SitesBLAST

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)
38% identity, 31% coverage: 73:162/290 of query aligns to 644:734/1068 of P15304

query
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P15304

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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.

4ob6A Complex structure of esterase rppe s159a/w187h and substrate (s)-ac- cpa (see paper)
32% identity, 32% coverage: 69:162/290 of query aligns to 77:171/319 of 4ob6A

query
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4ob6A

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active site: G88 (= G80), G89 (≠ Y81), A160 (≠ S151)
binding (2S)-(acetyloxy)(2-chlorophenyl)ethanoic acid: G88 (= G80), G89 (≠ Y81), A160 (≠ S151), V161 (≠ A152)

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

8pc7A Structure of ester-hydrolase eh3 from the metagenome of marine sediments at milazzo harbor (sicily, italy) complexed with a derivative of bipyridine phosphonate (see paper)
29% identity, 43% coverage: 65:189/290 of query aligns to 86:211/336 of 8pc7A

query
sites
8pc7A

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binding hexyl-[2-(3-oxidanylpyridin-2-yl)pyridin-3-yl]oxy-phosphinic acid: G100 (= G79), G101 (= G80), G102 (≠ Y81), M104 (≠ Q83), E180 (≠ H150), S181 (= S151), G182 (≠ A152)

Sites not aligning to the query:

binding hexyl-[2-(3-oxidanylpyridin-2-yl)pyridin-3-yl]oxy-phosphinic acid: 212, 310

6sylA Structure of ester-hydrolase eh3 from the metagenome of marine sediments at milazzo harbor (sicily, italy) complexed with a derivative of butyl 4-nitrophenyl hexylphosphonate (see paper)
29% identity, 43% coverage: 65:189/290 of query aligns to 89:214/339 of 6sylA

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6sylA

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binding butoxy(hexyl)phosphinic acid: G104 (= G80), G105 (≠ Y81), S184 (= S151), G185 (≠ A152)

Sites not aligning to the query:

binding butoxy(hexyl)phosphinic acid: 215, 235, 238, 313

P71668 Esterase LipI; EC 3.1.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
36% identity, 40% coverage: 45:161/290 of query aligns to 57:175/320 of P71668

query
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P71668

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S165 (= S151) mutation to A: Complete loss of activity.

Sites not aligning to the query:

291 H→A: 90% loss of activity.

6syaA Structure of s192a-ester-hydrolase eh3 from the metagenome of marine sediments at milazzo harbor (sicily, italy) complexed with methyl (2r)-2-phenylpropanoate (see paper)
28% identity, 43% coverage: 65:189/290 of query aligns to 89:214/339 of 6syaA

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6syaA

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binding methyl (2~{R})-2-phenylpropanoate: G104 (= G80), G105 (≠ Y81), M107 (≠ Q83), A184 (≠ S151)

Sites not aligning to the query:

binding methyl (2~{R})-2-phenylpropanoate: 215, 313

6sxyB Structure of s192a-ester-hydrolase eh3 from the metagenome of marine sediments at milazzo harbor (sicily, italy) complexed with methyl (2s)-2-phenylpropanoate (see paper)
28% identity, 43% coverage: 65:189/290 of query aligns to 89:214/340 of 6sxyB

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6sxyB

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binding methyl (2~{S})-2-phenylpropanoate: G104 (= G80), G105 (≠ Y81), A184 (≠ S151), G185 (≠ A152)

Sites not aligning to the query:

binding methyl (2~{S})-2-phenylpropanoate: 20, 215, 313

5mifC Crystal structure of carboxyl esterase 2 (tmelest2) from mycorrhizal fungus tuber melanosporum (see paper)
27% identity, 69% coverage: 72:271/290 of query aligns to 64:281/301 of 5mifC

query
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5mifC

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active site: G72 (= G80), G73 (≠ Y81), S144 (= S151), A174 (vs. gap), C179 (= C179), D241 (≠ E230), H271 (= H261)
binding fragment of triton x-100: G72 (= G80), G73 (≠ Y81), W74 (= W82), S144 (= S151), A145 (= A152), A174 (vs. gap), I198 (≠ L192), I243 (≠ F234)

