35486

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S232 (= S183) modified: Phosphoserine; by PDK1
S293 (= S246) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
S300 (≠ K252) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4
K336 (= K287) modified: N6-acetyllysine; mutation K->Q,R: Decreases phosphorylation at S-232 and S-300 but does not affect activity or substrate metabolism.

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)
43% identity, 96% coverage: 3:323/333 of query aligns to 57:375/393 of Q8H1Y0

query
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Q8H1Y0

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R121 (= R68) mutation to C: In iar4-1; reduced sensitivity to several IAA-amino acid conjugates.

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)
44% identity, 96% coverage: 4:324/333 of query aligns to 54:371/388 of P29803

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P29803

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A

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I

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A

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V

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F

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D

S

M227 (= M180) to V: in SPGF70; uncertain significance; dbSNP:rs200969445
S230 (= S183) mutation to A: Slightly reduces enzyme activity.
S291 (= S246) 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 (= S248) 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 (≠ K252) modified: Phosphoserine; by PDK3; mutation to A: Slightly reduces enzyme activity.

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)
43% identity, 95% coverage: 4:321/333 of query aligns to 52:367/396 of P26267

query
sites
P26267

I

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x
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S289 (= S246) modified: Phosphoserine
S296 (≠ K252) modified: Phosphoserine

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)
45% identity, 97% coverage: 4:327/333 of query aligns to 56:375/390 of P08559

query
sites
P08559

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F

Y118 (= Y67) binding thiamine diphosphate
R119 (= R68) binding thiamine diphosphate
A136 (= A85) to T: found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate; uncertain significance; dbSNP:rs138727886
G165 (= G116) binding thiamine diphosphate
V167 (= V118) binding thiamine diphosphate; to M: in PDHAD; disrupts magnesium binding and results in deficient activity of the pyruvate dehydrogenase complex; dbSNP:rs2063174067
D196 (= D147) binding Mg(2+); binding thiamine diphosphate
G197 (= G148) binding thiamine diphosphate
A198 (= A149) binding thiamine diphosphate
N225 (= N176) binding Mg(2+); binding thiamine diphosphate
Y227 (= Y178) binding Mg(2+)
S232 (= S183) modified: Phosphoserine; by PDK1; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.
M282 (≠ L235) to L: in dbSNP:rs2229137
H292 (= H245) binding thiamine diphosphate
S293 (= S246) 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 (≠ K252) modified: Phosphoserine; by PDK1, PDK2, PDK3 and PDK4; mutation to A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.
R302 (= R254) 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

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)
44% identity, 95% coverage: 3:320/333 of query aligns to 75:391/420 of P16387

query
sites
P16387

E

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Y

S313 (= S246) modified: Phosphoserine; by PDK1 and PDK2

Sites not aligning to the query:

1:33 modified: transit peptide, Mitochondrion

6cfoA Human pyruvate dehydrogenase e1 component complex with covalent tdp adduct acetyl phosphinate (see paper)
45% identity, 97% coverage: 4:327/333 of query aligns to 28:347/362 of 6cfoA

