SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 3609315 FitnessBrowser__Dino:3609315 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 10 hits to proteins with known functional sites (download)

Q51645 (S)-2-haloacid dehalogenase 4A; 2-haloalkanoic acid dehalogenase IVA; Halocarboxylic acid halidohydrolase IVA; L-2-haloacid dehalogenase IVA; EC 3.8.1.2 from Burkholderia cepacia (Pseudomonas cepacia) (see 2 papers)
39% identity, 99% coverage: 3:229/229 of query aligns to 5:227/231 of Q51645

query
sites
Q51645

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D11 (= D9) active site, Nucleophile
AY 12:13 (= AY 10:11) binding
R42 (= R45) binding
SN 119:120 (= SN 122:123) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

2no5B Crystal structure analysis of a dehalogenase with intermediate complex (see paper)
39% identity, 99% coverage: 3:228/229 of query aligns to 5:226/226 of 2no5B

query
sites
2no5B

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active site: D11 (= D9), T15 (= T13), R42 (= R45), S119 (= S122), N120 (= N123), K152 (= K155), S176 (= S179), N178 (= N181), W180 (= W183), D181 (= D184)
binding (2s)-2-chloropropanoic acid: H20 (≠ S18), E35 (≠ F33), S38 (≠ A41), M39 (≠ R42), N178 (= N181), A179 (≠ G182), W180 (= W183)

Q53464 (S)-2-haloacid dehalogenase; 2-haloalkanoic acid dehalogenase; Halocarboxylic acid halidohydrolase; L-2-haloacid dehalogenase; L-DEX; EC 3.8.1.2 from Pseudomonas sp. (strain YL) (see 2 papers)
39% identity, 98% coverage: 3:227/229 of query aligns to 4:223/232 of Q53464

query
sites
Q53464

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D10 (= D9) active site, Nucleophile; mutation D->E,S,A,G: Loss of catalytic activity.; mutation to N: Severe reduction in catalytic activity.
LY 11:12 (≠ AY 10:11) binding
T14 (= T13) Important for catalytic activity; mutation to A: Severe reduction in catalytic activity. No effect on substrate affinity.; mutation T->P,C: Severe reduction in catalytic activity.; mutation to S: Mild reduction in catalytic activity.
R41 (= R45) mutation to E: Severe reduction in catalytic activity.; mutation to K: Severe reduction in catalytic activity. 4-fold decrease in substrate affinity.; mutation to W: Loss of catalytic activity.
S118 (= S122) mutation to A: Severe reduction in catalytic activity. 25-fold decrease in substrate affinity.
SN 118:119 (= SN 122:123) binding
K151 (= K155) Important for catalytic activity; mutation to A: Loss of catalytic activity.; mutation to R: Severe reduction in catalytic activity.
Y157 (= Y161) Important for catalytic activity; mutation Y->C,S,H,W: Severe reduction in catalytic activity.; mutation to F: Severe reduction in catalytic activity. 1.5-fold decrease in substrate affinity.
S175 (= S179) mutation to A: Severe reduction in catalytic activity. 2-fold decrease in substrate affinity.; mutation to C: Severe reduction in catalytic activity.; mutation to T: Moderate reduction in catalytic activity.
SSNAWD 175:180 (≠ SSNGWD 179:184) Important for catalytic activity
N177 (= N181) mutation N->D,I: Loss of catalytic activity.; mutation N->W,K,H,Q: Severe reduction in catalytic activity.
D180 (= D184) mutation D->N,E,S,G: Loss of catalytic activity.

1zrmA Crystal structure of the reaction intermediate of l-2-haloacid dehalogenase with 2-chloro-n-butyrate (see paper)
39% identity, 95% coverage: 3:220/229 of query aligns to 2:214/220 of 1zrmA

query
sites
1zrmA

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active site: D8 (= D9), T12 (= T13), R39 (= R45), S116 (= S122), N117 (= N123), K149 (= K155), A173 (≠ S179), N175 (= N181), W177 (= W183), D178 (= D184)
binding butanoic acid: D8 (= D9), L9 (≠ A10), Y10 (= Y11), S116 (= S122)

3umbA Crystal structure of the l-2-haloacid dehalogenase rsc1362
41% identity, 98% coverage: 3:227/229 of query aligns to 3:226/227 of 3umbA

query
sites
3umbA

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S

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K

Q

active site: D9 (= D9), T13 (= T13), R40 (= R45), S121 (= S122), N122 (= N123), K154 (= K155), S178 (= S179), N180 (= N181), W182 (= W183), D183 (= D184)
binding magnesium ion: D41 (≠ L46), D45 (≠ Q50), A76 (≠ E77), N79 (≠ G80)

