MCRAM_METAC
ID MCRAM_METAC Reviewed; 411 AA.
AC Q8THG6;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=[Methyl-coenzyme M reductase subunit alpha]-arginine C-methyltransferase {ECO:0000305|PubMed:29743535};
DE EC=2.1.1.- {ECO:0000305|PubMed:29743535};
GN OrderedLocusNames=MA_4551 {ECO:0000312|EMBL:AAM07890.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP FUNCTION, COFACTOR, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=29743535; DOI=10.1038/s41598-018-25716-x;
RA Deobald D., Adrian L., Schoene C., Rother M., Layer G.;
RT "Identification of a unique radical SAM methyltransferase required for the
RT sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase.";
RL Sci. Rep. 8:7404-7404(2018).
CC -!- FUNCTION: Radical SAM methyltransferase that is responsible for the
CC C(5)-methylation of 'Arg-285' of the methyl-coenzyme M reductase (MCR)
CC subunit alpha McrA. This post-translational methylation, despite being
CC not essential in vivo, plays a role for the stability and structural
CC integrity of MCR. {ECO:0000269|PubMed:29743535}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:29743535};
CC Note=Binds at least 1 [4Fe-4S] cluster. This cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000305|PubMed:29743535};
CC -!- PATHWAY: Protein modification. {ECO:0000269|PubMed:29743535}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce an active MCR
CC lacking the C(5)-methylation of the respective arginine residue. The
CC mutant strain shows impaired growth under stress conditions, such as
CC the presence of 0.2 mM hydrogen peroxide (H2O2) or elevated temperature
CC (42 degrees Celsius). {ECO:0000269|PubMed:29743535}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MCR alpha subunit
CC C-methyltransferase family. {ECO:0000305}.
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DR EMBL; AE010299; AAM07890.1; -; Genomic_DNA.
DR RefSeq; WP_011024424.1; NC_003552.1.
DR AlphaFoldDB; Q8THG6; -.
DR SMR; Q8THG6; -.
DR STRING; 188937.MA_4551; -.
DR EnsemblBacteria; AAM07890; AAM07890; MA_4551.
DR GeneID; 1476445; -.
DR KEGG; mac:MA_4551; -.
DR HOGENOM; CLU_668380_0_0_2; -.
DR InParanoid; Q8THG6; -.
DR OMA; IHLGYTS; -.
DR OrthoDB; 21265at2157; -.
DR PhylomeDB; Q8THG6; -.
DR BioCyc; MetaCyc:MON-21042; -.
DR BRENDA; 2.1.1.379; 7224.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017672; MA_4551-like.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF04055; Radical_SAM; 1.
DR TIGRFAMs; TIGR03278; methan_mark_10; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..411
FT /note="[Methyl-coenzyme M reductase subunit alpha]-arginine
FT C-methyltransferase"
FT /id="PRO_0000446661"
FT DOMAIN 1..253
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305|PubMed:29743535"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305|PubMed:29743535"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305|PubMed:29743535"
SQ SEQUENCE 411 AA; 45222 MW; F92CDCD6E2158852 CRC64;
MEVVVDVGGN PGVDCKGFCK YCYFKKVKDI QPLGCKYCLP FKKGCDYCTR SVKESYSGFK
SLQMVLEETA NKLYFTSGEV KKFTVSGGGD LSCYPELKSL ITFLSQFNTP IHLGYTSGKG
FSKPDDALFY IDNGVTEVSF TVFATDPALR AEYMKDPEPE ASIQVLRDFC THCEVYGAIV
LLPGINDGEV LEKTLCDLEN MGAKGAILMR FANFQENGLI LNNSPIIPGI TPHTVSEFTE
IVRSSAEKHP SIRITGTPLE DPLIGSPFAI RNVPEALLKL PRVSKKATII TGQVAASRLT
EIFEALGGTV NVIPVKKDIG CLITIDDFKA LDLSEVTETV FIPGRAFVHD MEIKEALRRD
GVDRIVRRGP ERLSVDGEMS IGMTREEVLE LEVENFTELI GQINSLGLPL E