query
sites
6cfoA

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G

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F

F

C

I

V

C

E

E

N

N

N
|
N

G

R

Y
|
Y

A
x
G

M

M

G

G

T

T

S

S

V

V

K

E

R

R

T

A

A

A

N

A

H

S

E

T

D

D

I

Y

W

Y

K

K

L

-

G

-

L

R

G

G

Y

D

E

F

M

I

P

P

C

G

G

L

P

R

V

V

D

D

A

G

M

M

N

D

P

I

V

L

A

C

V

V

A

R

E

E

A

A

F

T

D

R

E

F

A

A

I

A

A

A

R

Y

A

C

R

R

R

S

G

G

D

K

G

G

P

P

T

I

F

L

L

M

E

E

L

L

K

Q

T

T

Y

Y

R
|
R

Y

Y

R

H

G

G

H
|
H

S
|
S

M

M

S

S

D

D

-

P

A

G

Q

V

K

S

Y
|
Y

R

R

T

T

K

R

D

E

E

E

V

I

A

Q

E

E

Y

V

Q

R

-

S

K

K

I

S

D

D

P

P

I

I

T

M

Q

L

V

L

K

K

D

D

I

R

L

M

L

V

E

N

K

S

K

N

F

L

A

A

T

S

E

V

E

E

L

L

K

K

A

E

I

I

D

D

K

V

R

E

V

V

K

R

K

K

R

E

V

I

A

E

E

D

C

A

E

A

K

Q

F

F

A

A

E

T

E

A

S

D

D

P

F

E

P

P

E

P

K

L

E

E

V

E

M

L

Y

G

D

Y

V

H

V

I

Y

Y

E

-

Q

S

E

S

D

D

Y

P

P

P

F

F

active site: Q52 (= Q28), G137 (= G116), R260 (= R241), H264 (= H245), S265 (= S246), Y273 (= Y253)
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 (= F38), Y90 (= Y67), R91 (= R68), G137 (= G116), V139 (= V118), G167 (= G146), D168 (= D147), G169 (= G148), N197 (= N176), Y199 (= Y178), G200 (≠ A179), H264 (= H245)
binding magnesium ion: D168 (= D147), N197 (= N176), Y199 (= Y178)

1ni4A Human pyruvate dehydrogenase (see paper)
45% identity, 97% coverage: 4:327/333 of query aligns to 28:347/362 of 1ni4A

query
sites
1ni4A

I

L

T

T

K

R

E

E

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Y

Y

Y

E

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M

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Q

F

T

W

V

R

R

K

R

F

M

E

E

D

L

K

K

L

A

A

D

Q
|
Q

V

L

Y

Y

I

K

Q

Q

Q

K

K

I

V

I

R

R

G

G

F

F

L

C

H

H

L

L

Y

C

N

D

G

G

Q

Q

E

E

A

A

I

C

L

C

A

V

G

G

A

L

L

E

H

A

A

G

M

I

D

N

L

P

T

T

K

-

D

D

K

H

M

L

I

I

T

T

A

A

Y
|
Y

R
|
R

N

A

H

H

V

G

Q

F

P

T

I

F

G

T

M

R

G

G

E

L

D

S

P

V

K

R

R

E

V

I

M

L

A

A

E

E

L

L

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G

K

R

K

K

T

G

G

G

T

C

S

A

M

K

G

G

L

K

G

G

S

S

M

M

H

H

I

M

F

Y

S

A

K

K

E

N

H

-

R

-

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
|
V

G

G

G

A

Q

Q

I

V

P

P

L

L

G

G

A

A

G

G

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I

A

A

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L

G

A

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C

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K

Y

Y

F

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C

L

L

T

T

F

L

F

Y

G
|
G

D
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D

G
|
G

A
|
A

A

A

R

N

Q

Q

G

G

S

Q

L

I

H

F

E

E

T

A

F

Y

N

N

M

M

A

A

M

A

N

L

W

W

K

K

L

L

P

P

V

C

V

I

F

F

C

I

V

C

E

E

N

N

N
|
N

G

R

Y
|
Y

A
x
G

M

M

G

G

T

T

S

S

V

V

K

E

R

R

T

A

A

A

N

A

H

S

E

T

D

D

I

Y

W

Y

K

K

L

-

G

-

L

R

G

G

Y

D

E

F

M

I

P

P

C

G

G

L

P

R

V

V

D

D

A

G

M

M

N

D

P

I

V

L

A

C

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V

A

R

E

E

A

A

F

T

D

R

E

F

A

A

I

A

A

A

R

Y

A

C

R

R

R

S

G

G

D

K

G

G

P

P

T

I

F

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L

M

E

E

L

L

K

Q

T

T

Y

Y

R
|
R

Y

Y

R

H

G

G

H
|
H

S
|
S

M

M

S

S

D

D

-

P

A

G

Q

V

K

S

Y
|
Y

R

R

T

T

K

R

D

E

E

E

V

I

A

Q

E

E

Y

V

Q

R

-

S

K

K

I

S

D

D

P

P

I

I

T

M

Q

L

V

L

K

K

D

D

I

R

L

M

L

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E

N

K

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K

N

F

L

A

A

T

S

E

V

E

E

L

L

K

K

A

E

I

I

D

D

K

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R

E

V

V

K

R

K

K

R

E

V

I

A

E

E

D

C

A

E

A

K

Q

F

F

A

A

E

T

E

A

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D

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P

F

E

P

P

E

P

K

L

E

E

V

E

M

L

Y

G

D

Y

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I

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Y

E

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S

E

S

D

D

Y

P

P

P

F

F

active site: Q52 (= Q28), G137 (= G116), R260 (= R241), H264 (= H245), S265 (= S246), Y273 (= Y253)
binding magnesium ion: D168 (= D147), N197 (= N176), Y199 (= Y178)
binding thiamine diphosphate: Y90 (= Y67), R91 (= R68), V139 (= V118), G167 (= G146), D168 (= D147), G169 (= G148), A170 (= A149), N197 (= N176), G200 (≠ A179), H264 (= H245)

