ID F6D2D1_METPW Unreviewed; 235 AA.
AC F6D2D1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit D {ECO:0000256|ARBA:ARBA00015129, ECO:0000256|HAMAP-Rule:MF_01097};
DE EC=2.1.1.86 {ECO:0000256|ARBA:ARBA00012514, ECO:0000256|HAMAP-Rule:MF_01097};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit D {ECO:0000256|ARBA:ARBA00029820, ECO:0000256|HAMAP-Rule:MF_01097};
GN Name=mtrD {ECO:0000256|HAMAP-Rule:MF_01097};
GN OrderedLocusNames=MSWAN_2054 {ECO:0000313|EMBL:AEG19063.1};
OS Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=868131 {ECO:0000313|EMBL:AEG19063.1, ECO:0000313|Proteomes:UP000009231};
RN [1] {ECO:0000313|Proteomes:UP000009231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC {ECO:0000313|Proteomes:UP000009231};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Chertkov O., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Cadillo-Quiroz H.,
RA Imachi H., Zinder S., Liu W., Woyke T.;
RT "Complete sequence of Methanobacterium sp. SWAN-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG19063.1, ECO:0000313|Proteomes:UP000009231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC {ECO:0000313|Proteomes:UP000009231};
RX PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT lacus isolated from northern peatlands.";
RL Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
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:0000256|ARBA:ARBA00002533, ECO:0000256|HAMAP-
CC Rule:MF_01097}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001816, ECO:0000256|HAMAP-
CC Rule:MF_01097};
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:0000256|ARBA:ARBA00004839, ECO:0000256|HAMAP-Rule:MF_01097}.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000256|ARBA:ARBA00011616,
CC ECO:0000256|HAMAP-Rule:MF_01097}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|HAMAP-Rule:MF_01097}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_01097}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MtrD family. {ECO:0000256|ARBA:ARBA00008822,
CC ECO:0000256|HAMAP-Rule:MF_01097}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01097}.
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DR EMBL; CP002772; AEG19063.1; -; Genomic_DNA.
DR RefSeq; WP_013826562.1; NC_015574.1.
DR AlphaFoldDB; F6D2D1; -.
DR STRING; 868131.MSWAN_2054; -.
DR GeneID; 10669572; -.
DR KEGG; mew:MSWAN_2054; -.
DR eggNOG; arCOG04869; Archaea.
DR HOGENOM; CLU_1109510_0_0_2; -.
DR OrthoDB; 147994at2157; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000009231; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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_01097; MtrD; 1.
DR InterPro; IPR005779; MeTrfase_D.
DR NCBIfam; TIGR01112; mtrD; 1.
DR Pfam; PF04207; MtrD; 1.
DR PIRSF; PIRSF016552; MtrD; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01097};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01097};
KW Methanogenesis {ECO:0000256|ARBA:ARBA00022994, ECO:0000256|HAMAP-
KW Rule:MF_01097};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01097}; One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_01097};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01097}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_01097};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01097}.
FT TRANSMEM 44..61
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 68..94
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 128..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 166..191
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
SQ SEQUENCE 235 AA; 23429 MW; 97B65AB3584C82E1 CRC64;
MDPLLLIGAI TAGGVLIGGG VHFIPVGGAP AAIATATGVG TGTAMLAAGS GMTGLITAAA
MTGSPLWVIL AAGAVGSMIM LDITMLVGNF IYVWGVGIVP ASAKVEYDPI TKYPQEKYVT
PGTEGHGIPT VCFVSGTIGA ALGGIGGGLV YWALYNALTT AGLSYTSLAA TTVAGIFAVG
MFFVNAVIAS YNIGGTIEGF HDPKFKRLGR GVLACLLASL VVGIFSVLLI KGGVF
//
