SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011800787.1 NCBI__GCF_000015505.1:WP_011800787.1 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)

1ssqD Serine acetyltransferase- complex with cysteine (see paper)
45% identity, 63% coverage: 8:169/259 of query aligns to 80:240/257 of 1ssqD

query
sites
1ssqD

D

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binding cysteine: D88 (= D16), D153 (= D81), H154 (= H82)

8i04A Crystal structure of serine acetyltransferase from salmonella typhimurium complexed with serine (see paper)
43% identity, 67% coverage: 1:174/259 of query aligns to 73:246/258 of 8i04A

query
sites
8i04A

M

M

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P

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binding serine: D88 (= D16), P89 (= P17), D153 (= D81), H154 (= H82), G180 (= G108), R188 (= R117), H189 (= H118)

7bw9A Crystal structure of serine acetyltransferase isoform 3 in complex with cysteine from entamoeba histolytica
44% identity, 58% coverage: 5:155/259 of query aligns to 103:252/280 of 7bw9A

query
sites
7bw9A

L

V

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binding cysteine: D114 (= D16), P115 (= P17), D179 (= D81), H180 (= H82), A206 (≠ G108), R214 (= R117), H215 (= H118)

8i06A Crystal structure of serine acetyltransferase from salmonella typhimurium complexed with coa (see paper)
44% identity, 65% coverage: 1:169/259 of query aligns to 77:244/244 of 8i06A

query
sites
8i06A

M

M

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binding coenzyme a: H158 (= H82), L177 (≠ Y101), Q178 (= Q102), G203 (= G128), A204 (= A129), G221 (= G146), A222 (≠ S147), T235 (= T160), A237 (≠ V162)
binding cysteine: P93 (= P17), H158 (= H82)

8i09A Crystal structure of serine acetyltransferase from salmonella typhimurium complexed with butyl gallate (see paper)
44% identity, 65% coverage: 1:169/259 of query aligns to 76:243/246 of 8i09A

query
sites
8i09A

M

M

F

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D

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x
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A

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V

binding cysteine: D91 (= D16), D156 (= D81), H157 (= H82), G164 (= G89), R191 (= R117), H192 (= H118)
binding butyl 3,4,5-tris(oxidanyl)benzoate: G183 (= G108), T184 (= T109), G202 (= G128), K218 (= K144), I219 (= I145), G220 (= G146), L226 (≠ V152), A236 (≠ V162)

1t3dA Crystal structure of serine acetyltransferase from e.Coli at 2.2a (see paper)
43% identity, 65% coverage: 1:169/259 of query aligns to 77:244/262 of 1t3dA

query
sites
1t3dA

M

M

F

I

S

A

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S

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A

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A

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D

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I

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Q

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A

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A

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Y

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Y

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A

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H

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A

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F

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E

D

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P

G

A

A

A

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K

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I

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F

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D
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D

H

H

A

A

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T

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I

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G

E

E

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G

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H

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A

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binding cysteine: D92 (= D16), P93 (= P17), D157 (= D81), G184 (= G108), R192 (= R117), H193 (= H118)

1sstA Serine acetyltransferase- complex with coa (see paper)
44% identity, 63% coverage: 8:169/259 of query aligns to 80:233/233 of 1sstA

query
sites
1sstA

D

D

I

I

Q

Q

C

A

I

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L

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E

H

R

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D

D

P

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A

A

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G

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x
L

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Q

G

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T

T

L

L

G

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G

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T

A

-

L

-

Y

-

K

-

G

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T

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K

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R

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H

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A

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G

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L

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V

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D

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Y

A

A

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K

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G

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x
A

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V

V

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x
L

K

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A

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x
A

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x
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P

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I
x
V

binding coenzyme a: H154 (= H82), L173 (≠ Y101), G180 (= G108), T181 (= T109), A193 (= A129), L198 (= L134), K208 (= K144), G210 (= G146), A211 (≠ S147), V214 (= V150), L216 (≠ V152), T224 (= T160), A226 (≠ V162), V228 (≠ N164), P229 (= P165), V233 (≠ I169)

