SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Ac3H11_545 FitnessBrowser__acidovorax_3H11:Ac3H11_545 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)

4ilvB Structure of the dioxygenase domain of sacte_2871, a novel dioxygenase carbohydrate-binding protein fusion from the cellulolytic bacterium streptomyces sp. Sirexaa-e (see paper)
38% identity, 63% coverage: 53:194/225 of query aligns to 5:132/157 of 4ilvB

query
sites
4ilvB

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active site: Y65 (= Y119), R87 (= R149), G96 (= G158), R99 (≠ P161), I101 (= I163)
binding fe (iii) ion: Y65 (= Y119), Y94 (= Y156), H100 (= H162), H102 (= H164)

3pckM Structure of protocatechuate 3,4-dioxygenase complexed with 6- hydroxynicotinic acid n-oxide (see paper)
38% identity, 57% coverage: 57:185/225 of query aligns to 45:181/233 of 3pckM

query
sites
3pckM

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active site: Y105 (= Y119), Y144 (= Y156), R154 (vs. gap), H157 (= H162), H159 (= H164)
binding fe (iii) ion: Y105 (= Y119), H157 (= H162), H159 (= H164)
binding 6-hydroxyisonicotinic acid n-oxide: Y105 (= Y119), W146 (≠ G158), R154 (vs. gap), H157 (= H162), H159 (= H164)

Sites not aligning to the query:

binding 6-hydroxyisonicotinic acid n-oxide: 24, 188

3pcjM Structure of protocatechuate 3,4-dioxygenase complexed with 2- hydroxyisonicotinic acid n-oxide (see paper)
38% identity, 57% coverage: 57:185/225 of query aligns to 45:181/233 of 3pcjM

query
sites
3pcjM

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active site: Y105 (= Y119), Y144 (= Y156), R154 (vs. gap), H157 (= H162), H159 (= H164)
binding fe (iii) ion: Y105 (= Y119), H157 (= H162), H159 (= H164)
binding 2-hydroxyisonicotinic acid n-oxide: Y144 (= Y156), W146 (≠ G158), R154 (vs. gap), H157 (= H162), H159 (= H164)

Sites not aligning to the query:

binding 2-hydroxyisonicotinic acid n-oxide: 24

3pciM Structure of protocatechuate 3,4-dioxygenase complexed with 3-iodo-4- hydroxybenzoate (see paper)
38% identity, 57% coverage: 57:185/225 of query aligns to 45:181/233 of 3pciM

query
sites
3pciM

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active site: Y105 (= Y119), Y144 (= Y156), R154 (vs. gap), H157 (= H162), H159 (= H164)
binding fe (iii) ion: Y105 (= Y119), Y144 (= Y156), H157 (= H162), H159 (= H164)
binding 3-iodo-4-hydroxybenzoic acid: Y105 (= Y119), Y144 (= Y156), H159 (= H164)

3pchM Structure of protocatechuate 3,4-dioxygenase complexed with 3-chloro- 4-hydroxybenzoate (see paper)
38% identity, 57% coverage: 57:185/225 of query aligns to 45:181/233 of 3pchM

query
sites
3pchM

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active site: Y105 (= Y119), Y144 (= Y156), R154 (vs. gap), H157 (= H162), H159 (= H164)
binding 3-chloro-4-hydroxybenzoic acid: Y144 (= Y156), W146 (≠ G158), R154 (vs. gap), H157 (= H162), H159 (= H164), Q174 (= Q178)
binding fe (iii) ion: Y105 (= Y119), Y144 (= Y156), H157 (= H162), H159 (= H164)

Sites not aligning to the query:

binding 3-chloro-4-hydroxybenzoic acid: 24, 188

3pcgM Structure of protocatechuate 3,4-dioxygenase complexed with the inhibitor 4-hydroxyphenylacetate (see paper)
38% identity, 57% coverage: 57:185/225 of query aligns to 45:181/233 of 3pcgM

query
sites
3pcgM

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active site: Y105 (= Y119), Y144 (= Y156), R154 (vs. gap), H157 (= H162), H159 (= H164)
binding 4-hydroxyphenylacetate: Y105 (= Y119), Y144 (= Y156), W146 (≠ G158), R154 (vs. gap), H159 (= H164)
binding fe (iii) ion: Y105 (= Y119), Y144 (= Y156), H157 (= H162), H159 (= H164)

