SitesBLAST

4i3pA 1.96 angstrom x-ray crystal structure of 3-hydroxyanthranilate-3,4- dioxygenase bound with 3-aminosalicylic acid from cupriavidus metallidurans
52% identity, 95% coverage: 6:170/173 of query aligns to 7:173/174 of 4i3pA

query
sites
4i3pA

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binding 3-amino-2-hydroxybenzoic acid: R47 (= R45), E57 (= E55), P97 (= P95), R99 (= R97), V108 (= V105), E110 (= E107)
binding fe (ii) ion: H51 (= H49), E57 (= E55), H95 (= H93), C125 (= C122), C128 (= C125), C162 (= C159), C165 (= C162)

4hvoA 1.75 angstrom x-ray crystal structure of cufe reconstituted 3- hydroxyanthranilate-3,4-dioxygenase from cupriavidus metallidurans (see paper)
52% identity, 95% coverage: 6:170/173 of query aligns to 7:173/174 of 4hvoA

query
sites
4hvoA

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binding copper (ii) ion: H51 (= H49), E57 (= E55), H95 (= H93)
binding fe (ii) ion: C125 (= C122), C128 (= C125), C162 (= C159), C165 (= C162)

4hsjA 1.88 angstrom x-ray crystal structure of piconlinic-bound 3- hydroxyanthranilate-3,4-dioxygenase (see paper)
52% identity, 95% coverage: 6:170/173 of query aligns to 7:173/174 of 4hsjA

query
sites
4hsjA

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binding pyridine-2-carboxylic acid: H51 (= H49), E57 (= E55), F59 (= F57), H95 (= H93), P97 (= P95), E110 (= E107)
binding fe (ii) ion: H51 (= H49), E57 (= E55), H95 (= H93), C125 (= C122), C128 (= C125), C162 (= C159), C165 (= C162)

1yfxA Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from ralstonia metallidurans complexed with 4-chloro-3-hydroxyanthranilic acid and no (see paper)
52% identity, 95% coverage: 6:170/173 of query aligns to 7:173/174 of 1yfxA

query
sites
1yfxA

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binding 4-chloro-3-hydroxyanthranilic acid: V25 (= V24), R47 (= R45), H51 (= H49), E57 (= E55), F59 (= F57), P97 (= P95), R99 (= R97), E110 (= E107), I142 (= I139)
binding fe (iii) ion: H51 (= H49), E57 (= E55), H95 (= H93), C125 (= C122), C128 (= C125), C162 (= C159), C165 (= C162)
binding nitric oxide: R47 (= R45), H51 (= H49), H95 (= H93), P97 (= P95)

1yfwA Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from ralstonia metallidurans complexed with 4-chloro-3-hydroxyanthranilic acid and o2 (see paper)
52% identity, 95% coverage: 6:170/173 of query aligns to 7:173/174 of 1yfwA

query
sites
1yfwA

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binding 4-chloro-3-hydroxyanthranilic acid: V25 (= V24), H51 (= H49), E57 (= E55), F59 (= F57), P97 (= P95), R99 (= R97), E110 (= E107), I142 (= I139), L146 (≠ F143)
binding fe (iii) ion: H51 (= H49), E57 (= E55), H95 (= H93), C125 (= C122), C128 (= C125), C162 (= C159), C165 (= C162)
binding oxygen molecule: R47 (= R45), H51 (= H49), H95 (= H93), P97 (= P95)

Q1LCS4 3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilate oxygenase; 3-HAO; 3-hydroxyanthranilic acid dioxygenase; HAD; EC 1.13.11.6 from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) (see paper)
52% identity, 95% coverage: 6:170/173 of query aligns to 7:173/174 of Q1LCS4

query
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Q1LCS4

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R47 (= R45) mutation to A: Increases KM for 3-hydroxyanthranilate 7-fold. Decreases activity 1000-fold.
R99 (= R97) mutation to A: Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold.
E110 (= E107) mutation to A: Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold.