Q60099 (S)-2-haloacid dehalogenase; 2-haloalkanoic acid dehalogenase; Halocarboxylic acid halidohydrolase; L-2-haloacid dehalogenase; EC 3.8.1.2 from Xanthobacter autotrophicus (see 2 papers)
43% identity, 83% coverage: 3:193/229 of query aligns to 2:185/253 of Q60099

query
sites
Q60099

I

I

T

K

T

A

C

V

I

V

F

F

D
|
D

A
|
A

Y
|
Y

G

G

T

T

L

L

F

F

D

D

V

V

S

Q

A

S

A

V

A

A

R

D

E

A

A

T

A

E

-

R

A

A

E

Y

P

P

G

G

R

R

A

G

A

E

F

Y

A

I

T

T

R

Q

W

V

P

-

Q

-

I

-

A

-

R

-

D

-

W

W

R
|
R

L

Q

K

K

Q

Q

L

L

Q

E

Y

Y

T

S

W

W

L

L

R

R

A

A

I

L

T

M

G

G

D

R

H

Y

C

A

D

D

F

F

W

W

Q

G

V

V

T

T

Q

R

D

E

G

A

L

L

D

A

W

Y

A

T

L

L

E

G

A

T

A

L

G

G

L

L

G

E

D

P

D

D

A

E

E

S

L

F

R

L

E

A

R

D

L

M

L

A

Q

Q

L

A

Y

Y

W

N

E

R

L

L

S

T

A

P

Y

Y

P

P

E

D

V

A

P

A

A

Q

M

C

L

L

G

A

A

E

L

L

K

A

D

P

Q

-

G

-

L

L

N

K

T

R

G

A

I

I

L

L

S
|
S

N
|
N

G

G

A

A

P

P

D

D

M

M

L

L

A

Q

G

A

A

L

V

V

D

A

S

N

A

A

G

G

I

L

G

T

A

D

L

S

L

F

D

D

D

A

V

V

L

I

S

S

V

V

E

D

S

A

V

K

S

R

I

V

F

F

K

K

P

P

A

H

R

P

L

D

V

S

Y

Y

D

A

L

L

V

V

G

E

A

E

R

V

F

L

G

G

C

V

S

T

P

P

E

A

Q

E

V

V

M

L

F

F

V

V

S

S

N

N

G

G

W

F

D

D

A

V

A

G

A

A

A

K

A

N

Y

F

G

G

F

F

D8 (= D9) active site, Nucleophile
AY 9:10 (= AY 10:11) binding
R39 (= R45) binding
SN 114:115 (= SN 122:123) binding

2yn4A L-2-chlorobutryic acid bound complex l-haloacid dehalogenase from a rhodobacteraceae family bacterium (see paper)
28% identity, 90% coverage: 7:212/229 of query aligns to 5:203/225 of 2yn4A