Sites not aligning to the query:

binding 4-hydroxyphenylacetate: 24, 188

3pcfM Structure of protocatechuate 3,4-dioxygenase complexed with 3-fluro-4- hydroxybenzoate (see paper)
38% identity, 57% coverage: 57:185/225 of query aligns to 45:181/233 of 3pcfM

query
sites
3pcfM

Q

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active site: Y105 (= Y119), Y144 (= Y156), R154 (vs. gap), H157 (= H162), H159 (= H164)
binding fe (iii) ion: Y105 (= Y119), Y144 (= Y156), H157 (= H162), H159 (= H164)
binding 3-fluoro-4-hydroxybenzoic acid: Y144 (= Y156), W146 (≠ G158), R154 (vs. gap), H157 (= H162), H159 (= H164)

Sites not aligning to the query:

binding 3-fluoro-4-hydroxybenzoic acid: 22, 24, 28, 188

3pceM Structure of protocatechuate 3,4-dioxygenase complexed with 3- hydroxyphenylacetate (see paper)
38% identity, 57% coverage: 57:185/225 of query aligns to 45:181/233 of 3pceM

query
sites
3pceM

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P

Y
|
Y

T

P

G
x
W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

active site: Y105 (= Y119), Y144 (= Y156), R154 (vs. gap), H157 (= H162), H159 (= H164)
binding 3-hydroxyphenylacetate: Y105 (= Y119), Y144 (= Y156), W146 (≠ G158), R154 (vs. gap), H159 (= H164)
binding fe (iii) ion: Y105 (= Y119), Y144 (= Y156), H157 (= H162), H159 (= H164)

Sites not aligning to the query:

binding 3-hydroxyphenylacetate: 188

3pcbM Structure of protocatechuate 3,4-dioxygenase complexed with 3- hydroxybenzoate (see paper)
38% identity, 57% coverage: 57:185/225 of query aligns to 45:181/233 of 3pcbM

query
sites
3pcbM

Q

E

T

T

E

T

G

G

P

P

Y

N

Y

F

P

S

V

H

R

L

F

G

P

F

S

G

D

A

S

H

D

D

G

H

D

D

L

L

R

L

N

N

G

F

L

G

M

L

R

P

Y

I

V

-

D

-

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H

R

H

H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
|
Y

T

P

G
x
W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

active site: Y105 (= Y119), Y144 (= Y156), R154 (vs. gap), H157 (= H162), H159 (= H164)
binding 3-hydroxybenzoic acid: Y144 (= Y156), W146 (≠ G158), R154 (vs. gap)
binding fe (iii) ion: Y105 (= Y119), Y144 (= Y156), H157 (= H162), H159 (= H164)

Sites not aligning to the query:

binding 3-hydroxybenzoic acid: 24, 188

P00437 Protocatechuate 3,4-dioxygenase beta chain; 3,4-PCD; EC 1.13.11.3 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
41% identity, 44% coverage: 86:185/225 of query aligns to 76:185/239 of P00437

query
sites
P00437

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H

R

H

H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
|
Y

T

P

G

W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-

R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

Y109 (= Y119) binding
Y148 (= Y156) binding
H161 (= H162) binding
H163 (= H164) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

4whqF Alkylperoxo reaction intermediate trapped in protocatechuate 3,4- dioxygenase (pseudomonas putida) at ph 6.5 (see paper)
41% identity, 44% coverage: 86:185/225 of query aligns to 75:184/236 of 4whqF

query
sites
4whqF

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H
x
R

H
|
H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q
x
G

G

G

F
x
V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
|
Y

T

P

G

W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

active site: Y108 (= Y119), Y147 (= Y156), R157 (vs. gap), H160 (= H162), H162 (= H164)
binding 4-fluorobenzene-1,2-diol: G124 (≠ Q133), V126 (≠ F135)
binding bicarbonate ion: R109 (≠ H120), H110 (= H121)
binding fe (iii) ion: Y108 (= Y119), H160 (= H162), H162 (= H164)

