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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 M0054

These two reactions have a combined similarity of 0.52


M0111

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Comparison

M0054

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EC 1.4.7.1
glutamate synthase (ferredoxin)
Class EC 4.2.1.10
3-dehydroquinate dehydratase (type I)

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 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

3.60.20.10
3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.16164

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
Glu 86 A Side Chain
His 143 A Side Chain
Lys 170 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

No Associated Metal Cofactors

Reaction occurs across 10 steps

0.7519

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.
0.16 Step 1
GIF of Reaction Step M0054.stg01

Glu86 deprotonates His143, which deprotonates Lys170, activating it.
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 Step 2
GIF of Reaction Step M0054.stg02

Lys170 attacks the carbonyl carbon of the substrate in a nucleophilic addition.
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.
0.11 Step 3
GIF of Reaction Step M0054.stg03

A proton is transferred from the covalently attached lysine to the newly formed hydroxide.
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
0.23 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
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.
0.16 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
GIF of Reaction Step M0111.stg06

The amine initiates an elimination of the bound hydroxide as water, which deprotonates Lys972.
0.45 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
GIF of Reaction Step M0111.stg07

FMN eliminates a hydride ion, which adds to the C2 imine carbon in an addition reaction.
0.38 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
GIF of Reaction Step M0111.stg08

Lys972 deprotonates water in an inferred step.
0.5 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
GIF of Reaction Step M0111.stg09

Ferredoxin donates a single electron, which is transferred to FMN through an iron-sulfur cluster. FMN deprotonates water.
0.57 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.
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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