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
MBAMbar_A0840
MBYMSBRM_0154
MBWMSBRW_0161
MBARMSBR2_2227
MBAKMSBR3_2278
MACMA_0150(ramA)
MMAMM_1440
MMAZMmTuc01_1498
MMJMSMAS_3224
MMACMSMAC_3246
MVCMSVAZ_3362
MEKMSKOL_3321
MLSMSLAZ_3207
METMMSMTP_3125
MEFMSWH1_3072
MEQMSWHS_3283
MSJMSSAC_0130
MSZMSSIH_0116
MSWMSSIT_0120
MTHRMSTHT_1930
MTHEMSTHC_1353
MHORMSHOH_3970
MFZAOB57_008950
MBUMbur_1370
MMETMCMEM_1861
MELOJ7W08_08255
MMHMmah_1683
MHAZBHR79_05305
MEVMetev_1953
MZHMzhil_0453
MPYMpsy_1725
MZIHWN40_00990
MHZMetho_0004
MEUZKRP56_04470
 » 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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