4n69A Soybean serine acetyltransferase complexed with serine (see paper)
44% identity, 63% coverage: 7:169/259 of query aligns to 82:243/243 of 4n69A

query
sites
4n69A

S

A

D

D

I

L

Q

R

C

A

I

A

L

R

E

E

R

R

D

D

P

P

A

A

A

C

R

V

T

S

R

Y

W

S

E

H

V

C

L

L

T

L

C

N

Y

Y

P

K

G

G

V

F

H

L

A

A

V

C

I

Q

L

A

H

H

R

R

W

V

A

A

H

H

A

L

C

L

W

W

T

R

H

Q

G

S

F

R

K

R

W

P

L

L

G

A

R

L

F

A

I

L

S

H

H

S

L

R

A

I

R

A

W

N

L

V

T

F

G

A

I

V

E

D

I

I

H

H

P

P

G

A

A

A

K

R

I

I

G

G

E

K

R

G

V

I

F

L

F

F

D

D

H

H

A

A

M

T

G

G

V

V

V

V

V

V

G

G

E

E

T

T

A

A

E

V

I

I

G

G

D

N

G

N

C

V

T

S

I

I

Y

L

Q

H

G

H

V

V

T

T

L

L

G

G

G
|
G

T

T

A

G

L

K

Y

V

K

G

G

G

T

-

K

D

R
|
R

H
|
H

P

P

T

K

L

I

G

G

K

D

N

G

V

V

V

L

V

I

G

G

A

A

G

G

A

A

Q

T

V

I

L

L

G

G

G

N

F

I

T

K

V

I

G

G

D

E

G

G

A

A

K

K

I

V

G

G

S

A

N

G

A

S

V

V

V

V

V

L

K

I

P

D

V

V

P

P

A

P

G

R

A

T

T

T

A

A

V

V

G

G

N

N

P

P

A

A

R

R

V

L

I

V

binding serine: G183 (= G108), R191 (= R117), H192 (= H118)

4hzdA Crystal structure of serine acetyltransferase in complex with coenzyme a from brucella abortus strain s19 (see paper)
42% identity, 64% coverage: 5:169/259 of query aligns to 81:244/250 of 4hzdA

query
sites
4hzdA

L

L

R

R

S

V

D

D

I

I

Q

Q

C

A

I

V

L

Y

E

D

R

R

D

D

P

P

A

A

A

Y

R

S

T

R

R

F

W

M

E

D

V

P

L

V

T

L

C

Y

Y

L

P

K

G

G

V

F

H

H

A

A

V

I

I

Q

L

T

H

H

R

R

W

L

A

A

H

H

A

W

C

L

W

Y

T

K

H

Q

G

G

F

R

K

K

W

D

L

F

G

A

R

Y

F

Y

I

L

S

Q

H

S

L

R

A

S

R

S

W

S

L

I

T

F

G

Q

I

T

E

D

I

I

H

H

P

P

G

A

A

A

K

R

I

L

G

G

E

S

R

G

V

L

F

F

F

L

D

D

H
|
H

A

A

M

T

G

G

V

L

V

V

V

V

G

G

E

E

T

T

A

A

E

V

I

V

G

E

D

D

G

N

C

V

T

S

I

I

Y

L

Q

H

G

G

V

V

T

T

L

L

G

G

G

G

T

T

A

G

L

K

Y

S

K

S

G

G

T

-

K

D

R

R

H

H

P

P

T

K

L

I

G

R

K

Q

N

G

V

V

V

L

V

I

G
|
G

A
|
A

G

G

A

A

Q

K

V

I

L

L

G

G

G

N

F

I

T

Q

V

V

G

G

D

Q

G

C

A

S

K

K

I

I

G
x
A

S
x
A

N

G

A
x
S

V

V

V

V

V

L

K

K

P

S

V

V

P

P

A

H

G

N

A

V

T
|
T

A

V

V
x
A

G
|
G

N

V

P

P

A

A

R

R

V

I

I
|
I

binding coenzyme a: H158 (= H82), G203 (= G128), A204 (= A129), A221 (≠ G146), A222 (≠ S147), T235 (= T160), A237 (≠ V162), I244 (= I169)
binding magnesium ion: S224 (≠ A149), A237 (≠ V162), G238 (= G163)

