SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_054255743.1 NCBI__GCF_001298675.1:WP_054255743.1 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)

Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
36% identity, 94% coverage: 24:539/548 of query aligns to 23:533/541 of Q5SKN9

query
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Q5SKN9

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T184 (= T193) binding Mg(2+)
G302 (= G308) binding tetradecanoyl-AMP
Q322 (≠ H328) binding tetradecanoyl-AMP
G323 (≠ V329) binding tetradecanoyl-AMP
T327 (= T333) binding tetradecanoyl-AMP
E328 (= E334) binding Mg(2+)
D418 (= D425) binding tetradecanoyl-AMP
K435 (= K442) binding tetradecanoyl-AMP
K439 (≠ I446) binding tetradecanoyl-AMP

P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
33% identity, 91% coverage: 44:543/548 of query aligns to 39:536/539 of P0DX84

query
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P0DX84

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H231 (= H237) mutation to A: Retains 74% of wild-type activity.
W235 (= W241) mutation to A: Almost completely abolishes the activity.
G302 (≠ A307) mutation to P: Almost completely abolishes the activity.
G303 (= G308) mutation to P: Almost completely abolishes the activity.
W326 (≠ Y330) mutation to A: Retains 7.7% of wild-type activity.
P333 (vs. gap) mutation to A: Retains 69% of wild-type activity.
R432 (= R440) mutation to A: Retains 4.3% of wild-type activity.
K434 (= K442) mutation to A: Retains 36% of wild-type activity.
D435 (= D443) mutation to A: Retains 76% of wild-type activity.
K438 (≠ I446) mutation to A: Retains 5.6% of wild-type activity.
G440 (= G448) mutation to P: Retains 3.6% of wild-type activity.
G441 (= G449) mutation to P: Retains 2.7% of wild-type activity.
E442 (= E450) mutation to A: Retains 27% of wild-type activity.
W443 (≠ N451) mutation to A: Retains 60% of wild-type activity.
E474 (= E482) mutation to A: Retains 33% of wild-type activity.
K523 (= K530) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
K526 (= K533) mutation to A: Retains 48% of wild-type activity.

6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
33% identity, 91% coverage: 44:543/548 of query aligns to 39:536/538 of 6ijbB

query
sites
6ijbB

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Y

Y

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|
T

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S

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G

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G

G

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P

K

K

G

G

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Y

Y

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H

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A

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H

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N

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W

C

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P

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A

C

A

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W

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G

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W

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A

active site: T185 (= T193), H205 (≠ N213), H231 (= H237), S329 (≠ T333), E330 (= E334), K438 (≠ I446), W443 (≠ N451), A523 (≠ K530)
binding 3-(methylsulfanyl)propanoic acid: W235 (= W241), G303 (= G308), A325 (≠ V329), W326 (≠ Y330), G327 (= G331), M328 (≠ L332)
binding adenosine monophosphate: G303 (= G308), A304 (= A309), A305 (= A310), H324 (= H328), W326 (≠ Y330), G327 (= G331), M328 (≠ L332), S329 (≠ T333), Q359 (= Q363), D417 (= D425)

1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 93% coverage: 24:532/548 of query aligns to 16:502/510 of 1v26B

query
sites
1v26B

F

F

I

L

E

E

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R

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A

A

A

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L

Y

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G

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|
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|
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|
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D

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G

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active site: T177 (= T193), H197 (≠ N213), H223 (= H237), T320 (= T333), E321 (= E334), K432 (≠ I446), W437 (≠ N451)
binding adenosine monophosphate: G295 (= G308), S296 (≠ A309), A297 (= A310), G316 (≠ V329), Y317 (= Y330), G318 (= G331), L319 (= L332), T320 (= T333), D411 (= D425), K428 (= K442), K432 (≠ I446), W437 (≠ N451)
binding magnesium ion: T177 (= T193), E321 (= E334)