Sites not aligning to the query:

binding 4-fluorobenzene-1,2-diol: 38, 39, 40, 66, 193, 195, 196, 201

4whrB Anhydride reaction intermediate trapped in protocatechuate 3,4- dioxygenase (pseudomonas putida) at ph 8.5 (see paper)
41% identity, 44% coverage: 86:185/225 of query aligns to 75:184/238 of 4whrB

query
sites
4whrB

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H

R

H

H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
|
Y

T

P

G
x
W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

active site: Y108 (= Y119), Y147 (= Y156), R157 (vs. gap), H160 (= H162), H162 (= H164)
binding 4-fluorooxepine-2,7-dione: Y147 (= Y156), W149 (≠ G158), R157 (vs. gap), H160 (= H162), H162 (= H164)
binding fe (iii) ion: Y108 (= Y119), Y147 (= Y156), H160 (= H162), H162 (= H164)

Sites not aligning to the query:

binding 4-fluorobenzene-1,2-diol: 7, 22, 28, 38, 40, 40, 41, 231, 236
binding 4-fluorooxepine-2,7-dione: 191

4whqB Alkylperoxo reaction intermediate trapped in protocatechuate 3,4- dioxygenase (pseudomonas putida) at ph 6.5 (see paper)
41% identity, 44% coverage: 86:185/225 of query aligns to 75:184/238 of 4whqB

query
sites
4whqB

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R
|
R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H
x
R

H
|
H

P
x
K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
|
Y

T

P

G
x
W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

active site: Y108 (= Y119), Y147 (= Y156), R157 (vs. gap), H160 (= H162), H162 (= H164)
binding 4-fluorobenzene-1,2-diol: R83 (= R94), R109 (≠ H120), H110 (= H121), K111 (≠ P122)
binding (6S)-4-fluoro-6-hydroperoxy-6-hydroxycyclohexa-2,4-dien-1-one: Y108 (= Y119), Y147 (= Y156), W149 (≠ G158), R157 (vs. gap), H160 (= H162), H162 (= H164)
binding fe (iii) ion: Y108 (= Y119), Y147 (= Y156), H160 (= H162), H162 (= H164)

Sites not aligning to the query:

3lxvM Tyrosine 447 of protocatechuate 3,4-dioxygenase controls efficient progress through catalysis
37% identity, 57% coverage: 57:185/225 of query aligns to 45:184/238 of 3lxvM

query
sites
3lxvM

Q

E

T

T

E

T

G

G

P

P

Y

N

Y

F

P

S

V

H

R

L

F

G

P

F

S

G

D

A

S

H

D

D

G

H

D

D

L

L

-

L

-

N

-

F

R

N

N

N

G

G

L

G

M

L

R

P

Y

I

V

-

D

-

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H

R

H

H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
x
H

T

P

G
x
W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

binding 4-nitrocatechol: Y108 (= Y119), H147 (≠ Y156), W149 (≠ G158), R157 (vs. gap), H160 (= H162), H162 (= H164)
binding fe (iii) ion: Y108 (= Y119), H160 (= H162), H162 (= H164)

Sites not aligning to the query:

binding 4-nitrocatechol: 24, 191

3lktM Tyrosine 447 of protocatechuate 3,4-dioxygenase controls efficient progress through catalysis
37% identity, 57% coverage: 57:185/225 of query aligns to 45:184/238 of 3lktM

query
sites
3lktM

Q

E

T

T

E

T

G

G

P

P

Y

N

Y

F

P

S

V

H

R

L

F

G

P

F

S

G

D

A

S

H

D

D

G

H

D

D

L

L

-

L

-

N

-

F

R

N

N

N

G

G

L

G

M

L

R

P

Y

I

V

-

D

-

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H

R

H

H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y

H

T

P

G

W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-

R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

binding fe (iii) ion: Y108 (= Y119), H160 (= H162), H162 (= H164)

