SitesBLAST

3 K→I: No effect on membrane topology. Inverted topology; when associated with N-24; Q-27 and Q-28, or with N-24; K-27 and K-28.
24 D→K: Inverted topology; when associated with I-3; Q-27 and Q-28, or with I-3; K-27 and K-28.
27:28 mutation EE->KK,QQ: No effect on topology; when associated with K-24. Inverted topology; when associated with I-3 and K-24.
339 modified: Disulfide link with 115

6xycA Truncated form of carbohydrate esterase from gut microbiota (see paper)
27% identity, 44% coverage: 44:166/282 of query aligns to 6:135/285 of 6xycA

query
sites
6xycA

D

D

T

T

L

Y

L

S

T

T

E

S

-

W

S

T

D

N

I

V

S

N

Y

Y

G

A

D

S

A

D

P

S

L

L

Q

E

-

S

-

H

R

N

F

L

D

D

F

I

Y

Y

-

L

-

P

R

K

A

E

E

Q

G

K

A

T

Q

A

R

Y

P

K

L

A

L

I

V

I

F

I

I

I

H

Y

G

G

G

S

Y
x
A

W

W

Q

F

G

A

G

N

D

N

K

A

R

K

D

A

I

M

G

A

F

S

-

A

-

S

I

I

A

G

A

A

P

P

Y

L

V

L

K

K

A

A

G

G

I

F

S

A

V

V

A

I

V

S

I

I

N

N

Y

H

S

R

L

S

A

S

P

M

Q

E

A

A

R

I

I

W

E

P

D

A

M

Q

V

I

K

Q

E

D

V

V

Q

K

A

A

C

A

L

I

S

R

T

Y

I

V

A

R

Q

S

Q

N

A

A

E

A

R

K

L

Y

G

N

I

I

D

D

V

P

D

S

R

F

I

I

S

G

L

I

M

T

G

G

H

F

S
|
S

A
x
S

G

G

H

H

L

L

A

S

A

A

F

F

V

A

A

G

A

V

Q

T

P

N

G

G

binding 4-(2-aminoethyl)benzenesulfonyl fluoride: A49 (≠ Y82), S121 (= S152), S122 (≠ A153)

Sites not aligning to the query:

binding 4-(2-aminoethyl)benzenesulfonyl fluoride: 189, 190, 232, 262

4v2iA Biochemical characterization and structural analysis of a new cold- active and salt tolerant esterase from the marine bacterium thalassospira sp (see paper)
24% identity, 41% coverage: 47:162/282 of query aligns to 49:167/315 of 4v2iA

query
sites
4v2iA

L

I

T

T

E

D

S

T

D

T

I

F

S

A

Y

V

G

G

D

P

A

T

P

G

L

A

Q

T

R

K

F

V

D

R

F

I

Y

I

R

R

A

P

E

Q

G

G

A

N

-

T

-

D

Q

R

R

L

P

P

L

V

L

I

V

V

F

Y

I

F

H

H

G

G

G
x
A

Y
x
G

W

W

Q

V

G

M

G

G

D

D

K

T

R

G

D

T

I

H

G

D

-

R

F

L

I

V

A

R

A

E

P

L

Y

S

V

V

K

R

A

A

G

N

I

A

S

A

V

L

A

V

V

F

I

V

N

D

Y

Y

S

E

L

R

A

S

P

P

Q

E

A

A

R

R

I

Y

E

P

D

V

M

A

V

I

K

E

E

Q

V

D

Q

Y

A

A

C

V

L

T

S

K

T

Y

I

V

A

A

Q

E

Q

H

A

S

E

E

R

Q

L

L

G

N

I

V

D

D

V

P

D

T

R

R

I

L

S

A

L

I

M

A

G

G

H

D

S
|
S

A

V

G

G

H

N

L

M

A

T

A

A

F

V

V

V

A

S

active site: A85 (≠ G81), G86 (≠ Y82), S157 (= S152)