6viaA Observing a ring-cleaving dioxygenase in action through a crystalline lens - a seven-membered lactone bound structure (see paper)
52% identity, 95% coverage: 6:170/173 of query aligns to 9:175/176 of 6viaA

query
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6viaA

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E

R

S

F

F

Y

Y

R

A

S

S

L

E

E

D

A

K

R

R

T

R

C
|
C

T

P

Q

H

C
|
C

G

G

T

Q

V

V

H

H

P

P

A

G

P

R

A

A

binding (2R,3E)-2-hydroxy-3-imino-2,3-dihydrooxepine-4-carboxylic acid: V43 (= V39), H53 (= H49), E59 (= E55), F61 (= F57), P99 (= P95), R101 (= R97), E112 (= E107)
binding fe (iii) ion: H53 (= H49), E59 (= E55), H97 (= H93)
binding fe (ii) ion: C127 (= C122), C130 (= C125), C164 (= C159), C167 (= C162)

6vi8A Observing a ring-cleaving dioxygenase in action through a crystalline lens - a superoxo bound structure (see paper)
52% identity, 95% coverage: 6:170/173 of query aligns to 9:175/176 of 6vi8A

query
sites
6vi8A

P

P

L

F

D

N

L

F

Q

P

R

R

W

W

I

I

D

D

E

E

H

H

R

A

H

H

L

L

K

K

P

P

V

V

G

G

N

N

K

R

C

Q

I

V

V

W

-

Q

D

D

G

S

D

D

F

F

I

I

V

V

M

T

I

V

V

V

G

G

P

P

N

N

A

H

R

R

T

T

D

D

Y

Y

H
|
H

Y

D

D

D

E

P

G

L

P

E

E
|
E

F

F

F
|
F

Y

Y

Q

Q

L

L

E

R

G

G

E

N

M

A

V

Y

L

L

K

N

V

L

Q

W

D

V

D

D

G

G

A

R

R

E

D

R

I

A

P

D

I

L

R

K

A

E

G

G

Q

D

M

I

F

F

Y

L

L

L

P

P

R

H

V

V

P

R

H
|
H

S

S

P
|
P

Q

Q

R
|
R

-

P

M

E

P

A

D

G

S

S

I

A

G

C

L

L

V

V

I

I

E
|
E

R

R

R

Q

R

R

L

P

A

A

G

G

E

M

Q

L

D

D

G

G

L

F

M

E

W

W

F

Y

C
|
C

Q

D

Q

A

C
|
C

N

G

H

H

K

L

L

V

Y

H

E

R

E

V

Y

E

F

V

T

Q

L

L

D

K

S

S

I

I

E

V

R

T

D

D

F

L

P

P

V

L

F

F

E

E

R

S

F

F

Y

Y

R

A

S

S

L

E

E

D

A

K

R

R

T

R

C
|
C

T

P

Q

H

C
|
C

G

G

T

Q

V

V

H

H

P

P

A

G

P

R

A

A

binding 3-hydroxyanthranilic acid: H53 (= H49), E59 (= E55), F61 (= F57), P99 (= P95), R101 (= R97), E112 (= E107)
binding fe (iii) ion: H53 (= H49), E59 (= E55), H97 (= H93)
binding fe (ii) ion: C127 (= C122), C130 (= C125), C164 (= C159), C167 (= C162)
binding oxygen atom: H53 (= H49), H97 (= H93)

6vi9A Observing a ring-cleaving dioxygenase in action through a crystalline lens - an alkylperoxo bound structure (see paper)
52% identity, 94% coverage: 6:168/173 of query aligns to 7:171/171 of 6vi9A