1qz3A Crystal structure of mutant m211s/r215l of carboxylesterase est2 complexed with hexadecanesulfonate (see paper)
34% identity, 31% coverage: 72:162/290 of query aligns to 74:165/309 of 1qz3A

query
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1qz3A

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A

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F

L

V

A

E

K

A

D

G

G

V

R

A

A

F

V

A

V

-

F

S

S

I

V

N

D

Y

Y

T

R

L

L

A

A

P

P

A

E

G

H

R

K

I

F

P

P

Q

A

M

A

V

V

E

E

E

D

I

A

E

Y

R

D

A

A

V

L

A

Q

W

W

L

I

Y

A

E

E

N

R

A

A

E

A

E

D

L

F

G

H

F

L

D

D

R

P

E

A

G

R

I

I

V

A

V

V

A

G

G

G

H

D

S
|
S

A
|
A

G

G

H

N

L

L

A

A

M

V

A

T

A

S

V

I

active site: G82 (= G80), G83 (≠ Y81), S154 (= S151)
binding 1-hexadecanosulfonic acid: G82 (= G80), G83 (≠ Y81), S154 (= S151), A155 (= A152)

Sites not aligning to the query:

active site: 184, 191, 251, 281
binding 1-hexadecanosulfonic acid: 12, 29, 35, 209, 213, 281

P16386 Hormone-sensitive lipase; HSL; Monoacylglycerol lipase LIPE; Retinyl ester hydrolase; REH; EC 3.1.1.79; EC 3.1.1.23 from Bos taurus (Bovine) (see 2 papers)
38% identity, 29% coverage: 73:157/290 of query aligns to 345:430/756 of P16386

query
sites
P16386

L

L

V

V

A

V

F

H

I

I

H

H

G

G

-

G

Y

F

W

V

Q

A

S

Q

L

T

D

S

K

K

G

S

D

H

F

E

S

P

Y

Y

L

L

A

K

P

S

A

W

F

A

V

Q

E

E

A

L

G

G

V

A

A

P

F

I

A

L

S

S

I

I

N

D

Y

Y

T

S

L

L

A

A

P

P

A

E

G

A

R

P

I

F

P

P

Q

R

M

A

V

L

E

E

I

C

E

F

R

Y

A

A

V

Y

A

C

W

W

L

A

Y

V

E

K

N

H

A

C

E

A

E

L

L

L

G

G

F

S

D

T

R

G

E

E

G

R

I

I

V

C

V

L

A

A

G

G

H

D

S

S

A

A

G

G

H

N

L

L

A

C

Sites not aligning to the query:

552 modified: Phosphoserine; by PKA
554 modified: Phosphoserine; by AMPK

P23872 Acetyl esterase; EcE; EC 3.1.1.- from Escherichia coli (strain K12) (see paper)
34% identity, 43% coverage: 44:167/290 of query aligns to 71:179/319 of P23872