6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
33% identity, 91% coverage: 44:543/548 of query aligns to 39:533/533 of 6ihkB

query
sites
6ihkB

R

R

Q

T

T

N

W

W

G

G

E

E

T

I

Y

A

K

A

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Y

Y

L

F

K

Q

N

-

P

-

Q

L

A

K

T

D

E

Q

E

E

A

L

F

L

R

Q

G

D

G

G

W

W

F

F

H

A

S

T

G

G

D
|
D

L

V

A

A

V

T

Q

L

Y

D

P

P

D

D

G

G

Y

Y

I

M

K

T

I

I

K

R

D

D

R
|
R

S

S

K

K

D

D

I

I

I

I

I
x
K

S

S

G

G

G

G

E

E

N
x
W

I

I

S

S

S

S

I

V

E

E

V

L

E

E

D

N

V

I

L

A

Y

V

R

A

H

H

P

P

D

K

V

L

L

A

A

T

V

A

A

A

V

V

V

I

A

G

K

V

P

P

D

H

P

P

K

K

W

W

G

D

E

E

T

R

P

P

C

L

A

L

F

V

V

A

E

V

L

K

K

A

A

E

G

G

A

E

L

D

T

P

T

S

V

E

D

A

D

E

I

L

V

L

Q

E

H

F

C

F

K

D

K

G

H

K

L

I

A

A

G

K

F

W

K

Q

V

V

P

P

R

D

A

K

V

V

V

V

F

F

G

V

E

D

-

A

L

L

P

P

K

L

T

N

S

A

T

T

G

G

K
|
K

I

V

Q

L

K

K

F

R

E

K

L

L

R

R

R

D

K

E

A

F

G

K

S

D

A

A

active site: T185 (= T193), H202 (≠ N213), H228 (= H237), S326 (≠ T333), E327 (= E334), K435 (≠ I446), W440 (≠ N451), K520 (= K530)
binding adenosine-5'-diphosphate: H228 (= H237), G300 (= G308), A301 (= A309), A302 (= A310), H321 (= H328), A322 (≠ V329), W323 (≠ Y330), G324 (= G331), M325 (≠ L332), S326 (≠ T333), Q356 (= Q363), D414 (= D425), R429 (= R440), K520 (= K530)

1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 85% coverage: 24:488/548 of query aligns to 16:464/491 of 1v25A

