MTRE_METAC
ID MTRE_METAC Reviewed; 304 AA.
AC Q8TTZ9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit E {ECO:0000255|HAMAP-Rule:MF_01098};
DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01098};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E {ECO:0000255|HAMAP-Rule:MF_01098};
GN Name=mtrE {ECO:0000255|HAMAP-Rule:MF_01098}; OrderedLocusNames=MA_0276;
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_01098}.
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_01098};
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_01098}.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01098}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01098};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01098}.
CC -!- SIMILARITY: Belongs to the MtrE family. {ECO:0000255|HAMAP-
CC Rule:MF_01098}.
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DR EMBL; AE010299; AAM03729.1; -; Genomic_DNA.
DR RefSeq; WP_011020334.1; NC_003552.1.
DR AlphaFoldDB; Q8TTZ9; -.
DR STRING; 188937.MA_0276; -.
DR EnsemblBacteria; AAM03729; AAM03729; MA_0276.
DR GeneID; 1472168; -.
DR KEGG; mac:MA_0276; -.
DR HOGENOM; CLU_958513_0_0_2; -.
DR InParanoid; Q8TTZ9; -.
DR OMA; QMGNIHR; -.
DR OrthoDB; 50292at2157; -.
DR PhylomeDB; Q8TTZ9; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0012506; C:vesicle membrane; IEA:InterPro.
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 GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR HAMAP; MF_01098; MtrE; 1.
DR InterPro; IPR005780; MeTrfase_E.
DR Pfam; PF04206; MtrE; 1.
DR PIRSF; PIRSF016509; MtrE; 1.
DR TIGRFAMs; TIGR01113; mtrE; 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..304
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT E"
FT /id="PRO_0000147536"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
SQ SEQUENCE 304 AA; 32434 MW; C5BEF98875C5FCAC CRC64;
MEPLIGMGVL ALIGVAATIA GASEDLESDV GSQSNPNSQV QLAPQMMFPH RIFNKAVSGE
PPSNALMCSV GAAVATVLIS EFTLSPLFAL VLGALIAACV HGTFAVTSTM GRAASQSRFK
QPVYLDMIRS HTPVIMGYSF ITTFCILVVS YLMTVVLGHP FPLTMLAFIW GITVGAIGSS
TGDVHYGAER EFQQFEFGSG LNASNSGNIV RYGESGVRNG YDNSWFCAKF GGPVTGMAFG
MTVFLGSWVT TVFDPAVSIS RGWISVVAGV IIVLILIFWN WKIEVKARNA YGPYKEDKTE
EASA
