SitesBLAST

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)
37% identity, 43% coverage: 128:222/223 of query aligns to 95:185/203 of P07464

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P07464

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H115 (≠ F148) mutation to A: Results in an 1800-fold decrease in catalytic activity.
S142 (≠ M179) binding in other chain
A160 (= A197) binding in other chain
TK 165:166 (≠ TR 202:203) binding acetyl-CoA
R180 (= R217) binding acetyl-CoA
R183 (= R220) binding in other chain

Sites not aligning to the query:

1 modified: Initiator methionine, Removed; Partial
17 binding substrate
71 binding substrate
85 binding in other chain; binding in other chain
93 binding substrate

3nz2J Crystal structure of hexapeptide-repeat containing-acetyltransferase vca0836 complexed with acetyl co enzyme a from vibrio cholerae o1 biovar eltor
38% identity, 43% coverage: 127:222/223 of query aligns to 73:184/185 of 3nz2J

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3nz2J

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binding acetyl coenzyme *a: G104 (≠ P153), Y110 (≠ D159), H114 (≠ F163), W138 (= W176), G140 (= G178), A158 (= A196), A159 (= A197), N164 (≠ T202), G174 (≠ A212), T176 (≠ V214), P177 (= P215), R182 (= R220)

3nz2C Crystal structure of hexapeptide-repeat containing-acetyltransferase vca0836 complexed with acetyl co enzyme a from vibrio cholerae o1 biovar eltor
38% identity, 43% coverage: 127:222/223 of query aligns to 70:181/183 of 3nz2C

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3nz2C

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binding acetyl coenzyme *a: Y107 (≠ D159), H111 (≠ F163), G137 (= G178), A155 (= A196), A156 (= A197), N161 (≠ T202), G171 (≠ A212), T173 (≠ V214), P174 (= P215), L178 (≠ V219), R179 (= R220)
binding magnesium ion: N157 (≠ G198), T173 (≠ V214)

3ectA Crystal structure of the hexapeptide-repeat containing- acetyltransferase vca0836 from vibrio cholerae
38% identity, 43% coverage: 127:222/223 of query aligns to 63:174/176 of 3ectA

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3ectA

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binding calcium ion: G138 (= G186), D156 (= D204)

3igjC Crystal structure of maltose o-acetyltransferase complexed with acetyl coenzyme a from bacillus anthracis
37% identity, 42% coverage: 128:220/223 of query aligns to 76:184/188 of 3igjC

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binding acetyl coenzyme *a: F84 (≠ M136), A106 (≠ P153), Y112 (≠ D159), A114 (≠ P161), H116 (≠ F163), G142 (= G178), N148 (≠ L184), A160 (= A196), S161 (≠ A197), T166 (= T202), N178 (≠ V214)

2wlgA Crystallographic analysis of the polysialic acid o-acetyltransferase oatwy (see paper)
28% identity, 76% coverage: 52:220/223 of query aligns to 33:186/211 of 2wlgA

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binding [(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl(3r)-3-hydroxy-2,2-dimethyl-4-oxo-4-{[3-oxo-3-({2-[(2-oxopropyl)thio]ethyl}amino)propyl]amino}butyl dihydrogendiphosphate: R112 (≠ T144), D115 (= D147), H117 (= H149), I119 (≠ M151), K150 (= K185), Y167 (≠ T202)

2wleC Crystallographic analysis of the polysialic acid o-acetyltransferase oatwy (see paper)
28% identity, 76% coverage: 52:220/223 of query aligns to 33:186/211 of 2wleC

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binding coenzyme a: A106 (= A138), R112 (≠ T144), D115 (= D147), I119 (≠ M151), W141 (= W176), R144 (≠ M179), K150 (= K185), G161 (≠ A196), S162 (≠ A197), Y167 (≠ T202), G179 (= G213), V185 (= V219), K186 (≠ R220)

2wlfA Crystallographic analysis of the polysialic acid o-acetyltransferase oatwy (see paper)
28% identity, 76% coverage: 52:220/223 of query aligns to 33:186/210 of 2wlfA

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binding acetyl coenzyme *a: M104 (= M136), R112 (≠ T144), D115 (= D147), H117 (= H149), I119 (≠ M151), R144 (≠ M179), L149 (= L184), K150 (= K185), G161 (≠ A196), S162 (≠ A197), Y167 (≠ T202), K168 (≠ R203), G179 (= G213), V185 (= V219)

8j40A Crystal structure of catb8 in complex with chloramphenicol (see paper)
36% identity, 33% coverage: 148:220/223 of query aligns to 89:161/209 of 8j40A

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G

A

A

I
x
V

V

I

A

G

A
x
S

G

R

S

S

V

L

V

V

T

T

R

K

D

D

V

V

P

E

P

P

A

Y

T

A

L

I

V

I

A

G

G

G

V

N

P

P

A

A

R

K

V

Q

V

I

R

K

binding chloramphenicol: Y90 (≠ H149), W117 (= W176), V135 (≠ I194), S138 (≠ A197)