3exeA Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
45% identity, 97% coverage: 4:327/333 of query aligns to 29:348/363 of 3exeA

query
sites
3exeA

I

L

T

T

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R

E

E

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Y

Y

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Q

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G

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Q

E

E

A

A

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C

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G

A

L

L

E

H

A

A

G

M

I

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N

L

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-

D

D

K

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M

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I

I

T

T

A

A

Y
|
Y

R
|
R

N

A

H

H

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G

Q

F

P

T

I

F

G

T

M

R

G

G

E

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E

V

I

M

L

A

A

E

E

L

L

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G

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R

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K

T

G

G

G

T

C

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A

M

K

G

G

L

K

G

G

S

S

M

M

H

H

I

M

F

Y

S

A

K

K

E

N

H

-

R

-

F

F

Y

Y

G

G

H

N

G
|
G

I

I

V
|
V

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G

G

A

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Q

I

V

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P

L

L

G

G

A

A

G

G

L

I

A

A

F

L

G

A

D

C

K

K

Y

Y

F

N

K

G

R

K

D

D

A

E

V

V

T

C

L

L

T

T

F

L

F

Y

G
|
G

D
|
D

G
|
G

A
|
A

A

A

R

N

Q

Q

G

G

S

Q

L

I

H

F

E

E

T

A

F

Y

N

N

M

M

A

A

M

A

N

L

W

W

K

K

L

L

P

P

V

C

V

I

F

F

C

I

V

C

E

E

N

N

N
|
N

G

R

Y
|
Y

A
x
G

M

M

G

G

T

T

S

S

V

V

K

E

R

R

T

A

A

A

N

A

H

S

E

T

D

D

I

Y

W

Y

K

K

L

-

G

-

L

R

G

G

Y

D

E

F

M

I

P

P

C

G

G

L

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V

V

D

D

A

G

M

M

N

D

P

I

V

L

A

C

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V

A

R

E

E

A

A

F

T

D

R

E

F

A

A

I

A

A

A

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Y

A

C

R

R

R

S

G

G

D

K

G

G

P

P

T

I

F

L

L

M

E

E

L

L

K

Q

T

T

Y

Y

R
|
R

Y

Y

R

H

G

G

H
|
H

S
|
S

M

M

S

S

D

D

-

P

A

G

Q

V

K

S

Y
|
Y

R

R

T

T

K

R

D

E

E

E

V

I

A

Q

E

E

Y

V

Q

R

-

S

K

K

I

S

D

D

P

P

I

I

T

M

Q

L

V

L

K

K

D

D

I

R

L

M

L

V

E

N

K

S

K

N

F

L

A

A

T

S

E

V

E

E

L

L

K

K

A

E

I

I

D

D

K

V

R

E

V

V

K

R

K

K

R

E

V

I

A

E

E

D

C

A

E

A

K

Q

F

F

A

A

E

T

E

A

S

D

D

P

F

E

P

P

E

P

K

L

E

E

V

E

M

L

Y

G

D

Y

V

H

V

I

Y

Y

E

-

Q

S

E

S

D

D

Y

P

P

P

F

F

active site: Q53 (= Q28), G138 (= G116), R261 (= R241), H265 (= H245), S266 (= S246), Y274 (= Y253)
binding manganese (ii) ion: D169 (= D147), N198 (= N176), Y200 (= Y178)
binding thiamine diphosphate: Y91 (= Y67), R92 (= R68), V140 (= V118), G168 (= G146), D169 (= D147), G170 (= G148), A171 (= A149), N198 (= N176), Y200 (= Y178), G201 (≠ A179), H265 (= H245)

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)
43% identity, 95% coverage: 3:320/333 of query aligns to 72:388/409 of Q10489