query
sites
2yn4A

I

V

F

F

D
|
D

A

V

Y
x
N

G

E

T
|
T

L

L

F

L

D

D

V

L

S

T

A

S

A

L

A

S

R

P

E

L

A

F

A

E

A

R

E

V

P

F

G

G

R

D

A

A

A

-

F

-

A

-

T

-

R

-

W

-

P

-

Q

K

I

V

A

L

R

R

D

E

W

W

R
x
F

L

P

K

E

Q

L

L

I

Q

L

Y

Y

T

S

W

Q

L

T

R

L

A

T

I

L

T

T

G

G

D

L

H

Y

C

R

D

P

F
|
F

W

G

Q

E

V

I

T

A

Q

A

D

A

G

V

L

F

D

E

W

M

A

V

-

A

-

N

L

H

E

Q

A

A

A

K

G

V

L

T

G

P

D

D

-

I

A

A

E

E

L

L

R

K

E

T

R

R

L

L

L

T

Q

S

L

M

Y

-

W

-

E

-

L

-

S

P

A

A

Y

Y

P

P

E

D

V

V

P

A

A

P

M

A

L

L

G

T

A

R

L

L

K

Q

D

D

Q

A

G

G

L

F

N

R

T

L

G

V

I

T

L

L

S
x
T

N
|
N

G

S

A

A

P

P

D

S

M

P

L

A

A

P

G

S

A

P

V

L

D

E

S

K

A

A

G

G

I

I

G

A

A

S

L

F

D

E

D

A

V

H

L

L

S

T

V

V

E

H

S

S

V

S

S

Q

I

R

F

F

K
|
K

P

P

A

H

R

P

L

S

V

V

Y

Y

D

D

L

S

V

T

G

A

A

E

R

T

F

L

G

G

C

A

S

K

P

P

E

E

Q

E

V

L

M

C

F

M

V

I

S
x
A

S

C

N
x
H

G

I

W
|
W

D
|
D

A

T

A

I

A

G

A

A

A

Q

A

A

Y

R

G

G

F

W

R

R

A

G

V

G

W

F

A

V

N

A

R

R

A

P

E

H

E

N

P

T

V

P

D

L

R

T

L

L

P

A

A

E

V

V

P

P

active site: D7 (= D9), T11 (= T13), F36 (≠ R45), T113 (≠ S122), N114 (= N123), K146 (= K155), A170 (≠ S179), H172 (≠ N181), W174 (= W183), D175 (= D184)
binding (2S)-2-chlorobutanoic acid: D7 (= D9), N9 (≠ Y11), F55 (= F64), T113 (≠ S122), N114 (= N123), H172 (≠ N181)

8wbtA Crystal structure of cis-epoxysuccinate hydrolases klcesh[l] mutant d48n complexed with l-ta (see paper)
26% identity, 93% coverage: 1:214/229 of query aligns to 1:217/237 of 8wbtA

query
sites
8wbtA

M

M

P

G

I

L

T

K

T

A

C

L

I

F

F

F

D
x
N

A
x
V

Y
x
Q

G

G

T

T

L

L

F

V

D

D

V

F

-

Y

S

S

A

T

A

I

A

T

R

R

E

E

A

G

A

E

A

A

E

F

P

S

G

A

R

V

A

R

A

G

F

F

A

Q

T

A

R

D

W

W

P

T

Q

T

I

V

A

T

R

E

D

Q

W

W

R

R

L

-

K

A

Q

E

L

Y

Q

R

Y

S

T

R

W

L

L

D

R

Q

A

V

I

I

T

K

G

G

D

E

H

R

C

P

D

-

F

-

W

W

Q

T

V

T

T

T

-

D

-

R

-

I

-

Y

Q

R

D

E

G

A

L

L

D

D

W

G

A

I

L

L

E

A

A

N

A

H

-

P

-

W

G

G

L

A

G

S

D

L

D

N

A

S

E

A

L

D

R

R

E

D

R

E

L

L

L

N

Q

S

L

L

Y

W

W

S

E

K

L

L

S

I

A

P

Y

W

P

D

E

D

V

T

P

A

A

P

M

G

L

L

G

A

A

R

L

L

K

R

D

S

Q

K

G

Y

L

I

N

-

T

T

G

S

I

T

L

L

S
|
S

N
|
N

G

G

A

S

P

-

D

-

M

-

L

M

A

A

G

S

A

V

V

L

D

R

S

I

A

S

G

K

I

L

G

G

A

A

L

L

-

P

L

F

D

D

D

A

V

I

L

L

S

T

V

A

E

E

S

L

V

V

S

R

I

S

F

S

K
|
K

P

P

A

D

R

P

L

K

V

V

Y

Y

D

Q

L

L

V

A

G

L

A

D

R

S

F

V

G

G

C

I

S

E

P

A

E

H

Q

Q

V

A

M

M

F

M

V

V

S

A

S

C

N

H

G

K

W
x
Y

D

D

A

L

A

Q

A

A

A

K

A

R

Y

L

G

G

F

F

R

K

A

V

V

A

W

F

A

I

N

A

R

R

A

P

E

F

E

E

-

F

-

G

P

P

V

N

D

K

R

K

L

V

P

D

A

T

V

K

P

P

D

E

R

Q

binding l(+)-tartaric acid: N9 (≠ D9), V10 (≠ A10), Q11 (≠ Y11), S125 (= S122), N126 (= N123), K156 (= K155), Y184 (≠ W183)

4ygrA Crystal structure of had phosphatase from thermococcus onnurineus (see paper)
32% identity, 49% coverage: 89:200/229 of query aligns to 75:187/215 of 4ygrA

