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The two reactions compared are done so using a Tanimoto similarity score (for more information, please see the MACiE FAQ) for the bond changes only. The score maay range from 0 to 1 where 1 indicates that the two reactions are identical at the bond change level and 0 indicates that there are no bond changes in common.


Key

1.0-0.9 0.9-0.8 0.8-0.7 0.7-0.6 0.6-0.5 0.5-0.4 0.4-0.3 0.3-0.2 0.2-0.1 0.1-0.0 =0

Results for Comparison of M0050 and M0054

These two reactions have a combined similarity of 0.07


M0050

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Comparison

M0054

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EC 4.1.1.23
orotidine-5'-phosphate decarboxylase
Sub-Class EC 4.2.1.10
3-dehydroquinate dehydratase (type I)

Image of orotidine 5'-phosphate

Image of proton

right arrow

Image of carbon dioxide

Image of UMP

orotidine 5'-phosphate
C01103
CHEBI:57538
proton
C00080
CHEBI:24636
carbon dioxide
C00011
CHEBI:16526
UMP
C00105
CHEBI:57865
0

Image of 3-dehydroquinic acid

right arrow

Image of 3-dehydroshikimate

Image of water

3-dehydroquinic acid
C00944
CHEBI:17947
3-dehydroshikimate
C02637
CHEBI:30918
water
C00001
CHEBI:15377

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.12852

Active Site



Catalytic Residues

Type Number Chain Location of Function
Asp 60 A Side Chain
Lys 62 A Side Chain
Asp 65 B Side Chain
0.1428

Catalytic Residues

Type Number Chain Location of Function
Glu 86 A Side Chain
His 143 A Side Chain
Lys 170 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

No Associated Metal Cofactors

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 2 steps

0.0597

Reaction occurs across 9 steps

Step 1
GIF of Reaction Step M0050.stg01

The substrate undergoes decarboxylation. The substrate concomitantly deprotonates Lys62 forming UMP.
0.2 Step 1
GIF of Reaction Step M0054.stg01

Glu86 deprotonates His143, which deprotonates Lys170, activating it.
Step 2
GIF of Reaction Step M0050.stg02

Lys62 deprotonates water.
0 Step 2
GIF of Reaction Step M0054.stg02

Lys170 attacks the carbonyl carbon of the substrate in a nucleophilic addition.
Step 3
No Step with this number present
N/A Step 3
GIF of Reaction Step M0054.stg03

A proton is transferred from the covalently attached lysine to the newly formed hydroxide.
Step 4
No Step with this number present
N/A Step 4
GIF of Reaction Step M0054.stg04

Lys170 initiates an elimination of water (which obtains its proton from His143, which deprotonates Glu86) forming the Schiff base intermediate.
Step 5
No Step with this number present
N/A Step 5
GIF of Reaction Step M0054.stg05

Glu86 deprotonates His143, which deprotonates the intermediate at the carbon adjacent to the covalently bound lysine which acts as an electron sink.
Step 6
No Step with this number present
N/A Step 6
GIF of Reaction Step M0054.stg06

Lys170 donates its lone pair of electrons back into the ring, initiating a double bond rearrangement and elimination of water, which obtains its proton from His143, which deprotonates Glu86.
Step 7
No Step with this number present
N/A Step 7
GIF of Reaction Step M0054.stg07

Glu86 deprotonates His143, which deprotonates water, which then attacks the carbon to which Lys170 is covalently attached.
Step 8
No Step with this number present
N/A Step 8
GIF of Reaction Step M0054.stg08

Lys170 deprotonates the hydroxide, which causes Lys170 to be eliminated and the product to be formed.
Step 9
No Step with this number present
N/A Step 9
GIF of Reaction Step M0054.stg09

Lys170 deprotonates His143, which deprotonates Glu86 in an inferred step that returns the enzyme to its starting state.

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