6wyeA Crystal structure of neisseria gonorrhoeae serine acetyltransferase (cyse) (see paper)
41% identity, 63% coverage: 5:167/259 of query aligns to 82:243/261 of 6wyeA

query
sites
6wyeA

L

V

R

E

S

A

D

D

I

L

Q

K

C

A

I

I

L

Y

E

E

R

R

D
|
D

P
|
P

A

A

A

C

R

D

T

E

R

Y

W

S

E

L

V

P

L

L

T

L

C

Y

Y

F

P

K

G

G

V

F

H

H

A

A

V

I

I

Q

L

A

H

H

R

R

W

I

A

N

H

H

A

R

C

L

W

Y

T

L

H

D

G

G

F

R

K

K

W

T

L

L

G

A

R

Y

F

F

I

L

S

Q

H

N

L

R

A

M

R

S

W

E

L

V

T

F

G

G

I

V

E

D

I

I

H

H

P

P

G

A

A

A

K

R

I

L

G

G

E

Y

R

G

V

L

F

M

F

L

D
|
D

H
|
H

A

A

M

T

G

G

V

F

V

V

V

A

G

G

E

E

T

T

A

A

E

V

I

L

G

G

D

N

G

N

C

I

T

S

I

I

Y

L

Q

H

G

G

V

V

T

T

L

L

G

G

G
|
G

T

S

A

G

L

-

Y

K

K

E

G

G

T

G

K

D

R
|
R

H
|
H

P

P

T

K

L

I

G

G

K

D

N

G

V

V

V

M

V

I

G

G

A

A

G

N

A

A

Q

S

V

I

L

L

G

G

G

N

F

I

T

R

V

I

G

G

D

S

G

N

A

A

K

K

I

I

G

G

S

A

N

G

A

S

V

V

V

V

V

V

K

S

P

D

V

V

P

P

A

P

G

S

A

I

T

T

A

V

V

V

G

G

N

V

P

P

A

A

R

K

binding (2S)-2-hydroxybutanedioic acid: D93 (= D16), P94 (= P17), D158 (= D81), H159 (= H82), G185 (= G108), R193 (= R117), H194 (= H118)

7ra4A Crystal structure of neisseria gonorrhoeae serine acetyltransferase (cyse) in complex with serine (see paper)
41% identity, 63% coverage: 5:167/259 of query aligns to 80:241/243 of 7ra4A