query
sites
1v25A

F

F

I

L

E

E

R

R

T

A

A

A

E

A

V

L

Y

F

P

G

D

R

R

K

L

E

A

V

I

V

V

S

H

R

-

L

-

H

-

T

G

G

E

E

L

V

-

H

R

R

Q

T

T

T

W

Y

G

A

E

E

T

V

Y

Y

K

Q

R

R

C

A

R

R

Q

R

L

L

A

M

S

G

S

G

L

L

R

R

R

A

A

L

G

G

I

V

G

G

K

V

N

G

D

D

T

R

V

V

A

A

V

T

M

L

L

G

P

F

N

N

T

H

P

F

P

R

M

H

V

L

E

E

A

A

H

Y

F

F

G

A

V

V

P

P

M

G

A

M

G

G

A

A

V

V

L

L

N

H

T

T

L

A

N

N

T

P

R

R

L

L

D

S

P

P

E

K

T

E

I

I

A

A

F

Y

M

I

L

L

D

N

H

H

G

A

E

E

A

D

K

K

A

V

L

L

I

L

V

F

D

D

P

P

E

N

F

L

S

L

A

P

V

L

V

V

A

E

K

A

A

I

L

R

P

G

L

E

R

L

K

K

N

T

P

V

A

Q

P

H

L

F

A

V

L

V

I

M

E

D

V

E

E

K

D

-

A

-

L

-

Y

-

G

-

A

A

P

P

A

E

Q

G

S

Y

L

L

G

A

G

-

T

-

R

-

Y

Y

E

E

D

E

F

-

V

-

A

A

A

L

G

G

D

E

P

E

A

A

F

D

A

P

W

V

E

R

L

V

P

P

G

-

D

-

E

E

W

R

D

A

A

A

I

C

A

G

L

M

N

A

Y

Y

T
|
T

S

T

G

G

T

T

T

T

G

G

N

L

P

P

K

K

G

G

V

V

V

V

Y

Y

H

S

H

H

R

R

G

A

A

L

A

V

I

L

N
x
H

A

S

I

L

S

A

N

A

V

S

L

L

-

V

-

D

E

G

W

T

D

A

M

L

P

S

K

E

H

K

A

D

V

V

Y

V

L

L

W

P

T

V

L

V

P

P

M

M

F

F

H
|
H

C
x
V

N

N

G

A

W

W

C

C

F

L

P

P

W

Y

T

A

V

-

A

A

A

T

R

L

A

V

G

G

V

A

N

K

V

Q

C

V

L

L

-

P

-

G

R

P

R

R

V

L

D

D

A

P

Q

A

A

S

I

L

F

V

D

E

A

L

I

F

R

D

N

G

H

E

G

G

V

V

T

T

H

F

Y

T

C

A

G

G

A

V

P

P

I

T

V

V

Q

W

G

L

L

A

L

L

V

A

N

D

A

Y

P

L

A

E

A

S

M

T

K

G

E

H

G

R

V

L

P

K

A

T

G

L

V

R

K

R

A

L

M

V

V

V

A

G

G
|
G

A
x
S

A
|
A

P

A

P

P

A

R

S

S

M

L

I

I

E

A

G

R

M

F

E

E

Q

R

M

M

G

G

F

V

D

E

L

V

T

R

H

Q

V

G

Y
|
Y

G
|
G

L
|
L

T
|
T

E
|
E

V

T

Y

S

G

P

P

V

A

V

T

V

V

Q

C

N

A

F

K

V

H

K

D

S

A

H

W

L

N

E

S

S

L

L

D

S

I

E

G

E

E

E

R

K

A

L

R

T

L

L

N

K

A

A

R

K

Q

T

G

G

V

L

R

P

Y

I

H

P

L

L

Q

V

R

R

A

-

A

L

M

R

V

V

C

A

D

D

P

E

E

E

T

G

M

-

Q

R

P

P

V

V

P

P

H

K

D

D

G

G

E

K

T

A

M

L

G

G

E

E

I

V

M

Q

F

L

R

K

G

G

N

P

I

W

A

I

M

T

K

G

G

G

Y

Y

L

Y

K

G

N

N

P

E

Q

E

A

A

T

T

E

R

E

S

A

A

F

L

R

T

-

P

G

D

G

G

W

F

F

F

H

R

S

T

G

G

D
|
D

L

I

A

A

V

V

Q

W

Y

D

P

E

D

E

G

G

Y

Y

I

V

K

E

I
|
I

K

K

D

D

R

R

S

L

K

K

D

D

I

L

I

I

I
x
K

S

S

G

G

G

G

E

E

N
x
W

I

I

S

S

S

S

I

V

E

D

V

L

E

E

D

N

V

-

L

-

Y

-

R

-

H

-

P

-

D

-

V

-

L

-

A

-

V

A

A

A

V

V

V

V

A

A

K

I

P

P

D

H

P

P

K

K

W

W

G

Q

E

E

T

R

P

P

C

L

A

A

F

V

V

V

active site: T177 (= T193), H197 (≠ N213), H223 (= H237), T320 (= T333), E321 (= E334), K432 (≠ I446), W437 (≠ N451)
binding phosphoaminophosphonic acid-adenylate ester: H223 (= H237), V224 (≠ C238), G295 (= G308), S296 (≠ A309), A297 (= A310), Y317 (= Y330), G318 (= G331), L319 (= L332), T320 (= T333), D411 (= D425), I423 (= I437), K432 (≠ I446), W437 (≠ N451)
binding magnesium ion: T177 (= T193), E321 (= E334)