3mv4M Axial ligand swapping in double mutant maintains intradiol-cleavage chemistry in protocatechuate 3,4-dioxygenase
39% identity, 44% coverage: 86:185/225 of query aligns to 75:184/238 of 3mv4M

query
sites
3mv4M

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H

R

H

H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
x
H

T

P

G

W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
x
Y

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

binding carbonate ion: Y108 (= Y119), H147 (≠ Y156), R157 (vs. gap), Y162 (≠ H164)
binding fe (iii) ion: Y108 (= Y119), H147 (≠ Y156), H160 (= H162), Y162 (≠ H164)

3mi5M Axial ligand swapping in double mutant maintains intradiol-cleavage chemistry in protocatechuate 3,4-dioxygenase
39% identity, 44% coverage: 86:185/225 of query aligns to 75:184/238 of 3mi5M

query
sites
3mi5M

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H

R

H

H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
x
H

T

P

G
x
W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
x
Y

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

binding catechol: Y108 (= Y119), H147 (≠ Y156), W149 (≠ G158), R157 (vs. gap), H160 (= H162), Y162 (≠ H164)
binding fe (iii) ion: Y108 (= Y119), H160 (= H162), Y162 (≠ H164)

3mflM Axial ligand swapping in double mutant maintains intradiol-cleavage chemistry in protocatechuate 3,4-dioxygenase
39% identity, 44% coverage: 86:185/225 of query aligns to 75:184/238 of 3mflM

query
sites
3mflM

G

G

Q

E

P

R

V

I

W

I

V

V

E

A

G

G

R

R

V

V

T

V

D

D

M

Q

Q

Y

G

G

V

K

P

P

L

V

A

P

G

N

G

T

T

L

V

V

E

E

I

M

W

W

Q

Q

C

A

D

N

A

A

D

G

G

G

H

R

Y
|
Y

H

R

H

H

P

K

G

N

D

D

G

R

N

Y

K

L

A

A

-

P

-

L

A

D

P

P

A

N

F

F

Q

G

G

G

F

V

G

G

R

R

V

C

V

L

L

T

G

D

R

S

D

D

G

G

R

Y

Y

Y

R

S

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
x
H

T

P

G
x
W

R

R

T

N

-

G

-

P

-

N

-

D

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
x
Y

F

F

K

G

V

I

R

S

L

G

P

P

D

S

-

I

R

A

E

T

L

K

L

L

T

I

T

T

Q

Q

M

L

Y

Y

V

F

A

E

G

G

N

D

P

P

binding 2-(3,4-dihydroxyphenyl)acetic acid: Y108 (= Y119), H147 (≠ Y156), W149 (≠ G158), R157 (vs. gap), H160 (= H162), Y162 (≠ H164)
binding fe (iii) ion: Y108 (= Y119), H160 (= H162), Y162 (≠ H164)

5vxtB Crystal structure of catechol 1,2-dioxygenase from burkholderia ambifaria
30% identity, 72% coverage: 54:214/225 of query aligns to 103:273/312 of 5vxtB

