KEGG   ENZYME: 2.1.1.379
Entry
EC 2.1.1.379                Enzyme                                 
Name
[methyl coenzyme M reductase]-L-arginine C-5-methyltransferase;
methanogenesis marker protein 10;
Mmp10
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:[methyl coenzyme M reductase]-L-arginine C-5-(S)-methyltransferase
Reaction(IUBMB)
2 S-adenosyl-L-methionine + a [methyl coenzyme-M reductase]-L-arginine + reduced acceptor = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + a [methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine + acceptor [RN:R12788]
Reaction(KEGG)
R12788
Substrate
S-adenosyl-L-methionine [CPD:C00019];
[methyl coenzyme-M reductase]-L-arginine;
reduced acceptor [CPD:C00030]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
L-methionine [CPD:C00073];
5'-deoxyadenosine [CPD:C05198];
[methyl coenzyme-M reductase]-(5S)-C-methyl-L-arginine;
acceptor [CPD:C00028]
Comment
The enzyme, present in methanogenic archaea, catalyses a modification of an L-arginine residue at the active site of EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase (better known as methyl-coenzyme M reductase), which catalyses the last and methane-releasing step of methanogenesis. The enzyme is a radical AdoMet (radical SAM) enzyme and contains a [4Fe-4S] cluster and a Coalpha-[alpha-(5-hydroxybenzimidazolyl)]-cobamide cofactor. The methyl group, which is derived from S-adenosyl-L-methionine, is transferred to the cob(I)amide cofactor, forming methylcob(III)amide as an intermediate carrier, before being transferred to the arginine residue.
History
EC 2.1.1.379 created 2021
Orthology
K25222  [methyl coenzyme M reductase]-L-arginine C-5-methyltransferase
Genes
MJAMJ_0841
MFEMefer_0933
MVUMetvu_0144
MFSMFS40622_1320
MIFMetin_0607
MJHJH146_1061
MESGMLAUSG7_0358
MESAMLASG1_1537
MIGMetig_1232
MMPMMP1554
MMQMmarC5_0022
MMXMmarC6_1116
MMZMmarC7_0801
MMDGYY_08620
MMAKMMKA1_17840
MMAOMMOS7_16660
MMADMMJJ_12820
MAEMaeo_1262
MVNMevan_0867
MVOMvol_1123
MOKMetok_0961
METFCFE53_01215
MTHMTH_1170
MMGMTBMA_c15530
MWOMWSIV6_1561
MTEEMTTB_02530
METCMTCT_1063
METEtca_01126
METZMETMT2_1177
METKFVF72_05740
MTHMFZP57_07480
METJFZP68_03195
MSTMsp_0298
METBAW729_05645
MEISPXD04_05290(mmp10)
MRUmru_1929
MSIMsm_1020
MEBAbm4_1531
MMILsm9_2032
MEYETL18_09345
MOLYLM1_1384
MAROMarbSA_15370
METVK4897_06365(mmp10)
MELMetbo_0348
MEWMSWAN_2061
METHMBMB1_1687
MFCBRM9_0940
MFIDSM1535_0910
MCUBMCBB_1990
MSUBBK009_07430
METNBK008_03085
METTCIT01_03655
METOCIT02_09455
MEMEHYG87_04650(mmp10) HYG87_05010(mmp10)
MFEGGCM10025860_02870
MFVMfer_0789
MKAMK0650
MBAMbar_A0898
MBYMSBRM_0096
MBWMSBRW_0100
MBARMSBR2_2284
MBAKMSBR3_2345
MACMA_4551
MMAMM_1245
MMJMSMAS_0068
MMACMSMAC_0067
MVCMSVAZ_3418
MEKMSKOL_3379
MLSMSLAZ_0161
METMMSMTP_0095
MEFMSWH1_0084
MEQMSWHS_0087
MSJMSSAC_4250
MSZMSSIH_3754
MSWMSSIT_3833
MTHRMSTHT_1639
MTHEMSTHC_1650
MHORMSHOH_0079
MFZAOB57_007310
MBUMbur_2422
MMETMCMEM_0564
MELOJ7W08_00855(mmp10)
MMHMmah_0617
MHAZBHR79_00285
MEVMetev_0908
MZHMzhil_1044
MPYMpsy_0834
MZIHWN40_04495(mmp10)
MMAVRE476_05675(mmp10)
MSEBRE474_02880(mmp10)
MHZMetho_1665
MEHFMmiHf6_13420
MEESMmiEs2_15810
MTPMthe_0508
MCJMCON_2443
MHIMhar_0503
MHUMhun_2512
MRTJKHC33_00230(mmp10)
MLAMlab_1316
MEMMemar_1632
MBGBN140_2007
MEMAMMAB1_2598
MCHKMchiMG62_17820
MSUMOH143_02375(mmp10)
MRCR6Y96_06550(mmp10)
MPIMpet_2296
MENDL6E24_03885(mmp10)
MEFWF1737_01495
MAQERJ40_01245
MOUOU421_01490(mmp10)
MESBL1S32_05010(mmp10)
MANQL1994_02440(mmp10)
MBNMboo_1781
MFOMetfor_1315
MPLMpal_1909
MPDMCP_1925
MEZMtc_1160
RCILRC180
MELUMTLP_08800
 » show all
Reference
1  [PMID:29743535]
  Authors
Deobald D, Adrian L, Schone C, Rother M, Layer G.
  Title
Identification of a unique Radical SAM methyltransferase required for the sp(3)-C-methylation of an arginine residue of methyl-coenzyme M reductase.
  Journal
Sci Rep 8:7404 (2018)
DOI:10.1038/s41598-018-25716-x
  Sequence
[mac:MA_4551]
Reference
2  [PMID:31113866]
  Authors
Radle MI, Miller DV, Laremore TN, Booker SJ.
  Title
Methanogenesis marker protein 10 (Mmp10) from Methanosarcina acetivorans is a radical S-adenosylmethionine methylase that unexpectedly requires cobalamin.
  Journal
J Biol Chem 294:11712-11725 (2019)
DOI:10.1074/jbc.RA119.007609
  Sequence
[mac:MA_4551]
Reference
3  [PMID:31740491]
  Authors
Lyu Z, Shao N, Chou CW, Shi H, Patel R, Duin EC, Whitman WB.
  Title
Posttranslational Methylation of Arginine in Methyl Coenzyme M Reductase Has a Profound Impact on both Methanogenesis and Growth of Methanococcus maripaludis.
  Journal
J Bacteriol 202:e00654-19 (2020)
DOI:10.1128/JB.00654-19
  Sequence
[mmp:MMP1554]
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.379
IUBMB Enzyme Nomenclature: 2.1.1.379
ExPASy - ENZYME nomenclature database: 2.1.1.379
BRENDA, the Enzyme Database: 2.1.1.379

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