Sites not aligning to the query:

binding chloramphenicol: 7, 8, 9, 29, 31, 47, 50, 187, 190, 191, 202, 203, 206

Q93S40 Polysialic acid O-acetyltransferase; Polysialyltransferase; PST; EC 2.3.1.- from Neisseria meningitidis (see paper)
28% identity, 76% coverage: 52:220/223 of query aligns to 37:190/215 of Q93S40

query
sites
Q93S40

I

V

T

Y

V

I

G

G

K

N

G

N

C

C

E

K

C

I

F

V

G

S

T

S

V

N

I

I

L

-

S

-

R

R

W

L

P

K

G

G

S

N

R

N

I

I

E

T

L

L

G

F

D

I

G

A

V

D

S

D

I

V

I

E

S

N

S

M

S

G

R

L

R

V

C

C

T

S

S

-

A

-

T

-

I

L

H

H

A

S

P

D

T

C

R

S

L

L

R

Q

T

I

F

Q

A

A

P

K

T

T

A

T

R

M

I

-

L

-

E

-

D

-

G

-

V

-

S

-

L

G

N

N

G

G

T

E

A

I

I

T

T

I

A

A

R

E

S

K

R

G

T

K

I

I

R

S

I

I

G

G

K

K

G

D

T

C

M

M

V

L

A

A

P

H

N

G

C

Y

V

E

I

I

T

R

D

N

S

T

D
|
D

F
x
M

H
|
H

A

P

M

I

W

Y

P

S

P

L

E

E

T

-

R

-

L

-

D

N

T

G

P

E

A

R

F

I

E

N

R

H

D

G

A

K

D

D

V

V

T

I

I

I

G

G

Q

N

H

H

V

V

W
|
W

L

L

G

G

M
x
R

R

N

C

V

I

T

V

I

L

L

K
|
K

G

G

V

V

T

C

I

I

G

P

D

N

G

N

A

V

I

V

V

V

A

G

A
x
S

G

H

S

T

V

V

V

L

T
x
Y

R
x
K

D

S

V

F

-

K

P

E

P

P

A

N

T

C

L

V

V

I

A

A

G

G

V

S

P

P

A

A

R

K

V

I

V

V

R
x
K

DMH 119:121 (≠ DFH 147:149) binding acetyl-CoA
H121 (= H149) mutation to A: Reduces activity 50-fold.
W145 (= W176) mutation to A: Reduces activity 56-fold.
R148 (≠ M179) binding acetyl-CoA
K154 (= K185) binding acetyl-CoA
S166 (≠ A197) binding acetyl-CoA
Y171 (≠ T202) mutation to A: Reduces activity 48-fold.
YK 171:172 (≠ TR 202:203) binding acetyl-CoA
K190 (≠ R220) binding acetyl-CoA

A1ADJ6 Polysialic acid O-acetyltransferase; Capsule O-acetyl transferase; EC 2.3.1.136 from Escherichia coli O1:K1 / APEC (see paper)
30% identity, 42% coverage: 128:220/223 of query aligns to 189:278/307 of A1ADJ6

query
sites
A1ADJ6

T

N

I

V

R

T

I

I

G

G

K

H

G

D

T

C

M

M

V

I

A

A

P

R

N

D

C

V

V

I

I

L

T

R

D

A

S

S

D

D

F

G

H
|
H

A

P

M

I

W

F

P

D

P

I

E

H

T

S

R

K

L

-

D

-

T

-

P

K

A

R

F

I

E

N

R

W

D

A

A

K

D

D

V

I

T

I

I

I

G

S

Q

S

H

Y

V

V

W
|
W

L

V

G

G

M

R

R

N

C

V

I

S

V

I

L

M

K

K

G

G

V

V

T

S

I

V

G

G

D

S

G

G

A

S

I

V

V

I

A

G

A

Y

G

G

S

S

V

I

V

V

T

T

R

K

D

D

V

V

P

P

P

S

A

M

T

C

L

A

V

A

A

A

G

G

V

N

P

P

A

A

R

K

V

I

R

K

H210 (= H149) mutation to A: Loss of activity.
W234 (= W176) mutation to A: Loss of activity.