query
sites
5vxtB

T

T

P

P

R

R

Q

T

T

I

E

E

G

G

P
|
P

Y
x
L

Y

Y

P

V

V

A

R

G

F

A

P

P

S

-

D

-

S

-

D

-

G

-

D

-

L

-

L

V

R

R

N

D

G

G

L

V

M

A

R

K

Y

I

-

D

V

L

D

D

G

A

Q

D

-

E

-

G

-

A

-

G

P

P

V

L

W

V

V

I

E

H

G

G

R

T

V

V

T

T

D

G

M

L

Q

D

G

G

V

K

P

P

L

V

A

A

G

G

G

A

T

L

V

V

E

E

I

C

W

W

Q

H

C

A

D

N

A

S

D

H

G

G

H

F

Y
|
Y

H

S

H

H

P

F

G

D

D

P

G

T

N

G

K

K

A

Q

A

S

P

D

A

-

F

F

Q

N

G

L

F

R

G

G

R

A

V

V

V

K

L

T

G

G

R

A

D

D

G

G

R

K

Y

Y

R

E

F

F

R

R

T

T

I

L

R

M

P

P

A

V

P

G

Y
|
Y

-

G

-

C

-

P

-

Q

-

G

-

A

-

T

-

Q

-

L

-

D

-

R

-

L

-

G

-

R

-

H

T

G

G

N

R
|
R

T

P

P

A

H
|
H

I

V

H
|
H

F

F

K

F

V

V

R

T

L

S

P

D

D

G

R

H

E

R

L

K

L

L

T

T

Q

Q

M

F

Y

N

V

I

A

E

G

G

N

D

P

P

G

-

N

-

T

-

S

-

D

-

F

L

L

I

W

W

S

D

R

D

L

F

S

A

A

Y

A

A

E

T

R

R

A

E

L

L

T

I

V

P

P

P

F

V

A

T

P

A

S

K

A

A

D

G

G

G

active site: Y166 (= Y119), Y202 (= Y156), R223 (= R159), H226 (= H162), H228 (= H164)
binding catechol: P110 (= P61), L111 (≠ Y62), Y166 (= Y119), Y202 (= Y156), R223 (= R159), H228 (= H164)
binding fe (iii) ion: Y166 (= Y119), H226 (= H162), H228 (= H164)

2buqB Crystal structure of wild-type protocatechuate 3,4-dioxygenase from acinetobacter sp. Adp1 in complex with catechol (see paper)
34% identity, 60% coverage: 50:184/225 of query aligns to 36:181/238 of 2buqB

query
sites
2buqB

A

S

L

I

T

A

P

E

T

T

P

L

R

S

Q

E

T

V

E

T

G

A

P

P

Y

H

Y

F

P

S

V

A

R

D

F

K

P

F

S

G

D

P

S

K

D

D

G

N

D

D

L

L

L

I

R

L

N

N

G

Y

L

A

M

K

R

-

Y

-

V

-

D

D

G

G

Q

L

P

P

-

I

-

G

-

E

-

R

V

V

W

I

V

V

E

H

G

G

R

Y

V

V

T

R

D

D

M

Q

Q

F

G

G

V

R

P

P

L

V

A

K

G

N

G

A

T

L

V

V

E

E

I

V

W

W

Q

Q

C

A

D

N

A

A

D

S

G

G

H

R

Y
|
Y

H

R

H

H

P

P

G

N

D

D

G

Q

N

Y

K

I

A

G

A

A

-

M

-

D

P

P

A

N

F

F

Q

G

G

G

F

C

G

G

R

R

V

M

V

L

L

T

G

D

R

D

D

N

G

G

R

Y

Y

Y

R

V

F

F

R

R

T

T

I

I

R

K

P

P

A

G

P

P

Y
|
Y

T

P

G

W

R

R

T

N

-

R

-

I

-

N

-

E

-

W

-
x
R

-

P

P

A

H
|
H

I

I

H
|
H

F

F

K

S

V

L

R

-

L

I

P

A

D

D

-

G

-

W

R

A

E

Q

L

R

L

L

T

I

T

S

Q

Q

M

F

Y

Y

V

F

A

E

G

G

N

D

active site: Y106 (= Y119), Y145 (= Y156), R155 (vs. gap), H158 (= H162), H160 (= H164)
binding catechol: Y106 (= Y119), R155 (vs. gap), H158 (= H162)
binding fe (iii) ion: Y106 (= Y119), H158 (= H162), H160 (= H164)

Query Sequence

>Ac3H11_545 FitnessBrowser__acidovorax_3H11:Ac3H11_545
MPVHTGSTPSSPRPAPAAVPTRRRLLRQGLWGSALVVAPALVPAALAQGALTPTPRQTEG
PYYPVRFPSDSDGDLLRNGLMRYVDGQPVWVEGRVTDMQGVPLAGGTVEIWQCDADGHYH
HPGDGNKAAPAFQGFGRVVLGRDGRYRFRTIRPAPYTGRTPHIHFKVRLPDRELLTTQMY
VAGNPGNTSDFLWSRLSAAERAALTVPFAPSADGVRAEFALVVQA

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