Entry
Name
methylornithine synthase;
PylB
Class
Isomerases;
Intramolecular transferases;
Transferring other groups
BRITE hierarchy
Sysname
L-lysine carboxy-aminomethylmutase
Reaction(IUBMB)
L-lysine = (3R)-3-methyl-D-ornithine [RN:
R10010 ]
Reaction(KEGG)
Substrate
Product
(3R)-3-methyl-D-ornithine [CPD:
C20277 ]
Comment
The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases.
History
EC 5.4.99.58 created 2012
Pathway
ec01120 Microbial metabolism in diverse environments
Orthology
K16180 methylornithine synthase
Genes
DOR : Desor_1148 Desor_1623 Desor_3055
DMI : Desmer_1592 Desmer_2996
FWA : DCMF_07900 DCMF_16375 DCMF_28145 DCMF_28345
AMIC : Ami3637_11535(pylB)
ABUT : Ami103574_12095(pylB)
MANA : MAMMFC1_01955(bioB_2)
SSPH : SPSPH_029840(pylB) SPSPH_029990(pylB)
SACV : SPACI_001430 SPACI_039560(bioB_3) SPACI_044140(bioB_4)
» show all
Taxonomy
Reference
Authors
Gaston MA, Zhang L, Green-Church KB, Krzycki JA
Title
The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine.
Journal
Sequence
Reference
Authors
Quitterer F, List A, Eisenreich W, Bacher A, Groll M
Title
Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 5.4.99.58