Sites not aligning to the query:

active site: 187, 192, 254, 284
binding magnesium ion: 185, 250, 254, 257

4ob6A Complex structure of esterase rppe s159a/w187h and substrate (s)-ac- cpa (see paper)
27% identity, 32% coverage: 73:162/282 of query aligns to 80:170/319 of 4ob6A

query
sites
4ob6A

P

P

L

V

L

F

V

M

F

F

I

F

H

H

G

G

G
|
G

Y
x
G

W

W

Q

V

G

L

G

G

D

D

-

F

-

P

-

T

-

H

-

Q

-

R

-

L

K

I

R

R

D

D

I

L

G

-

F

-

I

-

A

-

P

-

Y

V

V

V

K

G

A

S

G

G

I

A

S

V

V

A

A

V

V

Y

I

V

N

D

Y

Y

S

T

L

P

A

S

P

P

Q

E

A

S

R

H

I

Y

E

P

D

T

M

A

V

I

K

N

E

Q

V

A

Q

Y

A

A

C

A

L

T

S

Q

T

W

I

V

A

A

Q

E

Q

H

A

G

E

K

R

E

L

I

G

G

I

V

D

D

V

G

D

K

R

R

I

L

S

A

L

V

M

A

G

G

H

N

S
x
A

A
x
V

G

G

H

N

L

M

A

A

F

V

V

V

A

A

active site: G88 (= G81), G89 (≠ Y82), A160 (≠ S152)
binding (2S)-(acetyloxy)(2-chlorophenyl)ethanoic acid: G88 (= G81), G89 (≠ Y82), A160 (≠ S152), V161 (≠ A153)

Sites not aligning to the query:

active site: 190, 195, 257, 287
binding (2S)-(acetyloxy)(2-chlorophenyl)ethanoic acid: 13, 37, 37, 40, 208, 208, 209, 287, 288, 291, 292, 314, 315

P24484 Lipase 2; Triacylglycerol lipase; EC 3.1.1.3 from Moraxella sp. (strain TA144) (see paper)
33% identity, 35% coverage: 75:174/282 of query aligns to 161:260/433 of P24484

query
sites
P24484

L

M

V

L

F

F

I

F

H
|
H

G

G

Y

G

W

F

Q

C

G

I

G

G

D

D

-

I

K

D

R

T

D

H

I

H

G

E

F

F

I

C

A

H

A

T

P

V

Y

C

V

A

K

Q

A

T

G

G

I

W

S

A

V

V

A

V

V

S

I

V

N

D

Y

Y

S

R

L

M

A

A

P

P

Q

E

A

Y

R

P

I

A

E

P

D

T

M

A

V

L

K

K

E

D

V

C

Q

L

A

A

C

A

L

Y

S

A

T

W

I

L

A

A

Q

E

Q

H

A

S

E

Q

R

S

L

L

G

G

I

A

D

S

V

P

D

S

R

R

I

I

S

V

L

L

M

S

G

G

H

D

S
|
S

A

A

G

G

H

C

L

L

A

A

F

L

V

V

A

A

A

Q

Q

Q

P

V

G

I

R

K

M

-

P

P

V

I

Q

D

A

A

V

L

F

W

H165 (= H79) mutation to Q: Loss of lipase and esterase activity.
S239 (= S152) mutation to A: Loss of lipase and esterase activity.

5mifC Crystal structure of carboxyl esterase 2 (tmelest2) from mycorrhizal fungus tuber melanosporum (see paper)
29% identity, 30% coverage: 73:156/282 of query aligns to 64:148/301 of 5mifC

query
sites
5mifC

P

P

L

V

L

I

V

A

F

Y

I

F

H

H

G

G

G
|
G

Y
x
G

W
|
W

Q

V

-

F

G

G

D

P

K

K

R

S

D

Y

I

R

G

G

F

L

I

I

A

T

A

N

P

L

Y

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V

R

K

E

A

S

G

G

I

A

S

A

V

V

A

F

V

F

I

V

N

D

Y

Y

S

T

L

L

A

T

P

P

Q

K

A

V

R

A

I

Y

E

P

D

V

M

P

V

N

K

E

E

Q

V

C

Q

Y

A

A

C

A

L

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S

Q

T

W

I

L

A

L

Q

E

Q

H

A

G

E

E

R

K

L

L

G

G

I

V

D

D

V

P

D

T

R

N

I

M

S

G

L

F

M

G

G

G

H

D

S
|
S

A
|
A

G

G

H

E

active site: G72 (= G81), G73 (≠ Y82), S144 (= S152)
binding fragment of triton x-100: G72 (= G81), G73 (≠ Y82), W74 (= W83), S144 (= S152), A145 (= A153)