8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
30% identity, 95% coverage: 19:538/548 of query aligns to 17:519/522 of 8i3iA

query
sites
8i3iA

L

F

S

S

P

P

L

V

A

A

F

F

I

-

E

-

R

-

T

-

A

-

E

-

V

-

Y

N

P

P

D

E

R

Q

L

E

A

I

I

V

V

Y

H

A

G

N

E

H

L

R

R

R

Q

H

T

S

W

Y

G

K

E

T

T

F

Y

H

K

D

R

R

C

V

R

R

Q

Q

L

F

A

A

S

N

S

A

L

L

R

T

R

K

A

M

G

G

I

V

G

K

K

K

N

G

D

D

T

T

V

V

A

A

V

V

M

M

L

D

P

Y

N

D

T

S

P

H

P

R

M

Y

V

L

E

E

A

C

H

Y

F

F

G

A

V

I

P

P

M

M

A

I

G

G

A

A

V

K

L

L

N

H

T

M

L

I

N

N

T

V

R

R

L

L

D

S

P

P

E

E

T

Q

I

I

A

L

F

Y

M

T

L

I

D

D

H

H

G

A

E

E

A

D

K

D

A

I

L

I

I

L

V

I

D

H

P

E

E

E

F

F

S

L

A

P

V

I

-

L

-

D

-

Q

-

I

-

K

-

G

-

R

-

I

-

D

-

T

V

V

A

T

K

R

A

Y

L

V

P

V

L

L

R

R

K

D

N

D

P

E

A

E

-

C

-

E

P

Y

L

E

A

R

L

L

I

L

E

E

V

Q

E

E

D

S

A

T

L

E

Y

Y

G

N

A

F

P

P

A

-

Q

-

S

-

L

-

G

-

G

-

T

-

R

-

Y

-

E

-

D

D

F

F

V

-

A

-

A

-

G

-

D

-

P

-

A

-

F

-

A

-

W

-

E

-

L

-

P

-

G

-

D

D

E

E

W

N

D

T

A

V

I

A

A

T

L

T

N

F

Y

Y

T
|
T

S

T

G
|
G

T
|
T

T
|
T

G

G

N

F

P

P

K
|
K

G

G

V

V

V

F

Y

F

H

T

H

H

R

R

G

Q

A

L

A

V

I

L

N

H

A

T

I

M

-

G

-

I

-

L

-

S

-

T

-

I

-

G

S

T

N

N

V

A

L

S

E

Q

W

G

D

R

M

L

P

H

K

Q

H

G

A

D

V

I

Y

Y

L

M

W

P

T

I

L

T

P

P

M

M

F

F

H

H

C

V

N

H

G

A

W

W

C

G

F

L

P

P

W

Y

T

M

V

A

A

T

A

M

R

L

A

G

G

V

V

K

N

Q

V

V

C

Y

L

P

R

G

R

K

V

Y

D

V

A

P

Q

D

A

V

I

L

F

L

D

N

A

L

I

I

R

E

N

Q

H

E

G

K

V

V

T

T

H

F

Y

S

C

H

G

C

A

V

P

P

I

T

V

I

Q

L

G

H

L

L

L

L

V

L

N

S

A

S

P

P

A

K

A

S

M

-

K

K

E

A

G

M

V

D

P

F

A

S

G

G

V

W

K

K

A

V

M

V

V

I

A

G

G
|
G

A
|
A

A
|
A

P

L

P

P

A

K

S

A

M

L

I

C

E

K

G

S

M

A

E

L

Q

E

M

R

G

D

F

I

D

D

L

V

T

F

H

A

V

G

Y
|
Y

G

G

L
x
M

T
x
S

E

E

V

T

Y

G

G

P

P

I

A

L

T

S

V

I

C

V

A

Q

K

L

H

T

D

P

A

E

W

Q

N

L

S

E

L

L

D

D

I

V

G

D

E

Q

R

Q

A

A

R

E

L

Y

N

R

A

S

R

K

Q

T

G

G

V

K

R

K

Y

V

H

A

L

L

Q

V

R

E

A

A

A

Y

M

