MTRC_METAC
ID MTRC_METAC Reviewed; 267 AA.
AC Q8TU01;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit C {ECO:0000255|HAMAP-Rule:MF_01096};
DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01096};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit C {ECO:0000255|HAMAP-Rule:MF_01096};
GN Name=mtrC {ECO:0000255|HAMAP-Rule:MF_01096}; OrderedLocusNames=MA_0274;
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).
CC -!- FUNCTION: Part of a complex that catalyzes the formation of methyl-
CC coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-
CC tetrahydromethanopterin. This is an energy-conserving, sodium-ion
CC translocating step. {ECO:0000255|HAMAP-Rule:MF_01096}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2
CC Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2
CC Na(+)(out); Xref=Rhea:RHEA:53492, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:58103, ChEBI:CHEBI:58116, ChEBI:CHEBI:58286,
CC ChEBI:CHEBI:58319; EC=2.1.1.86; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01096};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl-
CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_01096}.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01096}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01096};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01096}.
CC -!- SIMILARITY: Belongs to the MtrC family. {ECO:0000255|HAMAP-
CC Rule:MF_01096}.
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DR EMBL; AE010299; AAM03727.1; -; Genomic_DNA.
DR RefSeq; WP_011020332.1; NC_003552.1.
DR AlphaFoldDB; Q8TU01; -.
DR STRING; 188937.MA_0274; -.
DR EnsemblBacteria; AAM03727; AAM03727; MA_0274.
DR GeneID; 1472166; -.
DR KEGG; mac:MA_0274; -.
DR HOGENOM; CLU_092286_0_0_2; -.
DR InParanoid; Q8TU01; -.
DR OMA; HPFNACL; -.
DR OrthoDB; 61293at2157; -.
DR PhylomeDB; Q8TU01; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01096; MtrC; 1.
DR InterPro; IPR005865; THM_MeTrfase_su_C.
DR Pfam; PF04211; MtrC; 1.
DR PIRSF; PIRSF006530; MtrC; 1.
DR TIGRFAMs; TIGR01148; mtrC; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Methanogenesis; Methyltransferase;
KW One-carbon metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..267
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT C"
FT /id="PRO_0000147520"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
SQ SEQUENCE 267 AA; 26950 MW; FD258F13BE4D92ED CRC64;
MSAGGAGGEA KGGFPPQTIM AIGAIGGLAG IYLGNFMPAQ FSFFGGLGAI CAMVWGADAV
RRVASYGLGT GVPSIGMISL GMGIVAALFG LSVGGIAGPI VSFIAAAIIG AVIGVLANKV
IGMGIPIMEQ AMVEIAGAGT LVIIGLSVVI AGTFDYAEVV EYVVANGYIA LIFIIGGMGI
LHPFNANLGP DEKQDRTLSV AVEKAAIALI ITGFASSLHE GLMAAGLNIA VGVIIWAWAF
MKYYGYVKRD SYAVVGTGLL PSAEELE