query
sites
6vi9A

P

P

L

F

D

N

L

F

Q

P

R

R

W

W

I

I

D

D

E

E

H

H

R

A

H

H

L

L

K

K

P

P

V

V

G

G

N

N

K

R

C

Q

I

V

V

W

-

Q

D

D

G

S

D

D

F

F

I

I

V

V

M

T

I

V

V

V

G

G

P

P

N

N

A

H

R
|
R

T

T

D

D

Y

Y

H
|
H

Y

D

D

D

E

P

G

L

P

E

E
|
E

F

F

F
|
F

Y

Y

Q

Q

L

L

E

R

G

G

E

N

M

A

V

Y

L

L

K

N

V

L

Q

W

D

V

D

D

G

G

A

R

R

E

D

R

I

A

P

D

I

L

R

K

A

E

G

G

Q

D

M

I

F

F

Y

L

L

L

P

P

R

H

V

V

P

R

H
|
H

S

S

P
|
P

Q

Q

R
|
R

-

P

M

E

P

A

D

G

S

S

I

A

G

C

L

L

V

V

I

I

E
|
E

R

R

R

Q

R

R

L

P

A

A

G

G

E

M

Q

L

D

D

G

G

L

F

M

E

W

W

F

Y

C
|
C

Q

D

Q

A

C
|
C

N

G

H

H

K

L

L

V

Y

H

E

R

E

V

Y

E

F

V

T

Q

L

L

D

K

S

S

I

I

E

V

R

T

D

D

F

L

P

P

V

L

F

F

E

E

R

S

F

F

Y

Y

R

A

S

S

L

E

E

D

A

K

R

R

T

R

C
|
C

T

P

Q

H

C
|
C

G

G

T

Q

V

V

H

H

P

P

A

G

binding fe (ii) ion: C125 (= C122), C128 (= C125), C162 (= C159), C165 (= C162)
binding (5R,6Z)-5-(hydroperoxy-kappaO)-5-(hydroxy-kappaO)-6-iminocyclohexa-1,3-diene-1-carboxylato(2-)iron: R47 (= R45), H51 (= H49), E57 (= E55), F59 (= F57), H95 (= H93), P97 (= P95), R99 (= R97), E110 (= E107)

4wzcA Understanding extradiol dioxygenase mechanism in NAD+ biosynthesis by viewing catalytic intermediates - 2,3-cis-4,5-trans acms bound to i142a mutant hao
51% identity, 95% coverage: 6:170/173 of query aligns to 7:173/174 of 4wzcA

query
sites
4wzcA

P

P

L

F

D

N

L

F

Q

P

R

R

W

W

I

I

D

D

E

E

H

H

R

A

H

H

L

L

K

K

P

P

V

V

G

G

N

N

K

R

C

Q

I

V

V

W

-

Q

D

D

G

S

D

D

F

F

I

I

V

V

M

T

I

V

V

V

G

G

P

P

N

N

A

H

R
|
R

T

T

D

D

Y

Y

H
|
H

Y

D

D

D

E

P

G

L

P

E

E
|
E

F

F

Y

Y

Q

Q

L

L

E

R

G

G

E

N

M

A

V

Y

L

L

K

N

V

L

Q

W

D

V

D

D

G

G

A

R

R

E

D

R

I

A

P

D

I

L

R

K

A

E

G

G

Q

D

M

I

F

F

Y

L

L

L

P

P

R

H

V

V

P

R

H
|
H

S

S

P
|
P

Q

Q

R
|
R

-

P

M

E

P

A

D

G

S

S

I

A

G

C

L

L

V

V

I

I

E
|
E

R

R

R

Q

R

R

L

P

A

A

G

G

E

M

Q

L

D

D

G

G

L

F

M

E

W

W

F

Y

C
|
C

Q

D

Q

A

C
|
C

N

G

H

H

K

L

L

V

Y

H

E

R

E

V

Y

E

F

V

T

Q

L

L

D

K

S

S

I

A

E

V

R

T

D

D

F

L

P

P

V

L

F

F

E

E

R

S

F

F

Y

Y

R

A

S

S

L

E

E

D

A

K

R

R

T

R

C
|
C

T

P

Q

H

C
|
C

G

G

T

Q

V

V

H

H

P

P

A

G

P

R

A

A

binding (2E)-2-amino-3-[(1E)-3-oxoprop-1-en-1-yl]but-2-enedioic acid: R47 (= R45), H51 (= H49), E57 (= E55), H95 (= H93), P97 (= P95), R99 (= R97), E110 (= E107)
binding fe (ii) ion: H51 (= H49), E57 (= E55), H95 (= H93), C125 (= C122), C128 (= C125), C162 (= C159), C165 (= C162)

