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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 M0052 and M0050

These two reactions have a combined similarity of 0.16


M0052

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Comparison

M0050

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EC 4.1.2.13
fructose-bisphosphate aldolase (Class II)
Sub-SubClass EC 4.1.1.23
orotidine-5'-phosphate decarboxylase

Image of D-glyceraldehyde 3-phosphate

Image of glycerone phosphate

right arrow

Image of D-fructosefuranose 1,6-bisphosphate

D-glyceraldehyde 3-phosphate
C00118
CHEBI:59776
glycerone phosphate
C00111
CHEBI:57642
D-fructosefuranose 1,6-bisphosphate
C00354
CHEBI:49299
0

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

Catalytic CATH Codes

3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.31267

Active Site



Catalytic Residues

Type Number Chain Location of Function
Asp 109 A Side Chain
Glu 182 A Side Chain
Asn 286 A Side Chain
0.3333

Catalytic Residues

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

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
zinc ZN 360 A
sodium NA 364 A

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 4 steps

0.1282

Reaction occurs across 2 steps

Step 1
GIF of Reaction Step M0052.stg01

Glu182 deprotonates the C1 carbon of the substrate, which initiates double bond rearrangement to form the enol-intermediate.
0 Step 1
GIF of Reaction Step M0050.stg01

The substrate undergoes decarboxylation. The substrate concomitantly deprotonates Lys62 forming UMP.
Step 2
GIF of Reaction Step M0052.stg02

The oxyanion collapses, initiating nucleophilic addition of the intermediate to the glyceraldehyde-3-phosphate at the carbonyl carbon. The oxyanion formed deprotonates Asp109.
0.14 Step 2
GIF of Reaction Step M0050.stg02

Lys62 deprotonates water.
Step 3
GIF of Reaction Step M0052.stg03

Asp109 deprotonates water which deprotonates Glu182 in an inferred step.
N/A Step 3
No Step with this number present
Step 4
GIF of Reaction Step M0052.stg04

The sugar cyclises outside the enzyme active site.
N/A Step 4
No Step with this number present

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