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Overview for MACiE Entry M0214

Version history

General Information

EC Number: 2.4.2.14 (A member of the Transferases, Glycosyltransferases, Pentosyltransferases)

Enzyme Name: amidophosphoribosyltransferase

Biological Species: Escherichia coli (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • P0AG16 - Amidophosphoribosyltransferase

Representative PDB Code: 1ecf - ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP)AMIDOTRANSFERASE (Resolution = 2.00 Å).

Catalytic CATH Codes:

  • 3.60.20.10 - Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of L-Glutamine

Image of Water

Image of 5-Phospho-alpha-D-ribose-1-diphosphate

right arrow

Image of 5-Phosphoribosylamine

Image of L-Glutamate

Image of diphosphate

L-Glutamine
C00064
CHEBI:29988
Water
C00001
CHEBI:15377
5-Phospho-alpha-D-ribose-1-diphosphate
C00119
CHEBI:17111
5-Phosphoribosylamine
C03090
CHEBI:17284
L-Glutamate
C00025
CHEBI:29985
diphosphate
C00013
CHEBI:33019

Overall Comment: Enzyme exhibits allostery and feedback inhibition from its products. Reaction occurs in two separate catalytic domains, however second half reaction shows no catalytic residues are required.


View similar reactions


Stepwise Description of the Reaction

Step 1The N-terminus of Cys1 deprotonates the thiol group of Cys1, which attacks the amino carbon in a nucleophilic addition.)ReactiveCentres=(N,H,O,H,S,C,O
Step 2The oxyanion initiates an elimination that cleaves ammonia from the bound L-Glutamine substrate. Ammonia deprotonates the N-terminus of Cys1.
Step 3The N-terminus of Cys1 deprotonates water, which attacks the carbonyl carbon of the covalently bound intermediate.
Step 4The oxyanion initiates an elimination that cleaves the C-S bond, the thiolate of Cys1 deprotonates the N-terminus of Cys1
Step 5Ammonia attacks the C1 of the 5-Phospho-alpha-D-ribose-1-diphosphate substrate in a nucleophilic substitution. The product pyrophosphate deprotonates the newly attached ammonia.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Cys 1 A Main Chain N Terminus
Side Chain
Asn 101 A Side Chain
Gly 102 A Main Chain Amide
Gly 27 A Main Chain Carbonyl
Tyr 258 A Side Chain

Metal Cofactors for M0214

Type Het group Number Chain
magnesium MN 506 A Overview
iron No Available PDB Information

References

  1. J. L. Smith (1998), Curr. Opin. Struct. Biol., 8, 686-694. Glutamine PRPP amidotransferase: snapshots of an enzyme in action.
    Medline: 9914248

Homologue information for M0214 (1ecf)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0304 glutamate synthase (NADPH)
1.4.1.13
1ea0 3.60.20.10
0.54870.6136Compare
M0111 glutamate synthase (ferredoxin)
1.4.7.1
1ofd 3.60.20.10
0.750.2571Compare
M0082 glutamine-fructose-6-phosphate transaminase (isomerizing)
2.6.1.16
1jxa 3.60.20.10
0.55550.2265Compare
M0177 proteasome endopeptidase complex
3.4.25.1
1ryp 3.60.20.10
0.50720.1058Compare
M0302 asparagine synthase (glutamine-hydrolysing)
6.3.5.4
1ct9 3.60.20.10
0.90.4145Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.60.20.10


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

GOA logo
amidophosphoribosyltransferase activity (molecular function)
metabolic process (biological process)
purine nucleobase biosynthetic process (biological process)
nucleoside metabolic process (biological process)
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