Entry
Name
S-methyl-1-thioxylulose 5-phosphate methylthiotransferase;
1-methylthioxylulose 5-phosphate sulfurylase (incorrect)
Class
Transferases;
Transferring sulfur-containing groups;
Transferring alkylthio groups
BRITE hierarchy
Sysname
S-methyl-1-thio-D-xylulose 5-phosphate:glutathione methylthiotransferase
Reaction(IUBMB)
S-methyl-1-thio-D-xylulose 5-phosphate + glutathione = 1-deoxy-D-xylulose 5-phosphate + S-(methylsulfanyl)glutathione [RN:
R12946 ]
Reaction(KEGG)
Substrate
S-methyl-1-thio-D-xylulose 5-phosphate [CPD:
C22359 ];
glutathione [CPD:
C00051 ]
Product
1-deoxy-D-xylulose 5-phosphate [CPD:
C11437 ];
S-(methylsulfanyl)glutathione [CPD:
C22462 ]
Comment
The enzyme, characterized from the bacterium Rhodospirillum rubrum, belongs to the cupin superfamily and contains a manganese ion. It participates in an anaerobic salvage pathway that restores methionine from S-methyl-5'-thioadenosine. The enzyme was assayed in vitro using L-dithiothreitol instead of glutathione.
History
EC 2.8.4.6 created 2021
Pathway
ec00270 Cysteine and methionine metabolism
Orthology
K01767 S-methyl-1-thioxylulose 5-phosphate methylthiotransferase
Genes
URU : DSM104443_00898(cupin)
UPL : DSM104440_00832(cupin)
THUG : KNN16_02745 KNN16_02770
» show all
Taxonomy
Reference
Authors
Erb TJ, Evans BS, Cho K, Warlick BP, Sriram J, Wood BM, Imker HJ, Sweedler JV, Tabita FR, Gerlt JA.
Title
A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis.
Journal
Sequence
Reference
Authors
Warlick BP, Evans BS, Erb TJ, Ramagopal UA, Sriram J, Imker HJ, Sauder JM, Bonanno JB, Burley SK, Tabita FR, Almo SC, Sweedler JS, Gerlt JA.
Title
1-methylthio-D-xylulose 5-phosphate methylsulfurylase: a novel route to 1-deoxy-D-xylulose 5-phosphate in Rhodospirillum rubrum.
Journal
Reference
Authors
Cho K, Evans BS, Wood BM, Kumar R, Erb TJ, Warlick BP, Gerlt JA, Sweedler JV.
Title
Integration of untargeted metabolomics with transcriptomics reveals active metabolic pathways.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.8.4.6
ExPASy - ENZYME nomenclature database: 2.8.4.6
BRENDA, the Enzyme Database: 2.8.4.6