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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 M0111 and M0052

These two reactions have a combined similarity of 0.27


M0111

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Comparison

M0052

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EC 1.4.7.1
glutamate synthase (ferredoxin)
Class EC 4.1.2.13
fructose-bisphosphate aldolase (Class II)

Image of L-glutamine

Image of proton

Image of reduced ferredoxin

Image of 2-oxoglutarate

right arrow

Image of oxidised ferredoxin

Image of L-glutamate

L-glutamine
C00064
CHEBI:58359
2 proton
C00080
CHEBI:24636
2 reduced ferredoxin
C00138
CHEBI:17513
2-oxoglutarate
C00026
CHEBI:16810
2 oxidised ferredoxin
C00139
CHEBI:17908
2 L-glutamate
C00025
CHEBI:29985
0.03

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

Catalytic CATH Codes

3.60.20.10
3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.15794

Active Site



Catalytic Residues

Type Number Chain Location of Function
Cys 1 A Main Chain N Terminus
Side Chain
Arg 31 A Main Chain Carbonyl
Phe 207 A Main Chain Amide
Asn 227 A Side Chain
Gly 228 A Main Chain Amide
Glu 903 A Side Chain
Gln 969 A Side Chain
Lys 972 A Side Chain
Gln 978 A Main Chain Amide
0.1666

Catalytic Residues

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

Organic Cofactors

Type Identity Chain
FMN FMN 2508 A

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
iron F3S 2509 A

Metal Cofactors

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

Reaction occurs across 10 steps

0.3576

Reaction occurs across 4 steps

Step 1
GIF of Reaction Step M0111.stg01

The N-terminus of Cys1 deprotonates deprotonates water, which deprotonates the thiol group of Cys1, initiating a nucleophilic attack on the amide carbon in an addition reaction.
0.25 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.
Step 2
GIF of Reaction Step M0111.stg02

The oxyanion initiates an elimination that cleaves ammonia from the bound L-glutamine substrate. Ammonia deprotonates water, which deprotonates the N-terminus of Cys1.
0.33 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.
Step 3
GIF of Reaction Step M0111.stg03

The N-terminus of Cys1 deprotonates water, which deprotonates another water that initiates a nucleophilic attack on the carbonyl carbon of the covalently bound intermediate in an addition reaction.
0.6 Step 3
GIF of Reaction Step M0052.stg03

Asp109 deprotonates water which deprotonates Glu182 in an inferred step.
Step 4
GIF of Reaction Step M0111.stg04

The oxyanion initiates an elimination that cleaves the C-S bond, the thiolate of Cys1 deprotonates water, which deprotonates the N-terminus of Cys1
0 Step 4
GIF of Reaction Step M0052.stg04

The sugar cyclises outside the enzyme active site.
Step 5
GIF of Reaction Step M0111.stg05

Ammonia initiates a nucleophilic attack on the C2 carbonyl carbon of the 2-oxoglutarate substrate in an addition reaction. The oxyanion formed deprotonates the bound ammonium.
N/A Step 5
No Step with this number present
Step 6
GIF of Reaction Step M0111.stg06

The amine initiates an elimination of the bound hydroxide as water, which deprotonates Lys972.
N/A Step 6
No Step with this number present
Step 7
GIF of Reaction Step M0111.stg07

FMN eliminates a hydride ion, which adds to the C2 imine carbon in an addition reaction.
N/A Step 7
No Step with this number present
Step 8
GIF of Reaction Step M0111.stg08

Lys972 deprotonates water in an inferred step.
N/A Step 8
No Step with this number present
Step 9
GIF of Reaction Step M0111.stg09

Ferredoxin donates a single electron, which is transferred to FMN through an iron-sulfur cluster. FMN deprotonates water.
N/A Step 9
No Step with this number present
Step 10
GIF of Reaction Step M0111.stg10

A second ferredoxin donates a single electron, which is transferred to FMN through an iron-sulfur cluster, which regenerates the reduced form of FMN.
N/A Step 10
No Step with this number present

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