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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 M0234 and M0279

These two reactions have a combined similarity of 0.15


M0234

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Comparison

M0279

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EC 6.3.5.2
GMP synthase (glutamine-hydrolysing)
Class EC 1.8.4.8
phosphoadenylyl-sulfate reductase (thioredoxin)

Image of xanthosine 5'-phosphate

Image of L-glutamine

Image of ATP

Image of Water

right arrow

Image of L-glutamic acid

Image of AMP

Image of GMP

Image of diphosphate

xanthosine 5'-phosphate
C00655
CHEBI:53012
L-glutamine
C00064
CHEBI:32666
ATP
C00002
CHEBI:30616
Water
C00001
CHEBI:15377
L-glutamic acid
C00025
CHEBI:16015
AMP
C00020
CHEBI:456215
GMP
C00144
CHEBI:58115
diphosphate
C00013
CHEBI:33019
0.25

Image of thioredoxin

Image of 3'-phosphoadenylyl sulfate

right arrow

Image of sulfite

Image of adenosine 3',5'-bisphosphate

Image of oxidised thioredoxin

thioredoxin
C00342
CHEBI:15967
3'-phosphoadenylyl sulfate
C00053
CHEBI:17980
sulfite
C00094
CHEBI:48854
adenosine 3',5'-bisphosphate
C00054
CHEBI:17985
oxidised thioredoxin
C00343
CHEBI:18191

Catalytic CATH Codes

3.40.50.880
3.40.50.620

Catalytic CATH Codes

3.40.50.620
0.0.0.0

Active Site



0.23994

Active Site



Catalytic Residues

Type Number Chain Location of Function
Lys 381 B Side Chain
Asp 239 B Side Chain
Glu 183 B Side Chain
His 181 B Side Chain
Cys 86 B Side Chain
Gly 59 B Main Chain Amide
Tyr 87 B Main Chain Amide
0.2666

Catalytic Residues

Type Number Chain Location of Function
Tyr 209 B Side Chain
Trp 204 B Side Chain
Cys 239 B Side Chain
Tyr 209 A Side Chain
Trp 204 A Side Chain
Cys 239 A Side Chain

Organic Cofactors

No Associated Organic Cofactors

Organic Cofactors

No Associated Organic Cofactors

Metal Cofactors

Type Het group Number Chain
magnesium MG 530 B

Metal Cofactors

No Associated Metal Cofactors

Reaction occurs across 6 steps

0.1076

Reaction occurs across 5 steps

Step 1
GIF of Reaction Step M0234.stg01

The beta-phosphate deprotonates the XMP substrate, which then initiates a nucleophilic attack on the alpha-phosphate of ATP, eliminating pyrophosphate.
0 Step 1
GIF of Reaction Step M0279.stg01

Thioredoxin reduces the active site disulfide bridge.
Step 2
GIF of Reaction Step M0234.stg02

His181 deprotonates Cys86, activating it for a nucleophilic attack upon L-glutamine, forming an enzyme-substrate covalent bond.
0.2 Step 2
GIF of Reaction Step M0279.stg02

Cys239' deprotonates the thioredoxin intermediate.
Step 3
GIF of Reaction Step M0234.stg03

The tetrahedral intermediate collapses, liberating ammonia, which deprotonates His181 and then passes to the other catalytic domain.
0 Step 3
GIF of Reaction Step M0279.stg03

The free thiol on Cys239 initiates nucleophilic attack at the substrate.
Step 4
GIF of Reaction Step M0234.stg04

Ammonia is deprotonated by the phosphate of the intermediate, activating it for a nucleophilic attack on the intermediate, which liberates AMP and the GMP product.
0.2 Step 4
GIF of Reaction Step M0279.stg04

The anionic phosphate leaving group accepts a proton from the covalently bound Cys239B.
Step 5
GIF of Reaction Step M0234.stg05

His181 deprotonates a water molecule, which initiates a nucleophilic attack on the Cys-bound intermediate.
0 Step 5
GIF of Reaction Step M0279.stg05

Cys239 attacks Cys239', eliminating sulfite with concomitant regeneration of the active site.
Step 6
GIF of Reaction Step M0234.stg06

The tetrahedral intermediate collapses, liberating Cys86, which deprotonates His181, and the glutamate product.
N/A Step 6
No Step with this number present

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