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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 M0223

These two reactions have a combined similarity of 0.36


M0111

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Comparison

M0223

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EC 1.4.7.1
glutamate synthase (ferredoxin)
Class EC 6.4.1.1
pyruvate carboxylase

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 ATP

Image of bicarbonate

Image of pyruvate

right arrow

Image of proton

Image of oxaloacetate

Image of phosphate

Image of ADP

ATP
C00002
CHEBI:30616
bicarbonate
C00288
CHEBI:17544
pyruvate
C00022
CHEBI:15361
proton
C00080
CHEBI:24636
oxaloacetate
C00036
CHEBI:16452
phosphate
C00009
CHEBI:18367
ADP
C00008
CHEBI:456216

Catalytic CATH Codes

3.60.20.10
3.20.20.70

Catalytic CATH Codes

3.20.20.70

Active Site



0.05994

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
0.0666

Catalytic Residues

Type Number Chain Location of Function
Asp 549 A Side Chain
Asp 655 A Side Chain
Lys 718 A Side Chain

Organic Cofactors

Type Identity Chain
FMN FMN 2508 A

Organic Cofactors

Type Identity Chain
Biotin BTN 0

Metal Cofactors

Type Het group Number Chain
iron F3S 2509 A

Metal Cofactors

Type Het group Number Chain
zinc ZN 1157 A
magnesium MG 1156 B
magnesium MG 1157 B

Reaction occurs across 10 steps

0.535

Reaction occurs across 7 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.
0.22 Step 1
GIF of Reaction Step M0223.stg01

Reaction occurs in the BC domain. The bicarbonate is deprotonated by an unidentified base. The activate bicarbonate then acts as a nucleophile and attacks the gamma-phosphate in a substitution reaction, liberating ADP. Mg(II) stabilises/activates the ATP
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.
0.14 Step 2
GIF of Reaction Step M0223.stg02

Reaction occurs in the BC domain. The phosphorylated bicarbonate undergoes a decarboxylation reaction (E1cb) to liberate carbon dioxide and phosphate.
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.
0.2 Step 3
GIF of Reaction Step M0223.stg03

Reaction occurs in the BC domain. The phosphate deprotonates one of the N-H groups of biotin with concomitant tautomerisation to produce an oxyanion.
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
0.11 Step 4
GIF of Reaction Step M0223.stg04

Reaction occurs in the BC domain. The oxyanion re-forms the carbonyl group, causing the C=N bond of the activated biotin to add to the carbon dioxide in a nucleophilic manner.
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 M0223.stg05

Reaction occurs in the CT domain. The Asp549 deprotonates pyruvate, activating the pyruvate in a keto-enol tautomerisation.
Step 6
GIF of Reaction Step M0111.stg06

The amine initiates an elimination of the bound hydroxide as water, which deprotonates Lys972.
0.33 Step 6
GIF of Reaction Step M0223.stg06

Reaction occurs in the CT domain. The activated pyruvate attacks the carboxylated biotin in a nucleophilic substitution, producing the oxaloacetate product and activated biotin.
Step 7
GIF of Reaction Step M0111.stg07

FMN eliminates a hydride ion, which adds to the C2 imine carbon in an addition reaction.
0.05 Step 7
GIF of Reaction Step M0223.stg07

Reaction occurs in the CT domain. Lys718 deprotonates the activated biotin, which in turn deprotonates Asp549, returning the enzyme to its ground state.
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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