Q83V26 3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilate oxygenase; 3-HAO; 3-hydroxyanthranilic acid dioxygenase; HAD; EC 1.13.11.6 from Pseudomonas fluorescens (see paper)
49% identity, 95% coverage: 6:170/173 of query aligns to 8:174/185 of Q83V26

query
sites
Q83V26

P

P

L

L

D

N

L

F

Q

Q

R

R

W

W

I

L

D

D

E

D

H

H

R

S

H

D

L

L

K

R

P

P

V

V

G

G

N

N

K

Q

C

Q

I

V

V

W

-

Q

D

D

G

S

D

D

F

F

I

I

V

V

M

T

I

V

V

V

G

G

P

P

N

N

A

F

R

R

T

T

D

D

Y

F

H
|
H

Y

D

D

D

E

P

G

M

P

E

E

E

F

F

Y

Y

Q

Q

L

F

E

K

G

G

E

N

M

A

V

Y

L

L

K

N

V

I

Q

M

D

D

D

R

G

G

A

Q

A

M

R

D

D

R

I

V

P

E

I

L

R

K

A

E

G

G

Q

D

M

I

F

F

Y

L

L

L

P

P

R

H

V

L

P

R

H
|
H

S

S

P

P

Q

Q

R

R

-

P

M

E

P

A

D

G

S

S

I

R

G

C

L

L

V

V

I

I

E

E

R

R

R

Q

R

R

L

P

A

K

G

G

E

M

Q

L

D

D

G

G

L

F

M

E

W

W

F

Y

C

C

Q

L

Q

S

C

C

N

N

H

G

K

L

L

V

Y

Y

E

R

E

V

Y

D

F

V

T

Q

L

L

D

N

S

S

I

I

E

V

R

T

D

D

F

L

P

P

V

L

F

F

E

D

R

I

F

F

Y

Y

R

G

S

N

L

V

E

G

A

L

R

R

T

K

C

C

T

P

Q

Q

C

C

G

G

T

Q

V

V

H

H

P

P

A

G

P

K

A

A

H52 (= H49) mutation to A: Loss of activity.
H96 (= H93) mutation to A: Loss of activity.

5tkqA Crystal structure of human 3hao with zinc bound in the active site (see paper)
45% identity, 88% coverage: 7:158/173 of query aligns to 3:154/283 of 5tkqA

query
sites
5tkqA

L

L

D

G

L

V

Q

R

R

A

W

W

I

V

D

K

E

E

H

N

R

R

H

G

L

S

L

F

K

Q

P

P

V

V

G

C

N

N

K

K

C

L

I

M

V

H

D

Q

G

E

D

Q

F

L

I

K

V

V

M

M

I

F

V

I

G

G

P

P

N

N

A

T

R

R

T

K

D

D

Y

Y

H
|
H

Y

I

D

E

E

E

G

G

P

E

E
|
E

F

V

F

F

Y

Y

Q

Q

L

L

E

E

G

G

E

D

M

M

V

V

L

L

K

R

V

V

Q

L

D

E

D

Q

G

G

A

K

A

H

R

R

D

D

I

V

P

V

I

I

R

R

A

Q

G

G

Q

E

M

I

F

F

Y

L

L

L

P

P

P

A

R

R

V

V

P

P

H
|
H

S

S

P

P

Q

Q

R

R

M

F

P

A

D

N

S

T

I

V

G

G

L

L

V

V

I

V

E

E

R

R

L

L

A

E

G

T

E

E

Q

L

D

D

G

G

L

L

M

R

W

Y

F

Y

C

V

Q

G

Q

D

C

T

N

M

H

D

K

V

L

L

Y

F

E

E

E

K

Y

W

F

F

T

Y

L

C

D

K

S

D

I

L

E

G

R

T

D

Q

F

L

P

A

P

P

V

I

F

I

E

Q

R

E

F

F

Y

F

R

S

S

S

L

E

E

Q

A

Y

R

R

T

T

binding zinc ion: H45 (= H49), E51 (= E55), H89 (= H93)

5tk5A Crystal structure of human 3hao with iron bound in the active site (see paper)
45% identity, 88% coverage: 7:158/173 of query aligns to 3:154/283 of 5tk5A

