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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 M0267

These two reactions have a combined similarity of 0.39


M0111

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Comparison

M0267

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EC 1.4.7.1
glutamate synthase (ferredoxin)
Class EC 4.2.1.52
dihydrodipicolinate synthase

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

Image of L-aspartate beta semi aldehyde (hydrate)

Image of Pyruvate

right arrow

Image of (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid

Image of water

L-aspartate beta semi aldehyde (hydrate)
X00125
Pyruvate
C00022
CHEBI:15361
(4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid
X00126
2 water
C00001
CHEBI:15377

Catalytic CATH Codes

3.60.20.10
3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.07851

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
0.0769

Catalytic Residues

Type Number Chain Location of Function
Lys 161 A Side Chain
Tyr 133 A Side Chain
Ile 203 A Main Chain Carbonyl

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

No Associated Metal Cofactors

Reaction occurs across 10 steps

0.5821

Reaction occurs across 9 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.
0.14 Step 1
GIF of Reaction Step M0267.stg01

Lys161 acts as a nucleophile towards the keto group of the pyruvate substrate, forming a covalently bound enzyme-substrate intermediate. The pyruvate is polarised by the presence of the main chain carbonyl of Ile203, increasing its electrophilicity.
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 M0267.stg02

Proton transfer activates Schiff base formation in the next reaction step.
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.
0.09 Step 3
GIF of Reaction Step M0267.stg03

Elimination of water results in Schiff base formation.
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 M0267.stg04

The covalently bound lysine abstracts a proton from the terminal carbon to form the ene tautomer.
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.
0.33 Step 5
GIF of Reaction Step M0267.stg05

L-aspartate semi aldehyde is thought to enter the active site in the hydrate form. It then undergoes reversible dehydration to form the protonated aldehyde form.
Step 6
GIF of Reaction Step M0111.stg06

The amine initiates an elimination of the bound hydroxide as water, which deprotonates Lys972.
0.14 Step 6
GIF of Reaction Step M0267.stg06

The enamine tautomer of the Schiff base adds to the dehydrated L-aspartate semi aldehyde in a conjugate nucleophilic attack.
Step 7
GIF of Reaction Step M0111.stg07

FMN eliminates a hydride ion, which adds to the C2 imine carbon in an addition reaction.
0.11 Step 7
GIF of Reaction Step M0267.stg07

A 6-exo-tet cyclisation (Baldwin's classification) occurs in the enzyme-substrate intermediate.
Step 8
GIF of Reaction Step M0111.stg08

Lys972 deprotonates water in an inferred step.
0.5 Step 8
GIF of Reaction Step M0267.stg08

Proton transfer is mediated through Tyr133.
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.
0 Step 9
GIF of Reaction Step M0267.stg09

The product is formed and the active site is regenerated for further catalysis.
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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