I

V

V

C

-

D

-

P

D

E

E

T

D

M

M

Q

N

P

K

V

L

P

P

H

H

D

D

G

G

E

E

T

T

M

A

G

G

E

E

I

I

M

V

F

V

R

R

G

A

N

P

I

W

A

L

M

T

K

P

G

N

Y

Y

L

Y

K

K

N

D

P

N

Q

K

A

N

T

S

E

K

E

A

A

L

F

W

R

R

G

G

G

G

W

Y

F

L

H

H

S

T

G

G

D
|
D

L

V

A

A

V

H

Q

I

Y

D

P

D

D

E

G

G

Y

F

I

I

K

K

I

I

K

T

D

D

R
|
R

S

V

K

K

D

D

I

M

I

I

I

K

S

I

G

S

G

G

E

E

N

W

I

V

S

S

S

S

I

L

E

E

V

L

E

E

D

D

V

I

L

L

Y

H

R

Q

H

H

P

Q

D

S

V

V

L

S

A

E

V

V

A

A

V

V

V

I

A

G

K

M

P

P

D

H

P

N

K

K

W

W

G

G

E

E

T

V

P

P

C

L

A

A

F

L

V

V

E

T

L

L

K

K

A

E

G

D

A

A

L

Q

T

V

T

T

V

-

D

-

D

-

I

-

V

-

Q

-

H

-

C

-

K

E

K

K

H

E

L

L

A

L

G

G

F

F

K

A

V

K

P

D

R

R

A

E

V

A

-

L

-

L

-

L

-

K

-

V

-

K

V

I

F

V

G

D

E

E

L

I

P

A

K

K

T

T

S

S

T

V

G

G

K

K

I

V

Q

D

K

K

F

K

E

E

L

L

R

R

R

K

binding phosphoaminophosphonic acid-adenylate ester: T172 (= T193), G174 (= G195), T175 (= T196), T176 (= T197), K180 (= K201), G293 (= G308), A294 (= A309), A295 (= A310), Y315 (= Y330), M317 (≠ L332), S318 (≠ T333), D408 (= D425), R423 (= R440)

8i6mA Acyl-acp synthetase structure bound to amp-c18:1
30% identity, 95% coverage: 19:538/548 of query aligns to 15:525/528 of 8i6mA

query
sites
8i6mA

L

F

S

S

P

P

L

V

A

A

F

F

I

-

E

-

R

-

T

-

A

-

E

-

V

-

Y

N

P

P

D

E

R

Q

L

E

A

I

I

V

V

Y

H

A

G

N

E

H

L

R

R

R

Q

H

T

S

W

Y

G

K

E

T

T

F

Y

H

K

D

R

R

C

V

R

R

Q

Q

L

F

A

A

S

N

S

A

L

L

R

T

R

K

A

M

G

G

I

V

G

K

K

K

N

G

D

D

T

T

V

V

A

A

V

V

M

M

L

D

P

Y

N

D

T

S

P

H

P

R

M

Y

V

L

E

E

A

C

H

Y

F

F

G

A

V

I

P

P

M

M

A

I

G

G

A

A

V

K

L

L

N

H

T

M

L

I

N

N

T

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binding adenosine monophosphate: G291 (= G308), A293 (= A310), G312 (≠ V329), Y313 (= Y330), G314 (= G331), M315 (≠ L332), S316 (≠ T333), D406 (= D425), R421 (= R440)
binding magnesium ion: M315 (≠ L332), S316 (≠ T333), E317 (= E334)

8i51A Acyl-acp synthetase structure bound to amp-mc7
30% identity, 95% coverage: 19:538/548 of query aligns to 15:525/528 of 8i51A

query
sites
8i51A

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