query
sites
7ra4A

L

V

R

E

S

A

D

D

I

L

Q

K

C

A

I

I

L

Y

E

E

R

R

D
|
D

P
|
P

A

A

A

C

R

D

T

E

R

Y

W

S

E

L

V

P

L

L

T

L

C

Y

Y

F

P

K

G

G

V

F

H

H

A

A

V

I

I

Q

L

A

H

H

R

R

W

I

A

N

H

H

A

R

C

L

W

Y

T

L

H

D

G

G

F

R

K

K

W

T

L

L

G

A

R

Y

F

F

I

L

S

Q

H

N

L

R

A

M

R

S

W

E

L

V

T

F

G

G

I

V

E

D

I

I

H

H

P

P

G

A

A

A

K

R

I

L

G

G

E

Y

R

G

V

L

F

M

F

L

D
|
D

H
|
H

A

A

M

T

G

G

V

F

V

V

V

A

G

G

E

E

T

T

A

A

E

V

I

L

G

G

D

N

G

N

C

I

T

S

I

I

Y

L

Q

H

G

G

V

V

T

T

L

L

G

G

G

G

T

S

A

G

L

-

Y

K

K

E

G

G

T

G

K

D

R
|
R

H
|
H

P

P

T

K

L

I

G

G

K

D

N

G

V

V

V

M

V

I

G

G

A

A

G

N

A

A

Q

S

V

I

L

L

G

G

G

N

F

I

T

R

V

I

G

G

D

S

G

N

A

A

K

K

I

I

G

G

S

A

N

G

A

S

V

V

V

V

V

V

K

S

P

D

V

V

P

P

A

P

G

S

A

I

T

T

A

V

V

V

G

G

N

V

P

P

A

A

R

K

binding serine: D91 (= D16), P92 (= P17), D156 (= D81), H157 (= H82), R191 (= R117), H192 (= H118)

3p47A Crystal structure of entamoeba histolytica serine acetyltransferase 1 in complex with l-cysteine (see paper)
42% identity, 61% coverage: 5:161/259 of query aligns to 105:268/270 of 3p47A

query
sites
3p47A

L

L

R

K

S

T

D

D

I

L

Q

I

C

A

I

A

L

Y

E

A

R

G

D

D

P

P

A

A

A

A

R

P

T

G

R

L

W

S

E

L

V

I

L

I

T

R

C

C

Y

Y

P

P

G

G

V

F

H

Q

A

A

V

V

I

I

L

V

H

Y

R

R

W

I

A

A

H

H

A

V

C

L

W

Y

T

E

H

C

G

G

F

E

K

R

W

Y

L

Y

G

C

R

R

F

E

I

M

S

M

H

E

L

S

A

V

R

H

W

S

L

Y

T

T

G

S

I

I

E

D

I

I

H

H

P

P

G

G

A

A

K

S

I

I

G

K

E

G

R

H

V

F

F

F

F

I

D

D

H

H

A

G

M

V

G

G

V

V

V

V

V

I

G

G

E

E

T

T

A

A

E

I

I

I

G

G

D

E

G

W

C

C

T

R

I

I

Y

Y

Q

Q

G

S

V

V

T

T

L

L

G

G

-
x
A

-

M

-
x
H

-

F

-

Q

-

E

-

E

G

G

T

G

A

V

L

I

Y

K

K

R

G

G

T

T

K

K

R
|
R

H
|
H

P

P

T

T

L

V

G

G

K

D

N

Y

V

V

V

T

V

I

G

G

A

T

G

G

A

A

Q

K

V

V

L

L

G

G

G

N

F

I

T

I

V

V

G

G

D

S

G

H

A

V

K

R

I

I

G

G

S

A

N

N

A

C

V

W

V

I

V

D

K

R

P

D

V

V

P

D

A

S

G

N

A

Q

T

T

A

V

binding cysteine: A208 (vs. gap), H210 (vs. gap), R224 (= R117), H225 (= H118)

3q1xA Crystal structure of entamoeba histolytica serine acetyltransferase 1 in complex with l-serine (see paper)
42% identity, 61% coverage: 5:161/259 of query aligns to 103:266/267 of 3q1xA