Sites not aligning to the query:

active site: 174, 179, 241, 271
binding fragment of triton x-100: 174, 198, 243

7bfrA Thermogutta terrifontis esterase 2 phosphorylated by paraoxon (see paper)
30% identity, 32% coverage: 71:159/282 of query aligns to 39:129/260 of 7bfrA

query
sites
7bfrA

Q

R

R

R

P

S

L

A

L

I

V

V

F

F

I

F

H

F

G

G

Y

G

W

W

Q

Q

G

S

G

G

D

S

K

P

R

A

D
x
Q

I

F

G

R

F

P

I

Q

A

C

A

E

P

Y

Y

F

V

A

K

G

A

R

G

G

I

M

S

V

V

A

A

M

V

A

I

A

N

D

Y

Y

S

R

L

V

A

G

P

S

Q

R

-

H

-

N

A

V

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K

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V

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A

D

D

M

C

V

V

K

A

E

D

V

A

Q

K

A

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C

A

L

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S

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T

W

I

V

A

R

Q

Q

Q

H

A

A

E

A

R

E

L

L

G

G

I

V

D

D

V

P

D

Q

R

K

I

I

S

V

L

A

M

S

G

G

H

G

S
|
S

A

A

G

G

H

H

L

L

A

A

binding carbonate ion: Q58 (≠ D90), S122 (= S152)

Sites not aligning to the query:

binding carbonate ion: 227

5aocA The structure of a novel thermophilic esterase from the planctomycetes species, thermogutta terrifontis, est2-valerate bound (see paper)
30% identity, 32% coverage: 71:159/282 of query aligns to 43:133/277 of 5aocA

query
sites
5aocA

Q

R

R

R

P

S

L

A

L

I

V

V

F

F

I

F

H

F

G

G

G
|
G

Y
x
G

W

W

Q

Q

G

S

G

G

D

S

K

P

R

A

D

Q

I

F

G

R

F

P

I

Q

A

C

A

E

P

Y

Y

F

V

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K

G

A

R

G

G

I

M

S

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V

A

A

M

V

A

I

A

N

D

Y

Y

S

R

L

V

A

G

P

S

Q

R

-

H

-

N

A

V

R

K

I

V

E

A

D

D

M

C

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V

K

A

E

D

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A

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C

A

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I

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A

R

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Q

Q

H

A

A

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A

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L

L

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G

I

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D

D

V

P

D

Q

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K

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S

V

L

A

M

S

G

G

H

G

S
|
S

A
|
A

G

G

H

H

L

L

A

A

binding pentanoic acid: G53 (= G81), G54 (≠ Y82), S126 (= S152), A127 (= A153)

Sites not aligning to the query:

binding pentanoic acid: 243

P71668 Esterase LipI; EC 3.1.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
31% identity, 33% coverage: 70:162/282 of query aligns to 82:175/320 of P71668

query
sites
P71668

A

A

Q

E

R

A

P

P

L

V

V

L

F

Y

I

F

H

H

G

G

Y

G

W

F

Q

V

G

M

G

G

D

D

-

L

K

D

R

T

D

H

I

D

G

G

F

T

I

C

A

R

A

Q

P

H

Y

A

V

V

K

G

A

A

G

D

I

A

S

I

V

V

A

V

V

S

I

V

N

D

Y

Y

S

R

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L

A

A

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P

Q

E

A

H

R

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I

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E

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D

A

M

A

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K

E

E

D

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A

Q

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A

A

C

A

L

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R

T

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A

A

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E

Q

H

A

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R

Q

L

V

G

G

I

A

D

D

V

L

D

G

R

R

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A

L

V

M

A

G

G

H

D

S
|
S

A

A

G

G

H

T

L

I

A

A

F

V

V

I

A

A

S165 (= S152) mutation to A: Complete loss of activity.