query
sites
4ygrA

E

E

R

E

L

L

Q

E

L

R

Y

Y

-

P

W

H

E

K

L

L

S

Q

A

V

Y

Y

P

P

E

D

V

T

P

I

A

P

M

T

L

L

G

E

A

W

L

L

K

R

D

D

Q

T

G

G

L

Y

N

K

T

L

G

G

I

I

L

V

S
x
T

N
x
S

G
|
G

A

-

P

P

D

K

M

Y

L

Q

A

R

G

L

A

K

V

L

D

K

S

L

A

T

G

G

I

L

G

L

A

D

L

Y

L

F

D

D

D

V

V

V

L

I

S

T

V

R

E

D

S

D

V

V

S

N

I

A

F

I

K
|
K

P

P

A

E

R

P

L

K

V

I

Y

F

D

L

L

Y

V

T

G

I

A

E

R

R

F

L

G

G

C

V

S

E

P

P

-

G

E

E

Q

A

V

V

M

M

F

V

V
x
G

S
x
D

S

S

N
x
L

G

S

W
x
Q

D
|
D

A

V

A

Y

A

G

A

A

A

K

A

S

Y

V

G

G

F

M

R

T

A

A

V

V

W

W

A

I

N

N

R

R

active site: T109 (≠ S122), S110 (≠ N123), G111 (= G124), K141 (= K155), G165 (≠ V178), D166 (≠ S179), L168 (≠ N181), Q170 (≠ W183), D171 (= D184)
binding magnesium ion: D166 (≠ S179)

Sites not aligning to the query:

active site: 7, 9, 15, 38
binding magnesium ion: 7, 9
binding 2-[n-cyclohexylamino]ethane sulfonic acid: 9, 50, 53, 58, 58, 61

8wbqB Crystal structure of cis-epoxysuccinate hydrolases rhcesh[l] mutant e212q complexed with l-ta. (see paper)
26% identity, 93% coverage: 1:213/229 of query aligns to 8:222/244 of 8wbqB

query
sites
8wbqB

M

M

P

Q

I

F

T

R

T

A

C

L

I

L

F

F

D
|
D

A

V

Y
x
Q

G

G

T

T

L

L

F

T

D

D

V

F

S

-

A

-

R

R

E

S

A

T

A

L

A

I

E

E

P

H

G

G

R

L

A

S

A

I

F

L

A

G

T

D

R

R

-

V

-

D

-

R

-

E

-

L

W

W

P

E

Q

E

I

L

A

V

R

D

D

Q

W

W

R
|
R

-

G

-

C

-
x
Y

-

R

-

D

-

E

-

L

-

D

-

S

-

L

L

V

K

K

Q

Q

L

E

Q

K

Y

W

T

R

W

S

L

V

R

R

A

A

I

V

T

Y

G

R

D

D

H

-

C

-

D

-

F

-

W

-

Q

-

V

-

T

S

Q

L

D

I

G

N

L

L

D

L

W

A

A

K

L

F

E

S

A

D

A

S

G

F

L

C

G

A

D

T

D

S

A

A

E

E

L

V

R

E

E

-

R

-

L

L

Q

T

L

D

Y

G

W

W

E

E

-

R

L

L

S

R

A

S

Y

W

P

P

E

D

V

V

P

P

A

S

M

G

L

L

G

E

A

Q

L

L

K

R

D

S

Q

K

G

Y

L

L

N

-

T

V

G

A

I

A

L

L

S
x
T

N
|
N

G

A

A

D

P

F

D

S

M

A

L

I

A

V

G

N

A

V

V

G

D

R

S

S

A

A

G

K

I

L

G

Q

A

-

L

-

L

W

D

D

D

A

V

V

L

L

S

S

V

A

E

Q

S

L

V

F

S

G

I

A

F

Y

K

K

P

P

A

H

R

R

L

S

V

T

Y

Y

D

E

L

G

V

A

G

A

A

T

R

L

F

L

G

G

C

I

S

A

P

P

E

S

Q

E

V

I

M

L

F

M

V

V

S

A

S

S

N
x
H

G

A

W

Y

D

D

A

L

A

E

A

A

A

R

A

E

Y

V

G

G

F

A

R

G

A

T

V

A

W

Y

A

V

N

R

R

R

A

P

E

L

E

Q

-

Y

-

G

P

P

V

T

D

G

R

R

L

T

P

E

A

D

V

V

P

P

D

D

binding l(+)-tartaric acid: D16 (= D9), Q18 (≠ Y11), R53 (= R45), Y56 (vs. gap), T131 (≠ S122), N132 (= N123), H188 (≠ N181)

Query Sequence

>3609315 FitnessBrowser__Dino:3609315
MPITTCIFDAYGTLFDVSAAAREAAAEPGRAAFATRWPQIARDWRLKQLQYTWLRAITGD
HCDFWQVTQDGLDWALEAAGLGDDAELRERLLQLYWELSAYPEVPAMLGALKDQGLNTGI
LSNGAPDMLAGAVDSAGIGALLDDVLSVESVSIFKPARLVYDLVGARFGCSPEQVMFVSS
NGWDAAAAAAYGFRAVWANRAEEPVDRLPAVPDRIVADLRPLPVLVKEL

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