query
sites
3q1xA

L

L

R

K

S

T

D

D

I

L

Q

I

C

A

I

A

L

Y

E

A

R

G

D

D

P

P

A

A

A

A

R

P

T

G

R

L

W

S

E

L

V

I

L

I

T

R

C

C

Y

Y

P

P

G

G

V

F

H

Q

A

A

V

V

I

I

L

V

H

Y

R

R

W

I

A

A

H

H

A

V

C

L

W

Y

T

E

H

C

G

G

F

E

K

R

W

Y

L

Y

G

C

R

R

F

E

I

M

S

M

H

E

L

S

A

V

R

H

W

S

L

Y

T

T

G

S

I

I

E

D

I

I

H

H

P

P

G

G

A

A

K

S

I

I

G

K

E

G

R

H

V

F

F

F

F

I

D

D

H

H

A

G

M

V

G

G

V

V

V

V

V

I

G

G

E

E

T

T

A

A

E

I

I

I

G

G

D

E

G

W

C

C

T

R

I

I

Y

Y

Q

Q

G

S

V

V

T

T

L

L

G

G

-

A

-

M

-
x
H

-

F

-

Q

-

E

-

E

G

G

T

G

A

V

L

I

Y

K

K

R

G

G

T

T

K

K

R
|
R

H
|
H

P

P

T

T

L

V

G

G

K

D

N

Y

V

V

V

T

V

I

G

G

A

T

G

G

A

A

Q

K

V

V

L

L

G

G

G

N

F

I

T

I

V

V

G

G

D

S

G

H

A

V

K

R

I

I

G

G

S

A

N

N

A

C

V

W

V

I

V

D

K

R

P

D

V

V

P

D

A

S

G

N

A

Q

T

T

A

V

binding serine: H208 (vs. gap), R222 (= R117), H223 (= H118)

3gvdI Crystal structure of serine acetyltransferase cyse from yersinia pestis
42% identity, 63% coverage: 8:169/259 of query aligns to 87:247/272 of 3gvdI

query
sites
3gvdI

D

D

I

I

Q

L

C

A

I

V

L

R

E

L

R

R

D
|
D

P
|
P

A

A

A

V

R

D

T

K

R

Y

W

S

E

T

V

P

L

L

T

L

C

Y

Y

L

P

K

G

G

V

F

H

H

A

A

V

L

I

Q

L

A

H

Y

R

R

W

I

A

G

H

H

A

W

C

L

W

W

T

A

H

Q

G

D

F

R

K

K

W

A

L

L

G

A

R

I

F

Y

I

L

S

Q

H

N

L

Q

A

V

R

S

W

V

L

A

T

F

G

G

I

V

E

D

I

I

H

H

P

P

G

A

A

A

K

T

I

I

G

G

E

C

R

G

V

I

F

M

F

L

D
|
D

H

H

A

A

M

T

G

G

V

I

V

V

V

I

G

G

E

E

T

T

A

A

E

V

I

V

G

E

D

N

G

D

C

V

T

S

I

I

Y

L

Q

Q

G

S

V

V

T

T

L

L

G
|
G

G
|
G

T

T

A

G

L

K

Y

T

K

S

G

G

T

-

K

D

R
|
R

H

H

P

P

T

K

L

I

G

R

K

E

N

G

V

V

V

M

V

I

G

G

A

A

G

G

A

A

Q

K

V

I

L

L

G

G

G

N

F

I

T

E

V

V

G

G

D

R

G

G

A

A

K

K

I

I

G

G

S

A

N

G

A

S

V

V

V

V

V

L

K

Q

P

S

V

V

P

P

A

A

G

H

A

T

T

T

A

A

V

A

G

G

N

V

P

P

A

A

R

R

V

I

I

V

binding cysteine: D95 (= D16), P96 (= P17), D160 (= D81), G186 (= G107), G187 (= G108), R195 (= R117)

4h7oA Crystal structure of serine acetyltransferase from vibrio cholerae o1 biovar el tor n16961
42% identity, 63% coverage: 8:169/259 of query aligns to 80:240/258 of 4h7oA