Sites not aligning to the query:

291 H→A: 90% loss of activity.

5aobA The structure of a novel thermophilic esterase from the planctomycetes species, thermogutta terrifontis, est2-butyrate bound (see paper)
30% identity, 32% coverage: 71:159/282 of query aligns to 39:129/278 of 5aobA

query
sites
5aobA

Q

R

R

R

P

S

L

A

L

I

V

V

F

F

I

F

H

F

G

G

G
|
G

Y
x
G

W

W

Q

Q

G

S

G

G

D

S

K

P

R

A

D

Q

I

F

G

R

F

P

I

Q

A

C

A

E

P

Y

Y

F

V

A

K

G

A

R

G

G

I

M

S

V

V

A

A

M

V

A

I

A

N

D

Y

Y

S

R

L

V

A

G

P

S

Q

R

-

H

-

N

A

V

R

K

I

V

E

A

D

D

M

C

V

V

K

A

E

D

V

A

Q

K

A

S

C

A

L

I

S

R

T

W

I

V

A

R

Q

Q

Q

H

A

A

E

A

R

E

L

L

G

G

I

V

D

D

V

P

D

Q

R

K

I

I

S

V

L

A

M

S

G

G

H

G

S
|
S

A
|
A

G

G

H

H

L

L

A

A

binding butanoic acid: G49 (= G81), G50 (≠ Y82), S122 (= S152), A123 (= A153)

P23872 Acetyl esterase; EcE; EC 3.1.1.- from Escherichia coli (strain K12) (see paper)
37% identity, 30% coverage: 75:158/282 of query aligns to 87:171/319 of P23872

query
sites
P23872

L

L

V

F

F

Y

I

L

H

H

G

G

Y

G

W

F

Q

I

G

L

G

G

-

N

-

L

D

D

K

T

R
x
H

D

D

-

R

I

I

G

M

F

R

I

L

A

L

A

A

P

S

Y

Y

V

S

K

Q

A

C

G

-

I

-

S

T

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V

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I

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G

I

I

N

D

Y

Y

S

T

L

L

A

S

P

P

Q
x
E

A

A

R

R

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F

E

P

D

Q

M

A

V

I

K

E

E

E

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I

Q

V

A

A

C

A

L

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S

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T

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I

F

A

H

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Q

A

A

E

E

R

D

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Y

G

Q

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I

D

N

V

M

D

S

R

R

I

I

S

G

L

F

M

A

G
|
G

H
x
D

S
|
S

A

A

G
|
G

G

A

H

M

L

L

A

A

H103 (≠ R89) mutation to A: Reduces enzymatic efficiency.
E128 (≠ Q115) mutation to A: Reduces enzymatic efficiency.
G163 (= G150) mutation to A: Diminishes catalytic efficiency.
D164 (≠ H151) mutation to A: Strongly reduces enzymatic activity.
S165 (= S152) mutation to A: Abolishes enzymatic activity.
G167 (= G154) mutation to A: Diminishes substrate affinity.

Sites not aligning to the query:

262 D→A: Strongly reduces enzymatic activity.
266 D→A: Reduces enzymatic efficiency.
292 H→A: Abolishes enzymatic activity.

P15304 Hormone-sensitive lipase; HSL; Monoacylglycerol lipase LIPE; Retinyl ester hydrolase; REH; EC 3.1.1.79; EC 3.1.1.23 from Rattus norvegicus (Rat) (see 2 papers)
34% identity, 32% coverage: 72:162/282 of query aligns to 642:733/1068 of P15304

query
sites
P15304

R

R

P

A

L

L

L

V

V

V

F

H

I

I

H

H

G

G

Y

-

W

-

Q

-

G

-

D

-

K

-

R

-

D

-

I

-

G

G

F

F

I

V

A

A

-

Q

-

T

-

S

-

K

-

S

-

H

A

E

P

P

Y

Y

V

L

K

K

A

N

-

W

-

A

-

Q

-

E

-

L

G

G

I

V

S

P

V

I

A

I

V

S

I

I

N

D

Y

Y

S

S

L

L

A

A

P

P

Q

E

A

A

R

P

I

F

E

P

D

R

M

A

V

L

K

E

E

E

V

C

Q

F

A

F

C

A

L

Y

S

C

T

W

I

A

A

V

Q

K

Q

H

A

C

E

E

R

L

L

L

G

G

I

S

D

T

V

G

D

E

R

R

I

I

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C

L

L

M

A

G

G

H

D

S

S

A

A

G

G

H

N

L

L

A

C

A

I

F

T

V

V

A

S

Sites not aligning to the query:

863 modified: Phosphoserine; by PKA; mutation S->A,E: No effect on activation by PKA.
865 modified: Phosphoserine; S→A: Increases activation by PKA.; S→E: No effect on activation by PKA.
959 modified: Phosphoserine; by PKA; S→A: Slightly decreases activation by PKA. Abolishes activation by PKA; when associated with A-960.
960 modified: Phosphoserine; by PKA; S→A: No effect on activation by PKA. Abolishes activation by PKA; when associated with A-959.

