KEGG   ENZYME: 1.16.99.1
Entry
EC 1.16.99.1                Enzyme                                 

Name
[Co(II) methylated amine-specific corrinoid protein] reductase
Class
Oxidoreductases;
Oxidizing metal ions;
With unknown physiological acceptors
Sysname
acceptor:[cobalt(II) methylated amines-specific corrinoid protein] oxidoreductase (ATP-hydrolysing)
Reaction(IUBMB)
(1) ATP + a [Co(II) methylamine-specific corrinoid protein] + reduced acceptor + H2O = ADP + phosphate + a [Co(I) methylamine-specific corrinoid protein] + acceptor;
(2) ATP + a [Co(II) dimethylamine-specific corrinoid protein] + reduced acceptor + H2O = ADP + phosphate + a [Co(I) dimethylamine-specific corrinoid protein] + acceptor;
(3) ATP + a [Co(II) trimethylamine-specific corrinoid protein] + reduced acceptor + H2O = ADP + phosphate + a [Co(I) trimethylamine-specific corrinoid protein] + acceptor
Substrate
ATP [CPD:C00002];
[Co(II) methylamine-specific corrinoid protein];
reduced acceptor [CPD:C00030];
H2O [CPD:C00001];
[Co(II) dimethylamine-specific corrinoid protein];
[Co(II) trimethylamine-specific corrinoid protein]
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
[Co(I) methylamine-specific corrinoid protein];
acceptor [CPD:C00028];
[Co(I) dimethylamine-specific corrinoid protein];
[Co(I) trimethylamine-specific corrinoid protein]
Comment
Methyltrophic corrinoid proteins must have the cobalt atom in the active cobalt(I) state to become methylated. Because the cobalt(I)/cobalt(II) transformation has a very low redox potential the corrinoid cofactor is subject to adventitious oxidation to the cobalt(II) state, which renders the proteins inactive. This enzyme, characterized from the methanogenic archaeon Methanosarcina barkeri, reduces cobalt(II) back to cobalt(I), restoring activity. The enzyme acts on the corrinoid proteins involved in methanogenesis from methylamine, dimethylamine, and trimethylamine, namely MtmC, MtbC, and MttC, respectively. While in vitro the enzyme can use Ti(III)-citrate as the electron donor, the in vivo donor is not known. The enzyme from Methanosarcina barkeri contains a C-terminal [4Fe-4S] ferredoxin-like domain.
History
EC 1.16.99.1 created 2021
Orthology
K16183  [Co(II) methylated amine-specific corrinoid protein] reductase
Genes
MBA: Mbar_A0840
MBY: MSBRM_0154
MBW: MSBRW_0161
MBAR: MSBR2_2227
MBAK: MSBR3_2278
MAC: MA_0150(ramA)
MMA: MM_1440
MMAZ: MmTuc01_1498
MMJ: MSMAS_3224
MMAC: MSMAC_3246
METM: MSMTP_3125
MTHR: MSTHT_1930
MTHE: MSTHC_1353
MHOR: MSHOH_3970
MBU: Mbur_1370
MMET: MCMEM_1861
MMH: Mmah_1683
MPY: Mpsy_1725
 » show all
Reference
1  [PMID:19043046]
  Authors
Ferguson T, Soares JA, Lienard T, Gottschalk G, Krzycki JA.
  Title
RamA, a protein required for reductive activation of corrinoid-dependent methylamine methyltransferase reactions in methanogenic archaea.
  Journal
J Biol Chem 284:2285-95 (2009)
DOI:10.1074/jbc.M807392200
  Sequence
Reference
2  [PMID:31359509]
  Authors
Durichen H, Diekert G, Studenik S.
  Title
Redox potential changes during ATP-dependent corrinoid reduction determined by redox titrations with europium(II)-DTPA.
  Journal
Protein Sci 28:1902-1908 (2019)
DOI:10.1002/pro.3699
Other DBs
ExplorEnz - The Enzyme Database: 1.16.99.1
IUBMB Enzyme Nomenclature: 1.16.99.1
ExPASy - ENZYME nomenclature database: 1.16.99.1
BRENDA, the Enzyme Database: 1.16.99.1

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