query
sites
4h7oA

D

D

I

I

Q

C

C

A

I

T

L

V

E

N

R

R

D
|
D

P
|
P

A

A

A

V

R

S

T

M

R

Y

W

S

E

M

V

P

L

L

T

L

C

Y

Y

L

P

K

G

G

V

Y

H

H

A

A

V

L

I

Q

L

G

H

Y

R

R

W

V

A

A

H

N

A

W

C

L

W

W

T

R

H

Q

G

G

F

R

K

K

W

A

L

L

G

A

R

T

F
x
Y

I

F

S

Q

H

N

L
x
Q

A

I

R

S

W

V

L

A

T

C

G

Q

I

V

E

D

I

I

H

H

P

P

G

A

A

A

K

R

I

I

G

G

E

R

R

G

V

I

F

M

F

L

D
|
D

H
|
H

A

A

M

T

G

G

V

I

V

V

V

I

G

G

E

E

T

T

A

A

E

V

I

V

G

E

D

D

G

D

C

V

T

S

I

I

Y

L

Q

Q

G

D

V

V

T

T

L

L

G

G

G
|
G

T

T

A

G

L

K

Y

E

K

C

G

G

T

-

K

D

R
|
R

H
|
H

P

P

T

K

L

I

G

R

K

E

N

G

V

V

V

M

V

I

G

G

A

A

G

G

A

A

Q

K

V

I

L

L

G

G

G

N

F

I

T

E

V

V

G

G

D

E

G

G

A

A

K

K

I

I

G

G

S

S

N

G

A

S

V

V

V

V

V

L

K

Q

P

A

V

V

P

P

A

P

G

H

A

T

T

T

A

V

V

A

G

G

N

V

P

P

A

A

R

R

V

I

I

V

binding arginine: Y127 (≠ F55), Q131 (≠ L59)
binding cysteine: D88 (= D16), P89 (= P17), D153 (= D81), H154 (= H82), G180 (= G108), R188 (= R117), H189 (= H118)

Sites not aligning to the query:

binding arginine: 51, 53

4n6bA Soybean serine acetyltransferase complexed with coa (see paper)
43% identity, 63% coverage: 7:169/259 of query aligns to 78:233/233 of 4n6bA

query
sites
4n6bA

S

A

D

D

I

L

Q

R

C

A

I

A

L

R

E

E

R

R

D

D

P

V

A

S

A

Y

R

S

T

-

R

-

W

-

E

H

V

C

L

L

T

L

C

N

Y

Y

P

K

G

G

V

F

H

L

A

A

V

C

I

Q

L

A

H

H

R

R

W

V

A

A

H

H

A

L

C

L

W

W

T

R

H

Q

G

S

F

R

K

R

W

P

L

L

G

A

R

L

F

A

I

L

S

H

H

S

L

R

A

I

R

A

W

N

L

V

T

F

G

A

I

V

E

D

I

I

H

H

P

P

G

A

A

A

K

R

I

I

G

G

E

K

R

G

V

I

F

L

F

F

D

D

H
|
H

A

A

M

T

G

G

V

V

V

V

V

V

G

G

E

E

T

T

A

A

E

V

I

I

G

G

D

N

G

N

C

V

T

S

I

I

Y
x
L

Q

H

G

H

V

V

T

T

L

L

G

G

G
|
G

T

T

A

-

L

-

Y

-

K

-

G

G

T

G

K

D

R

R

H

H

P

P

T

K

L

I

G

G

K

D

N

G

V

V

V

L

V

I

G

G

A

A

G

G

A

A

Q

T

V

I

L

L

G

G

G

N

F

I

T

K

V

I

G

G

D

E

G

G

A

A

K
|
K

I

V

G
|
G

S
x
A

N

G

A

S

V

V

V

V

V
x
L

K

I

P

D

V

V

P

P

A

P

G

R

A

T

T

T

A

A

V
|
V

G

G

N

N

P

P

A

A

R

R

V

L

I

V

binding coenzyme a: H150 (= H82), L169 (≠ Y101), G176 (= G108), K208 (= K144), G210 (= G146), A211 (≠ S147), L216 (≠ V152), V226 (= V162)

1krvA Galactoside acetyltransferase in complex with coa and pnp-beta-gal (see paper)
32% identity, 39% coverage: 74:174/259 of query aligns to 77:186/201 of 1krvA

