ID Q12VU5_METBU Unreviewed; 239 AA.
AC Q12VU5;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 ECO:0000313|EMBL:ABE52431.1};
GN OrderedLocusNames=Mbur_1524 {ECO:0000313|EMBL:ABE52431.1};
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564 {ECO:0000313|EMBL:ABE52431.1, ECO:0000313|Proteomes:UP000001979};
RN [1] {ECO:0000313|Proteomes:UP000001979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M
RC {ECO:0000313|Proteomes:UP000001979};
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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}.
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DR EMBL; CP000300; ABE52431.1; -; Genomic_DNA.
DR RefSeq; WP_011499575.1; NC_007955.1.
DR AlphaFoldDB; Q12VU5; -.
DR STRING; 259564.Mbur_1524; -.
DR GeneID; 3997347; -.
DR KEGG; mbu:Mbur_1524; -.
DR HOGENOM; CLU_1109510_0_0_2; -.
DR OrthoDB; 147994at2157; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000001979; 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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 52..69
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 76..103
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 143..164
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 176..197
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01097"
SQ SEQUENCE 239 AA; 24091 MW; 7353B87D0385FDBB CRC64;
MIDVAGILAE NILYIAMVTL GGMLISWSVH FVPVGGAPAA MAQATGIGTG TVQLAAGAGL
TGLVTAGAVM AVSDSLLLVV ASGGVGAMIM IAVTMIVGTW VYVYGVGVPP ASAKVDYDPI
TKDRQDIYVS QGTEGHGLPT VSYVSGVIGG ALGGIGGSAI YFALMSTSTT LIQSDLVALA
SIFAVGIFFV NAVIPSYNIG GTIEGFHDPK FKKWPKAVLA SFVATLMCAF VGIITIGGL
//