query
sites
5tk5A

L

L

D

G

L

V

Q

R

R

A

W

W

I

V

D

K

E

E

H

N

R

R

H

G

L

S

L

F

K

Q

P

P

V

V

G

C

N

N

K

K

C

L

I

M

V

H

D

Q

G

E

D

Q

F

L

I

K

V

V

M

M

I

F

V

I

G

G

P

P

N

N

A

T

R

R

T

K

D

D

Y

Y

H
|
H

Y

I

D

E

E

E

G

G

P

E

E
|
E

F

V

F

F

Y

Y

Q

Q

L

L

E

E

G

G

E

D

M

M

V

V

L

L

K

R

V

V

Q

L

D

E

D

Q

G

G

A

K

A

H

R

R

D

D

I

V

P

V

I

I

R

R

A

Q

G

G

Q

E

M

I

F

F

Y

L

L

L

P

P

P

A

R

R

V

V

P

P

H
|
H

S

S

P

P

Q

Q

R

R

M

F

P

A

D

N

S

T

I

V

G

G

L

L

V

V

I

V

E

E

R

R

L

L

A

E

G

T

E

E

Q

L

D

D

G

G

L

L

M

R

W

Y

F

Y

C

V

Q

G

Q

D

C

T

N

M

H

D

K

V

L

L

Y

F

E

E

E

K

Y

W

F

F

T

Y

L

C

D

K

S

D

I

L

E

G

R

T

D

Q

F

L

P

A

P

P

V

I

F

I

E

Q

R

E

F

F

Y

F

R

S

S

S

L

E

E

Q

A

Y

R

R

T

T

binding fe (iii) ion: H45 (= H49), E51 (= E55), H89 (= H93)

P46952 3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilate oxygenase; 3-HAO; h3HAO; 3-hydroxyanthranilic acid dioxygenase; HAD; EC 1.13.11.6 from Homo sapiens (Human) (see 3 papers)
45% identity, 88% coverage: 7:158/173 of query aligns to 5:156/286 of P46952

query
sites
P46952

L

L

D

G

L

V

Q

R

R

A

W

W

I

V

D

K

E

E

H

N

R

R

H

G

L

S

L

F

K

Q

P

P

V

V

G

C

N

N

K

K

C

L

I

M

V

H

D

Q

G

E

D

Q

F

L

I

K

V

V

M

M

I

F

V
x
I

G

G

P

P

N

N

A

T

R

R

T

K

D

D

Y

Y

H
|
H

Y

I

D

E

E

E

G

G

P

E

E
|
E

F

V

F

F

Y

Y

Q

Q

L

L

E

E

G

G

E

D

M

M

V

V

L

L

K

R

V

V

Q

L

D

E

D

Q

G

G

A

K

A

H

R

R

D

D

I

V

P

V

I

I

R

R

A

Q

G

G

Q

E

M

I

F

F

Y

L

L

L

P

P

P

A

R

R

V

V

P

P

H
|
H

S

S

P

P

Q

Q

R

R

M

F

P

A

D

N

S

T

I

V

G

G

L

L

V

V

I

V

E

E

R

R

L

L

A

E

G

T

E

E

Q

L

D

D

G

G

L

L

M

R

W

Y

F

Y

C

V

Q

G

Q

D

C

T

N

M

H

D

K

V

L

L

Y

F

E

E

E

K

Y

W

F

F

T

Y

L

C

D

K

S

D

I

L

E

G

R

T

D

Q

F

L

P

A

P

P

V

I

F

I

E

Q

R

E

F

F

Y

F

R

S

S

S

L

E

E

Q

A

Y

R

R

T

T

I37 (≠ V39) to V: in dbSNP:rs3816183
H47 (= H49) binding
E53 (= E55) binding
H91 (= H93) binding

Sites not aligning to the query:

162:286 natural variant: Missing (in VCRL1; strongly reduced 3-hydroxyanthranilate 3,4-dioxygenase activity in vitro)
186:286 natural variant: Missing (in VCRL1; strongly reduced 3-hydroxyanthranilate 3,4-dioxygenase activity in vitro)

3fe5A Crystal structure of 3-hydroxyanthranilate 3,4-dioxygenase from bovine kidney (see paper)
44% identity, 88% coverage: 6:158/173 of query aligns to 3:155/283 of 3fe5A

query
sites
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binding fe (iii) ion: H46 (= H49), E52 (= E55), H90 (= H93)

Query Sequence

>N515DRAFT_2922 FitnessBrowser__Dyella79:N515DRAFT_2922
MALPPPLDLQRWIDEHRHLLKPPVGNKCIVDGDFIVMIVGGPNARTDYHYDEGPEFFYQL
EGEMVLKVQDDGAARDIPIRAGQMFYLPPRVPHSPQRMPDSIGLVIERRRLAGEQDGLMW
FCQQCNHKLYEEYFTLDSIERDFPPVFERFYRSLEARTCTQCGTVHPAPAKYA

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