query
sites
1krvA

I

I

G

G

E

R

R

N

V

F

F
x
Y

F

A

D
x
N

H

F

A

N

M

L

G

T

V

I

V
|
V

V

D

G
x
D

E

Y

T

T

A

V

E

T

I

I

G

G

D

D

G

N

C

V

T

L

I

I

Y
x
A

Q

P

G

N

V

V

T

T

L

L

G
x
S

G

V

T
|
T

A

G

-

H

-

P

-

V

-

H

-

H

-

E

L

L

Y

R

K

K

G

N

T

G

K

E

R
x
M

H

Y

P

S

-

F

-

P

-

I

T

T

L

I

G

G

K

N

N

N

V

V

V
x
W

V

I

G
|
G

A
x
S

G

H

A

V

Q

V

V

I

L
x
N

G

P

G

G

F

V

T

T

V

I

G

G

D

D

G

N

A

S

K

V

I

I

G

G

S
x
A

N

G

A

S

V

I

V

V

V

T

K

K

P

D

V

I

P

P

A

P

G

N

A

V

T

V

A

A

V

A

G

G

N

V

P
|
P

A

C

R
|
R

V

V

I

I

Q
x
R

A

E

G

I

A

N

D

D

binding 4-nitrophenyl beta-D-galactopyranoside: Y82 (≠ F79), N84 (≠ D81), V90 (= V87), D92 (≠ G89), M126 (≠ R117)
binding coenzyme a: A104 (≠ Y101), S110 (≠ G107), T112 (= T109), W138 (≠ V126), G140 (= G128), S141 (≠ A129), N146 (≠ L134), A159 (≠ S147), P177 (= P165), R179 (= R167), R182 (≠ Q170)

Sites not aligning to the query:

binding 4-nitrophenyl beta-D-galactopyranoside: 16, 25, 70

1kruA Galactoside acetyltransferase in complex with iptg and coenzyme a (see paper)
32% identity, 39% coverage: 74:174/259 of query aligns to 77:186/201 of 1kruA

query
sites
1kruA

I

I

G

G

E

R

R

N

V

F

F
x
Y

F

A

D
x
N

H

F

A

N

M

L

G

T

V

I

V
|
V

V

D

G
x
D

E

Y

T

T

A

V

E

T

I

I

G

G

D

D

G

N

C

V

T
x
L

I

I

Y

A

Q

P

G

N

V

V

T

T

L

L

G

S

G

V

T

T

A

G

-
x
H

-

P

-

V

-

H

-

H

-

E

L

L

Y

R

K

K

G

N

T

G

K

E

R
x
M

H

Y

P

S

-

F

-

P

-

I

T

T

L

I

G

G

K

N

N

N

V

V

V
x
W

V

I

G
|
G

A
x
S

G

H

A

V

Q

V

V

I

L

N

G

P

G

G

F

V

T

T

V

I

G

G

D

D

G

N

A

S

K

V

I

I

G
|
G

S
x
A

N

G

A

S

V

I

V

V

V

T

K

K

P

D

V

I

P

P

A

P

G

N

A

V

T

V

A

A

V

A

G

G

N

V

P
|
P

A

C

R

R

V

V

I

I

Q
x
R

A

E

G

I

A

N

D

D

binding coenzyme a: H114 (vs. gap), W138 (≠ V126), G140 (= G128), S141 (≠ A129), G158 (= G146), A159 (≠ S147), P177 (= P165), R182 (≠ Q170)
binding 1-methylethyl 1-thio-beta-D-galactopyranoside: Y82 (≠ F79), Y82 (≠ F79), N84 (≠ D81), V90 (= V87), D92 (≠ G89), L102 (≠ T99), H114 (vs. gap), M126 (≠ R117)

Sites not aligning to the query:

binding 1-methylethyl 1-thio-beta-D-galactopyranoside: 16, 22, 25, 62, 70

1krrA Galactoside acetyltransferase in complex with acetyl-coenzyme a (see paper)
32% identity, 39% coverage: 74:174/259 of query aligns to 77:186/200 of 1krrA