query
sites
P23872

Q

Q

L

V

D

E

C

T

R

R

L

L

D

F

L

C

P

P

Y

Q

G

P

E

D

Q

S

P

P

L

-

Q

A

T

T

L

L

D

F

Y

Y

F

L

P

H

A

G

G

G

G

-

E

-

A

-

P

-

L

-

V

-

A

-

F

F

I

I

H

L

G

G

G

-

Y

-

W

-

Q

-

S

N

L

L

D

D

K

T

G
x
H

D

D

-

R

F

I

S

M

Y

R

L

L

A

L

P

A

A

S

F

Y

V

S

E

Q

A

C

G

T

V

V

A

I

F

-

A

-

S

G

I

I

N

D

Y

Y

T

T

L

L

A

S

P

P

A
x
E

G

A

R

R

I

F

P

P

Q

Q

M

A

V

I

E

E

I

I

E

V

R

A

A

A

V

C

A

C

W

Y

L

F

Y

H

E

Q

N

Q

A

A

E

E

E

D

L

Y

G

Q

F

I

D

N

R

M

E

S

G

R

I

I

V

G

V

F

A

A

G
|
G

H
x
D

S
|
S

A

A

G
|
G

G

A

H

M

L

L

A

A

A

L

M

A

A

S

A

A

V

L

A

-

D

-

W

W

S

L

R

R

H103 (≠ G88) mutation to A: Reduces enzymatic efficiency.
E128 (≠ A114) mutation to A: Reduces enzymatic efficiency.
G163 (= G149) mutation to A: Diminishes catalytic efficiency.
D164 (≠ H150) mutation to A: Strongly reduces enzymatic activity.
S165 (= S151) mutation to A: Abolishes enzymatic activity.
G167 (= G153) 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.

5hc0A Structure of esterase est22 with p-nitrophenol (see paper)
30% identity, 43% coverage: 65:189/290 of query aligns to 87:212/338 of 5hc0A

query
sites
5hc0A

P

P

A

D

G

S

G

T

G

D

E

K

A

L

P

P

L

C

V

V

A

Y

F

Y

I

I

H

H

G

G

G
|
G

Y
x
G

W

M

Q

Q

S

S

L
|
L

D

S

K

C

-

Y

G

G

D

N

F

Y

S

R

Y

A

L

W

A

G

P

K

A

I

F

I

V

A

E

S

A

N

G

G

V

V

A

A

F

V

A

A

S

M

I

V

N

E

Y

F

-

R

-

N

T

A

L

L

A

V

P

P

A

S

G

A

R

L

-

P

-

E

-

V

-

A

-

P

I

Y

P

P

Q

A

M

G

V

L

E
x
N

E

D

I

C

E

V

R

S

A

G

V

V

A
x
K

W

W

L

V

Y

A

E

S

N

H

A

A

E

D

E

E

L

L

G

G

F

I

D

D

R

A

E

S

G

R

I

I

V

I

A

A

G

G

H
x
E

S
|
S

A

G

G

G

H

N

L

L

A

T

A

L

M

A

A

A

A

G

V

L

A
x
R

D

-

W

-

S

L

R

K

H

Q

D
x
E

L

G

P

S

R

Q

D

D

L

L

L

I

R
x
Q

G

-

A

-

C

-

A

-

V

-

S

-

G

G

L

L

Y

Y

Q

A

L

L

Q

C

P

P

active site: G102 (= G80), G103 (≠ Y81), S182 (= S151)
binding glycerol: N153 (≠ E122), K160 (≠ A129), R194 (≠ A163), E198 (≠ D169), Q205 (≠ R176)
binding p-nitrophenol: L107 (= L85), E181 (≠ H150)

Sites not aligning to the query:

active site: 213, 218, 281, 311
binding glycerol: 74, 213, 218, 236, 238, 241, 251, 253, 272, 334
binding p-nitrophenol: 311

Query Sequence

>WP_159460143.1 NCBI__GCF_900177295.1:WP_159460143.1
MGGTLWRGYDKAALDRQINLRARTPEHVEFFAHWADDSRRVRAQLDCRLDLPYGEQPLQT
LDYFPAGGGEAPLVAFIHGGYWQSLDKGDFSYLAPAFVEAGVAFASINYTLAPAGRIPQM
VEEIERAVAWLYENAEELGFDREGIVVAGHSAGGHLAAMAAVADWSRHDLPRDLLRGACA
VSGLYQLQPIRLSYQQEVLQLDDAAVAAGSPQALIPEDGPPILLAVGDEEPEEFRDQQAE
FLAAWQARGLSGAAVPLPGRHHFSAIDALGEKDHALHRSVCYLAQNGAIS

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