1mrlA Crystal structure of streptogramin a acetyltransferase with dalfopristin (see paper)
48% identity, 24% coverage: 168:221/223 of query aligns to 113:166/204 of 1mrlA

query
sites
1mrlA

D

D

V

T

T

I

I

I

G

G

Q

N

H

D

V

V

W

W

L

I

G

G

M

K

R

D

C

V

I

V

V

I

L

M

K

P

G

G

V

V

T

K

I

I

G

G

D

D

G

G

A

A

I

I

V

V

A

A

G

N

S

S

V

V

T

V

R

K

D

D

V

I

P

A

P

P

A

Y

T

M

L

L

V

A

A

G

G

G

V

N

P

P

A

A

R

N

V

E

V

I

R

K

H

Q

Sites not aligning to the query:

binding 5-(2-diethylamino-ethanesulfonyl)-21-hydroxy-10-isopropyl-11,19-dimethyl-9,26-dioxa-3,15,28-triaza-tricyclo[23.2.1.00,255]octacosa-1(27),12,17,19,25(28)-pentaene-2,8,14,23-tetraone: 37, 39, 54, 56, 81, 82, 93, 102, 108

1kk4A Crystal structure of vat(d) in complex with acetyl-coa (see paper)
48% identity, 24% coverage: 168:221/223 of query aligns to 113:166/205 of 1kk4A

query
sites
1kk4A

D

D

V

T

T

I

I

I

G

G

Q

N

H

D

V

V

W
|
W

L

I

G
|
G

M
x
K

R

D

C

V

I

V

V

I

L

M

K

P

G

G

V

V

T

K

I

I

G

G

D

D

G

G

A

A

I

I

V

V

A
|
A

G

N

S

S

V

V

T
x
V

R
x
K

D

D

V

I

P

A

P

P

A

Y

T

M

L
|
L

V

A

A
x
G

G
|
G

V

N

P
|
P

A

A

R

N

V

E

V
x
I

R

K

H

Q

binding acetyl coenzyme *a: W121 (= W176), G123 (= G178), K124 (≠ M179), A141 (= A196), A142 (= A197), V147 (≠ T202), K148 (≠ R203), L155 (= L210), G157 (≠ A212), G158 (= G213), P160 (= P215), I164 (≠ V219)

Sites not aligning to the query:

binding acetyl coenzyme *a: 69, 70, 111

3dhoA Structure of streptogramin acetyltransferase in complex with an inhibitor
47% identity, 25% coverage: 167:221/223 of query aligns to 112:166/203 of 3dhoA

query
sites
3dhoA

A

G

D

D

V

T

T

I

I

I

G

G

Q

N

H

D

V

V

W

W

L

I

G

G

M

K

R

D

C

V

I

V

V

I

L

M

K

P

G

G

V

V

T

K

I

I

G

G

D

D

G

G

A

A

I
|
I

V

V

A
|
A

A

A

G

N

S

S

V

V

T
x
V

R

K

D

D

V

I

P

A

P

P

A

Y

T

M

L
|
L

V

A

A
x
G

G

G

V

N

P
|
P

A

A

R

N

V

E

V
x
I

R

K

H

Q

binding 6-bromo-N'-[(1Z)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-2-methylquinoline-4-carbohydrazide: I139 (= I194), A141 (= A196), V147 (≠ T202), L155 (= L210), G157 (≠ A212), P160 (= P215), I164 (≠ V219)

Sites not aligning to the query:

binding 6-bromo-N'-[(1Z)-(3,5-dichloro-2-hydroxyphenyl)methylidene]-2-methylquinoline-4-carbohydrazide: 84

1khrA Crystal structure of vat(d) in complex with virginiamycin and coenzyme a (see paper)
48% identity, 24% coverage: 168:221/223 of query aligns to 113:166/206 of 1khrA

query
sites
1khrA

D

D

V

T

T

I

I

I

G

G

Q

N

H

D

V

V

W
|
W

L

I

G

G

M

K

R

D

C

V

I

V

V

I

L

M

K

P

G

G

V

V

T

K

I

I

G

G

D

D

G

G

A

A

I

I

V

V

A
|
A

G

N

S

S

V

V

T
x
V

R

K

D

D

V

I

P

A

P

P

A

Y

T

M

L
|
L

V

A

A
x
G

G

G

V

N

P
|
P

A

A

R

N

V

E

V
x
I

R

K

H

Q

binding coenzyme a: W121 (= W176), A141 (= A196), A142 (= A197), V147 (≠ T202), L155 (= L210), G157 (≠ A212), P160 (= P215), I164 (≠ V219)

Sites not aligning to the query:

binding coenzyme a: 82, 84
binding virginiamycin m1: 37, 39, 54, 80, 81, 82, 93

Query Sequence

>209281 FitnessBrowser__DvH:209281
MSGRLRNALHKIRDRGLTPRDLFSYGCIAGHRLLSGAWGTLMLRAKAGCLGITVGKGCEC
FGTVILSRWPGSRIELGDGVSIISSSRRCTSATIHAPTRLRTFAPTARIILEDGVSLNGT
AITARSRTIRIGKGTMVAPNCVITDSDFHAMWPPETRLDTPAFERDADVTIGQHVWLGMR
CIVLKGVTIGDGAIVAAGSVVTRDVPPATLVAGVPARVVRHLP

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