query
sites
1krrA

I

I

G

G

E

R

R

N

V

F

F

Y

F

A

D
x
N

H

F

A

N

M

L

G

T

V

I

V

V

V

D

G

D

E

Y

T

T

A

V

E

T

I

I

G

G

D

D

G

N

C

V

T

L

I
|
I

Y
x
A

Q
x
P

G

N

V

V

T

T

L

L

G

S

G

V

T
|
T

A

G

-
x
H

-

P

-

V

-

H

-

H

-

E

L

L

Y

R

K

K

G

N

T

G

K

E

R

M

H

Y

P

S

-

F

-

P

-

I

T

T

L

I

G

G

K

N

N

N

V

V

V

W

V

I

G
|
G

A
x
S

G

H

A

V

Q

V

V

I

L
x
N

G

P

G

G

F

V

T

T

V

I

G

G

D

D

G

N

A

S

K

V

I

I

G
|
G

S
x
A

N

G

A

S

V

I

V

V

V

T

K

K

P

D

V

I

P

P

A

P

G

N

A

V

T

V

A

A

V
x
A

G

G

N

V

P
|
P

A

C

R

R

V

V

I

I

Q
x
R

A

E

G

I

A

N

D

D

binding acetyl coenzyme *a: N84 (≠ D81), I103 (= I100), A104 (≠ Y101), P105 (≠ Q102), T112 (= T109), H114 (vs. gap), G140 (= G128), S141 (≠ A129), N146 (≠ L134), G158 (= G146), A159 (≠ S147), A174 (≠ V162), P177 (= P165), R182 (≠ Q170)

P07464 Galactoside O-acetyltransferase; GAT; Acetyl-CoA:galactoside 6-O-acetyltransferase; Thiogalactoside acetyltransferase; Thiogalactoside transacetylase; EC 2.3.1.18 from Escherichia coli (strain K12) (see 3 papers)
32% identity, 39% coverage: 74:174/259 of query aligns to 78:187/203 of P07464

query
sites
P07464

I

I

G

G

E

R

R

N

V

F

F

Y

F

A

D
x
N

H

F

A

N

M

L

G

T

V

I

V

V

V

D

G
x
D

E

Y

T

T

A

V

E

T

I

I

G

G

D

D

G

N

C

V

T

L

I

I

Y

A

Q

P

G

N

V

V

T

T

L

L

G

S

G

V

T

T

-

G

-
x
H

-

P

-

V

-

H

-

H

A

E

L

L

Y

R

K

K

G

N

T

G

K

E

R

M

H

Y

P

S

-

F

-

P

-

I

T

T

L

I

G

G

K

N

N

N

V

V

V

W

V

I

G

G

A
x
S

G

H

A

V

Q

V

V

I

L

N

G

P

G

G

F

V

T

T

V

I

G

G

D

D

G

N

A

S

K

V

I

I

G

G

S
x
A

N

G

A

S

V

I

V

V

V
x
T

K
|
K

P

D

V

I

P

P

A

P

G

N

A

V

T

V

A

A

V

A

G

G

N

V

P

P

A

C

R
|
R

V

V

I

I

Q
x
R

A

E

G

I

A

N

D

D

N85 (≠ D81) binding in other chain; binding in other chain
D93 (≠ G89) binding substrate
H115 (vs. gap) mutation to A: Results in an 1800-fold decrease in catalytic activity.
S142 (≠ A129) binding in other chain
A160 (≠ S147) binding in other chain
TK 165:166 (≠ VK 152:153) binding acetyl-CoA
R180 (= R167) binding acetyl-CoA
R183 (≠ Q170) binding in other chain

Sites not aligning to the query:

1 modified: Initiator methionine, Removed; Partial
17 binding substrate
71 binding substrate

Query Sequence

>WP_011800787.1 NCBI__GCF_000015505.1:WP_011800787.1
MFSRLRSDIQCILERDPAARTRWEVLTCYPGVHAVILHRWAHACWTHGFKWLGRFISHLA
RWLTGIEIHPGAKIGERVFFDHAMGVVVGETAEIGDGCTIYQGVTLGGTALYKGTKRHPT
LGKNVVVGAGAQVLGGFTVGDGAKIGSNAVVVKPVPAGATAVGNPARVIQAGADVKREQV
ASQMGFSAYGVTQNDDPLSQALRGLIDNASGQEHQIALLWQAIEKLSHPKSPGPQDCVPK
DAALQENFEADKLNQLVGK

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