KEGG   ENZYME: 2.1.1.258Help
Entry
EC 2.1.1.258                Enzyme                                 

Name
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase;
acsE (gene name)
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
5-methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
Reaction(IUBMB)
a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate [RN:R02289]
Reaction(KEGG)
R02289;
(other) R10243
Show
Substrate
[methyl-Co(III) corrinoid Fe-S protein];
tetrahydrofolate [CPD:C00101]
Product
[Co(I) corrinoid Fe-S protein];
5-methyltetrahydrofolate [CPD:C00440]
Comment
Catalyses the transfer of a methyl group from the N5 group of methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein. Involved, together with EC 1.2.7.4, carbon-monoxide dehydrogenase (ferredoxin) and EC 2.3.1.169, CO-methylating acetyl-CoA synthase, in the reductive acetyl coenzyme A (Wood-Ljungdahl) pathway of autotrophic carbon fixation in various bacteria and archaea.
History
EC 2.1.1.258 created 2012
Pathway
Carbon fixation pathways in prokaryotes
Microbial metabolism in diverse environments
Orthology
K15023  
5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase
Genes
DAK: 
DSF: 
DOL: 
DAL: 
DAT: 
HRM2_16640(metH3)
DTO: 
DAO: 
DTI: 
SFU: 
DBR: 
CLJ: 
CAH: 
CSQ: 
CACE: 
CCK: 
AMT: 
RUM: 
ROB: 
CDF: 
PDC: 
CDC: 
CDL: 
CDG: 
PDF: 
CST: 
DSY: 
DHD: 
DDH: 
DDL: 
DMT: 
DAE: 
DKU: 
DGI: 
PTH: 
PTH_1004(MetH)
DAU: 
TJR: 
DOR: 
DAI: 
DMI: 
DED: 
DEC: 
DRS: 
ELM: 
AWO: 
TKI: 
CHY: 
CHY_1227(acsE)
TEP: 
TAE: 
MTA: 
ADG: 
TPZ: 
TOC: 
AAR: 
DLY: 
DEW: 
TAZ: 
TPI: 
TYE: 
TID: 
TCM: 
CTHI: 
MER: 
 » show all
Taxonomy
Reference
1  [PMID:7928975]
  Authors
Roberts DL, Zhao S, Doukov T, Ragsdale SW
  Title
The reductive acetyl coenzyme A pathway: sequence and heterologous expression of  active methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase from Clostridium thermoaceticum.
  Journal
J. Bacteriol. 176 (1994) 6127-30.
  Sequence
[mta:Moth_1197]
Reference
2  [PMID:10997901]
  Authors
Doukov T, Seravalli J, Stezowski JJ, Ragsdale SW
  Title
Crystal structure of a methyltetrahydrofolate- and corrinoid-dependent methyltransferase.
  Journal
Structure. 8 (2000) 817-30.
  Sequence
[mta:Moth_1197]
Reference
3  [PMID:17172470]
  Authors
Doukov TI, Hemmi H, Drennan CL, Ragsdale SW
  Title
Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in  activation of methyl transfer by methyltransferases.
  Journal
J. Biol. Chem. 282 (2007) 6609-18.
  Sequence
[mta:Moth_1197]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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