query
sites
Q10489

E

E

I

V

T

T

K

K

E

G

V

E

Y

L

L

L

N

G

W

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Y

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K

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F

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A

L

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A

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A

V

L

Y

Y

I

K

Q

A

Q

K

K

K

V

I

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R

G

G

F

F

L

C

H

H

L

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Y

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N

I

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G

Q

Q

E

E

A

A

I

V

L

A

A

A

G

G

A

I

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E

H

G

A

A

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I

D

T

L

L

T

-

K

D

D

D

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M

I

I

I

T

T

A

S

Y

Y

R

R

N

C

H

H

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G

Q

F

P

A

I

Y

G

T

M

R

G

G

E

L

D

S

P

I

K

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S

V

I

M

I

A

G

E

E

L

L

Y

M

G

G

K

R

K

Q

T

C

G

G

T

A

S

S

M

K

G

G

L

K

G

G

S

S

M

M

H

H

I

I

F

F

S

A

K

K

E

N

H

-

R

-

F

F

Y

Y

G

G

H

N

G

G

I

I

V

V

G

G

G

A

Q

Q

I

I

P

P

L

L

G

G

A

A

G

G

L

I

A

G

F

F

G

A

D

Q

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K

Y

Y

F

L

K

E

R

K

D

P

A

T

V

T

T

T

L

F

T

A

F

L

F

Y

G

G

D

D

G

G

A

A

A

S

R

N

Q

Q

G

G

S

Q

L

A

H

F

E

E

T

A

F

F

N

N

M

M

A

A

M

K

N

L

W

W

K

G

L

L

P

P

V

V

V

I

F

F

C

A

V

C

E

E

N

N

G

K

Y

Y

A

G

M

M

G

G

T

T

S

S

V

A

K

E

R

R

T

S

A

S

N

A

H

M

E

T

D

E

I

F

W

Y

K

K

L

-

G

-

L

R

G

G

Y

Q

E

Y

M

I

P

P

C

G

G

L

P

L

V

V

D

N

A

G

M

M

N

D

P

V

V

L

A

A

V

V

A

L

E

Q

A

A

F

S

D

K

E

F

A

A

I

K

A

K

R

Y

A

T

R

V

R

E

G

N

D

S

G

Q

P

P

T

L

F

L

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M

E

E

L

F

K

V

T

T

Y

Y

R

R

Y
|
Y

R

G

G

G

H

H

S
|
S

M

M

S
|
S

D

D

-

P

A

G

Q

T

K

T

Y

Y

R

R

T

S

K

R

D

E

E

E

V

V

A

Q

E

K

Y

V

Q

R

K

A

I

A

-

R

D

D

P

P

I

I

T

E

Q

G

V

L

K

K

D

K

I

H

L

I

L

M

E

E

K

W

K

G

F

V

A

A

T

N

E

A

E

N

E

E

L

L

K

K

A

N

I

I

D

E

K

K

R

R

V

I

K

R

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G

R

M

V

V

A

D

E

E

C

E

E

V

K

R

F

I

A

A

E

E

S

S

D

P

F

F

P

P

E

D

-

P

-

I

K

E

E

E

V

S

M

L

Y

F

D

S

V

D

V

V

Y

Y

Y306 (= Y242) modified: Phosphotyrosine
S310 (= S246) modified: Phosphoserine
S312 (= S248) modified: Phosphoserine

Sites not aligning to the query:

6 modified: Phosphothreonine

6cerA Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
41% identity, 97% coverage: 4:327/333 of query aligns to 29:327/342 of 6cerA

query
sites
6cerA

I

L

T

T

K

R

E

E

V

D

Y

G

L

L

N

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W

Y

Y

Y

E

R

E

M

M

M

S

Q

F

T

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V

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R

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M

E

E

D

L

K

K

L

A

A

D

Q
|
Q

V

L

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Y

I

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Q

Q

K

K

I

V

I

R

R

G

G

F

F

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H

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Y

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N

D

G

G

Q

Q

E

E

A

A

I

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L

C

A

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G

G

A

L

L

E

H

A

A

G

M

I

D

N

L

P

T

T

K

-

D

D

K

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M

L

I

I

T

T

A

A

Y
|
Y

R
|
R

N

A

H

H

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G

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F

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T

I

F

G

T

M

R

G

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R

R

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active site: Q53 (= Q28), G138 (= G116), R252 (= R241)
binding thiamine diphosphate: Y91 (= Y67), R92 (= R68), M140 (≠ V118), R252 (= R241)

6cerE Human pyruvate dehydrogenase complex e1 component v138m mutation (see paper)
40% identity, 97% coverage: 4:327/333 of query aligns to 28:325/340 of 6cerE

query
sites
6cerE

I

L

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F

active site: Q52 (= Q28), G137 (= G116), R252 (= R241)
binding magnesium ion: R252 (= R241), H254 (≠ R243)
binding thiamine diphosphate: Y90 (= Y67), R91 (= R68), M139 (≠ V118), R252 (= R241)

3exhE Crystal structure of the pyruvate dehydrogenase (e1p) component of human pyruvate dehydrogenase complex (see paper)
40% identity, 97% coverage: 4:327/333 of query aligns to 28:316/331 of 3exhE

query
sites
3exhE

I

L

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