P22760 Arylacetamide deacetylase; EC 3.1.1.3 from Homo sapiens (Human) (see 6 papers)
27% identity, 43% coverage: 43:164/282 of query aligns to 75:201/399 of P22760

query
sites
P22760

A

S

D

D

T

E

L
x
N

L

V

T

T

E

V

S

T

D

E

I

T

S

K

Y

F

G

N

D

N

A

I

P

L

L

V

Q

R

R

V

F

Y

D

V

F

P

Y

K

R

R

A

K

E

S

G

E

A

A

Q

L

R

R

P

R

L

G

L

L

V

F

F

Y

I

I

H

H

G

G

Y

G

W

W

Q

C

G

V

G

G

D

S

K

A

R

A

D

L

I

S

G

G

F

Y

-

D

I

L

A

L

A

S

P

R

Y

W

V

T

K

A

A

D

G

R

I

L

S

D

V

A

A

V

V

V

I

V

-

S

-

T

N

N

Y

Y

S

R

L

L

A

A

P

P

Q

K

A

Y

R

H

I

F

E

P

D

I

M

Q

V

F

K

E

E

D

V

V

Q

Y

A

N

C

A

L

L

S

R

T

W

I

F

A

L

Q

R

Q

K

A

K

-

V

-

L

E

A

R

K

L

Y

G

G

I

V

D

N

V

P

D

E

R

R

I

I

S

G

L

I

M

S

G

G

H

D

S

S

A

A

G

G

H

N

L

L

A

A

F

A

V

V

A

T

A

Q

Q

Q

N78 (≠ L46) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Abolishes glycosylation at this site and causes moderate decrease in activity.

Sites not aligning to the query:

281 V → I: in alleles AADAC*2 and AADAC*3; mildly decreased enzyme activity; dbSNP:rs1803155
282 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Abolishes glycosylation at this site and causes substantial decrease in activity and reduced substrate affinity.
399 natural variant: L -> LQ (in allele AADAC*3; decreased enzyme activity)

P95125 Carboxylic ester hydrolase LipN; EC 3.1.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 34% coverage: 65:161/282 of query aligns to 126:225/376 of P95125

query
sites
P95125

Y

Y

R

R

-

P

A

S

E

G

G

G

A

G

Q

A

R

T

P

P

L

L

V

V

F

F

I

Y

H

H

G

G

Y

G

W
|
W

Q

T

G

L

G

G

D

D

K

L

R

D

D

T

I

H

G

D

F

A

I

L

A

C

A

R

P

L

Y

T

V

C

K

R

-

D

A

A

G

D

I

I

S

Q

V

V

A

L

V

S

I

I

N

D

Y

Y

S

R

L

L

A

A

P

P

Q

E

A

H

R

P

I

A

E

P

D

A

M

A

V

V

K

E

E

D

V

A

Q

Y

A

A

C

A

L

F

S

V

T

W

I

A

A

H

Q

E

Q

H

A

A

-

S

E

D

R

E

L

F

G

G

I

A

D

L

V

P

D

G

R

R

I

V

S

A

L

V

M

G

G

G

H

D

S
|
S

A

A

G

G

H

N

L

L

A

S

A

A

F

V

V

V

W145 (= W83) mutation to A: Loss of activity.
S216 (= S152) mutation to A: Loss of activity.

Sites not aligning to the query:

316 D→A: Loss of activity.
320 D→A: No change in activity.
346 H→A: Loss of activity.

Query Sequence

>HSERO_RS18245 FitnessBrowser__HerbieS:HSERO_RS18245
ISTDTRRVLCPVAECEAGYNLKAAFPDFPQVLQQWQQATAAIADTLLTESDISYGDAPLQ
RFDFYRAEGAQRPLLVFIHGGYWQGGDKRDIGFIAAPYVKAGISVAVINYSLAPQARIED
MVKEVQACLSTIAQQAERLGIDVDRISLMGHSAGGHLAAFVAAQPGRMPVQAVFAISGVF
DLAPLIPTSLNKALTLDQVRADALSPVLQTGPAQTRVHTIIGELETLQFHLQAAVMANCW
PQVVAHHVVPDTHHYTVLFPLADADSSVCRAVIAEMNSAGRR

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